--- _id: '13362' abstract: - lang: eng text: Aggregation of organic molecules can drastically affect their physicochemical properties. For instance, the optical properties of BODIPY dyes are inherently related to the degree of aggregation and the mutual orientation of BODIPY units within these aggregates. Whereas the noncovalent aggregation of various BODIPY dyes has been studied in diverse media, the ill-defined nature of these aggregates has made it difficult to elucidate the structure–property relationships. Here, we studied the encapsulation of three structurally simple BODIPY derivatives within the hydrophobic cavity of a water-soluble, flexible PdII6L4 coordination cage. The cavity size allowed for the selective encapsulation of two dye molecules, irrespective of the substitution pattern on the BODIPY core. Working with a model, a pentamethyl-substituted derivative, we found that the mutual orientation of two BODIPY units in the cage’s cavity was remarkably similar to that in the crystalline state of the free dye, allowing us to isolate and characterize the smallest possible noncovalent H-type BODIPY aggregate, namely, an H-dimer. Interestingly, a CF3-substituted BODIPY, known for forming J-type aggregates, was also encapsulated as an H-dimer. Taking advantage of the dynamic nature of encapsulation, we developed a system in which reversible switching between H- and J-aggregates can be induced for multiple cycles simply by addition and subsequent destruction of the cage. We expect that the ability to rapidly and reversibly manipulate the optical properties of supramolecular inclusion complexes in aqueous media will open up avenues for developing detection systems that operate within biological environments. article_processing_charge: No article_type: original author: - first_name: Julius full_name: Gemen, Julius last_name: Gemen - first_name: Johannes full_name: Ahrens, Johannes last_name: Ahrens - first_name: Linda J. W. full_name: Shimon, Linda J. W. last_name: Shimon - first_name: Rafal full_name: Klajn, Rafal id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b last_name: Klajn citation: ama: Gemen J, Ahrens J, Shimon LJW, Klajn R. Modulating the optical properties of BODIPY dyes by noncovalent dimerization within a flexible coordination cage. Journal of the American Chemical Society. 2020;142(41):17721-17729. doi:10.1021/jacs.0c08589 apa: Gemen, J., Ahrens, J., Shimon, L. J. W., & Klajn, R. (2020). Modulating the optical properties of BODIPY dyes by noncovalent dimerization within a flexible coordination cage. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.0c08589 chicago: Gemen, Julius, Johannes Ahrens, Linda J. W. Shimon, and Rafal Klajn. “Modulating the Optical Properties of BODIPY Dyes by Noncovalent Dimerization within a Flexible Coordination Cage.” Journal of the American Chemical Society. American Chemical Society, 2020. https://doi.org/10.1021/jacs.0c08589. ieee: J. Gemen, J. Ahrens, L. J. W. Shimon, and R. Klajn, “Modulating the optical properties of BODIPY dyes by noncovalent dimerization within a flexible coordination cage,” Journal of the American Chemical Society, vol. 142, no. 41. American Chemical Society, pp. 17721–17729, 2020. ista: Gemen J, Ahrens J, Shimon LJW, Klajn R. 2020. Modulating the optical properties of BODIPY dyes by noncovalent dimerization within a flexible coordination cage. Journal of the American Chemical Society. 142(41), 17721–17729. mla: Gemen, Julius, et al. “Modulating the Optical Properties of BODIPY Dyes by Noncovalent Dimerization within a Flexible Coordination Cage.” Journal of the American Chemical Society, vol. 142, no. 41, American Chemical Society, 2020, pp. 17721–29, doi:10.1021/jacs.0c08589. short: J. Gemen, J. Ahrens, L.J.W. Shimon, R. Klajn, Journal of the American Chemical Society 142 (2020) 17721–17729. date_created: 2023-08-01T09:36:10Z date_published: 2020-10-04T00:00:00Z date_updated: 2023-08-07T10:09:54Z day: '04' doi: 10.1021/jacs.0c08589 extern: '1' external_id: pmid: - '33006898' intvolume: ' 142' issue: '41' keyword: - Colloid and Surface Chemistry - Biochemistry - General Chemistry - Catalysis language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1021/jacs.0c08589 month: '10' oa: 1 oa_version: Published Version page: 17721-17729 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: eissn: - 1520-5126 issn: - 0002-7863 publication_status: published publisher: American Chemical Society quality_controlled: '1' scopus_import: '1' status: public title: Modulating the optical properties of BODIPY dyes by noncovalent dimerization within a flexible coordination cage type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 142 year: '2020' ... --- _id: '13364' abstract: - lang: eng text: Photochromic molecules undergo reversible isomerization upon irradiation with light at different wavelengths, a process that can alter their physical and chemical properties. For instance, dihydropyrene (DHP) is a deep-colored compound that isomerizes to light-brown cyclophanediene (CPD) upon irradiation with visible light. CPD can then isomerize back to DHP upon irradiation with UV light or thermally in the dark. Conversion between DHP and CPD is thought to proceed via a biradical intermediate; bimolecular events involving this unstable intermediate thus result in rapid decomposition and poor cycling performance. Here, we show that the reversible isomerization of DHP can be stabilized upon confinement within a PdII6L4 coordination cage. By protecting this reactive intermediate using the cage, each isomerization reaction proceeds to higher yield, which significantly decreases the fatigue experienced by the system upon repeated photocycling. Although molecular confinement is known to help stabilize reactive species, this effect is not typically employed to protect reactive intermediates and thus improve reaction yields. We envisage that performing reactions under confinement will not only improve the cyclic performance of photochromic molecules, but may also increase the amount of product obtainable from traditionally low-yielding organic reactions. article_processing_charge: No article_type: original author: - first_name: Martina full_name: Canton, Martina last_name: Canton - first_name: Angela B. full_name: Grommet, Angela B. last_name: Grommet - first_name: Luca full_name: Pesce, Luca last_name: Pesce - first_name: Julius full_name: Gemen, Julius last_name: Gemen - first_name: Shiming full_name: Li, Shiming last_name: Li - first_name: Yael full_name: Diskin-Posner, Yael last_name: Diskin-Posner - first_name: Alberto full_name: Credi, Alberto last_name: Credi - first_name: Giovanni M. full_name: Pavan, Giovanni M. last_name: Pavan - first_name: Joakim full_name: Andréasson, Joakim last_name: Andréasson - first_name: Rafal full_name: Klajn, Rafal id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b last_name: Klajn citation: ama: Canton M, Grommet AB, Pesce L, et al. Improving fatigue resistance of dihydropyrene by encapsulation within a coordination cage. Journal of the American Chemical Society. 2020;142(34):14557-14565. doi:10.1021/jacs.0c06146 apa: Canton, M., Grommet, A. B., Pesce, L., Gemen, J., Li, S., Diskin-Posner, Y., … Klajn, R. (2020). Improving fatigue resistance of dihydropyrene by encapsulation within a coordination cage. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.0c06146 chicago: Canton, Martina, Angela B. Grommet, Luca Pesce, Julius Gemen, Shiming Li, Yael Diskin-Posner, Alberto Credi, Giovanni M. Pavan, Joakim Andréasson, and Rafal Klajn. “Improving Fatigue Resistance of Dihydropyrene by Encapsulation within a Coordination Cage.” Journal of the American Chemical Society. American Chemical Society, 2020. https://doi.org/10.1021/jacs.0c06146. ieee: M. Canton et al., “Improving fatigue resistance of dihydropyrene by encapsulation within a coordination cage,” Journal of the American Chemical Society, vol. 142, no. 34. American Chemical Society, pp. 14557–14565, 2020. ista: Canton M, Grommet AB, Pesce L, Gemen J, Li S, Diskin-Posner Y, Credi A, Pavan GM, Andréasson J, Klajn R. 2020. Improving fatigue resistance of dihydropyrene by encapsulation within a coordination cage. Journal of the American Chemical Society. 142(34), 14557–14565. mla: Canton, Martina, et al. “Improving Fatigue Resistance of Dihydropyrene by Encapsulation within a Coordination Cage.” Journal of the American Chemical Society, vol. 142, no. 34, American Chemical Society, 2020, pp. 14557–65, doi:10.1021/jacs.0c06146. short: M. Canton, A.B. Grommet, L. Pesce, J. Gemen, S. Li, Y. Diskin-Posner, A. Credi, G.M. Pavan, J. Andréasson, R. Klajn, Journal of the American Chemical Society 142 (2020) 14557–14565. date_created: 2023-08-01T09:36:59Z date_published: 2020-08-14T00:00:00Z date_updated: 2023-08-07T10:15:38Z day: '14' doi: 10.1021/jacs.0c06146 extern: '1' external_id: pmid: - '32791832' intvolume: ' 142' issue: '34' keyword: - Colloid and Surface Chemistry - Biochemistry - General Chemistry - Catalysis language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1021/jacs.0c06146 month: '08' oa: 1 oa_version: Published Version page: 14557-14565 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: eissn: - 1520-5126 issn: - 0002-7863 publication_status: published publisher: American Chemical Society quality_controlled: '1' scopus_import: '1' status: public title: Improving fatigue resistance of dihydropyrene by encapsulation within a coordination cage type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 142 year: '2020' ... --- _id: '13365' abstract: - lang: eng text: Photoswitchable molecules are employed for many applications, from the development of active materials to the design of stimuli-responsive molecular systems and light-powered molecular machines. To fully exploit their potential, we must learn ways to control the mechanism and kinetics of their photoinduced isomerization. One possible strategy involves confinement of photoresponsive switches such as azobenzenes or spiropyrans within crowded molecular environments, which may allow control over their light-induced conversion. However, the molecular factors that influence and control the switching process under realistic conditions and within dynamic molecular regimes often remain difficult to ascertain. As a case study, here we have employed molecular models to probe the isomerization of azobenzene guests within a Pd(II)-based coordination cage host in water. Atomistic molecular dynamics and metadynamics simulations allow us to characterize the flexibility of the cage in the solvent, the (rare) guest encapsulation and release events, and the relative probability/kinetics of light-induced isomerization of azobenzene analogues in these host–guest systems. In this way, we can reconstruct the mechanism of azobenzene switching inside the cage cavity and explore key molecular factors that may control this event. We obtain a molecular-level insight on the effects of crowding and host–guest interactions on azobenzene isomerization. The detailed picture elucidated by this study may enable the rational design of photoswitchable systems whose reactivity can be controlled via host–guest interactions. article_processing_charge: No article_type: original author: - first_name: Luca full_name: Pesce, Luca last_name: Pesce - first_name: Claudio full_name: Perego, Claudio last_name: Perego - first_name: Angela B. full_name: Grommet, Angela B. last_name: Grommet - first_name: Rafal full_name: Klajn, Rafal id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b last_name: Klajn - first_name: Giovanni M. full_name: Pavan, Giovanni M. last_name: Pavan citation: ama: Pesce L, Perego C, Grommet AB, Klajn R, Pavan GM. Molecular factors controlling the isomerization of Azobenzenes in the cavity of a flexible coordination cage. Journal of the American Chemical Society. 2020;142(21):9792-9802. doi:10.1021/jacs.0c03444 apa: Pesce, L., Perego, C., Grommet, A. B., Klajn, R., & Pavan, G. M. (2020). Molecular factors controlling the isomerization of Azobenzenes in the cavity of a flexible coordination cage. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.0c03444 chicago: Pesce, Luca, Claudio Perego, Angela B. Grommet, Rafal Klajn, and Giovanni M. Pavan. “Molecular Factors Controlling the Isomerization of Azobenzenes in the Cavity of a Flexible Coordination Cage.” Journal of the American Chemical Society. American Chemical Society, 2020. https://doi.org/10.1021/jacs.0c03444. ieee: L. Pesce, C. Perego, A. B. Grommet, R. Klajn, and G. M. Pavan, “Molecular factors controlling the isomerization of Azobenzenes in the cavity of a flexible coordination cage,” Journal of the American Chemical Society, vol. 142, no. 21. American Chemical Society, pp. 9792–9802, 2020. ista: Pesce L, Perego C, Grommet AB, Klajn R, Pavan GM. 2020. Molecular factors controlling the isomerization of Azobenzenes in the cavity of a flexible coordination cage. Journal of the American Chemical Society. 142(21), 9792–9802. mla: Pesce, Luca, et al. “Molecular Factors Controlling the Isomerization of Azobenzenes in the Cavity of a Flexible Coordination Cage.” Journal of the American Chemical Society, vol. 142, no. 21, American Chemical Society, 2020, pp. 9792–802, doi:10.1021/jacs.0c03444. short: L. Pesce, C. Perego, A.B. Grommet, R. Klajn, G.M. Pavan, Journal of the American Chemical Society 142 (2020) 9792–9802. date_created: 2023-08-01T09:37:12Z date_published: 2020-04-30T00:00:00Z date_updated: 2023-08-07T10:18:53Z day: '30' doi: 10.1021/jacs.0c03444 extern: '1' external_id: pmid: - '32353237' intvolume: ' 142' issue: '21' keyword: - Colloid and Surface Chemistry - Biochemistry - General Chemistry - Catalysis language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1021/jacs.0c03444 month: '04' oa: 1 oa_version: Published Version page: 9792-9802 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: eissn: - 1520-5126 issn: - 0002-7863 publication_status: published publisher: American Chemical Society quality_controlled: '1' scopus_import: '1' status: public title: Molecular factors controlling the isomerization of Azobenzenes in the cavity of a flexible coordination cage type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 142 year: '2020' ... --- _id: '14125' abstract: - lang: eng text: "Motivation: Recent technological advances have led to an increase in the production and availability of single-cell data. The ability to integrate a set of multi-technology measurements would allow the identification of biologically or clinically meaningful observations through the unification of the perspectives afforded by each technology. In most cases, however, profiling technologies consume the used cells and thus pairwise correspondences between datasets are lost. Due to the sheer size single-cell datasets can acquire, scalable algorithms that are able to universally match single-cell measurements carried out in one cell to its corresponding sibling in another technology are needed.\r\nResults: We propose Single-Cell data Integration via Matching (SCIM), a scalable approach to recover such correspondences in two or more technologies. SCIM assumes that cells share a common (low-dimensional) underlying structure and that the underlying cell distribution is approximately constant across technologies. It constructs a technology-invariant latent space using an autoencoder framework with an adversarial objective. Multi-modal datasets are integrated by pairing cells across technologies using a bipartite matching scheme that operates on the low-dimensional latent representations. We evaluate SCIM on a simulated cellular branching process and show that the cell-to-cell matches derived by SCIM reflect the same pseudotime on the simulated dataset. Moreover, we apply our method to two real-world scenarios, a melanoma tumor sample and a human bone marrow sample, where we pair cells from a scRNA dataset to their sibling cells in a CyTOF dataset achieving 90% and 78% cell-matching accuracy for each one of the samples, respectively." article_processing_charge: No article_type: original author: - first_name: Stefan G full_name: Stark, Stefan G last_name: Stark - first_name: Joanna full_name: Ficek, Joanna last_name: Ficek - first_name: Francesco full_name: Locatello, Francesco id: 26cfd52f-2483-11ee-8040-88983bcc06d4 last_name: Locatello orcid: 0000-0002-4850-0683 - first_name: Ximena full_name: Bonilla, Ximena last_name: Bonilla - first_name: Stéphane full_name: Chevrier, Stéphane last_name: Chevrier - first_name: Franziska full_name: Singer, Franziska last_name: Singer - first_name: Rudolf full_name: Aebersold, Rudolf last_name: Aebersold - first_name: Faisal S full_name: Al-Quaddoomi, Faisal S last_name: Al-Quaddoomi - first_name: Jonas full_name: Albinus, Jonas last_name: Albinus - first_name: Ilaria full_name: Alborelli, Ilaria last_name: Alborelli - first_name: Sonali full_name: Andani, Sonali last_name: Andani - first_name: Per-Olof full_name: Attinger, Per-Olof last_name: Attinger - first_name: Marina full_name: Bacac, Marina last_name: Bacac - first_name: Daniel full_name: Baumhoer, Daniel last_name: Baumhoer - first_name: Beatrice full_name: Beck-Schimmer, Beatrice last_name: Beck-Schimmer - first_name: Niko full_name: Beerenwinkel, Niko last_name: Beerenwinkel - first_name: Christian full_name: Beisel, Christian last_name: Beisel - first_name: Lara full_name: Bernasconi, Lara last_name: Bernasconi - first_name: Anne full_name: Bertolini, Anne last_name: Bertolini - first_name: Bernd full_name: Bodenmiller, Bernd last_name: Bodenmiller - first_name: Ximena full_name: Bonilla, Ximena last_name: Bonilla - first_name: Ruben full_name: Casanova, Ruben last_name: Casanova - first_name: Stéphane full_name: Chevrier, Stéphane last_name: Chevrier - first_name: Natalia full_name: Chicherova, Natalia last_name: Chicherova - first_name: Maya full_name: D'Costa, Maya last_name: D'Costa - first_name: Esther full_name: Danenberg, Esther last_name: Danenberg - first_name: Natalie full_name: Davidson, Natalie last_name: Davidson - first_name: Monica-Andreea Dră full_name: gan, Monica-Andreea Dră last_name: gan - first_name: Reinhard full_name: Dummer, Reinhard last_name: Dummer - first_name: Stefanie full_name: Engler, Stefanie last_name: Engler - first_name: Martin full_name: Erkens, Martin last_name: Erkens - first_name: Katja full_name: Eschbach, Katja last_name: Eschbach - first_name: Cinzia full_name: Esposito, Cinzia last_name: Esposito - first_name: André full_name: Fedier, André last_name: Fedier - first_name: Pedro full_name: Ferreira, Pedro last_name: Ferreira - first_name: Joanna full_name: Ficek, Joanna last_name: Ficek - first_name: Anja L full_name: Frei, Anja L last_name: Frei - first_name: Bruno full_name: Frey, Bruno last_name: Frey - first_name: Sandra full_name: Goetze, Sandra last_name: Goetze - first_name: Linda full_name: Grob, Linda last_name: Grob - first_name: Gabriele full_name: Gut, Gabriele last_name: Gut - first_name: Detlef full_name: Günther, Detlef last_name: Günther - first_name: Martina full_name: Haberecker, Martina last_name: Haberecker - first_name: Pirmin full_name: Haeuptle, Pirmin last_name: Haeuptle - first_name: Viola full_name: Heinzelmann-Schwarz, Viola last_name: Heinzelmann-Schwarz - first_name: Sylvia full_name: Herter, Sylvia last_name: Herter - first_name: Rene full_name: Holtackers, Rene last_name: Holtackers - first_name: Tamara full_name: Huesser, Tamara last_name: Huesser - first_name: Anja full_name: Irmisch, Anja last_name: Irmisch - first_name: Francis full_name: Jacob, Francis last_name: Jacob - first_name: Andrea full_name: Jacobs, Andrea last_name: Jacobs - first_name: Tim M full_name: Jaeger, Tim M last_name: Jaeger - first_name: Katharina full_name: Jahn, Katharina last_name: Jahn - first_name: Alva R full_name: James, Alva R last_name: James - first_name: Philip M full_name: Jermann, Philip M last_name: Jermann - first_name: André full_name: Kahles, André last_name: Kahles - first_name: Abdullah full_name: Kahraman, Abdullah last_name: Kahraman - first_name: Viktor H full_name: Koelzer, Viktor H last_name: Koelzer - first_name: Werner full_name: Kuebler, Werner last_name: Kuebler - first_name: Jack full_name: Kuipers, Jack last_name: Kuipers - first_name: Christian P full_name: Kunze, Christian P last_name: Kunze - first_name: Christian full_name: Kurzeder, Christian last_name: Kurzeder - first_name: Kjong-Van full_name: Lehmann, Kjong-Van last_name: Lehmann - first_name: Mitchell full_name: Levesque, Mitchell last_name: Levesque - first_name: Sebastian full_name: Lugert, Sebastian last_name: Lugert - first_name: Gerd full_name: Maass, Gerd last_name: Maass - first_name: Markus full_name: Manz, Markus last_name: Manz - first_name: Philipp full_name: Markolin, Philipp last_name: Markolin - first_name: Julien full_name: Mena, Julien last_name: Mena - first_name: Ulrike full_name: Menzel, Ulrike last_name: Menzel - first_name: Julian M full_name: Metzler, Julian M last_name: Metzler - first_name: Nicola full_name: Miglino, Nicola last_name: Miglino - first_name: Emanuela S full_name: Milani, Emanuela S last_name: Milani - first_name: Holger full_name: Moch, Holger last_name: Moch - first_name: Simone full_name: Muenst, Simone last_name: Muenst - first_name: Riccardo full_name: Murri, Riccardo last_name: Murri - first_name: Charlotte KY full_name: Ng, Charlotte KY last_name: Ng - first_name: Stefan full_name: Nicolet, Stefan last_name: Nicolet - first_name: Marta full_name: Nowak, Marta last_name: Nowak - first_name: Patrick GA full_name: Pedrioli, Patrick GA last_name: Pedrioli - first_name: Lucas full_name: Pelkmans, Lucas last_name: Pelkmans - first_name: Salvatore full_name: Piscuoglio, Salvatore last_name: Piscuoglio - first_name: Michael full_name: Prummer, Michael last_name: Prummer - first_name: Mathilde full_name: Ritter, Mathilde last_name: Ritter - first_name: Christian full_name: Rommel, Christian last_name: Rommel - first_name: María L full_name: Rosano-González, María L last_name: Rosano-González - first_name: Gunnar full_name: Rätsch, Gunnar last_name: Rätsch - first_name: Natascha full_name: Santacroce, Natascha last_name: Santacroce - first_name: Jacobo Sarabia del full_name: Castillo, Jacobo Sarabia del last_name: Castillo - first_name: Ramona full_name: Schlenker, Ramona last_name: Schlenker - first_name: Petra C full_name: Schwalie, Petra C last_name: Schwalie - first_name: Severin full_name: Schwan, Severin last_name: Schwan - first_name: Tobias full_name: Schär, Tobias last_name: Schär - first_name: Gabriela full_name: Senti, Gabriela last_name: Senti - first_name: Franziska full_name: Singer, Franziska last_name: Singer - first_name: Sujana full_name: Sivapatham, Sujana last_name: Sivapatham - first_name: Berend full_name: Snijder, Berend last_name: Snijder - first_name: Bettina full_name: Sobottka, Bettina last_name: Sobottka - first_name: Vipin T full_name: Sreedharan, Vipin T last_name: Sreedharan - first_name: Stefan full_name: Stark, Stefan last_name: Stark - first_name: Daniel J full_name: Stekhoven, Daniel J last_name: Stekhoven - first_name: Alexandre PA full_name: Theocharides, Alexandre PA last_name: Theocharides - first_name: Tinu M full_name: Thomas, Tinu M last_name: Thomas - first_name: Markus full_name: Tolnay, Markus last_name: Tolnay - first_name: Vinko full_name: Tosevski, Vinko last_name: Tosevski - first_name: Nora C full_name: Toussaint, Nora C last_name: Toussaint - first_name: Mustafa A full_name: Tuncel, Mustafa A last_name: Tuncel - first_name: Marina full_name: Tusup, Marina last_name: Tusup - first_name: Audrey Van full_name: Drogen, Audrey Van last_name: Drogen - first_name: Marcus full_name: Vetter, Marcus last_name: Vetter - first_name: Tatjana full_name: Vlajnic, Tatjana last_name: Vlajnic - first_name: Sandra full_name: Weber, Sandra last_name: Weber - first_name: Walter P full_name: Weber, Walter P last_name: Weber - first_name: Rebekka full_name: Wegmann, Rebekka last_name: Wegmann - first_name: Michael full_name: Weller, Michael last_name: Weller - first_name: Fabian full_name: Wendt, Fabian last_name: Wendt - first_name: Norbert full_name: Wey, Norbert last_name: Wey - first_name: Andreas full_name: Wicki, Andreas last_name: Wicki - first_name: Bernd full_name: Wollscheid, Bernd last_name: Wollscheid - first_name: Shuqing full_name: Yu, Shuqing last_name: Yu - first_name: Johanna full_name: Ziegler, Johanna last_name: Ziegler - first_name: Marc full_name: Zimmermann, Marc last_name: Zimmermann - first_name: Martin full_name: Zoche, Martin last_name: Zoche - first_name: Gregor full_name: Zuend, Gregor last_name: Zuend - first_name: Gunnar full_name: Rätsch, Gunnar last_name: Rätsch - first_name: Kjong-Van full_name: Lehmann, Kjong-Van last_name: Lehmann citation: ama: 'Stark SG, Ficek J, Locatello F, et al. SCIM: Universal single-cell matching with unpaired feature sets. Bioinformatics. 2020;36(Supplement_2):i919-i927. doi:10.1093/bioinformatics/btaa843' apa: 'Stark, S. G., Ficek, J., Locatello, F., Bonilla, X., Chevrier, S., Singer, F., … Lehmann, K.-V. (2020). SCIM: Universal single-cell matching with unpaired feature sets. Bioinformatics. Oxford University Press. https://doi.org/10.1093/bioinformatics/btaa843' chicago: 'Stark, Stefan G, Joanna Ficek, Francesco Locatello, Ximena Bonilla, Stéphane Chevrier, Franziska Singer, Rudolf Aebersold, et al. “SCIM: Universal Single-Cell Matching with Unpaired Feature Sets.” Bioinformatics. Oxford University Press, 2020. https://doi.org/10.1093/bioinformatics/btaa843.' ieee: 'S. G. Stark et al., “SCIM: Universal single-cell matching with unpaired feature sets,” Bioinformatics, vol. 36, no. Supplement_2. Oxford University Press, pp. i919–i927, 2020.' ista: 'Stark SG et al. 2020. SCIM: Universal single-cell matching with unpaired feature sets. Bioinformatics. 36(Supplement_2), i919–i927.' mla: 'Stark, Stefan G., et al. “SCIM: Universal Single-Cell Matching with Unpaired Feature Sets.” Bioinformatics, vol. 36, no. Supplement_2, Oxford University Press, 2020, pp. i919–27, doi:10.1093/bioinformatics/btaa843.' short: S.G. Stark, J. Ficek, F. Locatello, X. Bonilla, S. Chevrier, F. Singer, R. Aebersold, F.S. Al-Quaddoomi, J. Albinus, I. Alborelli, S. Andani, P.-O. Attinger, M. Bacac, D. Baumhoer, B. Beck-Schimmer, N. Beerenwinkel, C. Beisel, L. Bernasconi, A. Bertolini, B. Bodenmiller, X. Bonilla, R. Casanova, S. Chevrier, N. Chicherova, M. D’Costa, E. Danenberg, N. Davidson, M.-A.D. gan, R. Dummer, S. Engler, M. Erkens, K. Eschbach, C. Esposito, A. Fedier, P. Ferreira, J. Ficek, A.L. Frei, B. Frey, S. Goetze, L. Grob, G. Gut, D. Günther, M. Haberecker, P. Haeuptle, V. Heinzelmann-Schwarz, S. Herter, R. Holtackers, T. Huesser, A. Irmisch, F. Jacob, A. Jacobs, T.M. Jaeger, K. Jahn, A.R. James, P.M. Jermann, A. Kahles, A. Kahraman, V.H. Koelzer, W. Kuebler, J. Kuipers, C.P. Kunze, C. Kurzeder, K.-V. Lehmann, M. Levesque, S. Lugert, G. Maass, M. Manz, P. Markolin, J. Mena, U. Menzel, J.M. Metzler, N. Miglino, E.S. Milani, H. Moch, S. Muenst, R. Murri, C.K. Ng, S. Nicolet, M. Nowak, P.G. Pedrioli, L. Pelkmans, S. Piscuoglio, M. Prummer, M. Ritter, C. Rommel, M.L. Rosano-González, G. Rätsch, N. Santacroce, J.S. del Castillo, R. Schlenker, P.C. Schwalie, S. Schwan, T. Schär, G. Senti, F. Singer, S. Sivapatham, B. Snijder, B. Sobottka, V.T. Sreedharan, S. Stark, D.J. Stekhoven, A.P. Theocharides, T.M. Thomas, M. Tolnay, V. Tosevski, N.C. Toussaint, M.A. Tuncel, M. Tusup, A.V. Drogen, M. Vetter, T. Vlajnic, S. Weber, W.P. Weber, R. Wegmann, M. Weller, F. Wendt, N. Wey, A. Wicki, B. Wollscheid, S. Yu, J. Ziegler, M. Zimmermann, M. Zoche, G. Zuend, G. Rätsch, K.-V. Lehmann, Bioinformatics 36 (2020) i919–i927. date_created: 2023-08-21T12:28:20Z date_published: 2020-12-01T00:00:00Z date_updated: 2023-09-11T10:21:00Z day: '01' department: - _id: FrLo doi: 10.1093/bioinformatics/btaa843 extern: '1' external_id: pmid: - '33381818' intvolume: ' 36' issue: Supplement_2 keyword: - Computational Mathematics - Computational Theory and Mathematics - Computer Science Applications - Molecular Biology - Biochemistry - Statistics and Probability language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1093/bioinformatics/btaa843 month: '12' oa: 1 oa_version: Published Version page: i919-i927 pmid: 1 publication: Bioinformatics publication_identifier: eissn: - 1367-4811 publication_status: published publisher: Oxford University Press quality_controlled: '1' related_material: link: - relation: software url: https://github.com/ratschlab/scim scopus_import: '1' status: public title: 'SCIM: Universal single-cell matching with unpaired feature sets' type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 36 year: '2020' ... --- _id: '10348' abstract: - lang: eng text: The endosomal sorting complex required for transport-III (ESCRT-III) catalyzes membrane fission from within membrane necks, a process that is essential for many cellular functions, from cell division to lysosome degradation and autophagy. How it breaks membranes, though, remains unknown. Here, we characterize a sequential polymerization of ESCRT-III subunits that, driven by a recruitment cascade and by continuous subunit-turnover powered by the ATPase Vps4, induces membrane deformation and fission. During this process, the exchange of Vps24 for Did2 induces a tilt in the polymer-membrane interface, which triggers transition from flat spiral polymers to helical filament to drive the formation of membrane protrusions, and ends with the formation of a highly constricted Did2-Ist1 co-polymer that we show is competent to promote fission when bound on the inside of membrane necks. Overall, our results suggest a mechanism of stepwise changes in ESCRT-III filament structure and mechanical properties via exchange of the filament subunits to catalyze ESCRT-III activity. acknowledgement: The authors thank Nicolas Chiaruttini, Jean Gruenberg, and Lena Harker-Kirschneck for careful correction of this manuscript and helpful discussions. The authors want to thank the NCCR Chemical Biology for constant support during this project. A.R. acknowledges funding from the Swiss National Fund for Research (31003A_130520, 31003A_149975, and 31003A_173087) and the European Research Council Consolidator (311536). A.Š. acknowledges the European Research Council (802960). B.B. thanks the BBSRC (BB/K009001/1) and Wellcome Trust (203276/Z/16/Z) for support. J.M.v.F. acknowledges funding through an EMBO Long-Term Fellowship (ALTF 1065-2015), the European Commission FP7 (Marie Curie Actions, LTFCOFUND2013, and GA-2013-609409), and a Transitional Postdoc fellowship (2015/345) from the Swiss SystemsX.ch initiative, evaluated by the Swiss National Science Foundation and Swiss National Science Foundation Research (SNSF SINERGIA 160728/1 [leader, Sophie Martin]). article_processing_charge: No article_type: original author: - first_name: Anna-Katharina full_name: Pfitzner, Anna-Katharina last_name: Pfitzner - first_name: Vincent full_name: Mercier, Vincent last_name: Mercier - first_name: Xiuyun full_name: Jiang, Xiuyun last_name: Jiang - first_name: Joachim full_name: Moser von Filseck, Joachim last_name: Moser von Filseck - first_name: Buzz full_name: Baum, Buzz last_name: Baum - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 - first_name: Aurélien full_name: Roux, Aurélien last_name: Roux citation: ama: Pfitzner A-K, Mercier V, Jiang X, et al. An ESCRT-III polymerization sequence drives membrane deformation and fission. Cell. 2020;182(5):1140-1155.e18. doi:10.1016/j.cell.2020.07.021 apa: Pfitzner, A.-K., Mercier, V., Jiang, X., Moser von Filseck, J., Baum, B., Šarić, A., & Roux, A. (2020). An ESCRT-III polymerization sequence drives membrane deformation and fission. Cell. Elsevier. https://doi.org/10.1016/j.cell.2020.07.021 chicago: Pfitzner, Anna-Katharina, Vincent Mercier, Xiuyun Jiang, Joachim Moser von Filseck, Buzz Baum, Anđela Šarić, and Aurélien Roux. “An ESCRT-III Polymerization Sequence Drives Membrane Deformation and Fission.” Cell. Elsevier, 2020. https://doi.org/10.1016/j.cell.2020.07.021. ieee: A.-K. Pfitzner et al., “An ESCRT-III polymerization sequence drives membrane deformation and fission,” Cell, vol. 182, no. 5. Elsevier, p. 1140–1155.e18, 2020. ista: Pfitzner A-K, Mercier V, Jiang X, Moser von Filseck J, Baum B, Šarić A, Roux A. 2020. An ESCRT-III polymerization sequence drives membrane deformation and fission. Cell. 182(5), 1140–1155.e18. mla: Pfitzner, Anna-Katharina, et al. “An ESCRT-III Polymerization Sequence Drives Membrane Deformation and Fission.” Cell, vol. 182, no. 5, Elsevier, 2020, p. 1140–1155.e18, doi:10.1016/j.cell.2020.07.021. short: A.-K. Pfitzner, V. Mercier, X. Jiang, J. Moser von Filseck, B. Baum, A. Šarić, A. Roux, Cell 182 (2020) 1140–1155.e18. date_created: 2021-11-26T08:02:27Z date_published: 2020-08-18T00:00:00Z date_updated: 2021-11-26T08:58:37Z day: '18' doi: 10.1016/j.cell.2020.07.021 extern: '1' external_id: pmid: - '32814015' intvolume: ' 182' issue: '5' keyword: - general biochemistry - genetics and molecular biology language: - iso: eng main_file_link: - open_access: '1' url: https://www.sciencedirect.com/science/article/pii/S0092867420309296 month: '08' oa: 1 oa_version: Published Version page: 1140-1155.e18 pmid: 1 publication: Cell publication_identifier: issn: - 0092-8674 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: An ESCRT-III polymerization sequence drives membrane deformation and fission type: journal_article user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9 volume: 182 year: '2020' ... --- _id: '11055' abstract: - lang: eng text: Vascular dysfunctions are a common feature of multiple age-related diseases. However, modeling healthy and pathological aging of the human vasculature represents an unresolved experimental challenge. Here, we generated induced vascular endothelial cells (iVECs) and smooth muscle cells (iSMCs) by direct reprogramming of healthy human fibroblasts from donors of different ages and Hutchinson-Gilford Progeria Syndrome (HGPS) patients. iVECs induced from old donors revealed upregulation of GSTM1 and PALD1, genes linked to oxidative stress, inflammation and endothelial junction stability, as vascular aging markers. A functional assay performed on PALD1 KD VECs demonstrated a recovery in vascular permeability. We found that iSMCs from HGPS donors overexpressed bone morphogenetic protein (BMP)−4, which plays a key role in both vascular calcification and endothelial barrier damage observed in HGPS. Strikingly, BMP4 concentrations are higher in serum from HGPS vs. age-matched mice. Furthermore, targeting BMP4 with blocking antibody recovered the functionality of the vascular barrier in vitro, hence representing a potential future therapeutic strategy to limit cardiovascular dysfunction in HGPS. These results show that iVECs and iSMCs retain disease-related signatures, allowing modeling of vascular aging and HGPS in vitro. article_number: e54383 article_processing_charge: No article_type: original author: - first_name: Simone full_name: Bersini, Simone last_name: Bersini - first_name: Roberta full_name: Schulte, Roberta last_name: Schulte - first_name: Ling full_name: Huang, Ling last_name: Huang - first_name: Hannah full_name: Tsai, Hannah last_name: Tsai - first_name: Martin W full_name: HETZER, Martin W id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed last_name: HETZER orcid: 0000-0002-2111-992X citation: ama: Bersini S, Schulte R, Huang L, Tsai H, Hetzer M. Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome. eLife. 2020;9. doi:10.7554/elife.54383 apa: Bersini, S., Schulte, R., Huang, L., Tsai, H., & Hetzer, M. (2020). Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome. ELife. eLife Sciences Publications. https://doi.org/10.7554/elife.54383 chicago: Bersini, Simone, Roberta Schulte, Ling Huang, Hannah Tsai, and Martin Hetzer. “Direct Reprogramming of Human Smooth Muscle and Vascular Endothelial Cells Reveals Defects Associated with Aging and Hutchinson-Gilford Progeria Syndrome.” ELife. eLife Sciences Publications, 2020. https://doi.org/10.7554/elife.54383. ieee: S. Bersini, R. Schulte, L. Huang, H. Tsai, and M. Hetzer, “Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome,” eLife, vol. 9. eLife Sciences Publications, 2020. ista: Bersini S, Schulte R, Huang L, Tsai H, Hetzer M. 2020. Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome. eLife. 9, e54383. mla: Bersini, Simone, et al. “Direct Reprogramming of Human Smooth Muscle and Vascular Endothelial Cells Reveals Defects Associated with Aging and Hutchinson-Gilford Progeria Syndrome.” ELife, vol. 9, e54383, eLife Sciences Publications, 2020, doi:10.7554/elife.54383. short: S. Bersini, R. Schulte, L. Huang, H. Tsai, M. Hetzer, ELife 9 (2020). date_created: 2022-04-07T07:43:48Z date_published: 2020-09-08T00:00:00Z date_updated: 2022-07-18T08:30:37Z day: '08' ddc: - '570' doi: 10.7554/elife.54383 extern: '1' external_id: pmid: - '32896271' file: - access_level: open_access checksum: f8b3821349a194050be02570d8fe7d4b content_type: application/pdf creator: dernst date_created: 2022-04-08T06:53:10Z date_updated: 2022-04-08T06:53:10Z file_id: '11132' file_name: 2020_eLife_Bersini.pdf file_size: 4399825 relation: main_file success: 1 file_date_updated: 2022-04-08T06:53:10Z has_accepted_license: '1' intvolume: ' 9' keyword: - General Immunology and Microbiology - General Biochemistry - Genetics and Molecular Biology - General Medicine - General Neuroscience language: - iso: eng month: '09' oa: 1 oa_version: Published Version pmid: 1 publication: eLife publication_identifier: issn: - 2050-084X publication_status: published publisher: eLife Sciences Publications quality_controlled: '1' scopus_import: '1' status: public title: Direct reprogramming of human smooth muscle and vascular endothelial cells reveals defects associated with aging and Hutchinson-Gilford progeria syndrome tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd volume: 9 year: '2020' ... --- _id: '11056' abstract: - lang: eng text: Aging of the circulatory system correlates with the pathogenesis of a large spectrum of diseases. However, it is largely unknown which factors drive the age-dependent or pathological decline of the vasculature and how vascular defects relate to tissue aging. The goal of the study is to design a multianalytical approach to identify how the cellular microenvironment (i.e., fibroblasts) and serum from healthy donors of different ages or Alzheimer disease (AD) patients can modulate the functionality of organ-specific vascular endothelial cells (VECs). Long-living human microvascular networks embedding VECs and fibroblasts from skin biopsies are generated. RNA-seq, secretome analyses, and microfluidic assays demonstrate that fibroblasts from young donors restore the functionality of aged endothelial cells, an effect also achieved by serum from young donors. New biomarkers of vascular aging are validated in human biopsies and it is shown that young serum induces angiopoietin-like-4, which can restore compromised vascular barriers. This strategy is then employed to characterize transcriptional/functional changes induced on the blood–brain barrier by AD serum, demonstrating the importance of PTP4A3 in the regulation of permeability. Features of vascular degeneration during aging and AD are recapitulated, and a tool to identify novel biomarkers that can be exploited to develop future therapeutics modulating vascular function is established. article_number: '2000044' article_processing_charge: No article_type: original author: - first_name: Simone full_name: Bersini, Simone last_name: Bersini - first_name: Rafael full_name: Arrojo e Drigo, Rafael last_name: Arrojo e Drigo - first_name: Ling full_name: Huang, Ling last_name: Huang - first_name: Maxim N. full_name: Shokhirev, Maxim N. last_name: Shokhirev - first_name: Martin W full_name: HETZER, Martin W id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed last_name: HETZER orcid: 0000-0002-2111-992X citation: ama: Bersini S, Arrojo e Drigo R, Huang L, Shokhirev MN, Hetzer M. Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease. Advanced Biosystems. 2020;4(5). doi:10.1002/adbi.202000044 apa: Bersini, S., Arrojo e Drigo, R., Huang, L., Shokhirev, M. N., & Hetzer, M. (2020). Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease. Advanced Biosystems. Wiley. https://doi.org/10.1002/adbi.202000044 chicago: Bersini, Simone, Rafael Arrojo e Drigo, Ling Huang, Maxim N. Shokhirev, and Martin Hetzer. “Transcriptional and Functional Changes of the Human Microvasculature during Physiological Aging and Alzheimer Disease.” Advanced Biosystems. Wiley, 2020. https://doi.org/10.1002/adbi.202000044. ieee: S. Bersini, R. Arrojo e Drigo, L. Huang, M. N. Shokhirev, and M. Hetzer, “Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease,” Advanced Biosystems, vol. 4, no. 5. Wiley, 2020. ista: Bersini S, Arrojo e Drigo R, Huang L, Shokhirev MN, Hetzer M. 2020. Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease. Advanced Biosystems. 4(5), 2000044. mla: Bersini, Simone, et al. “Transcriptional and Functional Changes of the Human Microvasculature during Physiological Aging and Alzheimer Disease.” Advanced Biosystems, vol. 4, no. 5, 2000044, Wiley, 2020, doi:10.1002/adbi.202000044. short: S. Bersini, R. Arrojo e Drigo, L. Huang, M.N. Shokhirev, M. Hetzer, Advanced Biosystems 4 (2020). date_created: 2022-04-07T07:43:57Z date_published: 2020-05-01T00:00:00Z date_updated: 2022-07-18T08:30:48Z day: '01' ddc: - '570' doi: 10.1002/adbi.202000044 extern: '1' external_id: pmid: - '32402127' file: - access_level: open_access checksum: 5584d9a1609812dc75c02ce1e35d2ec0 content_type: application/pdf creator: dernst date_created: 2022-04-08T07:06:05Z date_updated: 2022-04-08T07:06:05Z file_id: '11134' file_name: 2020_AdvancedBiosystems_Bersini.pdf file_size: 2490829 relation: main_file success: 1 file_date_updated: 2022-04-08T07:06:05Z has_accepted_license: '1' intvolume: ' 4' issue: '5' keyword: - General Biochemistry - Genetics and Molecular Biology - Biomedical Engineering - Biomaterials language: - iso: eng month: '05' oa: 1 oa_version: Published Version pmid: 1 publication: Advanced Biosystems publication_identifier: issn: - 2366-7478 - 2366-7478 publication_status: published publisher: Wiley quality_controlled: '1' scopus_import: '1' status: public title: Transcriptional and functional changes of the human microvasculature during physiological aging and Alzheimer disease tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd volume: 4 year: '2020' ... --- _id: '11058' abstract: - lang: eng text: Nucleoporin 93 (Nup93) expression inversely correlates with the survival of triple-negative breast cancer patients. However, our knowledge of Nup93 function in breast cancer besides its role as structural component of the nuclear pore complex is not understood. Combination of functional assays and genetic analyses suggested that chromatin interaction of Nup93 partially modulates the expression of genes associated with actin cytoskeleton remodeling and epithelial to mesenchymal transition, resulting in impaired invasion of triple-negative, claudin-low breast cancer cells. Nup93 depletion induced stress fiber formation associated with reduced cell migration/proliferation and impaired expression of mesenchymal-like genes. Silencing LIMCH1, a gene responsible for actin cytoskeleton remodeling and up-regulated upon Nup93 depletion, partially restored the invasive phenotype of cancer cells. Loss of Nup93 led to significant defects in tumor establishment/propagation in vivo, whereas patient samples revealed that high Nup93 and low LIMCH1 expression correlate with late tumor stage. Our approach identified Nup93 as contributor of triple-negative, claudin-low breast cancer cell invasion and paves the way to study the role of nuclear envelope proteins during breast cancer tumorigenesis. article_number: e201900623 article_processing_charge: No article_type: original author: - first_name: Simone full_name: Bersini, Simone last_name: Bersini - first_name: Nikki K full_name: Lytle, Nikki K last_name: Lytle - first_name: Roberta full_name: Schulte, Roberta last_name: Schulte - first_name: Ling full_name: Huang, Ling last_name: Huang - first_name: Geoffrey M full_name: Wahl, Geoffrey M last_name: Wahl - first_name: Martin W full_name: HETZER, Martin W id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed last_name: HETZER orcid: 0000-0002-2111-992X citation: ama: Bersini S, Lytle NK, Schulte R, Huang L, Wahl GM, Hetzer M. Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling. Life Science Alliance. 2020;3(1). doi:10.26508/lsa.201900623 apa: Bersini, S., Lytle, N. K., Schulte, R., Huang, L., Wahl, G. M., & Hetzer, M. (2020). Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling. Life Science Alliance. Life Science Alliance. https://doi.org/10.26508/lsa.201900623 chicago: Bersini, Simone, Nikki K Lytle, Roberta Schulte, Ling Huang, Geoffrey M Wahl, and Martin Hetzer. “Nup93 Regulates Breast Tumor Growth by Modulating Cell Proliferation and Actin Cytoskeleton Remodeling.” Life Science Alliance. Life Science Alliance, 2020. https://doi.org/10.26508/lsa.201900623. ieee: S. Bersini, N. K. Lytle, R. Schulte, L. Huang, G. M. Wahl, and M. Hetzer, “Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling,” Life Science Alliance, vol. 3, no. 1. Life Science Alliance, 2020. ista: Bersini S, Lytle NK, Schulte R, Huang L, Wahl GM, Hetzer M. 2020. Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling. Life Science Alliance. 3(1), e201900623. mla: Bersini, Simone, et al. “Nup93 Regulates Breast Tumor Growth by Modulating Cell Proliferation and Actin Cytoskeleton Remodeling.” Life Science Alliance, vol. 3, no. 1, e201900623, Life Science Alliance, 2020, doi:10.26508/lsa.201900623. short: S. Bersini, N.K. Lytle, R. Schulte, L. Huang, G.M. Wahl, M. Hetzer, Life Science Alliance 3 (2020). date_created: 2022-04-07T07:44:18Z date_published: 2020-01-01T00:00:00Z date_updated: 2022-07-18T08:31:20Z day: '01' ddc: - '570' doi: 10.26508/lsa.201900623 extern: '1' external_id: pmid: - '31959624' file: - access_level: open_access checksum: 3bf33e7e93bef7823287807206b69b38 content_type: application/pdf creator: dernst date_created: 2022-04-08T07:33:01Z date_updated: 2022-04-08T07:33:01Z file_id: '11137' file_name: 2020_LifeScienceAlliance_Bersini.pdf file_size: 2653960 relation: main_file success: 1 file_date_updated: 2022-04-08T07:33:01Z has_accepted_license: '1' intvolume: ' 3' issue: '1' keyword: - Health - Toxicology and Mutagenesis - Plant Science - Biochemistry - Genetics and Molecular Biology (miscellaneous) - Ecology language: - iso: eng month: '01' oa: 1 oa_version: Published Version pmid: 1 publication: Life Science Alliance publication_identifier: issn: - 2575-1077 publication_status: published publisher: Life Science Alliance quality_controlled: '1' scopus_import: '1' status: public title: Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd volume: 3 year: '2020' ... --- _id: '12190' abstract: - lang: eng text: Meiotic crossover frequency varies within genomes, which influences genetic diversity and adaptation. In turn, genetic variation within populations can act to modify crossover frequency in cis and trans. To identify genetic variation that controls meiotic crossover frequency, we screened Arabidopsis accessions using fluorescent recombination reporters. We mapped a genetic modifier of crossover frequency in Col × Bur populations of Arabidopsis to a premature stop codon within TBP-ASSOCIATED FACTOR 4b (TAF4b), which encodes a subunit of the RNA polymerase II general transcription factor TFIID. The Arabidopsis taf4b mutation is a rare variant found in the British Isles, originating in South-West Ireland. Using genetics, genomics, and immunocytology, we demonstrate a genome-wide decrease in taf4b crossovers, with strongest reduction in the sub-telomeric regions. Using RNA sequencing (RNA-seq) from purified meiocytes, we show that TAF4b expression is meiocyte enriched, whereas its paralog TAF4 is broadly expressed. Consistent with the role of TFIID in promoting gene expression, RNA-seq of wild-type and taf4b meiocytes identified widespread transcriptional changes, including in genes that regulate the meiotic cell cycle and recombination. Therefore, TAF4b duplication is associated with acquisition of meiocyte-specific expression and promotion of germline transcription, which act directly or indirectly to elevate crossovers. This identifies a novel mode of meiotic recombination control via a general transcription factor. acknowledgement: "We thank Gregory Copenhaver (University of North Carolina), Avraham Levy (The Weizmann Institute), and Scott Poethig (University of Pennsylvania) for FTLs; Piotr Ziolkowski for Col-420/Bur seed; Sureshkumar Balasubramanian\r\n(Monash University) for providing British and Irish Arabidopsis accessions; Mathilde Grelon (INRA, Versailles) for providing the MLH1 antibody; and the Gurdon Institute for access to microscopes. This work was supported by a BBSRC DTP studentship (E.J.L.), European Research Area Network for Coordinating Action in Plant Sciences/BBSRC ‘‘DeCOP’’ (BB/M004937/1; C.L.), a BBSRC David Phillips Fellowship (BB/L025043/1; H.G. and X.F.), the European Research Council (CoG ‘‘SynthHotspot,’’ A.J.T., C.L., and I.R.H.; StG ‘‘SexMeth,’’ X.F.), and a Sainsbury Charitable Foundation Studentship (A.R.B.)." article_processing_charge: No article_type: original author: - first_name: Emma J. full_name: Lawrence, Emma J. last_name: Lawrence - first_name: Hongbo full_name: Gao, Hongbo last_name: Gao - first_name: Andrew J. full_name: Tock, Andrew J. last_name: Tock - first_name: Christophe full_name: Lambing, Christophe last_name: Lambing - first_name: Alexander R. full_name: Blackwell, Alexander R. last_name: Blackwell - first_name: Xiaoqi full_name: Feng, Xiaoqi id: e0164712-22ee-11ed-b12a-d80fcdf35958 last_name: Feng orcid: 0000-0002-4008-1234 - first_name: Ian R. full_name: Henderson, Ian R. last_name: Henderson citation: ama: Lawrence EJ, Gao H, Tock AJ, et al. Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. Current Biology. 2019;29(16):2676-2686.e3. doi:10.1016/j.cub.2019.06.084 apa: Lawrence, E. J., Gao, H., Tock, A. J., Lambing, C., Blackwell, A. R., Feng, X., & Henderson, I. R. (2019). Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. Current Biology. Elsevier BV. https://doi.org/10.1016/j.cub.2019.06.084 chicago: Lawrence, Emma J., Hongbo Gao, Andrew J. Tock, Christophe Lambing, Alexander R. Blackwell, Xiaoqi Feng, and Ian R. Henderson. “Natural Variation in TBP-ASSOCIATED FACTOR 4b Controls Meiotic Crossover and Germline Transcription in Arabidopsis.” Current Biology. Elsevier BV, 2019. https://doi.org/10.1016/j.cub.2019.06.084. ieee: E. J. Lawrence et al., “Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis,” Current Biology, vol. 29, no. 16. Elsevier BV, p. 2676–2686.e3, 2019. ista: Lawrence EJ, Gao H, Tock AJ, Lambing C, Blackwell AR, Feng X, Henderson IR. 2019. Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis. Current Biology. 29(16), 2676–2686.e3. mla: Lawrence, Emma J., et al. “Natural Variation in TBP-ASSOCIATED FACTOR 4b Controls Meiotic Crossover and Germline Transcription in Arabidopsis.” Current Biology, vol. 29, no. 16, Elsevier BV, 2019, p. 2676–2686.e3, doi:10.1016/j.cub.2019.06.084. short: E.J. Lawrence, H. Gao, A.J. Tock, C. Lambing, A.R. Blackwell, X. Feng, I.R. Henderson, Current Biology 29 (2019) 2676–2686.e3. date_created: 2023-01-16T09:16:33Z date_published: 2019-08-19T00:00:00Z date_updated: 2023-05-08T10:54:54Z day: '19' department: - _id: XiFe doi: 10.1016/j.cub.2019.06.084 extern: '1' external_id: pmid: - '31378616' intvolume: ' 29' issue: '16' keyword: - General Agricultural and Biological Sciences - General Biochemistry - Genetics and Molecular Biology language: - iso: eng month: '08' oa_version: None page: 2676-2686.e3 pmid: 1 publication: Current Biology publication_identifier: issn: - 0960-9822 publication_status: published publisher: Elsevier BV quality_controlled: '1' scopus_import: '1' status: public title: Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 29 year: '2019' ... --- _id: '12192' abstract: - lang: eng text: Transposable elements (TEs), the movement of which can damage the genome, are epigenetically silenced in eukaryotes. Intriguingly, TEs are activated in the sperm companion cell – vegetative cell (VC) – of the flowering plant Arabidopsis thaliana. However, the extent and mechanism of this activation are unknown. Here we show that about 100 heterochromatic TEs are activated in VCs, mostly by DEMETER-catalyzed DNA demethylation. We further demonstrate that DEMETER access to some of these TEs is permitted by the natural depletion of linker histone H1 in VCs. Ectopically expressed H1 suppresses TEs in VCs by reducing DNA demethylation and via a methylation-independent mechanism. We demonstrate that H1 is required for heterochromatin condensation in plant cells and show that H1 overexpression creates heterochromatic foci in the VC progenitor cell. Taken together, our results demonstrate that the natural depletion of H1 during male gametogenesis facilitates DEMETER-directed DNA demethylation, heterochromatin relaxation, and TE activation. acknowledgement: We thank David Twell for the pDONR-P4-P1R-pLAT52 and pDONR-P2R-P3-mRFP vectors, the John Innes Centre Bioimaging Facility (Elaine Barclay and Grant Calder) for their assistance with microscopy, and the Norwich BioScience Institute Partnership Computing infrastructure for Science Group for High Performance Computing resources. This work was funded by a Biotechnology and Biological Sciences Research Council (BBSRC) David Phillips Fellowship (BB/L025043/1; SH, JZ and XF), a European Research Council Starting Grant ('SexMeth' 804981; XF) and a Grant to Exceptional Researchers by the Gatsby Charitable Foundation (SH and XF). article_number: '42530' article_processing_charge: No article_type: original author: - first_name: Shengbo full_name: He, Shengbo last_name: He - first_name: Martin full_name: Vickers, Martin last_name: Vickers - first_name: Jingyi full_name: Zhang, Jingyi last_name: Zhang - first_name: Xiaoqi full_name: Feng, Xiaoqi id: e0164712-22ee-11ed-b12a-d80fcdf35958 last_name: Feng orcid: 0000-0002-4008-1234 citation: ama: He S, Vickers M, Zhang J, Feng X. Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. eLife. 2019;8. doi:10.7554/elife.42530 apa: He, S., Vickers, M., Zhang, J., & Feng, X. (2019). Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. ELife. eLife Sciences Publications, Ltd. https://doi.org/10.7554/elife.42530 chicago: He, Shengbo, Martin Vickers, Jingyi Zhang, and Xiaoqi Feng. “Natural Depletion of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation and Transposon Activation.” ELife. eLife Sciences Publications, Ltd, 2019. https://doi.org/10.7554/elife.42530. ieee: S. He, M. Vickers, J. Zhang, and X. Feng, “Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation,” eLife, vol. 8. eLife Sciences Publications, Ltd, 2019. ista: He S, Vickers M, Zhang J, Feng X. 2019. Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation. eLife. 8, 42530. mla: He, Shengbo, et al. “Natural Depletion of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation and Transposon Activation.” ELife, vol. 8, 42530, eLife Sciences Publications, Ltd, 2019, doi:10.7554/elife.42530. short: S. He, M. Vickers, J. Zhang, X. Feng, ELife 8 (2019). date_created: 2023-01-16T09:17:21Z date_published: 2019-05-28T00:00:00Z date_updated: 2023-05-08T10:54:12Z day: '28' ddc: - '580' department: - _id: XiFe doi: 10.7554/elife.42530 extern: '1' external_id: unknown: - '31135340' file: - access_level: open_access checksum: ea6b89c20d59e5eb3646916fe5d568ad content_type: application/pdf creator: alisjak date_created: 2023-02-07T09:42:46Z date_updated: 2023-02-07T09:42:46Z file_id: '12525' file_name: 2019_elife_He.pdf file_size: 2493837 relation: main_file success: 1 file_date_updated: 2023-02-07T09:42:46Z has_accepted_license: '1' intvolume: ' 8' keyword: - General Immunology and Microbiology - General Biochemistry - Genetics and Molecular Biology - General Medicine - General Neuroscience language: - iso: eng main_file_link: - open_access: '1' url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6594752/ month: '05' oa: 1 oa_version: Published Version publication: eLife publication_identifier: issn: - 2050-084X publication_status: published publisher: eLife Sciences Publications, Ltd quality_controlled: '1' scopus_import: '1' status: public title: Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 8 year: '2019' ... --- _id: '8405' abstract: - lang: eng text: Atomic-resolution structure determination is crucial for understanding protein function. Cryo-EM and NMR spectroscopy both provide structural information, but currently cryo-EM does not routinely give access to atomic-level structural data, and, generally, NMR structure determination is restricted to small (<30 kDa) proteins. We introduce an integrated structure determination approach that simultaneously uses NMR and EM data to overcome the limits of each of these methods. The approach enables structure determination of the 468 kDa large dodecameric aminopeptidase TET2 to a precision and accuracy below 1 Å by combining secondary-structure information obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large subunits, distance restraints from backbone amides and ILV methyl groups, and a 4.1 Å resolution EM map. The resulting structure exceeds current standards of NMR and EM structure determination in terms of molecular weight and precision. Importantly, the approach is successful even in cases where only medium-resolution cryo-EM data are available. article_number: '2697' article_processing_charge: No article_type: original author: - first_name: Diego F. full_name: Gauto, Diego F. last_name: Gauto - first_name: Leandro F. full_name: Estrozi, Leandro F. last_name: Estrozi - first_name: Charles D. full_name: Schwieters, Charles D. last_name: Schwieters - first_name: Gregory full_name: Effantin, Gregory last_name: Effantin - first_name: Pavel full_name: Macek, Pavel last_name: Macek - first_name: Remy full_name: Sounier, Remy last_name: Sounier - first_name: Astrid C. full_name: Sivertsen, Astrid C. last_name: Sivertsen - first_name: Elena full_name: Schmidt, Elena last_name: Schmidt - first_name: Rime full_name: Kerfah, Rime last_name: Kerfah - first_name: Guillaume full_name: Mas, Guillaume last_name: Mas - first_name: Jacques-Philippe full_name: Colletier, Jacques-Philippe last_name: Colletier - first_name: Peter full_name: Güntert, Peter last_name: Güntert - first_name: Adrien full_name: Favier, Adrien last_name: Favier - first_name: Guy full_name: Schoehn, Guy last_name: Schoehn - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Jerome full_name: Boisbouvier, Jerome last_name: Boisbouvier citation: ama: Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 2019;10. doi:10.1038/s41467-019-10490-9 apa: Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-019-10490-9 chicago: Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin, Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.” Nature Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-10490-9. ieee: D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex,” Nature Communications, vol. 10. Springer Nature, 2019. ista: Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen AC, Schmidt E, Kerfah R, Mas G, Colletier J-P, Güntert P, Favier A, Schoehn G, Schanda P, Boisbouvier J. 2019. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 10, 2697. mla: Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.” Nature Communications, vol. 10, 2697, Springer Nature, 2019, doi:10.1038/s41467-019-10490-9. short: D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier, A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A. Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019). date_created: 2020-09-17T10:28:25Z date_published: 2019-06-19T00:00:00Z date_updated: 2021-01-12T08:19:03Z day: '19' doi: 10.1038/s41467-019-10490-9 extern: '1' external_id: pmid: - '31217444' intvolume: ' 10' keyword: - General Biochemistry - Genetics and Molecular Biology - General Physics and Astronomy - General Chemistry language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1038/s41467-019-10490-9 month: '06' oa: 1 oa_version: Published Version pmid: 1 publication: Nature Communications publication_identifier: issn: - 2041-1723 publication_status: published publisher: Springer Nature quality_controlled: '1' status: public title: Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 10 year: '2019' ... --- _id: '8407' article_processing_charge: No article_type: original author: - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Schanda P. Relaxing with liquids and solids – A perspective on biomolecular dynamics. Journal of Magnetic Resonance. 2019;306:180-186. doi:10.1016/j.jmr.2019.07.025 apa: Schanda, P. (2019). Relaxing with liquids and solids – A perspective on biomolecular dynamics. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2019.07.025 chicago: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular Dynamics.” Journal of Magnetic Resonance. Elsevier, 2019. https://doi.org/10.1016/j.jmr.2019.07.025. ieee: P. Schanda, “Relaxing with liquids and solids – A perspective on biomolecular dynamics,” Journal of Magnetic Resonance, vol. 306. Elsevier, pp. 180–186, 2019. ista: Schanda P. 2019. Relaxing with liquids and solids – A perspective on biomolecular dynamics. Journal of Magnetic Resonance. 306, 180–186. mla: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular Dynamics.” Journal of Magnetic Resonance, vol. 306, Elsevier, 2019, pp. 180–86, doi:10.1016/j.jmr.2019.07.025. short: P. Schanda, Journal of Magnetic Resonance 306 (2019) 180–186. date_created: 2020-09-17T10:28:47Z date_published: 2019-09-01T00:00:00Z date_updated: 2021-01-12T08:19:04Z day: '01' doi: 10.1016/j.jmr.2019.07.025 extern: '1' external_id: pmid: - '31350165' intvolume: ' 306' keyword: - Nuclear and High Energy Physics - Biophysics - Biochemistry - Condensed Matter Physics language: - iso: eng month: '09' oa_version: Submitted Version page: 180-186 pmid: 1 publication: Journal of Magnetic Resonance publication_identifier: issn: - 1090-7807 publication_status: published publisher: Elsevier quality_controlled: '1' status: public title: Relaxing with liquids and solids – A perspective on biomolecular dynamics type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 306 year: '2019' ... --- _id: '8408' abstract: - lang: eng text: Aromatic residues are located at structurally important sites of many proteins. Probing their interactions and dynamics can provide important functional insight but is challenging in large proteins. Here, we introduce approaches to characterize dynamics of phenylalanine residues using 1H-detected fast magic-angle spinning (MAS) NMR combined with a tailored isotope-labeling scheme. Our approach yields isolated two-spin systems that are ideally suited for artefact-free dynamics measurements, and allows probing motions effectively without molecular-weight limitations. The application to the TET2 enzyme assembly of ~0.5 MDa size, the currently largest protein assigned by MAS NMR, provides insights into motions occurring on a wide range of time scales (ps-ms). We quantitatively probe ring flip motions, and show the temperature dependence by MAS NMR measurements down to 100 K. Interestingly, favorable line widths are observed down to 100 K, with potential implications for DNP NMR. Furthermore, we report the first 13C R1ρ MAS NMR relaxation-dispersion measurements and detect structural excursions occurring on a microsecond time scale in the entry pore to the catalytic chamber and at a trimer interface that was proposed as exit pore. We show that the labeling scheme with deuteration at ca. 50 kHz MAS provides superior resolution compared to 100 kHz MAS experiments with protonated, uniformly 13C-labeled samples. article_processing_charge: No article_type: original author: - first_name: Diego F. full_name: Gauto, Diego F. last_name: Gauto - first_name: Pavel full_name: Macek, Pavel last_name: Macek - first_name: Alessandro full_name: Barducci, Alessandro last_name: Barducci - first_name: Hugo full_name: Fraga, Hugo last_name: Fraga - first_name: Audrey full_name: Hessel, Audrey last_name: Hessel - first_name: Tsutomu full_name: Terauchi, Tsutomu last_name: Terauchi - first_name: David full_name: Gajan, David last_name: Gajan - first_name: Yohei full_name: Miyanoiri, Yohei last_name: Miyanoiri - first_name: Jerome full_name: Boisbouvier, Jerome last_name: Boisbouvier - first_name: Roman full_name: Lichtenecker, Roman last_name: Lichtenecker - first_name: Masatsune full_name: Kainosho, Masatsune last_name: Kainosho - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Gauto DF, Macek P, Barducci A, et al. Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical Society. 2019;141(28):11183-11195. doi:10.1021/jacs.9b04219 apa: Gauto, D. F., Macek, P., Barducci, A., Fraga, H., Hessel, A., Terauchi, T., … Schanda, P. (2019). Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.9b04219 chicago: Gauto, Diego F., Pavel Macek, Alessandro Barducci, Hugo Fraga, Audrey Hessel, Tsutomu Terauchi, David Gajan, et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle Spinning NMR.” Journal of the American Chemical Society. American Chemical Society, 2019. https://doi.org/10.1021/jacs.9b04219. ieee: D. F. Gauto et al., “Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR,” Journal of the American Chemical Society, vol. 141, no. 28. American Chemical Society, pp. 11183–11195, 2019. ista: Gauto DF, Macek P, Barducci A, Fraga H, Hessel A, Terauchi T, Gajan D, Miyanoiri Y, Boisbouvier J, Lichtenecker R, Kainosho M, Schanda P. 2019. Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical Society. 141(28), 11183–11195. mla: Gauto, Diego F., et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle Spinning NMR.” Journal of the American Chemical Society, vol. 141, no. 28, American Chemical Society, 2019, pp. 11183–95, doi:10.1021/jacs.9b04219. short: D.F. Gauto, P. Macek, A. Barducci, H. Fraga, A. Hessel, T. Terauchi, D. Gajan, Y. Miyanoiri, J. Boisbouvier, R. Lichtenecker, M. Kainosho, P. Schanda, Journal of the American Chemical Society 141 (2019) 11183–11195. date_created: 2020-09-17T10:29:00Z date_published: 2019-06-14T00:00:00Z date_updated: 2021-01-12T08:19:04Z day: '14' doi: 10.1021/jacs.9b04219 extern: '1' external_id: pmid: - '31199882' intvolume: ' 141' issue: '28' keyword: - Colloid and Surface Chemistry - Biochemistry - General Chemistry - Catalysis language: - iso: eng month: '06' oa_version: Submitted Version page: 11183-11195 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: issn: - 0002-7863 - 1520-5126 publication_status: published publisher: American Chemical Society quality_controlled: '1' status: public title: Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 141 year: '2019' ... --- _id: '8413' abstract: - lang: eng text: NMR relaxation dispersion methods provide a holistic way to observe microsecond time-scale protein backbone motion both in solution and in the solid state. Different nuclei (1H and 15N) and different relaxation dispersion techniques (Bloch–McConnell and near-rotary-resonance) give complementary information about the amplitudes and time scales of the conformational dynamics and provide comprehensive insights into the mechanistic details of the structural rearrangements. In this paper, we exemplify the benefits of the combination of various solution- and solid-state relaxation dispersion methods on a microcrystalline protein (α-spectrin SH3 domain), for which we are able to identify and model the functionally relevant conformational rearrangements around the ligand recognition loop occurring on multiple microsecond time scales. The observed loop motions suggest that the SH3 domain exists in a binding-competent conformation in dynamic equilibrium with a sterically impaired ground-state conformation both in solution and in crystalline form. This inherent plasticity between the interconverting macrostates is compatible with a conformational-preselection model and provides new insights into the recognition mechanisms of SH3 domains. article_processing_charge: No article_type: original author: - first_name: Petra full_name: Rovó, Petra last_name: Rovó - first_name: Colin A. full_name: Smith, Colin A. last_name: Smith - first_name: Diego full_name: Gauto, Diego last_name: Gauto - first_name: Bert L. full_name: de Groot, Bert L. last_name: de Groot - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Rasmus full_name: Linser, Rasmus last_name: Linser citation: ama: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. 2019;141(2):858-869. doi:10.1021/jacs.8b09258 apa: Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., & Linser, R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09258 chicago: Rovó, Petra, Colin A. Smith, Diego Gauto, Bert L. de Groot, Paul Schanda, and Rasmus Linser. “Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.” Journal of the American Chemical Society. American Chemical Society, 2019. https://doi.org/10.1021/jacs.8b09258. ieee: P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, and R. Linser, “Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques,” Journal of the American Chemical Society, vol. 141, no. 2. American Chemical Society, pp. 858–869, 2019. ista: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. 2019. Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. 141(2), 858–869. mla: Rovó, Petra, et al. “Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.” Journal of the American Chemical Society, vol. 141, no. 2, American Chemical Society, 2019, pp. 858–69, doi:10.1021/jacs.8b09258. short: P. Rovó, C.A. Smith, D. Gauto, B.L. de Groot, P. Schanda, R. Linser, Journal of the American Chemical Society 141 (2019) 858–869. date_created: 2020-09-17T10:29:50Z date_published: 2019-01-08T00:00:00Z date_updated: 2021-01-12T08:19:07Z day: '08' doi: 10.1021/jacs.8b09258 extern: '1' external_id: pmid: - '30620186' intvolume: ' 141' issue: '2' keyword: - Colloid and Surface Chemistry - Biochemistry - General Chemistry - Catalysis language: - iso: eng month: '01' oa_version: Submitted Version page: 858-869 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: issn: - 0002-7863 - 1520-5126 publication_status: published publisher: American Chemical Society quality_controlled: '1' status: public title: Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 141 year: '2019' ... --- _id: '9018' abstract: - lang: eng text: Anti-silencing function 1 (ASF1) is a conserved H3-H4 histone chaperone involved in histone dynamics during replication, transcription, and DNA repair. Overexpressed in proliferating tissues including many tumors, ASF1 has emerged as a promising therapeutic target. Here, we combine structural, computational, and biochemical approaches to design peptides that inhibit the ASF1-histone interaction. Starting from the structure of the human ASF1-histone complex, we developed a rational design strategy combining epitope tethering and optimization of interface contacts to identify a potent peptide inhibitor with a dissociation constant of 3 nM. When introduced into cultured cells, the inhibitors impair cell proliferation, perturb cell-cycle progression, and reduce cell migration and invasion in a manner commensurate with their affinity for ASF1. Finally, we find that direct injection of the most potent ASF1 peptide inhibitor in mouse allografts reduces tumor growth. Our results open new avenues to use ASF1 inhibitors as promising leads for cancer therapy. article_processing_charge: No article_type: original author: - first_name: May M full_name: Bakail, May M id: FB3C3F8E-522F-11EA-B186-22963DDC885E last_name: Bakail orcid: 0000-0002-9592-1587 - first_name: Albane full_name: Gaubert, Albane last_name: Gaubert - first_name: Jessica full_name: Andreani, Jessica last_name: Andreani - first_name: Gwenaëlle full_name: Moal, Gwenaëlle last_name: Moal - first_name: Guillaume full_name: Pinna, Guillaume last_name: Pinna - first_name: Ekaterina full_name: Boyarchuk, Ekaterina last_name: Boyarchuk - first_name: Marie-Cécile full_name: Gaillard, Marie-Cécile last_name: Gaillard - first_name: Regis full_name: Courbeyrette, Regis last_name: Courbeyrette - first_name: Carl full_name: Mann, Carl last_name: Mann - first_name: Jean-Yves full_name: Thuret, Jean-Yves last_name: Thuret - first_name: Bérengère full_name: Guichard, Bérengère last_name: Guichard - first_name: Brice full_name: Murciano, Brice last_name: Murciano - first_name: Nicolas full_name: Richet, Nicolas last_name: Richet - first_name: Adeline full_name: Poitou, Adeline last_name: Poitou - first_name: Claire full_name: Frederic, Claire last_name: Frederic - first_name: Marie-Hélène full_name: Le Du, Marie-Hélène last_name: Le Du - first_name: Morgane full_name: Agez, Morgane last_name: Agez - first_name: Caroline full_name: Roelants, Caroline last_name: Roelants - first_name: Zachary A. full_name: Gurard-Levin, Zachary A. last_name: Gurard-Levin - first_name: Geneviève full_name: Almouzni, Geneviève last_name: Almouzni - first_name: Nadia full_name: Cherradi, Nadia last_name: Cherradi - first_name: Raphael full_name: Guerois, Raphael last_name: Guerois - first_name: Françoise full_name: Ochsenbein, Françoise last_name: Ochsenbein citation: ama: Bakail MM, Gaubert A, Andreani J, et al. Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology. 2019;26(11):1573-1585.e10. doi:10.1016/j.chembiol.2019.09.002 apa: Bakail, M. M., Gaubert, A., Andreani, J., Moal, G., Pinna, G., Boyarchuk, E., … Ochsenbein, F. (2019). Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology. Elsevier. https://doi.org/10.1016/j.chembiol.2019.09.002 chicago: Bakail, May M, Albane Gaubert, Jessica Andreani, Gwenaëlle Moal, Guillaume Pinna, Ekaterina Boyarchuk, Marie-Cécile Gaillard, et al. “Design on a Rational Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1.” Cell Chemical Biology. Elsevier, 2019. https://doi.org/10.1016/j.chembiol.2019.09.002. ieee: M. M. Bakail et al., “Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1,” Cell Chemical Biology, vol. 26, no. 11. Elsevier, p. 1573–1585.e10, 2019. ista: Bakail MM, Gaubert A, Andreani J, Moal G, Pinna G, Boyarchuk E, Gaillard M-C, Courbeyrette R, Mann C, Thuret J-Y, Guichard B, Murciano B, Richet N, Poitou A, Frederic C, Le Du M-H, Agez M, Roelants C, Gurard-Levin ZA, Almouzni G, Cherradi N, Guerois R, Ochsenbein F. 2019. Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology. 26(11), 1573–1585.e10. mla: Bakail, May M., et al. “Design on a Rational Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1.” Cell Chemical Biology, vol. 26, no. 11, Elsevier, 2019, p. 1573–1585.e10, doi:10.1016/j.chembiol.2019.09.002. short: M.M. Bakail, A. Gaubert, J. Andreani, G. Moal, G. Pinna, E. Boyarchuk, M.-C. Gaillard, R. Courbeyrette, C. Mann, J.-Y. Thuret, B. Guichard, B. Murciano, N. Richet, A. Poitou, C. Frederic, M.-H. Le Du, M. Agez, C. Roelants, Z.A. Gurard-Levin, G. Almouzni, N. Cherradi, R. Guerois, F. Ochsenbein, Cell Chemical Biology 26 (2019) 1573–1585.e10. date_created: 2021-01-19T11:04:50Z date_published: 2019-11-21T00:00:00Z date_updated: 2023-02-23T13:46:53Z day: '21' doi: 10.1016/j.chembiol.2019.09.002 extern: '1' external_id: pmid: - '31543461' intvolume: ' 26' issue: '11' keyword: - Clinical Biochemistry - Molecular Medicine - Biochemistry - Molecular Biology - Pharmacology - Drug Discovery language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1016/j.chembiol.2019.09.002 month: '11' oa: 1 oa_version: Published Version page: 1573-1585.e10 pmid: 1 publication: Cell Chemical Biology publication_identifier: issn: - 2451-9456 publication_status: published publisher: Elsevier quality_controlled: '1' status: public title: Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1 type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 26 year: '2019' ... --- _id: '9060' abstract: - lang: eng text: Molecular motors are essential to the living, generating fluctuations that boost transport and assist assembly. Active colloids, that consume energy to move, hold similar potential for man-made materials controlled by forces generated from within. Yet, their use as a powerhouse in materials science lacks. Here we show a massive acceleration of the annealing of a monolayer of passive beads by moderate addition of self-propelled microparticles. We rationalize our observations with a model of collisions that drive active fluctuations and activate the annealing. The experiment is quantitatively compared with Brownian dynamic simulations that further unveil a dynamical transition in the mechanism of annealing. Active dopants travel uniformly in the system or co-localize at the grain boundaries as a result of the persistence of their motion. Our findings uncover the potential of internal activity to control materials and lay the groundwork for the rise of materials science beyond equilibrium. article_number: '3380' article_processing_charge: No article_type: original arxiv: 1 author: - first_name: Sophie full_name: Ramananarivo, Sophie last_name: Ramananarivo - first_name: Etienne full_name: Ducrot, Etienne last_name: Ducrot - first_name: Jérémie A full_name: Palacci, Jérémie A id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d last_name: Palacci orcid: 0000-0002-7253-9465 citation: ama: Ramananarivo S, Ducrot E, Palacci JA. Activity-controlled annealing of colloidal monolayers. Nature Communications. 2019;10(1). doi:10.1038/s41467-019-11362-y apa: Ramananarivo, S., Ducrot, E., & Palacci, J. A. (2019). Activity-controlled annealing of colloidal monolayers. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-019-11362-y chicago: Ramananarivo, Sophie, Etienne Ducrot, and Jérémie A Palacci. “Activity-Controlled Annealing of Colloidal Monolayers.” Nature Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-11362-y. ieee: S. Ramananarivo, E. Ducrot, and J. A. Palacci, “Activity-controlled annealing of colloidal monolayers,” Nature Communications, vol. 10, no. 1. Springer Nature, 2019. ista: Ramananarivo S, Ducrot E, Palacci JA. 2019. Activity-controlled annealing of colloidal monolayers. Nature Communications. 10(1), 3380. mla: Ramananarivo, Sophie, et al. “Activity-Controlled Annealing of Colloidal Monolayers.” Nature Communications, vol. 10, no. 1, 3380, Springer Nature, 2019, doi:10.1038/s41467-019-11362-y. short: S. Ramananarivo, E. Ducrot, J.A. Palacci, Nature Communications 10 (2019). date_created: 2021-02-02T13:43:36Z date_published: 2019-07-29T00:00:00Z date_updated: 2023-02-23T13:47:59Z day: '29' ddc: - '530' doi: 10.1038/s41467-019-11362-y extern: '1' external_id: arxiv: - '1909.07382' pmid: - '31358762' file: - access_level: open_access checksum: 70c6e5d6fbea0932b0669505ab6633ec content_type: application/pdf creator: cziletti date_created: 2021-02-02T13:47:21Z date_updated: 2021-02-02T13:47:21Z file_id: '9061' file_name: 2019_NatureComm_Ramananarivo.pdf file_size: 2820337 relation: main_file success: 1 file_date_updated: 2021-02-02T13:47:21Z has_accepted_license: '1' intvolume: ' 10' issue: '1' keyword: - General Biochemistry - Genetics and Molecular Biology - General Physics and Astronomy - General Chemistry language: - iso: eng month: '07' oa: 1 oa_version: Published Version pmid: 1 publication: Nature Communications publication_identifier: issn: - 2041-1723 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: Activity-controlled annealing of colloidal monolayers tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425 volume: 10 year: '2019' ... --- _id: '13371' abstract: - lang: eng text: Diamondoid nanoporous crystals represent a synthetically challenging class of materials that typically have been obtained from tetrahedral building blocks. In this issue of Chem, Stoddart and coworkers demonstrate that it is possible to generate diamondoid frameworks from a hexacationic building block lacking a tetrahedral symmetry. These results highlight the great potential of self-assembly for rapidly transforming small molecules into structurally complex functional materials. article_processing_charge: No article_type: original author: - first_name: Michał J. full_name: Białek, Michał J. last_name: Białek - first_name: Rafal full_name: Klajn, Rafal id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b last_name: Klajn citation: ama: Białek MJ, Klajn R. Diamond grows up. Chem. 2019;5(9):2283-2285. doi:10.1016/j.chempr.2019.08.012 apa: Białek, M. J., & Klajn, R. (2019). Diamond grows up. Chem. Elsevier. https://doi.org/10.1016/j.chempr.2019.08.012 chicago: Białek, Michał J., and Rafal Klajn. “Diamond Grows Up.” Chem. Elsevier, 2019. https://doi.org/10.1016/j.chempr.2019.08.012. ieee: M. J. Białek and R. Klajn, “Diamond grows up,” Chem, vol. 5, no. 9. Elsevier, pp. 2283–2285, 2019. ista: Białek MJ, Klajn R. 2019. Diamond grows up. Chem. 5(9), 2283–2285. mla: Białek, Michał J., and Rafal Klajn. “Diamond Grows Up.” Chem, vol. 5, no. 9, Elsevier, 2019, pp. 2283–85, doi:10.1016/j.chempr.2019.08.012. short: M.J. Białek, R. Klajn, Chem 5 (2019) 2283–2285. date_created: 2023-08-01T09:38:38Z date_published: 2019-09-12T00:00:00Z date_updated: 2023-08-07T10:46:50Z day: '12' doi: 10.1016/j.chempr.2019.08.012 extern: '1' intvolume: ' 5' issue: '9' keyword: - Materials Chemistry - Biochemistry (medical) - General Chemical Engineering - Environmental Chemistry - Biochemistry - General Chemistry language: - iso: eng main_file_link: - open_access: '1' url: https://doi.org/10.1016/j.chempr.2019.08.012 month: '09' oa: 1 oa_version: Published Version page: 2283-2285 publication: Chem publication_identifier: eissn: - 2451-9294 issn: - 2451-9308 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: Diamond grows up type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 5 year: '2019' ... --- _id: '13373' abstract: - lang: eng text: The reversible photoisomerization of azobenzene has been utilized to construct a plethora of systems in which optical, electronic, catalytic, and other properties can be controlled by light. However, owing to azobenzene’s hydrophobic nature, most of these examples have been realized only in organic solvents, and systems operating in water are relatively scarce. Here, we show that by coadsorbing the inherently hydrophobic azobenzenes with water-solubilizing ligands on the same nanoparticulate platforms, it is possible to render them essentially water-soluble. To this end, we developed a modified nanoparticle functionalization procedure allowing us to precisely fine-tune the amount of azobenzene on the functionalized nanoparticles. Molecular dynamics simulations helped us to identify two distinct supramolecular architectures (depending on the length of the background ligand) on these nanoparticles, which can explain their excellent aqueous solubilities. Azobenzenes adsorbed on these water-soluble nanoparticles exhibit highly reversible photoisomerization upon exposure to UV and visible light. Importantly, the mixed-monolayer approach allowed us to systematically investigate how the background ligand affects the switching properties of azobenzene. We found that the nature of the background ligand has a profound effect on the kinetics of azobenzene switching. For example, a hydroxy-terminated background ligand is capable of accelerating the back-isomerization reaction by more than 6000-fold. These results pave the way toward the development of novel light-responsive nanomaterials operating in aqueous media and, in the long run, in biological environments. article_processing_charge: No article_type: original author: - first_name: Zonglin full_name: Chu, Zonglin last_name: Chu - first_name: Yanxiao full_name: Han, Yanxiao last_name: Han - first_name: Tong full_name: Bian, Tong last_name: Bian - first_name: Soumen full_name: De, Soumen last_name: De - first_name: Petr full_name: Král, Petr last_name: Král - first_name: Rafal full_name: Klajn, Rafal id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b last_name: Klajn citation: ama: Chu Z, Han Y, Bian T, De S, Král P, Klajn R. Supramolecular control of azobenzene switching on nanoparticles. Journal of the American Chemical Society. 2019;141(5):1949-1960. doi:10.1021/jacs.8b09638 apa: Chu, Z., Han, Y., Bian, T., De, S., Král, P., & Klajn, R. (2019). Supramolecular control of azobenzene switching on nanoparticles. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09638 chicago: Chu, Zonglin, Yanxiao Han, Tong Bian, Soumen De, Petr Král, and Rafal Klajn. “Supramolecular Control of Azobenzene Switching on Nanoparticles.” Journal of the American Chemical Society. American Chemical Society, 2019. https://doi.org/10.1021/jacs.8b09638. ieee: Z. Chu, Y. Han, T. Bian, S. De, P. Král, and R. Klajn, “Supramolecular control of azobenzene switching on nanoparticles,” Journal of the American Chemical Society, vol. 141, no. 5. American Chemical Society, pp. 1949–1960, 2019. ista: Chu Z, Han Y, Bian T, De S, Král P, Klajn R. 2019. Supramolecular control of azobenzene switching on nanoparticles. Journal of the American Chemical Society. 141(5), 1949–1960. mla: Chu, Zonglin, et al. “Supramolecular Control of Azobenzene Switching on Nanoparticles.” Journal of the American Chemical Society, vol. 141, no. 5, American Chemical Society, 2019, pp. 1949–60, doi:10.1021/jacs.8b09638. short: Z. Chu, Y. Han, T. Bian, S. De, P. Král, R. Klajn, Journal of the American Chemical Society 141 (2019) 1949–1960. date_created: 2023-08-01T09:39:19Z date_published: 2019-02-06T00:00:00Z date_updated: 2023-08-07T10:51:12Z day: '06' doi: 10.1021/jacs.8b09638 extern: '1' external_id: pmid: - '30595017' intvolume: ' 141' issue: '5' keyword: - Colloid and Surface Chemistry - Biochemistry - General Chemistry - Catalysis language: - iso: eng month: '02' oa_version: Published Version page: 1949-1960 pmid: 1 publication: Journal of the American Chemical Society publication_identifier: eissn: - 1520-5126 issn: - 0002-7863 publication_status: published publisher: American Chemical Society quality_controlled: '1' scopus_import: '1' status: public title: Supramolecular control of azobenzene switching on nanoparticles type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 141 year: '2019' ... --- _id: '11060' abstract: - lang: eng text: The inner nuclear membrane (INM) is a subdomain of the endoplasmic reticulum (ER) that is gated by the nuclear pore complex. It is unknown whether proteins of the INM and ER are degraded through shared or distinct pathways in mammalian cells. We applied dynamic proteomics to profile protein half-lives and report that INM and ER residents turn over at similar rates, indicating that the INM’s unique topology is not a barrier to turnover. Using a microscopy approach, we observed that the proteasome can degrade INM proteins in situ. However, we also uncovered evidence for selective, vesicular transport-mediated turnover of a single INM protein, emerin, that is potentiated by ER stress. Emerin is rapidly cleared from the INM by a mechanism that requires emerin’s LEM domain to mediate vesicular trafficking to lysosomes. This work demonstrates that the INM can be dynamically remodeled in response to environmental inputs. article_number: e49796 article_processing_charge: No article_type: original author: - first_name: Abigail full_name: Buchwalter, Abigail last_name: Buchwalter - first_name: Roberta full_name: Schulte, Roberta last_name: Schulte - first_name: Hsiao full_name: Tsai, Hsiao last_name: Tsai - first_name: Juliana full_name: Capitanio, Juliana last_name: Capitanio - first_name: Martin W full_name: HETZER, Martin W id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed last_name: HETZER orcid: 0000-0002-2111-992X citation: ama: Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. eLife. 2019;8. doi:10.7554/elife.49796 apa: Buchwalter, A., Schulte, R., Tsai, H., Capitanio, J., & Hetzer, M. (2019). Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. ELife. eLife Sciences Publications. https://doi.org/10.7554/elife.49796 chicago: Buchwalter, Abigail, Roberta Schulte, Hsiao Tsai, Juliana Capitanio, and Martin Hetzer. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress.” ELife. eLife Sciences Publications, 2019. https://doi.org/10.7554/elife.49796. ieee: A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, and M. Hetzer, “Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress,” eLife, vol. 8. eLife Sciences Publications, 2019. ista: Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. 2019. Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress. eLife. 8, e49796. mla: Buchwalter, Abigail, et al. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin by Vesicular Transport during ER Stress.” ELife, vol. 8, e49796, eLife Sciences Publications, 2019, doi:10.7554/elife.49796. short: A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, M. Hetzer, ELife 8 (2019). date_created: 2022-04-07T07:45:02Z date_published: 2019-10-10T00:00:00Z date_updated: 2023-05-31T06:36:22Z day: '10' ddc: - '570' doi: 10.7554/elife.49796 extern: '1' external_id: pmid: - '31599721' file: - access_level: open_access checksum: 1e8672a1e9c3dc0a2d3d0dad89673616 content_type: application/pdf creator: dernst date_created: 2022-04-08T08:18:01Z date_updated: 2022-04-08T08:18:01Z file_id: '11138' file_name: 2019_eLife_Buchwalter.pdf file_size: 6984654 relation: main_file success: 1 file_date_updated: 2022-04-08T08:18:01Z has_accepted_license: '1' intvolume: ' 8' keyword: - General Immunology and Microbiology - General Biochemistry - Genetics and Molecular Biology - General Medicine - General Neuroscience language: - iso: eng month: '10' oa: 1 oa_version: Published Version pmid: 1 publication: eLife publication_identifier: issn: - 2050-084X publication_status: published publisher: eLife Sciences Publications quality_controlled: '1' related_material: record: - id: '13079' relation: research_data status: public scopus_import: '1' status: public title: Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd volume: 8 year: '2019' ... --- _id: '8436' abstract: - lang: eng text: The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial “transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins in a “nascent chain-like” conformation through a ribosome-free compartment. article_processing_charge: No article_type: original author: - first_name: Katharina full_name: Weinhäupl, Katharina last_name: Weinhäupl - first_name: Caroline full_name: Lindau, Caroline last_name: Lindau - first_name: Audrey full_name: Hessel, Audrey last_name: Hessel - first_name: Yong full_name: Wang, Yong last_name: Wang - first_name: Conny full_name: Schütze, Conny last_name: Schütze - first_name: Tobias full_name: Jores, Tobias last_name: Jores - first_name: Laura full_name: Melchionda, Laura last_name: Melchionda - first_name: Birgit full_name: Schönfisch, Birgit last_name: Schönfisch - first_name: Hubert full_name: Kalbacher, Hubert last_name: Kalbacher - first_name: Beate full_name: Bersch, Beate last_name: Bersch - first_name: Doron full_name: Rapaport, Doron last_name: Rapaport - first_name: Martha full_name: Brennich, Martha last_name: Brennich - first_name: Kresten full_name: Lindorff-Larsen, Kresten last_name: Lindorff-Larsen - first_name: Nils full_name: Wiedemann, Nils last_name: Wiedemann - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 citation: ama: Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 2018;175(5):1365-1379.e25. doi:10.1016/j.cell.2018.10.039 apa: Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., … Schanda, P. (2018). Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. Elsevier. https://doi.org/10.1016/j.cell.2018.10.039 chicago: Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” Cell. Elsevier, 2018. https://doi.org/10.1016/j.cell.2018.10.039. ieee: K. Weinhäupl et al., “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” Cell, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018. ista: Weinhäupl K, Lindau C, Hessel A, Wang Y, Schütze C, Jores T, Melchionda L, Schönfisch B, Kalbacher H, Bersch B, Rapaport D, Brennich M, Lindorff-Larsen K, Wiedemann N, Schanda P. 2018. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 175(5), 1365–1379.e25. mla: Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” Cell, vol. 175, no. 5, Elsevier, 2018, p. 1365–1379.e25, doi:10.1016/j.cell.2018.10.039. short: K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda, B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen, N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25. date_created: 2020-09-18T10:04:39Z date_published: 2018-11-15T00:00:00Z date_updated: 2021-01-12T08:19:15Z day: '15' doi: 10.1016/j.cell.2018.10.039 extern: '1' intvolume: ' 175' issue: '5' keyword: - General Biochemistry - Genetics and Molecular Biology language: - iso: eng month: '11' oa_version: None page: 1365-1379.e25 publication: Cell publication_identifier: issn: - 0092-8674 publication_status: published publisher: Elsevier quality_controlled: '1' status: public title: Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 175 year: '2018' ...