[{"page":"3559-3607","issue":"7","volume":118,"keyword":["General Chemistry"],"date_published":"2018-02-28T00:00:00Z","publisher":"American Chemical Society","article_type":"original","publication_identifier":{"issn":["0009-2665","1520-6890"]},"intvolume":"       118","status":"public","month":"02","date_created":"2020-09-18T10:05:35Z","article_processing_charge":"No","author":[{"full_name":"Chipot, Christophe","first_name":"Christophe","last_name":"Chipot"},{"last_name":"Dehez","first_name":"François","full_name":"Dehez, François"},{"last_name":"Schnell","first_name":"Jason R.","full_name":"Schnell, Jason R."},{"last_name":"Zitzmann","first_name":"Nicole","full_name":"Zitzmann, Nicole"},{"full_name":"Pebay-Peyroula, Eva","last_name":"Pebay-Peyroula","first_name":"Eva"},{"last_name":"Catoire","first_name":"Laurent J.","full_name":"Catoire, Laurent J."},{"last_name":"Miroux","first_name":"Bruno","full_name":"Miroux, Bruno"},{"full_name":"Kunji, Edmund R. S.","last_name":"Kunji","first_name":"Edmund R. S."},{"full_name":"Veglia, Gianluigi","last_name":"Veglia","first_name":"Gianluigi"},{"full_name":"Cross, Timothy A.","first_name":"Timothy A.","last_name":"Cross"},{"first_name":"Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","quality_controlled":"1","citation":{"mla":"Chipot, Christophe, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.” <i>Chemical Reviews</i>, vol. 118, no. 7, American Chemical Society, 2018, pp. 3559–607, doi:<a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">10.1021/acs.chemrev.7b00570</a>.","apa":"Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire, L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. <i>Chemical Reviews</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">https://doi.org/10.1021/acs.chemrev.7b00570</a>","short":"C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire, B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118 (2018) 3559–3607.","chicago":"Chipot, Christophe, François Dehez, Jason R. Schnell, Nicole Zitzmann, Eva Pebay-Peyroula, Laurent J. Catoire, Bruno Miroux, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.” <i>Chemical Reviews</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">https://doi.org/10.1021/acs.chemrev.7b00570</a>.","ista":"Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ, Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P. 2018. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. Chemical Reviews. 118(7), 3559–3607.","ieee":"C. Chipot <i>et al.</i>, “Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies,” <i>Chemical Reviews</i>, vol. 118, no. 7. American Chemical Society, pp. 3559–3607, 2018.","ama":"Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. <i>Chemical Reviews</i>. 2018;118(7):3559-3607. doi:<a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">10.1021/acs.chemrev.7b00570</a>"},"year":"2018","day":"28","oa_version":"None","type":"journal_article","date_updated":"2021-01-12T08:19:18Z","_id":"8442","language":[{"iso":"eng"}],"doi":"10.1021/acs.chemrev.7b00570","publication":"Chemical Reviews","title":"Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies","abstract":[{"text":"Membrane proteins perform a host of vital cellular functions. Deciphering the molecular mechanisms whereby they fulfill these functions requires detailed biophysical and structural investigations. Detergents have proven pivotal to extract the protein from its native surroundings. Yet, they provide a milieu that departs significantly from that of the biological membrane, to the extent that the structure, the dynamics, and the interactions of membrane proteins in detergents may considerably vary, as compared to the native environment. Understanding the impact of detergents on membrane proteins is, therefore, crucial to assess the biological relevance of results obtained in detergents. Here, we review the strengths and weaknesses of alkyl phosphocholines (or foscholines), the most widely used detergent in solution-NMR studies of membrane proteins. While this class of detergents is often successful for membrane protein solubilization, a growing list of examples points to destabilizing and denaturing properties, in particular for α-helical membrane proteins. Our comprehensive analysis stresses the importance of stringent controls when working with this class of detergents and when analyzing the structure and dynamics of membrane proteins in alkyl phosphocholine detergents.","lang":"eng"}],"publication_status":"published"},{"_id":"9053","oa":1,"pmid":1,"title":"Diffusiophoretic design of self-spinning microgears from colloidal microswimmers","publication":"Soft Matter","abstract":[{"text":"The development of strategies to assemble microscopic machines from dissipative building blocks are essential on the route to novel active materials. We recently demonstrated the hierarchical self-assembly of phoretic microswimmers into self-spinning microgears and their synchronization by diffusiophoretic interactions [Aubret et al., Nat. Phys., 2018]. In this paper, we adopt a pedagogical approach and expose our strategy to control self-assembly and build machines using phoretic phenomena. We notably introduce Highly Inclined Laminated Optical sheets microscopy (HILO) to image and characterize anisotropic and dynamic diffusiophoretic interactions, which cannot be performed by conventional fluorescence microscopy. The dynamics of a (haematite) photocatalytic material immersed in (hydrogen peroxide) fuel under various illumination patterns is first described and quantitatively rationalized by a model of diffusiophoresis, the migration of a colloidal particle in a concentration gradient. It is further exploited to design phototactic microswimmers that direct towards the high intensity of light, as a result of the reorientation of the haematite in a light gradient. We finally show the assembly of self-spinning microgears from colloidal microswimmers and carefully characterize the interactions using HILO techniques. The results are compared with analytical and numerical predictions and agree quantitatively, stressing the important role played by concentration gradients induced by chemical activity to control and design interactions. Because the approach described hereby is generic, this works paves the way for the rational design of machines by controlling phoretic phenomena.","lang":"eng"}],"publication_status":"published","quality_controlled":"1","extern":"1","author":[{"first_name":"Antoine","last_name":"Aubret","full_name":"Aubret, Antoine"},{"first_name":"Jérémie A","last_name":"Palacci","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d","full_name":"Palacci, Jérémie A","orcid":"0000-0002-7253-9465"}],"main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1909.11121"}],"citation":{"ista":"Aubret A, Palacci JA. 2018. Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. Soft Matter. 14(47), 9577–9588.","chicago":"Aubret, Antoine, and Jérémie A Palacci. “Diffusiophoretic Design of Self-Spinning Microgears from Colloidal Microswimmers.” <i>Soft Matter</i>. Royal Society of Chemistry , 2018. <a href=\"https://doi.org/10.1039/c8sm01760c\">https://doi.org/10.1039/c8sm01760c</a>.","short":"A. Aubret, J.A. Palacci, Soft Matter 14 (2018) 9577–9588.","ama":"Aubret A, Palacci JA. Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. <i>Soft Matter</i>. 2018;14(47):9577-9588. doi:<a href=\"https://doi.org/10.1039/c8sm01760c\">10.1039/c8sm01760c</a>","ieee":"A. Aubret and J. A. Palacci, “Diffusiophoretic design of self-spinning microgears from colloidal microswimmers,” <i>Soft Matter</i>, vol. 14, no. 47. Royal Society of Chemistry , pp. 9577–9588, 2018.","apa":"Aubret, A., &#38; Palacci, J. A. (2018). Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. <i>Soft Matter</i>. Royal Society of Chemistry . <a href=\"https://doi.org/10.1039/c8sm01760c\">https://doi.org/10.1039/c8sm01760c</a>","mla":"Aubret, Antoine, and Jérémie A. Palacci. “Diffusiophoretic Design of Self-Spinning Microgears from Colloidal Microswimmers.” <i>Soft Matter</i>, vol. 14, no. 47, Royal Society of Chemistry , 2018, pp. 9577–88, doi:<a href=\"https://doi.org/10.1039/c8sm01760c\">10.1039/c8sm01760c</a>."},"year":"2018","intvolume":"        14","status":"public","month":"12","date_created":"2021-02-01T13:44:41Z","issue":"47","volume":14,"publisher":"Royal Society of Chemistry ","article_type":"original","doi":"10.1039/c8sm01760c","language":[{"iso":"eng"}],"article_processing_charge":"No","user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","day":"21","oa_version":"Preprint","type":"journal_article","date_updated":"2023-02-23T13:47:43Z","scopus_import":"1","publication_identifier":{"issn":["1744-683X"],"eissn":["1744-6848"]},"arxiv":1,"page":"9577-9588","keyword":["General Chemistry","Condensed Matter Physics"],"external_id":{"arxiv":["1909.11121"],"pmid":["30456407"]},"date_published":"2018-12-21T00:00:00Z"},{"article_number":"641","status":"public","date_created":"2023-08-01T09:39:32Z","month":"02","intvolume":"         9","publisher":"Springer Nature","article_type":"original","volume":9,"publication_status":"published","abstract":[{"lang":"eng","text":"Confining molecules to volumes only slightly larger than the molecules themselves can profoundly alter their properties. Molecular switches—entities that can be toggled between two or more forms upon exposure to an external stimulus—often require conformational freedom to isomerize. Therefore, placing these switches in confined spaces can render them non-operational. To preserve the switchability of these species under confinement, we work with a water-soluble coordination cage that is flexible enough to adapt its shape to the conformation of the encapsulated guest. We show that owing to its flexibility, the cage is not only capable of accommodating—and solubilizing in water—several light-responsive spiropyran-based molecular switches, but, more importantly, it also provides an environment suitable for the efficient, reversible photoisomerization of the bound guests. Our findings pave the way towards studying various molecular switching processes in confined environments."}],"oa":1,"related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/s41467-018-03701-2"}]},"_id":"13374","publication":"Nature Communications","title":"Reversible chromism of spiropyran in the cavity of a flexible coordination cage","pmid":1,"year":"2018","extern":"1","quality_controlled":"1","author":[{"first_name":"Dipak","last_name":"Samanta","full_name":"Samanta, Dipak"},{"last_name":"Galaktionova","first_name":"Daria","full_name":"Galaktionova, Daria"},{"full_name":"Gemen, Julius","first_name":"Julius","last_name":"Gemen"},{"first_name":"Linda J. W.","last_name":"Shimon","full_name":"Shimon, Linda J. W."},{"full_name":"Diskin-Posner, Yael","last_name":"Diskin-Posner","first_name":"Yael"},{"full_name":"Avram, Liat","first_name":"Liat","last_name":"Avram"},{"full_name":"Král, Petr","first_name":"Petr","last_name":"Král"},{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal","first_name":"Rafal","last_name":"Klajn"}],"citation":{"apa":"Samanta, D., Galaktionova, D., Gemen, J., Shimon, L. J. W., Diskin-Posner, Y., Avram, L., … Klajn, R. (2018). Reversible chromism of spiropyran in the cavity of a flexible coordination cage. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-02715-6\">https://doi.org/10.1038/s41467-017-02715-6</a>","mla":"Samanta, Dipak, et al. “Reversible Chromism of Spiropyran in the Cavity of a Flexible Coordination Cage.” <i>Nature Communications</i>, vol. 9, 641, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-017-02715-6\">10.1038/s41467-017-02715-6</a>.","ieee":"D. Samanta <i>et al.</i>, “Reversible chromism of spiropyran in the cavity of a flexible coordination cage,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018.","ama":"Samanta D, Galaktionova D, Gemen J, et al. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-017-02715-6\">10.1038/s41467-017-02715-6</a>","ista":"Samanta D, Galaktionova D, Gemen J, Shimon LJW, Diskin-Posner Y, Avram L, Král P, Klajn R. 2018. Reversible chromism of spiropyran in the cavity of a flexible coordination cage. Nature Communications. 9, 641.","short":"D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L. Avram, P. Král, R. Klajn, Nature Communications 9 (2018).","chicago":"Samanta, Dipak, Daria Galaktionova, Julius Gemen, Linda J. W. Shimon, Yael Diskin-Posner, Liat Avram, Petr Král, and Rafal Klajn. “Reversible Chromism of Spiropyran in the Cavity of a Flexible Coordination Cage.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-017-02715-6\">https://doi.org/10.1038/s41467-017-02715-6</a>."},"main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-02715-6","open_access":"1"}],"publication_identifier":{"eissn":["2041-1723"]},"scopus_import":"1","date_published":"2018-02-13T00:00:00Z","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"external_id":{"pmid":["29440687"]},"language":[{"iso":"eng"}],"doi":"10.1038/s41467-017-02715-6","day":"13","type":"journal_article","date_updated":"2023-08-07T10:54:05Z","oa_version":"Published Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No"},{"title":"“Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles","publication":"Angewandte Chemie International Edition","pmid":1,"oa":1,"_id":"13377","publication_status":"published","abstract":[{"text":"Confining organic molecules to the surfaces of inorganic nanoparticles can induce intermolecular interactions between them, which can affect the composition of the mixed self-assembled monolayers obtained by co-adsorption from solution of two different molecules. Two thiolated ligands (a dialkylviologen and a zwitterionic sulfobetaine) that can interact with each other electrostatically were coadsorbed onto gold nanoparticles. The nanoparticles favor a narrow range of ratios of these two molecules that is largely independent of the molar ratio in solution. Changing the solution molar ratio of the two ligands by a factor of 5 000 affects the on-nanoparticle ratio of these ligands by only threefold. This behavior is reminiscent of the formation of insoluble inorganic salts (such as AgCl), which similarly compensate positive and negative charges upon crystallizing. Our results pave the way towards developing well-defined hybrid organic–inorganic nanostructures.","lang":"eng"}],"citation":{"short":"Z. Chu, Y. Han, P. Král, R. Klajn, Angewandte Chemie International Edition 57 (2018) 7023–7027.","chicago":"Chu, Zonglin, Yanxiao Han, Petr Král, and Rafal Klajn. “‘Precipitation on Nanoparticles’: Attractive Intermolecular Interactions Stabilize Specific Ligand Ratios on the Surfaces of Nanoparticles.” <i>Angewandte Chemie International Edition</i>. Wiley, 2018. <a href=\"https://doi.org/10.1002/anie.201800673\">https://doi.org/10.1002/anie.201800673</a>.","ista":"Chu Z, Han Y, Král P, Klajn R. 2018. “Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles. Angewandte Chemie International Edition. 57(24), 7023–7027.","ama":"Chu Z, Han Y, Král P, Klajn R. “Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles. <i>Angewandte Chemie International Edition</i>. 2018;57(24):7023-7027. doi:<a href=\"https://doi.org/10.1002/anie.201800673\">10.1002/anie.201800673</a>","ieee":"Z. Chu, Y. Han, P. Král, and R. Klajn, “‘Precipitation on nanoparticles’: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles,” <i>Angewandte Chemie International Edition</i>, vol. 57, no. 24. Wiley, pp. 7023–7027, 2018.","apa":"Chu, Z., Han, Y., Král, P., &#38; Klajn, R. (2018). “Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles. <i>Angewandte Chemie International Edition</i>. Wiley. <a href=\"https://doi.org/10.1002/anie.201800673\">https://doi.org/10.1002/anie.201800673</a>","mla":"Chu, Zonglin, et al. “‘Precipitation on Nanoparticles’: Attractive Intermolecular Interactions Stabilize Specific Ligand Ratios on the Surfaces of Nanoparticles.” <i>Angewandte Chemie International Edition</i>, vol. 57, no. 24, Wiley, 2018, pp. 7023–27, doi:<a href=\"https://doi.org/10.1002/anie.201800673\">10.1002/anie.201800673</a>."},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1002/anie.201800673"}],"author":[{"first_name":"Zonglin","last_name":"Chu","full_name":"Chu, Zonglin"},{"last_name":"Han","first_name":"Yanxiao","full_name":"Han, Yanxiao"},{"last_name":"Král","first_name":"Petr","full_name":"Král, Petr"},{"first_name":"Rafal","last_name":"Klajn","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"quality_controlled":"1","extern":"1","year":"2018","intvolume":"        57","date_created":"2023-08-01T09:40:16Z","month":"06","status":"public","volume":57,"issue":"24","publisher":"Wiley","article_type":"original","doi":"10.1002/anie.201800673","language":[{"iso":"eng"}],"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","type":"journal_article","date_updated":"2023-08-07T11:14:28Z","oa_version":"Published Version","day":"11","publication_identifier":{"eissn":["1521-3773"],"issn":["1433-7851"]},"scopus_import":"1","date_published":"2018-06-11T00:00:00Z","external_id":{"pmid":["29673022"]},"keyword":["General Chemistry","Catalysis"],"page":"7023-7027"},{"volume":9,"publisher":"Springer Nature","article_type":"original","intvolume":"         9","date_created":"2023-09-06T12:07:33Z","month":"05","article_number":"1806","status":"public","citation":{"mla":"Bräuning, Bastian, et al. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>, vol. 9, 1806, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>.","apa":"Bräuning, B., Bertosin, E., Praetorius, F. M., Ihling, C., Schatt, A., Adler, A., … Groll, M. (2018). Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>","ama":"Bräuning B, Bertosin E, Praetorius FM, et al. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. <i>Nature Communications</i>. 2018;9. doi:<a href=\"https://doi.org/10.1038/s41467-018-04139-2\">10.1038/s41467-018-04139-2</a>","ieee":"B. Bräuning <i>et al.</i>, “Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB,” <i>Nature Communications</i>, vol. 9. Springer Nature, 2018.","ista":"Bräuning B, Bertosin E, Praetorius FM, Ihling C, Schatt A, Adler A, Richter K, Sinz A, Dietz H, Groll M. 2018. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Nature Communications. 9, 1806.","short":"B. Bräuning, E. Bertosin, F.M. Praetorius, C. Ihling, A. Schatt, A. Adler, K. Richter, A. Sinz, H. Dietz, M. Groll, Nature Communications 9 (2018).","chicago":"Bräuning, Bastian, Eva Bertosin, Florian M Praetorius, Christian Ihling, Alexandra Schatt, Agnes Adler, Klaus Richter, Andrea Sinz, Hendrik Dietz, and Michael Groll. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming Toxin YaxAB.” <i>Nature Communications</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41467-018-04139-2\">https://doi.org/10.1038/s41467-018-04139-2</a>."},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-018-04139-2"}],"author":[{"full_name":"Bräuning, Bastian","last_name":"Bräuning","first_name":"Bastian"},{"last_name":"Bertosin","first_name":"Eva","full_name":"Bertosin, Eva"},{"full_name":"Praetorius, Florian M","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62","first_name":"Florian M","last_name":"Praetorius"},{"full_name":"Ihling, Christian","last_name":"Ihling","first_name":"Christian"},{"last_name":"Schatt","first_name":"Alexandra","full_name":"Schatt, Alexandra"},{"last_name":"Adler","first_name":"Agnes","full_name":"Adler, Agnes"},{"last_name":"Richter","first_name":"Klaus","full_name":"Richter, Klaus"},{"full_name":"Sinz, Andrea","first_name":"Andrea","last_name":"Sinz"},{"full_name":"Dietz, Hendrik","first_name":"Hendrik","last_name":"Dietz"},{"last_name":"Groll","first_name":"Michael","full_name":"Groll, Michael"}],"quality_controlled":"1","extern":"1","year":"2018","title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","publication":"Nature Communications","pmid":1,"oa":1,"_id":"14284","publication_status":"published","abstract":[{"lang":"eng","text":"Pore-forming toxins (PFT) are virulence factors that transform from soluble to membrane-bound states. The Yersinia YaxAB system represents a family of binary α-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures. YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the molecular basis for its two-component lytic mechanism remains elusive. Here, we present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy map of the YaxAB complex. Our structures reveal a pore predominantly composed of decamers of YaxA–YaxB heterodimers. Both subunits bear membrane-active moieties, but only YaxA is capable of binding to membranes by itself. YaxB can subsequently be recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices. Pore formation can progress by further oligomerization of YaxA–YaxB dimers. Our results allow for a comparison between pore assemblies belonging to the wider ClyA-like family of α-PFTs, highlighting diverse pore architectures."}],"date_published":"2018-05-04T00:00:00Z","external_id":{"pmid":["29728606"]},"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"publication_identifier":{"issn":["2041-1723"]},"scopus_import":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","type":"journal_article","date_updated":"2023-11-07T11:46:12Z","oa_version":"Published Version","day":"04","language":[{"iso":"eng"}],"doi":"10.1038/s41467-018-04139-2"},{"scopus_import":"1","publication_identifier":{"issn":["1755-4330"],"eissn":["1755-4349"]},"keyword":["general chemical engineering","general chemistry"],"external_id":{"pmid":["29581486"]},"date_published":"2018-03-26T00:00:00Z","page":"523-531","acknowledgement":"We thank B. Jönsson and I. André for helpful discussions. We acknowledge financial support from the Schiff Foundation (S.I.A.C.), St John’s College, Cambridge (S.I.A.C.), the Royal Physiographic Society (R.C.), the Research School FLÄK of Lund University (S.L., R.C.), the Swedish Research Council (S.L.) and its Linneaus Centre Organizing Molecular Matter (S.L.), the Crafoord Foundation (S.L.), Alzheimerfonden (S.L.), the European Research Council (S.L.), NanoLund (S.L.), Knut and Alice Wallenberg Foundation (S.L.), Peterhouse, Cambridge (T.C.T.M.), the Swiss National Science Foundation (T.C.T.M.), Magdalene College, Cambridge (A.K.B.), the Leverhulme Trust (A.K.B.), the Royal Society (A.Š.), the Academy of Medical Sciences (A.Š.), the Wellcome Trust (C.M.D., T.P.J.K., A.Š.), and the Centre for Misfolding Diseases (C.M.D., T.P.J.K, M.V.). A.K.B. thanks the Alzheimer Forschung Initiative (AFI).","doi":"10.1038/s41557-018-0023-x","language":[{"iso":"eng"}],"oa_version":"None","type":"journal_article","date_updated":"2021-11-26T15:14:00Z","day":"26","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","article_processing_charge":"No","month":"03","date_created":"2021-11-26T12:41:38Z","status":"public","intvolume":"        10","publisher":"Springer Nature","article_type":"original","volume":10,"issue":"5","abstract":[{"text":"Mapping free-energy landscapes has proved to be a powerful tool for studying reaction mechanisms. Many complex biomolecular assembly processes, however, have remained challenging to access using this approach, including the aggregation of peptides and proteins into amyloid fibrils implicated in a range of disorders. Here, we generalize the strategy used to probe free-energy landscapes in protein folding to determine the activation energies and entropies that characterize each of the molecular steps in the aggregation of the amyloid-β peptide (Aβ42), which is associated with Alzheimer’s disease. Our results reveal that interactions between monomeric Aβ42 and amyloid fibrils during fibril-dependent secondary nucleation fundamentally reverse the thermodynamic signature of this process relative to primary nucleation, even though both processes generate aggregates from soluble peptides. By mapping the energetic and entropic contributions along the reaction trajectories, we show that the catalytic efficiency of Aβ42 fibril surfaces results from the enthalpic stabilization of adsorbing peptides in conformations amenable to nucleation, resulting in a dramatic lowering of the activation energy for nucleation.","lang":"eng"}],"publication_status":"published","pmid":1,"publication":"Nature Chemistry","title":"Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide","_id":"10360","year":"2018","citation":{"ama":"Cohen SIA, Cukalevski R, Michaels TCT, et al. Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. <i>Nature Chemistry</i>. 2018;10(5):523-531. doi:<a href=\"https://doi.org/10.1038/s41557-018-0023-x\">10.1038/s41557-018-0023-x</a>","ieee":"S. I. A. Cohen <i>et al.</i>, “Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide,” <i>Nature Chemistry</i>, vol. 10, no. 5. Springer Nature, pp. 523–531, 2018.","ista":"Cohen SIA, Cukalevski R, Michaels TCT, Šarić A, Törnquist M, Vendruscolo M, Dobson CM, Buell AK, Knowles TPJ, Linse S. 2018. Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. Nature Chemistry. 10(5), 523–531.","short":"S.I.A. Cohen, R. Cukalevski, T.C.T. Michaels, A. Šarić, M. Törnquist, M. Vendruscolo, C.M. Dobson, A.K. Buell, T.P.J. Knowles, S. Linse, Nature Chemistry 10 (2018) 523–531.","chicago":"Cohen, Samuel I. A., Risto Cukalevski, Thomas C. T. Michaels, Anđela Šarić, Mattias Törnquist, Michele Vendruscolo, Christopher M. Dobson, Alexander K. Buell, Tuomas P. J. Knowles, and Sara Linse. “Distinct Thermodynamic Signatures of Oligomer Generation in the Aggregation of the Amyloid-β Peptide.” <i>Nature Chemistry</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41557-018-0023-x\">https://doi.org/10.1038/s41557-018-0023-x</a>.","mla":"Cohen, Samuel I. A., et al. “Distinct Thermodynamic Signatures of Oligomer Generation in the Aggregation of the Amyloid-β Peptide.” <i>Nature Chemistry</i>, vol. 10, no. 5, Springer Nature, 2018, pp. 523–31, doi:<a href=\"https://doi.org/10.1038/s41557-018-0023-x\">10.1038/s41557-018-0023-x</a>.","apa":"Cohen, S. I. A., Cukalevski, R., Michaels, T. C. T., Šarić, A., Törnquist, M., Vendruscolo, M., … Linse, S. (2018). Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide. <i>Nature Chemistry</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41557-018-0023-x\">https://doi.org/10.1038/s41557-018-0023-x</a>"},"quality_controlled":"1","extern":"1","author":[{"first_name":"Samuel I. A.","last_name":"Cohen","full_name":"Cohen, Samuel I. A."},{"first_name":"Risto","last_name":"Cukalevski","full_name":"Cukalevski, Risto"},{"first_name":"Thomas C. T.","last_name":"Michaels","full_name":"Michaels, Thomas C. T."},{"last_name":"Šarić","first_name":"Anđela","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b"},{"full_name":"Törnquist, Mattias","first_name":"Mattias","last_name":"Törnquist"},{"last_name":"Vendruscolo","first_name":"Michele","full_name":"Vendruscolo, Michele"},{"last_name":"Dobson","first_name":"Christopher M.","full_name":"Dobson, Christopher M."},{"full_name":"Buell, Alexander K.","first_name":"Alexander K.","last_name":"Buell"},{"last_name":"Knowles","first_name":"Tuomas P. J.","full_name":"Knowles, Tuomas P. J."},{"last_name":"Linse","first_name":"Sara","full_name":"Linse, Sara"}]},{"month":"10","date_created":"2020-09-18T10:06:18Z","status":"public","intvolume":"        87","publication_identifier":{"issn":["0926-2040"]},"publisher":"Elsevier","article_type":"original","keyword":["Nuclear and High Energy Physics","Instrumentation","General Chemistry","Radiation"],"date_published":"2017-10-01T00:00:00Z","volume":87,"page":"86-95","issue":"10","abstract":[{"text":"Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region that undergoes microsecond motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation dispersion, to probe how the G53A mutation alters these dynamics. We report a population-inversion of conformational states: the conformation that in the wild-type protein is populated only sparsely becomes the predominant state. We furthermore explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics. We show that while quantitative interpretation of 1H relaxation remains beyond reach under the experimental conditions, due to coherent contributions to decay, one may extract qualitative information about flexibility.","lang":"eng"}],"publication_status":"published","publication":"Solid State Nuclear Magnetic Resonance","title":"Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals","_id":"8447","doi":"10.1016/j.ssnmr.2017.04.002","language":[{"iso":"eng"}],"oa_version":"None","date_updated":"2021-01-12T08:19:20Z","type":"journal_article","year":"2017","day":"01","citation":{"apa":"Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., &#38; Schanda, P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State Nuclear Magnetic Resonance</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>","mla":"Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10, Elsevier, 2017, pp. 86–95, doi:<a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">10.1016/j.ssnmr.2017.04.002</a>.","ieee":"D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda, “Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals,” <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.","ama":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State Nuclear Magnetic Resonance</i>. 2017;87(10):86-95. doi:<a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">10.1016/j.ssnmr.2017.04.002</a>","ista":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. 2017. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 87(10), 86–95.","short":"D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid State Nuclear Magnetic Resonance 87 (2017) 86–95.","chicago":"Gauto, Diego F., Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser, and Paul Schanda. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” <i>Solid State Nuclear Magnetic Resonance</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>."},"author":[{"last_name":"Gauto","first_name":"Diego F.","full_name":"Gauto, Diego F."},{"full_name":"Hessel, Audrey","first_name":"Audrey","last_name":"Hessel"},{"last_name":"Rovó","first_name":"Petra","full_name":"Rovó, Petra"},{"last_name":"Kurauskas","first_name":"Vilius","full_name":"Kurauskas, Vilius"},{"first_name":"Rasmus","last_name":"Linser","full_name":"Linser, Rasmus"},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"}],"article_processing_charge":"No","extern":"1","quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"},{"day":"01","type":"journal_article","date_updated":"2023-08-07T11:19:30Z","oa_version":"None","article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","doi":"10.1021/jacs.7b09111","language":[{"iso":"eng"}],"page":"17973-17978","date_published":"2017-12-01T00:00:00Z","external_id":{"pmid":["29193964"]},"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"scopus_import":"1","year":"2017","author":[{"full_name":"Sawczyk, Michał","first_name":"Michał","last_name":"Sawczyk"},{"full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","first_name":"Rafal","last_name":"Klajn"}],"extern":"1","quality_controlled":"1","citation":{"short":"M. Sawczyk, R. Klajn, Journal of the American Chemical Society 139 (2017) 17973–17978.","chicago":"Sawczyk, Michał, and Rafal Klajn. “Out-of-Equilibrium Aggregates and Coatings during Seeded Growth of Metallic Nanoparticles.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2017. <a href=\"https://doi.org/10.1021/jacs.7b09111\">https://doi.org/10.1021/jacs.7b09111</a>.","ista":"Sawczyk M, Klajn R. 2017. Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. Journal of the American Chemical Society. 139(49), 17973–17978.","ieee":"M. Sawczyk and R. Klajn, “Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles,” <i>Journal of the American Chemical Society</i>, vol. 139, no. 49. American Chemical Society, pp. 17973–17978, 2017.","ama":"Sawczyk M, Klajn R. Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. <i>Journal of the American Chemical Society</i>. 2017;139(49):17973-17978. doi:<a href=\"https://doi.org/10.1021/jacs.7b09111\">10.1021/jacs.7b09111</a>","apa":"Sawczyk, M., &#38; Klajn, R. (2017). Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jacs.7b09111\">https://doi.org/10.1021/jacs.7b09111</a>","mla":"Sawczyk, Michał, and Rafal Klajn. “Out-of-Equilibrium Aggregates and Coatings during Seeded Growth of Metallic Nanoparticles.” <i>Journal of the American Chemical Society</i>, vol. 139, no. 49, American Chemical Society, 2017, pp. 17973–78, doi:<a href=\"https://doi.org/10.1021/jacs.7b09111\">10.1021/jacs.7b09111</a>."},"publication_status":"published","abstract":[{"lang":"eng","text":"Although dissipative self-assembly is ubiquitous in nature, where it gives rise to structures and functions critical to life, examples of artificial systems featuring this mode of self-assembly are rare. Here, we identify the presence of ephemeral assemblies during seeded growth of gold nanoparticles. In this process, hydrazine reduces Au(III) ions, which attach to the existing nanoparticles “seeds”. The attachment is accompanied by a local increase in the concentration of a surfactant, which therefore forms a bilayer on nanoparticle surfaces, inducing their assembly. The resulting aggregates gradually disassemble as the surfactant concentration throughout the solution equilibrates. The lifetimes of the out-of-equilibrium aggregates depend on and can be controlled by the size of the constituent nanoparticles. We demonstrate the utility of our out-of-equilibrium aggregates to form transient reflective coatings on polar surfaces."}],"_id":"13380","publication":"Journal of the American Chemical Society","title":"Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles","pmid":1,"article_type":"original","publisher":"American Chemical Society","issue":"49","volume":139,"status":"public","date_created":"2023-08-01T09:41:01Z","month":"12","intvolume":"       139"},{"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1039/c7cs90088k"}],"citation":{"mla":"van Esch, Jan H., et al. “Chemical Systems out of Equilibrium.” <i>Chemical Society Reviews</i>, vol. 46, no. 18, Royal Society of Chemistry, 2017, pp. 5474–75, doi:<a href=\"https://doi.org/10.1039/c7cs90088k\">10.1039/c7cs90088k</a>.","apa":"van Esch, J. H., Klajn, R., &#38; Otto, S. (2017). Chemical systems out of equilibrium. <i>Chemical Society Reviews</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/c7cs90088k\">https://doi.org/10.1039/c7cs90088k</a>","ieee":"J. H. van Esch, R. Klajn, and S. Otto, “Chemical systems out of equilibrium,” <i>Chemical Society Reviews</i>, vol. 46, no. 18. Royal Society of Chemistry, pp. 5474–5475, 2017.","ama":"van Esch JH, Klajn R, Otto S. Chemical systems out of equilibrium. <i>Chemical Society Reviews</i>. 2017;46(18):5474-5475. doi:<a href=\"https://doi.org/10.1039/c7cs90088k\">10.1039/c7cs90088k</a>","ista":"van Esch JH, Klajn R, Otto S. 2017. Chemical systems out of equilibrium. Chemical Society Reviews. 46(18), 5474–5475.","chicago":"Esch, Jan H. van, Rafal Klajn, and Sijbren Otto. “Chemical Systems out of Equilibrium.” <i>Chemical Society Reviews</i>. Royal Society of Chemistry, 2017. <a href=\"https://doi.org/10.1039/c7cs90088k\">https://doi.org/10.1039/c7cs90088k</a>.","short":"J.H. van Esch, R. Klajn, S. Otto, Chemical Society Reviews 46 (2017) 5474–5475."},"extern":"1","author":[{"full_name":"van Esch, Jan H.","last_name":"van Esch","first_name":"Jan H."},{"full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","first_name":"Rafal","last_name":"Klajn"},{"first_name":"Sijbren","last_name":"Otto","full_name":"Otto, Sijbren"}],"quality_controlled":"1","year":"2017","pmid":1,"publication":"Chemical Society Reviews","title":"Chemical systems out of equilibrium","_id":"13382","oa":1,"publication_status":"published","volume":46,"issue":"18","article_type":"letter_note","publisher":"Royal Society of Chemistry","intvolume":"        46","month":"09","date_created":"2023-08-01T09:41:30Z","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","oa_version":"Published Version","date_updated":"2023-08-07T11:27:42Z","type":"journal_article","day":"08","doi":"10.1039/c7cs90088k","language":[{"iso":"eng"}],"external_id":{"pmid":["28884760"]},"keyword":["General Chemistry"],"date_published":"2017-09-08T00:00:00Z","page":"5474-5475","scopus_import":"1","publication_identifier":{"issn":["0306-0012"],"eissn":["1460-4744"]}},{"date_published":"2017-06-15T00:00:00Z","external_id":{"pmid":["28643771"]},"keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"publication_identifier":{"eissn":["2041-1723"]},"scopus_import":"1","article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"15","type":"journal_article","date_updated":"2023-08-22T08:26:06Z","oa_version":"Published Version","doi":"10.1038/ncomms15651","language":[{"iso":"eng"}],"volume":8,"publisher":"Springer Nature","article_type":"original","intvolume":"         8","article_number":"15651","status":"public","date_created":"2023-08-10T06:36:09Z","month":"06","author":[{"full_name":"Walt, Samuel G.","first_name":"Samuel G.","last_name":"Walt"},{"last_name":"Bhargava Ram","first_name":"Niraghatam","full_name":"Bhargava Ram, Niraghatam"},{"first_name":"Marcos","last_name":"Atala","full_name":"Atala, Marcos"},{"first_name":"Nikolay I","last_name":"Shvetsov-Shilovski","full_name":"Shvetsov-Shilovski, Nikolay I"},{"full_name":"von Conta, Aaron","first_name":"Aaron","last_name":"von Conta"},{"full_name":"Baykusheva, Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530","last_name":"Baykusheva","first_name":"Denitsa Rangelova"},{"full_name":"Lein, Manfred","first_name":"Manfred","last_name":"Lein"},{"full_name":"Wörner, Hans Jakob","last_name":"Wörner","first_name":"Hans Jakob"}],"extern":"1","quality_controlled":"1","citation":{"ama":"Walt SG, Bhargava Ram N, Atala M, et al. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>","ieee":"S. G. Walt <i>et al.</i>, “Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","ista":"Walt SG, Bhargava Ram N, Atala M, Shvetsov-Shilovski NI, von Conta A, Baykusheva DR, Lein M, Wörner HJ. 2017. Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. Nature Communications. 8, 15651.","chicago":"Walt, Samuel G., Niraghatam Bhargava Ram, Marcos Atala, Nikolay I Shvetsov-Shilovski, Aaron von Conta, Denitsa Rangelova Baykusheva, Manfred Lein, and Hans Jakob Wörner. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/ncomms15651\">https://doi.org/10.1038/ncomms15651</a>.","short":"S.G. Walt, N. Bhargava Ram, M. Atala, N.I. Shvetsov-Shilovski, A. von Conta, D.R. Baykusheva, M. Lein, H.J. Wörner, Nature Communications 8 (2017).","mla":"Walt, Samuel G., et al. “Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography and Rescattering.” <i>Nature Communications</i>, vol. 8, 15651, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/ncomms15651\">10.1038/ncomms15651</a>.","apa":"Walt, S. G., Bhargava Ram, N., Atala, M., Shvetsov-Shilovski, N. I., von Conta, A., Baykusheva, D. R., … Wörner, H. J. (2017). Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms15651\">https://doi.org/10.1038/ncomms15651</a>"},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms15651"}],"year":"2017","oa":1,"_id":"14005","publication":"Nature Communications","title":"Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering","pmid":1,"publication_status":"published","abstract":[{"text":"Strong-field photoelectron holography and laser-induced electron diffraction (LIED) are two powerful emerging methods for probing the ultrafast dynamics of molecules. However, both of them have remained restricted to static systems and to nuclear dynamics induced by strong-field ionization. Here we extend these promising methods to image purely electronic valence-shell dynamics in molecules using photoelectron holography. In the same experiment, we use LIED and photoelectron holography simultaneously, to observe coupled electronic-rotational dynamics taking place on similar timescales. These results offer perspectives for imaging ultrafast dynamics of molecules on femtosecond to attosecond timescales.","lang":"eng"}]},{"main_file_link":[{"url":"https://pubs.acs.org/doi/10.1021/acscentsci.7b00392","open_access":"1"}],"citation":{"mla":"Simunovic, Mijo, et al. “Long-Range Organization of Membrane-Curving Proteins.” <i>ACS Central Science</i>, vol. 3, no. 12, American Chemical Society, 2017, pp. 1246–53, doi:<a href=\"https://doi.org/10.1021/acscentsci.7b00392\">10.1021/acscentsci.7b00392</a>.","apa":"Simunovic, M., Šarić, A., Henderson, J. M., Lee, K. Y. C., &#38; Voth, G. A. (2017). Long-range organization of membrane-curving proteins. <i>ACS Central Science</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acscentsci.7b00392\">https://doi.org/10.1021/acscentsci.7b00392</a>","ieee":"M. Simunovic, A. Šarić, J. M. Henderson, K. Y. C. Lee, and G. A. Voth, “Long-range organization of membrane-curving proteins,” <i>ACS Central Science</i>, vol. 3, no. 12. American Chemical Society, pp. 1246–1253, 2017.","ama":"Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. Long-range organization of membrane-curving proteins. <i>ACS Central Science</i>. 2017;3(12):1246-1253. doi:<a href=\"https://doi.org/10.1021/acscentsci.7b00392\">10.1021/acscentsci.7b00392</a>","short":"M. Simunovic, A. Šarić, J.M. Henderson, K.Y.C. Lee, G.A. Voth, ACS Central Science 3 (2017) 1246–1253.","chicago":"Simunovic, Mijo, Anđela Šarić, J. Michael Henderson, Ka Yee C. Lee, and Gregory A. Voth. “Long-Range Organization of Membrane-Curving Proteins.” <i>ACS Central Science</i>. American Chemical Society, 2017. <a href=\"https://doi.org/10.1021/acscentsci.7b00392\">https://doi.org/10.1021/acscentsci.7b00392</a>.","ista":"Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. 2017. Long-range organization of membrane-curving proteins. ACS Central Science. 3(12), 1246–1253."},"author":[{"full_name":"Simunovic, Mijo","last_name":"Simunovic","first_name":"Mijo"},{"last_name":"Šarić","first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139"},{"full_name":"Henderson, J. Michael","last_name":"Henderson","first_name":"J. Michael"},{"full_name":"Lee, Ka Yee C.","first_name":"Ka Yee C.","last_name":"Lee"},{"last_name":"Voth","first_name":"Gregory A.","full_name":"Voth, Gregory A."}],"quality_controlled":"1","extern":"1","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"year":"2017","publication":"ACS Central Science","title":"Long-range organization of membrane-curving proteins","pmid":1,"ddc":["540"],"oa":1,"_id":"10369","publication_status":"published","abstract":[{"lang":"eng","text":"Biological membranes have a central role in mediating the organization of membrane-curving proteins, a dynamic process that has proven to be challenging to probe experimentally. Using atomic force microscopy, we capture the hierarchically organized assemblies of Bin/amphiphysin/Rvs (BAR) proteins on supported lipid membranes. Their structure reveals distinct long linear aggregates of proteins, regularly spaced by up to 300 nm. Employing accurate free-energy calculations from large-scale coarse-grained computer simulations, we found that the membrane mediates the interaction among protein filaments as a combination of short- and long-ranged interactions. The long-ranged component acts at strikingly long distances, giving rise to a variety of micron-sized ordered patterns. This mechanism may contribute to the long-ranged spatiotemporal control of membrane remodeling by proteins in the cell."}],"issue":"12","volume":3,"file_date_updated":"2021-11-29T09:00:40Z","article_type":"original","publisher":"American Chemical Society","intvolume":"         3","date_created":"2021-11-29T08:49:50Z","month":"11","status":"public","article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","type":"journal_article","date_updated":"2021-11-29T09:28:06Z","oa_version":"Published Version","day":"21","doi":"10.1021/acscentsci.7b00392","language":[{"iso":"eng"}],"has_accepted_license":"1","acknowledgement":"M.S. and G.A.V. acknowledge their research reported in this publication as being supported by the National Institute of General Medical Sciences of the National Institutes of Health under Award Number R01-GM063796. Computational resources were provided to M.S. and G.A.V. by the National Science Foundation through XSEDE (Grant TG-MCA94P017, supercomputers Stampede and Gordon), and also by the Blue Waters computing project at the National Center for Supercomputing Applications (University of Illinois at Urbana–Champaign, NSF Awards OCI-0725070 and ACI-1238993). A.Š. acknowledges support from the Human Frontier Science Program and Royal Society. J.M.H. and K.Y.C.L. acknowledge the support from the National Science Foundation (Grant MCB-1413613) and the NSF-supported MRSEC program at the University of Chicago (Grant DMR-1420709). We are grateful to Carsten Mim and Vinzenz Unger of Northwestern University for generously providing us with the protein. We thank all the members of the Voth group for fruitful discussions, especially John M. A. Grime.","date_published":"2017-11-21T00:00:00Z","keyword":["general chemical engineering","general chemistry"],"file":[{"date_created":"2021-11-29T09:00:40Z","relation":"main_file","creator":"cchlebak","content_type":"application/pdf","file_size":2635263,"file_id":"10371","date_updated":"2021-11-29T09:00:40Z","success":1,"access_level":"open_access","checksum":"1cf3e5e5342f2d728f47560acc3ec560","file_name":"2017_ACSCentSci_Simunovic.pdf"}],"external_id":{"pmid":["29296664"]},"page":"1246-1253","publication_identifier":{"eissn":["2374-7951"],"issn":["2374-7943"]},"scopus_import":"1"},{"intvolume":"         8","status":"public","month":"08","date_created":"2021-11-29T09:29:31Z","volume":8,"issue":"10","article_type":"original","publisher":"Royal Society of Chemistry","_id":"10374","ddc":["540"],"oa":1,"pmid":1,"publication":"Chemical Science","title":"Scaling behaviour and rate-determining steps in filamentous self-assembly","abstract":[{"lang":"eng","text":"The formation of filaments from naturally occurring protein molecules is a process at the core of a range of functional and aberrant biological phenomena, such as the assembly of the cytoskeleton or the appearance of aggregates in Alzheimer's disease. The macroscopic behaviour associated with such processes is remarkably diverse, ranging from simple nucleated growth to highly cooperative processes with a well-defined lagtime. Thus, conventionally, different molecular mechanisms have been used to explain the self-assembly of different proteins. Here we show that this range of behaviour can be quantitatively captured by a single unifying Petri net that describes filamentous growth in terms of aggregate number and aggregate mass concentrations. By considering general features associated with a particular network connectivity, we are able to establish directly the rate-determining steps of the overall aggregation reaction from the system's scaling behaviour. We illustrate the power of this framework on a range of different experimental and simulated aggregating systems. The approach is general and will be applicable to any future extensions of the reaction network of filamentous self-assembly."}],"publication_status":"published","quality_controlled":"1","author":[{"full_name":"Meisl, Georg","first_name":"Georg","last_name":"Meisl"},{"first_name":"Luke","last_name":"Rajah","full_name":"Rajah, Luke"},{"first_name":"Samuel A. I.","last_name":"Cohen","full_name":"Cohen, Samuel A. I."},{"last_name":"Pfammatter","first_name":"Manuela","full_name":"Pfammatter, Manuela"},{"first_name":"Anđela","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139"},{"full_name":"Hellstrand, Erik","last_name":"Hellstrand","first_name":"Erik"},{"first_name":"Alexander K.","last_name":"Buell","full_name":"Buell, Alexander K."},{"first_name":"Adriano","last_name":"Aguzzi","full_name":"Aguzzi, Adriano"},{"last_name":"Linse","first_name":"Sara","full_name":"Linse, Sara"},{"full_name":"Vendruscolo, Michele","first_name":"Michele","last_name":"Vendruscolo"},{"first_name":"Christopher M.","last_name":"Dobson","full_name":"Dobson, Christopher M."},{"full_name":"Knowles, Tuomas P. J.","first_name":"Tuomas P. J.","last_name":"Knowles"}],"extern":"1","citation":{"mla":"Meisl, Georg, et al. “Scaling Behaviour and Rate-Determining Steps in Filamentous Self-Assembly.” <i>Chemical Science</i>, vol. 8, no. 10, Royal Society of Chemistry, 2017, pp. 7087–97, doi:<a href=\"https://doi.org/10.1039/c7sc01965c\">10.1039/c7sc01965c</a>.","apa":"Meisl, G., Rajah, L., Cohen, S. A. I., Pfammatter, M., Šarić, A., Hellstrand, E., … Knowles, T. P. J. (2017). Scaling behaviour and rate-determining steps in filamentous self-assembly. <i>Chemical Science</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/c7sc01965c\">https://doi.org/10.1039/c7sc01965c</a>","chicago":"Meisl, Georg, Luke Rajah, Samuel A. I. Cohen, Manuela Pfammatter, Anđela Šarić, Erik Hellstrand, Alexander K. Buell, et al. “Scaling Behaviour and Rate-Determining Steps in Filamentous Self-Assembly.” <i>Chemical Science</i>. Royal Society of Chemistry, 2017. <a href=\"https://doi.org/10.1039/c7sc01965c\">https://doi.org/10.1039/c7sc01965c</a>.","short":"G. Meisl, L. Rajah, S.A.I. Cohen, M. Pfammatter, A. Šarić, E. Hellstrand, A.K. Buell, A. Aguzzi, S. Linse, M. Vendruscolo, C.M. Dobson, T.P.J. Knowles, Chemical Science 8 (2017) 7087–7097.","ista":"Meisl G, Rajah L, Cohen SAI, Pfammatter M, Šarić A, Hellstrand E, Buell AK, Aguzzi A, Linse S, Vendruscolo M, Dobson CM, Knowles TPJ. 2017. Scaling behaviour and rate-determining steps in filamentous self-assembly. Chemical Science. 8(10), 7087–7097.","ama":"Meisl G, Rajah L, Cohen SAI, et al. Scaling behaviour and rate-determining steps in filamentous self-assembly. <i>Chemical Science</i>. 2017;8(10):7087-7097. doi:<a href=\"https://doi.org/10.1039/c7sc01965c\">10.1039/c7sc01965c</a>","ieee":"G. Meisl <i>et al.</i>, “Scaling behaviour and rate-determining steps in filamentous self-assembly,” <i>Chemical Science</i>, vol. 8, no. 10. Royal Society of Chemistry, pp. 7087–7097, 2017."},"main_file_link":[{"url":"https://pubs.rsc.org/en/content/articlelanding/2017/SC/C7SC01965C","open_access":"1"}],"year":"2017","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc/3.0/legalcode","short":"CC BY-NC (3.0)","name":"Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)","image":"/images/cc_by_nc.png"},"scopus_import":"1","publication_identifier":{"eissn":["2041-6539"],"issn":["2041-6520"]},"page":"7087-7097","keyword":["general chemistry"],"external_id":{"pmid":["29147538"]},"date_published":"2017-08-31T00:00:00Z","doi":"10.1039/c7sc01965c","license":"https://creativecommons.org/licenses/by-nc/3.0/","language":[{"iso":"eng"}],"acknowledgement":"The research leading to these results has received funding from the European Research Council under the European Union's Seventh Framework Programme (FP7/2007-2013) through the ERC grant PhysProt (agreement no. 337969) (SL, TPJK), Sidney Sussex College Cambridge (GM), the Frances and Augusta Newman Foundation (TPJK), the Biotechnology and Biological Science Research Council (TPJK), the Swedish Research Council (SL), the Academy of Medical Sciences (AŠ), Wellcome Trust (AŠ), and the Cambridge Centre for Misfolding Diseases (CMD, TPJK, MV).","article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","day":"31","oa_version":"Published Version","type":"journal_article","date_updated":"2021-11-29T10:00:00Z"},{"volume":13,"issue":"28","publisher":"Royal Society of Chemistry","article_type":"original","intvolume":"        13","month":"06","date_created":"2021-11-29T10:00:39Z","status":"public","citation":{"ieee":"A. Vahid, A. Šarić, and T. Idema, “Curvature variation controls particle aggregation on fluid vesicles,” <i>Soft Matter</i>, vol. 13, no. 28. Royal Society of Chemistry, pp. 4924–4930, 2017.","ama":"Vahid A, Šarić A, Idema T. Curvature variation controls particle aggregation on fluid vesicles. <i>Soft Matter</i>. 2017;13(28):4924-4930. doi:<a href=\"https://doi.org/10.1039/c7sm00433h\">10.1039/c7sm00433h</a>","ista":"Vahid A, Šarić A, Idema T. 2017. Curvature variation controls particle aggregation on fluid vesicles. Soft Matter. 13(28), 4924–4930.","short":"A. Vahid, A. Šarić, T. Idema, Soft Matter 13 (2017) 4924–4930.","chicago":"Vahid, Afshin, Anđela Šarić, and Timon Idema. “Curvature Variation Controls Particle Aggregation on Fluid Vesicles.” <i>Soft Matter</i>. Royal Society of Chemistry, 2017. <a href=\"https://doi.org/10.1039/c7sm00433h\">https://doi.org/10.1039/c7sm00433h</a>.","apa":"Vahid, A., Šarić, A., &#38; Idema, T. (2017). Curvature variation controls particle aggregation on fluid vesicles. <i>Soft Matter</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/c7sm00433h\">https://doi.org/10.1039/c7sm00433h</a>","mla":"Vahid, Afshin, et al. “Curvature Variation Controls Particle Aggregation on Fluid Vesicles.” <i>Soft Matter</i>, vol. 13, no. 28, Royal Society of Chemistry, 2017, pp. 4924–30, doi:<a href=\"https://doi.org/10.1039/c7sm00433h\">10.1039/c7sm00433h</a>."},"main_file_link":[{"url":"https://pubs.rsc.org/en/content/articlelanding/2017/SM/C7SM00433H","open_access":"1"}],"extern":"1","author":[{"full_name":"Vahid, Afshin","first_name":"Afshin","last_name":"Vahid"},{"first_name":"Anđela","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela"},{"first_name":"Timon","last_name":"Idema","full_name":"Idema, Timon"}],"quality_controlled":"1","tmp":{"short":"CC BY (3.0)","legal_code_url":"https://creativecommons.org/licenses/by/3.0/legalcode","name":"Creative Commons Attribution 3.0 Unported (CC BY 3.0)","image":"/images/cc_by.png"},"year":"2017","pmid":1,"title":"Curvature variation controls particle aggregation on fluid vesicles","publication":"Soft Matter","_id":"10375","oa":1,"abstract":[{"text":"Cellular membranes exhibit a large variety of shapes, strongly coupled to their function. Many biological processes involve dynamic reshaping of membranes, usually mediated by proteins. This interaction works both ways: while proteins influence the membrane shape, the membrane shape affects the interactions between the proteins. To study these membrane-mediated interactions on closed and anisotropically curved membranes, we use colloids adhered to ellipsoidal membrane vesicles as a model system. We find that two particles on a closed system always attract each other, and tend to align with the direction of largest curvature. Multiple particles form arcs, or, at large enough numbers, a complete ring surrounding the vesicle in its equatorial plane. The resulting vesicle shape resembles a snowman. Our results indicate that these physical interactions on membranes with anisotropic shapes can be exploited by cells to drive macromolecules to preferred regions of cellular or intracellular membranes, and utilized to initiate dynamic processes such as cell division. The same principle could be used to find the midplane of an artificial vesicle, as a first step towards dividing it into two equal parts.","lang":"eng"}],"publication_status":"published","keyword":["condensed matter physics","general chemistry"],"external_id":{"arxiv":["1703.00776"],"pmid":["28677712"]},"date_published":"2017-06-15T00:00:00Z","page":"4924-4930","scopus_import":"1","publication_identifier":{"issn":["1744-683X"],"eissn":["1744-6848"]},"arxiv":1,"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","article_processing_charge":"No","oa_version":"Published Version","type":"journal_article","date_updated":"2021-11-29T10:33:36Z","day":"15","doi":"10.1039/c7sm00433h","language":[{"iso":"eng"}],"acknowledgement":"This work was supported by the Netherlands Organisation for Scientific Research (NWO/OCW), as part of the Frontiers of Nanoscience program."},{"status":"public","article_number":"328","date_created":"2022-04-07T07:45:50Z","month":"08","intvolume":"         8","article_type":"original","publisher":"Springer Nature","volume":8,"publication_status":"published","abstract":[{"text":"Premature aging disorders provide an opportunity to study the mechanisms that drive aging. In Hutchinson-Gilford progeria syndrome (HGPS), a mutant form of the nuclear scaffold protein lamin A distorts nuclei and sequesters nuclear proteins. We sought to investigate protein homeostasis in this disease. Here, we report a widespread increase in protein turnover in HGPS-derived cells compared to normal cells. We determine that global protein synthesis is elevated as a consequence of activated nucleoli and enhanced ribosome biogenesis in HGPS-derived fibroblasts. Depleting normal lamin A or inducing mutant lamin A expression are each sufficient to drive nucleolar expansion. We further show that nucleolar size correlates with donor age in primary fibroblasts derived from healthy individuals and that ribosomal RNA production increases with age, indicating that nucleolar size and activity can serve as aging biomarkers. While limiting ribosome biogenesis extends lifespan in several systems, we show that increased ribosome biogenesis and activity are a hallmark of premature aging.","lang":"eng"}],"oa":1,"_id":"11065","publication":"Nature Communications","title":"Nucleolar expansion and elevated protein translation in premature aging","pmid":1,"year":"2017","quality_controlled":"1","extern":"1","author":[{"full_name":"Buchwalter, Abigail","last_name":"Buchwalter","first_name":"Abigail"},{"id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","first_name":"Martin W","last_name":"HETZER"}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-017-00322-z"}],"citation":{"apa":"Buchwalter, A., &#38; Hetzer, M. (2017). Nucleolar expansion and elevated protein translation in premature aging. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>","mla":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>, vol. 8, 328, Springer Nature, 2017, doi:<a href=\"https://doi.org/10.1038/s41467-017-00322-z\">10.1038/s41467-017-00322-z</a>.","ieee":"A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","ama":"Buchwalter A, Hetzer M. Nucleolar expansion and elevated protein translation in premature aging. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/s41467-017-00322-z\">10.1038/s41467-017-00322-z</a>","ista":"Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328.","chicago":"Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein Translation in Premature Aging.” <i>Nature Communications</i>. Springer Nature, 2017. <a href=\"https://doi.org/10.1038/s41467-017-00322-z\">https://doi.org/10.1038/s41467-017-00322-z</a>.","short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (2017)."},"publication_identifier":{"issn":["2041-1723"]},"scopus_import":"1","date_published":"2017-08-30T00:00:00Z","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"external_id":{"pmid":["28855503"]},"doi":"10.1038/s41467-017-00322-z","language":[{"iso":"eng"}],"day":"30","date_updated":"2022-07-18T08:33:03Z","type":"journal_article","oa_version":"Published Version","article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd"},{"quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"full_name":"Kurauskas, Vilius","last_name":"Kurauskas","first_name":"Vilius"},{"full_name":"Crublet, Elodie","last_name":"Crublet","first_name":"Elodie"},{"full_name":"Macek, Pavel","last_name":"Macek","first_name":"Pavel"},{"full_name":"Kerfah, Rime","last_name":"Kerfah","first_name":"Rime"},{"first_name":"Diego F.","last_name":"Gauto","full_name":"Gauto, Diego F."},{"last_name":"Boisbouvier","first_name":"Jérôme","full_name":"Boisbouvier, Jérôme"},{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"extern":"1","article_processing_charge":"No","citation":{"ama":"Kurauskas V, Crublet E, Macek P, et al. Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. <i>Chemical Communications</i>. 2016;52(61):9558-9561. doi:<a href=\"https://doi.org/10.1039/c6cc04484k\">10.1039/c6cc04484k</a>","ieee":"V. Kurauskas <i>et al.</i>, “Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit,” <i>Chemical Communications</i>, vol. 52, no. 61. Royal Society of Chemistry, pp. 9558–9561, 2016.","chicago":"Kurauskas, Vilius, Elodie Crublet, Pavel Macek, Rime Kerfah, Diego F. Gauto, Jérôme Boisbouvier, and Paul Schanda. “Sensitive Proton-Detected Solid-State NMR Spectroscopy of Large Proteins with Selective CH3labelling: Application to the 50S Ribosome Subunit.” <i>Chemical Communications</i>. Royal Society of Chemistry, 2016. <a href=\"https://doi.org/10.1039/c6cc04484k\">https://doi.org/10.1039/c6cc04484k</a>.","short":"V. Kurauskas, E. Crublet, P. Macek, R. Kerfah, D.F. Gauto, J. Boisbouvier, P. Schanda, Chemical Communications 52 (2016) 9558–9561.","ista":"Kurauskas V, Crublet E, Macek P, Kerfah R, Gauto DF, Boisbouvier J, Schanda P. 2016. Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. Chemical Communications. 52(61), 9558–9561.","mla":"Kurauskas, Vilius, et al. “Sensitive Proton-Detected Solid-State NMR Spectroscopy of Large Proteins with Selective CH3labelling: Application to the 50S Ribosome Subunit.” <i>Chemical Communications</i>, vol. 52, no. 61, Royal Society of Chemistry, 2016, pp. 9558–61, doi:<a href=\"https://doi.org/10.1039/c6cc04484k\">10.1039/c6cc04484k</a>.","apa":"Kurauskas, V., Crublet, E., Macek, P., Kerfah, R., Gauto, D. F., Boisbouvier, J., &#38; Schanda, P. (2016). Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit. <i>Chemical Communications</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/c6cc04484k\">https://doi.org/10.1039/c6cc04484k</a>"},"year":"2016","day":"04","oa_version":"None","type":"journal_article","date_updated":"2021-01-12T08:19:23Z","_id":"8455","language":[{"iso":"eng"}],"doi":"10.1039/c6cc04484k","title":"Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit","publication":"Chemical Communications","abstract":[{"text":"Solid-state NMR spectroscopy allows the characterization of the structure, interactions and dynamics of insoluble and/or very large proteins. Sensitivity and resolution are often major challenges for obtaining atomic-resolution information, in particular for very large protein complexes. Here we show that the use of deuterated, specifically CH3-labelled proteins result in significant sensitivity gains compared to previously employed CHD2 labelling, while line widths increase only marginally. We apply this labelling strategy to a 468 kDa-large dodecameric aminopeptidase, TET2, and the 1.6 MDa-large 50S ribosome subunit of Thermus thermophilus.","lang":"eng"}],"publication_status":"published","volume":52,"issue":"61","page":"9558-9561","keyword":["Materials Chemistry","Electronic","Optical and Magnetic Materials","General Chemistry","Surfaces","Coatings and Films","Metals and Alloys","Ceramics and Composites","Catalysis"],"date_published":"2016-07-04T00:00:00Z","article_type":"original","publisher":"Royal Society of Chemistry","publication_identifier":{"issn":["1359-7345","1364-548X"]},"intvolume":"        52","status":"public","month":"07","date_created":"2020-09-18T10:07:29Z"},{"day":"06","oa_version":"Published Version","date_updated":"2023-02-23T13:46:55Z","type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","has_accepted_license":"1","language":[{"iso":"eng"}],"doi":"10.1016/j.crci.2015.12.004","page":"19-27","keyword":["General Chemistry","General Chemical Engineering"],"file":[{"content_type":"application/pdf","creator":"dernst","file_size":2045260,"relation":"main_file","date_created":"2021-01-22T12:36:52Z","file_name":"2016_ComptesRendueChimie_Bakail.pdf","checksum":"c262814ffdbfe95900256ab9ff42cdf5","access_level":"open_access","success":1,"date_updated":"2021-01-22T12:36:52Z","file_id":"9035"}],"date_published":"2016-02-06T00:00:00Z","publication_identifier":{"issn":["1631-0748"]},"year":"2016","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","image":"/images/cc_by_nc_nd.png"},"extern":"1","author":[{"last_name":"Bakail","first_name":"May M","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E","full_name":"Bakail, May M","orcid":"0000-0002-9592-1587"},{"last_name":"Ochsenbein","first_name":"Francoise","full_name":"Ochsenbein, Francoise"}],"quality_controlled":"1","citation":{"apa":"Bakail, M. M., &#38; Ochsenbein, F. (2016). Targeting protein–protein interactions, a wide open field for drug design. <i>Comptes Rendus Chimie</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.crci.2015.12.004\">https://doi.org/10.1016/j.crci.2015.12.004</a>","mla":"Bakail, May M., and Francoise Ochsenbein. “Targeting Protein–Protein Interactions, a Wide Open Field for Drug Design.” <i>Comptes Rendus Chimie</i>, vol. 19, no. 1–2, Elsevier, 2016, pp. 19–27, doi:<a href=\"https://doi.org/10.1016/j.crci.2015.12.004\">10.1016/j.crci.2015.12.004</a>.","ieee":"M. M. Bakail and F. Ochsenbein, “Targeting protein–protein interactions, a wide open field for drug design,” <i>Comptes Rendus Chimie</i>, vol. 19, no. 1–2. Elsevier, pp. 19–27, 2016.","ama":"Bakail MM, Ochsenbein F. Targeting protein–protein interactions, a wide open field for drug design. <i>Comptes Rendus Chimie</i>. 2016;19(1-2):19-27. doi:<a href=\"https://doi.org/10.1016/j.crci.2015.12.004\">10.1016/j.crci.2015.12.004</a>","ista":"Bakail MM, Ochsenbein F. 2016. Targeting protein–protein interactions, a wide open field for drug design. Comptes Rendus Chimie. 19(1–2), 19–27.","short":"M.M. Bakail, F. Ochsenbein, Comptes Rendus Chimie 19 (2016) 19–27.","chicago":"Bakail, May M, and Francoise Ochsenbein. “Targeting Protein–Protein Interactions, a Wide Open Field for Drug Design.” <i>Comptes Rendus Chimie</i>. Elsevier, 2016. <a href=\"https://doi.org/10.1016/j.crci.2015.12.004\">https://doi.org/10.1016/j.crci.2015.12.004</a>."},"abstract":[{"lang":"eng","text":"Targeting protein–protein interactions has long been considered as a very difficult if impossible task, but over the past decade, front lines have moved. The number of successful examples is exponentially growing. This review presents a rapid overview of recent advances in this field considering the strengths and weaknesses of the small molecule approaches and alternative strategies such as the selection or design of artificial antibodies, peptides or peptidomimetics."},{"text":"Cibler les interactions protéine–protéine a longtemps été considéré comme une tâche très difficile, voire impossible, mais, depuis les dix dernières années, les lignes ont bougé. Le nombre d’exemples de réussites s’accroît exponentiellement. Cette revue présente un rapide panorama des avancées récentes dans ce domaine, considérant les forces et les faiblesses de l’approche « petite molécule » ainsi que des stratégies alternatives comme la sélection ou le design d’anticorps artificiels, de peptides ou de peptidomimétiques.","lang":"fre"}],"publication_status":"published","_id":"9019","ddc":["570"],"oa":1,"publication":"Comptes Rendus Chimie","title":"Targeting protein–protein interactions, a wide open field for drug design","article_type":"original","publisher":"Elsevier","file_date_updated":"2021-01-22T12:36:52Z","issue":"1-2","volume":19,"status":"public","month":"02","date_created":"2021-01-19T11:11:54Z","intvolume":"        19"},{"language":[{"iso":"eng"}],"doi":"10.1039/c6sm01163b","day":"14","oa_version":"Preprint","type":"journal_article","date_updated":"2023-02-23T13:47:40Z","user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","article_processing_charge":"No","arxiv":1,"scopus_import":"1","publication_identifier":{"eissn":["1744-6848"],"issn":["1744-683X"]},"page":"6357-6364","keyword":["General Chemistry","Condensed Matter Physics"],"external_id":{"pmid":["27338294"],"arxiv":["1609.01497"]},"date_published":"2016-08-14T00:00:00Z","abstract":[{"text":"We describe colloidal Janus particles with metallic and dielectric faces that swim vigorously when illuminated by defocused optical tweezers without consuming any chemical fuel. Rather than wandering randomly, these optically-activated colloidal swimmers circulate back and forth through the beam of light, tracing out sinuous rosette patterns. We propose a model for this mode of light-activated transport that accounts for the observed behavior through a combination of self-thermophoresis and optically-induced torque. In the deterministic limit, this model yields trajectories that resemble rosette curves known as hypotrochoids.","lang":"eng"}],"publication_status":"published","_id":"9052","oa":1,"pmid":1,"publication":"Soft Matter","title":"Trochoidal trajectories of self-propelled Janus particles in a diverging laser beam","year":"2016","author":[{"first_name":"Henrique","last_name":"Moyses","full_name":"Moyses, Henrique"},{"last_name":"Palacci","first_name":"Jérémie A","orcid":"0000-0002-7253-9465","full_name":"Palacci, Jérémie A","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d"},{"last_name":"Sacanna","first_name":"Stefano","full_name":"Sacanna, Stefano"},{"full_name":"Grier, David G.","first_name":"David G.","last_name":"Grier"}],"quality_controlled":"1","extern":"1","citation":{"mla":"Moyses, Henrique, et al. “Trochoidal Trajectories of Self-Propelled Janus Particles in a Diverging Laser Beam.” <i>Soft Matter</i>, vol. 12, no. 30, Royal Society of Chemistry , 2016, pp. 6357–64, doi:<a href=\"https://doi.org/10.1039/c6sm01163b\">10.1039/c6sm01163b</a>.","apa":"Moyses, H., Palacci, J. A., Sacanna, S., &#38; Grier, D. G. (2016). Trochoidal trajectories of self-propelled Janus particles in a diverging laser beam. <i>Soft Matter</i>. Royal Society of Chemistry . <a href=\"https://doi.org/10.1039/c6sm01163b\">https://doi.org/10.1039/c6sm01163b</a>","ieee":"H. Moyses, J. A. Palacci, S. Sacanna, and D. G. Grier, “Trochoidal trajectories of self-propelled Janus particles in a diverging laser beam,” <i>Soft Matter</i>, vol. 12, no. 30. Royal Society of Chemistry , pp. 6357–6364, 2016.","ama":"Moyses H, Palacci JA, Sacanna S, Grier DG. Trochoidal trajectories of self-propelled Janus particles in a diverging laser beam. <i>Soft Matter</i>. 2016;12(30):6357-6364. doi:<a href=\"https://doi.org/10.1039/c6sm01163b\">10.1039/c6sm01163b</a>","ista":"Moyses H, Palacci JA, Sacanna S, Grier DG. 2016. Trochoidal trajectories of self-propelled Janus particles in a diverging laser beam. Soft Matter. 12(30), 6357–6364.","chicago":"Moyses, Henrique, Jérémie A Palacci, Stefano Sacanna, and David G. Grier. “Trochoidal Trajectories of Self-Propelled Janus Particles in a Diverging Laser Beam.” <i>Soft Matter</i>. Royal Society of Chemistry , 2016. <a href=\"https://doi.org/10.1039/c6sm01163b\">https://doi.org/10.1039/c6sm01163b</a>.","short":"H. Moyses, J.A. Palacci, S. Sacanna, D.G. Grier, Soft Matter 12 (2016) 6357–6364."},"main_file_link":[{"url":"https://arxiv.org/abs/1609.01497","open_access":"1"}],"status":"public","month":"08","date_created":"2021-02-01T13:44:15Z","intvolume":"        12","article_type":"original","publisher":"Royal Society of Chemistry ","issue":"30","volume":12},{"extern":"1","quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","author":[{"first_name":"Rafal","last_name":"Klajn","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"citation":{"ista":"Klajn R. 2016. Borrowing titania’s photoinduced electrons for molecular switching. Science China Chemistry. 59(4), 420–421.","short":"R. Klajn, Science China Chemistry 59 (2016) 420–421.","chicago":"Klajn, Rafal. “Borrowing Titania’s Photoinduced Electrons for Molecular Switching.” <i>Science China Chemistry</i>. Springer Nature, 2016. <a href=\"https://doi.org/10.1007/s11426-016-5573-4\">https://doi.org/10.1007/s11426-016-5573-4</a>.","ieee":"R. Klajn, “Borrowing titania’s photoinduced electrons for molecular switching,” <i>Science China Chemistry</i>, vol. 59, no. 4. Springer Nature, pp. 420–421, 2016.","ama":"Klajn R. Borrowing titania’s photoinduced electrons for molecular switching. <i>Science China Chemistry</i>. 2016;59(4):420-421. doi:<a href=\"https://doi.org/10.1007/s11426-016-5573-4\">10.1007/s11426-016-5573-4</a>","mla":"Klajn, Rafal. “Borrowing Titania’s Photoinduced Electrons for Molecular Switching.” <i>Science China Chemistry</i>, vol. 59, no. 4, Springer Nature, 2016, pp. 420–21, doi:<a href=\"https://doi.org/10.1007/s11426-016-5573-4\">10.1007/s11426-016-5573-4</a>.","apa":"Klajn, R. (2016). Borrowing titania’s photoinduced electrons for molecular switching. <i>Science China Chemistry</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s11426-016-5573-4\">https://doi.org/10.1007/s11426-016-5573-4</a>"},"year":"2016","day":"08","oa_version":"None","date_updated":"2023-08-07T12:49:01Z","type":"journal_article","_id":"13390","doi":"10.1007/s11426-016-5573-4","language":[{"iso":"eng"}],"publication":"Science China Chemistry","title":"Borrowing titania’s photoinduced electrons for molecular switching","publication_status":"published","page":"420-421","volume":59,"issue":"4","keyword":["General Chemistry"],"date_published":"2016-03-08T00:00:00Z","article_type":"original","publisher":"Springer Nature","scopus_import":"1","publication_identifier":{"eissn":["1869-1870"],"issn":["1674-7291"]},"intvolume":"        59","status":"public","month":"03","date_created":"2023-08-01T09:43:33Z"},{"doi":"10.1002/cplu.201500417","language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","day":"01","oa_version":"None","date_updated":"2023-08-07T12:51:56Z","type":"journal_article","scopus_import":"1","publication_identifier":{"eissn":["2192-6506"]},"page":"44-48","external_id":{"pmid":["31968727"]},"keyword":["General Chemistry"],"date_published":"2016-01-01T00:00:00Z","_id":"13391","pmid":1,"publication":"ChemPlusChem","title":"Noncovalent interactions with proteins modify the physicochemical properties of a molecular switch","abstract":[{"text":"It is reported that spiropyran—a widely investigated molecular photoswitch—can be stabilized in aqueous environments in the presence of a variety of proteins, including human serum albumin, insulin fibrils, lysozyme, and glucose oxidase. The optical properties of the complexed photoswitch are protein dependent, with human serum albumin providing the spiropyran with emission features previously observed for a photoswitch confined in media of high viscosity. Despite being bound to the protein molecules, spiropyran can undergo a ring-opening reaction upon exposure to UV light. This photoisomerization process can affect the properties of the proteins: here, it is shown that the electrical conduction through human serum albumin to which the spiropyran is bound increases following the ring-opening reaction.","lang":"eng"}],"publication_status":"published","extern":"1","author":[{"full_name":"Amdursky, Nadav","first_name":"Nadav","last_name":"Amdursky"},{"last_name":"Kundu","first_name":"Pintu K.","full_name":"Kundu, Pintu K."},{"first_name":"Johannes","last_name":"Ahrens","full_name":"Ahrens, Johannes"},{"full_name":"Huppert, Dan","last_name":"Huppert","first_name":"Dan"},{"last_name":"Klajn","first_name":"Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal"}],"quality_controlled":"1","citation":{"chicago":"Amdursky, Nadav, Pintu K. Kundu, Johannes Ahrens, Dan Huppert, and Rafal Klajn. “Noncovalent Interactions with Proteins Modify the Physicochemical Properties of a Molecular Switch.” <i>ChemPlusChem</i>. Wiley, 2016. <a href=\"https://doi.org/10.1002/cplu.201500417\">https://doi.org/10.1002/cplu.201500417</a>.","short":"N. Amdursky, P.K. Kundu, J. Ahrens, D. Huppert, R. Klajn, ChemPlusChem 81 (2016) 44–48.","ista":"Amdursky N, Kundu PK, Ahrens J, Huppert D, Klajn R. 2016. Noncovalent interactions with proteins modify the physicochemical properties of a molecular switch. ChemPlusChem. 81(1), 44–48.","ama":"Amdursky N, Kundu PK, Ahrens J, Huppert D, Klajn R. Noncovalent interactions with proteins modify the physicochemical properties of a molecular switch. <i>ChemPlusChem</i>. 2016;81(1):44-48. doi:<a href=\"https://doi.org/10.1002/cplu.201500417\">10.1002/cplu.201500417</a>","ieee":"N. Amdursky, P. K. Kundu, J. Ahrens, D. Huppert, and R. Klajn, “Noncovalent interactions with proteins modify the physicochemical properties of a molecular switch,” <i>ChemPlusChem</i>, vol. 81, no. 1. Wiley, pp. 44–48, 2016.","mla":"Amdursky, Nadav, et al. “Noncovalent Interactions with Proteins Modify the Physicochemical Properties of a Molecular Switch.” <i>ChemPlusChem</i>, vol. 81, no. 1, Wiley, 2016, pp. 44–48, doi:<a href=\"https://doi.org/10.1002/cplu.201500417\">10.1002/cplu.201500417</a>.","apa":"Amdursky, N., Kundu, P. K., Ahrens, J., Huppert, D., &#38; Klajn, R. (2016). Noncovalent interactions with proteins modify the physicochemical properties of a molecular switch. <i>ChemPlusChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cplu.201500417\">https://doi.org/10.1002/cplu.201500417</a>"},"year":"2016","intvolume":"        81","status":"public","month":"01","date_created":"2023-08-01T09:43:46Z","volume":81,"issue":"1","publisher":"Wiley","article_type":"original"},{"month":"08","date_created":"2021-11-29T11:09:55Z","status":"public","intvolume":"        12","publisher":"Royal Society of Chemistry","article_type":"original","issue":"37","volume":12,"abstract":[{"text":"We study phase behaviour of lipid-bilayer vesicles functionalised by ligand–receptor complexes made of synthetic DNA by introducing a modelling framework and a dedicated experimental platform. In particular, we perform Monte Carlo simulations that combine a coarse grained description of the lipid bilayer with state of art analytical models for multivalent ligand–receptor interactions. Using density of state calculations, we derive the partition function in pairs of vesicles and compute the number of ligand–receptor bonds as a function of temperature. Numerical results are compared to microscopy and fluorimetry experiments on large unilamellar vesicles decorated by DNA linkers carrying complementary overhangs. We find that vesicle aggregation is suppressed when the total number of linkers falls below a threshold value. Within the model proposed here, this is due to the higher configurational costs required to form inter-vesicle bridges as compared to intra-vesicle loops, which are in turn related to membrane deformability. Our findings and our numerical/experimental methodologies are applicable to the rational design of liposomes used as functional materials and drug delivery applications, as well as to study inter-membrane interactions in living systems, such as cell adhesion.","lang":"eng"}],"publication_status":"published","pmid":1,"publication":"Soft Matter","title":"Melting transition in lipid vesicles functionalised by mobile DNA linkers","_id":"10381","oa":1,"year":"2016","main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1608.05788"}],"citation":{"apa":"Bachmann, S. J., Kotar, J., Parolini, L., Šarić, A., Cicuta, P., Di Michele, L., &#38; Mognetti, B. M. (2016). Melting transition in lipid vesicles functionalised by mobile DNA linkers. <i>Soft Matter</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/c6sm01515h\">https://doi.org/10.1039/c6sm01515h</a>","mla":"Bachmann, Stephan Jan, et al. “Melting Transition in Lipid Vesicles Functionalised by Mobile DNA Linkers.” <i>Soft Matter</i>, vol. 12, no. 37, Royal Society of Chemistry, 2016, pp. 7804–17, doi:<a href=\"https://doi.org/10.1039/c6sm01515h\">10.1039/c6sm01515h</a>.","ista":"Bachmann SJ, Kotar J, Parolini L, Šarić A, Cicuta P, Di Michele L, Mognetti BM. 2016. Melting transition in lipid vesicles functionalised by mobile DNA linkers. Soft Matter. 12(37), 7804–7817.","short":"S.J. Bachmann, J. Kotar, L. Parolini, A. Šarić, P. Cicuta, L. Di Michele, B.M. Mognetti, Soft Matter 12 (2016) 7804–7817.","chicago":"Bachmann, Stephan Jan, Jurij Kotar, Lucia Parolini, Anđela Šarić, Pietro Cicuta, Lorenzo Di Michele, and Bortolo Matteo Mognetti. “Melting Transition in Lipid Vesicles Functionalised by Mobile DNA Linkers.” <i>Soft Matter</i>. Royal Society of Chemistry, 2016. <a href=\"https://doi.org/10.1039/c6sm01515h\">https://doi.org/10.1039/c6sm01515h</a>.","ama":"Bachmann SJ, Kotar J, Parolini L, et al. Melting transition in lipid vesicles functionalised by mobile DNA linkers. <i>Soft Matter</i>. 2016;12(37):7804-7817. doi:<a href=\"https://doi.org/10.1039/c6sm01515h\">10.1039/c6sm01515h</a>","ieee":"S. J. Bachmann <i>et al.</i>, “Melting transition in lipid vesicles functionalised by mobile DNA linkers,” <i>Soft Matter</i>, vol. 12, no. 37. Royal Society of Chemistry, pp. 7804–7817, 2016."},"quality_controlled":"1","extern":"1","author":[{"full_name":"Bachmann, Stephan Jan","last_name":"Bachmann","first_name":"Stephan Jan"},{"full_name":"Kotar, Jurij","first_name":"Jurij","last_name":"Kotar"},{"full_name":"Parolini, Lucia","first_name":"Lucia","last_name":"Parolini"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","last_name":"Šarić","first_name":"Anđela"},{"last_name":"Cicuta","first_name":"Pietro","full_name":"Cicuta, Pietro"},{"first_name":"Lorenzo","last_name":"Di Michele","full_name":"Di Michele, Lorenzo"},{"full_name":"Mognetti, Bortolo Matteo","last_name":"Mognetti","first_name":"Bortolo Matteo"}],"arxiv":1,"scopus_import":"1","publication_identifier":{"eissn":["1744-6848"],"issn":["1744-683X"]},"external_id":{"arxiv":["1608.05788"],"pmid":["27722701"]},"keyword":["condensed matter physics","general chemistry"],"date_published":"2016-08-19T00:00:00Z","page":"7804-7817","doi":"10.1039/c6sm01515h","language":[{"iso":"eng"}],"oa_version":"Preprint","date_updated":"2021-11-29T13:09:00Z","type":"journal_article","day":"19","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","article_processing_charge":"No"}]