[{"status":"public","type":"journal_article","doi":"10.1021/acs.chemrev.7b00570","language":[{"iso":"eng"}],"year":"2018","publisher":"American Chemical Society","date_updated":"2021-01-12T08:19:18Z","day":"28","date_published":"2018-02-28T00:00:00Z","page":"3559-3607","publication_status":"published","oa_version":"None","abstract":[{"lang":"eng","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."}],"author":[{"first_name":"Christophe","full_name":"Chipot, Christophe","last_name":"Chipot"},{"first_name":"François","full_name":"Dehez, François","last_name":"Dehez"},{"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","first_name":"Eva","last_name":"Pebay-Peyroula"},{"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.","first_name":"Edmund R. S.","last_name":"Kunji"},{"last_name":"Veglia","full_name":"Veglia, Gianluigi","first_name":"Gianluigi"},{"last_name":"Cross","full_name":"Cross, Timothy A.","first_name":"Timothy A."},{"orcid":"0000-0002-9350-7606","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","full_name":"Schanda, Paul"}],"_id":"8442","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","issue":"7","extern":"1","intvolume":"       118","keyword":["General Chemistry"],"date_created":"2020-09-18T10:05:35Z","citation":{"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>","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.","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>.","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.","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>."},"publication":"Chemical Reviews","title":"Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies","volume":118,"article_type":"original","month":"02","publication_identifier":{"issn":["0009-2665","1520-6890"]},"quality_controlled":"1"},{"month":"02","publication_identifier":{"eissn":["2041-1723"]},"quality_controlled":"1","article_type":"original","volume":9,"article_number":"641","date_created":"2023-08-01T09:39:32Z","pmid":1,"extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","intvolume":"         9","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"author":[{"last_name":"Samanta","first_name":"Dipak","full_name":"Samanta, Dipak"},{"last_name":"Galaktionova","full_name":"Galaktionova, Daria","first_name":"Daria"},{"full_name":"Gemen, Julius","first_name":"Julius","last_name":"Gemen"},{"first_name":"Linda J. W.","full_name":"Shimon, Linda J. W.","last_name":"Shimon"},{"full_name":"Diskin-Posner, Yael","first_name":"Yael","last_name":"Diskin-Posner"},{"last_name":"Avram","first_name":"Liat","full_name":"Avram, Liat"},{"last_name":"Král","first_name":"Petr","full_name":"Král, Petr"},{"full_name":"Klajn, Rafal","first_name":"Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"_id":"13374","oa":1,"date_published":"2018-02-13T00:00:00Z","doi":"10.1038/s41467-017-02715-6","language":[{"iso":"eng"}],"year":"2018","publisher":"Springer Nature","type":"journal_article","main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-02715-6","open_access":"1"}],"publication":"Nature Communications","title":"Reversible chromism of spiropyran in the cavity of a flexible coordination cage","external_id":{"pmid":["29440687"]},"related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/s41467-018-03701-2"}]},"citation":{"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>","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>.","short":"D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L. Avram, P. Král, R. Klajn, Nature Communications 9 (2018).","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.","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.","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>."},"scopus_import":"1","day":"13","publication_status":"published","oa_version":"Published Version","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."}],"date_updated":"2023-08-07T10:54:05Z","status":"public"},{"date_updated":"2023-08-07T11:14:28Z","status":"public","day":"11","page":"7023-7027","publication_status":"published","oa_version":"Published Version","abstract":[{"lang":"eng","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."}],"citation":{"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.","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>.","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>","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>","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.","short":"Z. Chu, Y. Han, P. Král, R. Klajn, Angewandte Chemie International Edition 57 (2018) 7023–7027.","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>."},"scopus_import":"1","issue":"24","main_file_link":[{"url":"https://doi.org/10.1002/anie.201800673","open_access":"1"}],"publication":"Angewandte Chemie International Edition","title":"“Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles","external_id":{"pmid":["29673022"]},"doi":"10.1002/anie.201800673","language":[{"iso":"eng"}],"year":"2018","publisher":"Wiley","type":"journal_article","author":[{"first_name":"Zonglin","full_name":"Chu, Zonglin","last_name":"Chu"},{"last_name":"Han","first_name":"Yanxiao","full_name":"Han, Yanxiao"},{"last_name":"Král","first_name":"Petr","full_name":"Král, Petr"},{"first_name":"Rafal","full_name":"Klajn, Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"_id":"13377","oa":1,"date_published":"2018-06-11T00:00:00Z","date_created":"2023-08-01T09:40:16Z","pmid":1,"extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","intvolume":"        57","keyword":["General Chemistry","Catalysis"],"month":"06","publication_identifier":{"issn":["1433-7851"],"eissn":["1521-3773"]},"quality_controlled":"1","article_type":"original","volume":57},{"abstract":[{"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.","lang":"eng"}],"oa_version":"Published Version","publication_status":"published","day":"04","status":"public","date_updated":"2023-11-07T11:46:12Z","external_id":{"pmid":["29728606"]},"title":"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB","publication":"Nature Communications","main_file_link":[{"url":"https://doi.org/10.1038/s41467-018-04139-2","open_access":"1"}],"scopus_import":"1","citation":{"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).","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.","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>","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>.","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."},"date_published":"2018-05-04T00:00:00Z","oa":1,"_id":"14284","author":[{"last_name":"Bräuning","full_name":"Bräuning, Bastian","first_name":"Bastian"},{"last_name":"Bertosin","full_name":"Bertosin, Eva","first_name":"Eva"},{"last_name":"Praetorius","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62","first_name":"Florian M","full_name":"Praetorius, Florian M"},{"last_name":"Ihling","first_name":"Christian","full_name":"Ihling, Christian"},{"full_name":"Schatt, Alexandra","first_name":"Alexandra","last_name":"Schatt"},{"last_name":"Adler","first_name":"Agnes","full_name":"Adler, Agnes"},{"last_name":"Richter","first_name":"Klaus","full_name":"Richter, Klaus"},{"last_name":"Sinz","first_name":"Andrea","full_name":"Sinz, Andrea"},{"full_name":"Dietz, Hendrik","first_name":"Hendrik","last_name":"Dietz"},{"last_name":"Groll","full_name":"Groll, Michael","first_name":"Michael"}],"type":"journal_article","publisher":"Springer Nature","year":"2018","language":[{"iso":"eng"}],"doi":"10.1038/s41467-018-04139-2","article_type":"original","volume":9,"quality_controlled":"1","publication_identifier":{"issn":["2041-1723"]},"month":"05","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"intvolume":"         9","extern":"1","article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","pmid":1,"article_number":"1806","date_created":"2023-09-06T12:07:33Z"},{"pmid":1,"date_created":"2021-02-01T13:44:41Z","intvolume":"        14","keyword":["General Chemistry","Condensed Matter Physics"],"user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","extern":"1","article_processing_charge":"No","publication_identifier":{"eissn":["1744-6848"],"issn":["1744-683X"]},"quality_controlled":"1","month":"12","article_type":"original","volume":14,"year":"2018","publisher":"Royal Society of Chemistry ","doi":"10.1039/c8sm01760c","language":[{"iso":"eng"}],"type":"journal_article","_id":"9053","oa":1,"author":[{"last_name":"Aubret","full_name":"Aubret, Antoine","first_name":"Antoine"},{"orcid":"0000-0002-7253-9465","last_name":"Palacci","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d","full_name":"Palacci, Jérémie A","first_name":"Jérémie A"}],"date_published":"2018-12-21T00:00:00Z","arxiv":1,"citation":{"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>","short":"A. Aubret, J.A. Palacci, Soft Matter 14 (2018) 9577–9588.","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>.","ista":"Aubret A, Palacci JA. 2018. Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. Soft Matter. 14(47), 9577–9588.","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.","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>."},"scopus_import":"1","issue":"47","main_file_link":[{"url":"https://arxiv.org/abs/1909.11121","open_access":"1"}],"title":"Diffusiophoretic design of self-spinning microgears from colloidal microswimmers","external_id":{"arxiv":["1909.11121"],"pmid":["30456407"]},"publication":"Soft Matter","date_updated":"2023-02-23T13:47:43Z","status":"public","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"}],"day":"21","publication_status":"published","oa_version":"Preprint","page":"9577-9588"},{"type":"journal_article","doi":"10.1038/s41557-018-0023-x","language":[{"iso":"eng"}],"year":"2018","publisher":"Springer Nature","date_published":"2018-03-26T00:00:00Z","author":[{"last_name":"Cohen","first_name":"Samuel I. A.","full_name":"Cohen, Samuel I. A."},{"last_name":"Cukalevski","full_name":"Cukalevski, Risto","first_name":"Risto"},{"last_name":"Michaels","first_name":"Thomas C. T.","full_name":"Michaels, Thomas C. T."},{"first_name":"Anđela","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b"},{"last_name":"Törnquist","first_name":"Mattias","full_name":"Törnquist, Mattias"},{"last_name":"Vendruscolo","first_name":"Michele","full_name":"Vendruscolo, Michele"},{"last_name":"Dobson","full_name":"Dobson, Christopher M.","first_name":"Christopher M."},{"last_name":"Buell","first_name":"Alexander K.","full_name":"Buell, Alexander K."},{"full_name":"Knowles, Tuomas P. J.","first_name":"Tuomas P. J.","last_name":"Knowles"},{"last_name":"Linse","full_name":"Linse, Sara","first_name":"Sara"}],"_id":"10360","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","article_processing_charge":"No","extern":"1","intvolume":"        10","keyword":["general chemical engineering","general chemistry"],"date_created":"2021-11-26T12:41:38Z","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).","pmid":1,"article_type":"original","volume":10,"month":"03","publication_identifier":{"issn":["1755-4330"],"eissn":["1755-4349"]},"quality_controlled":"1","status":"public","date_updated":"2021-11-26T15:14:00Z","day":"26","publication_status":"published","oa_version":"None","page":"523-531","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"}],"scopus_import":"1","issue":"5","citation":{"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>.","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.","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>","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.","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>.","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>"},"publication":"Nature Chemistry","title":"Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide","external_id":{"pmid":["29581486"]}},{"oa":1,"_id":"11065","author":[{"full_name":"Buchwalter, Abigail","first_name":"Abigail","last_name":"Buchwalter"},{"orcid":"0000-0002-2111-992X","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W","full_name":"HETZER, Martin W"}],"date_published":"2017-08-30T00:00:00Z","publisher":"Springer Nature","year":"2017","language":[{"iso":"eng"}],"doi":"10.1038/s41467-017-00322-z","type":"journal_article","quality_controlled":"1","publication_identifier":{"issn":["2041-1723"]},"month":"08","article_type":"original","volume":8,"pmid":1,"article_number":"328","date_created":"2022-04-07T07:45:50Z","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"intvolume":"         8","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","extern":"1","article_processing_charge":"No","abstract":[{"lang":"eng","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."}],"publication_status":"published","oa_version":"Published Version","day":"30","date_updated":"2022-07-18T08:33:03Z","status":"public","main_file_link":[{"url":"https://doi.org/10.1038/s41467-017-00322-z","open_access":"1"}],"external_id":{"pmid":["28855503"]},"title":"Nucleolar expansion and elevated protein translation in premature aging","publication":"Nature Communications","citation":{"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>.","ieee":"A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” <i>Nature Communications</i>, vol. 8. Springer Nature, 2017.","ista":"Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. 8, 328.","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>.","short":"A. Buchwalter, M. Hetzer, Nature Communications 8 (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>"},"scopus_import":"1"},{"title":"Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals","article_type":"original","volume":87,"publication":"Solid State Nuclear Magnetic Resonance","publication_identifier":{"issn":["0926-2040"]},"quality_controlled":"1","month":"10","intvolume":"        87","keyword":["Nuclear and High Energy Physics","Instrumentation","General Chemistry","Radiation"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","issue":"10","article_processing_charge":"No","citation":{"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.","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>.","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.","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>.","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>"},"date_created":"2020-09-18T10:06:18Z","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"}],"day":"01","oa_version":"None","publication_status":"published","page":"86-95","date_published":"2017-10-01T00:00:00Z","_id":"8447","author":[{"last_name":"Gauto","full_name":"Gauto, Diego F.","first_name":"Diego F."},{"last_name":"Hessel","full_name":"Hessel, Audrey","first_name":"Audrey"},{"last_name":"Rovó","first_name":"Petra","full_name":"Rovó, Petra"},{"full_name":"Kurauskas, Vilius","first_name":"Vilius","last_name":"Kurauskas"},{"full_name":"Linser, Rasmus","first_name":"Rasmus","last_name":"Linser"},{"first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"}],"type":"journal_article","status":"public","year":"2017","publisher":"Elsevier","date_updated":"2021-01-12T08:19:20Z","doi":"10.1016/j.ssnmr.2017.04.002","language":[{"iso":"eng"}]},{"title":"Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles","external_id":{"pmid":["29193964"]},"publication":"Journal of the American Chemical Society","citation":{"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>.","short":"M. Sawczyk, R. Klajn, Journal of the American Chemical Society 139 (2017) 17973–17978.","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.","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>."},"scopus_import":"1","issue":"49","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."}],"day":"01","page":"17973-17978","oa_version":"None","publication_status":"published","date_updated":"2023-08-07T11:19:30Z","status":"public","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"quality_controlled":"1","month":"12","article_type":"original","volume":139,"pmid":1,"date_created":"2023-08-01T09:41:01Z","intvolume":"       139","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","_id":"13380","author":[{"full_name":"Sawczyk, Michał","first_name":"Michał","last_name":"Sawczyk"},{"first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn"}],"date_published":"2017-12-01T00:00:00Z","year":"2017","publisher":"American Chemical Society","doi":"10.1021/jacs.7b09111","language":[{"iso":"eng"}],"type":"journal_article"},{"pmid":1,"date_created":"2023-08-01T09:41:30Z","intvolume":"        46","keyword":["General Chemistry"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","article_processing_charge":"No","publication_identifier":{"issn":["0306-0012"],"eissn":["1460-4744"]},"quality_controlled":"1","month":"09","article_type":"letter_note","volume":46,"year":"2017","publisher":"Royal Society of Chemistry","doi":"10.1039/c7cs90088k","language":[{"iso":"eng"}],"type":"journal_article","_id":"13382","oa":1,"author":[{"first_name":"Jan H.","full_name":"van Esch, Jan H.","last_name":"van Esch"},{"last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","full_name":"Klajn, Rafal","first_name":"Rafal"},{"full_name":"Otto, Sijbren","first_name":"Sijbren","last_name":"Otto"}],"date_published":"2017-09-08T00:00:00Z","citation":{"ista":"van Esch JH, Klajn R, Otto S. 2017. Chemical systems out of equilibrium. Chemical Society Reviews. 46(18), 5474–5475.","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>","short":"J.H. van Esch, R. Klajn, S. Otto, Chemical Society Reviews 46 (2017) 5474–5475.","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>.","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>","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>.","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."},"scopus_import":"1","issue":"18","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1039/c7cs90088k"}],"title":"Chemical systems out of equilibrium","external_id":{"pmid":["28884760"]},"publication":"Chemical Society Reviews","date_updated":"2023-08-07T11:27:42Z","status":"public","day":"08","oa_version":"Published Version","publication_status":"published","page":"5474-5475"},{"date_updated":"2023-08-22T08:26:06Z","status":"public","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"}],"day":"15","oa_version":"Published Version","publication_status":"published","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>","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.","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>","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>.","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.","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>."},"scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms15651"}],"title":"Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering","external_id":{"pmid":["28643771"]},"publication":"Nature Communications","year":"2017","publisher":"Springer Nature","doi":"10.1038/ncomms15651","language":[{"iso":"eng"}],"type":"journal_article","_id":"14005","oa":1,"author":[{"first_name":"Samuel G.","full_name":"Walt, Samuel G.","last_name":"Walt"},{"last_name":"Bhargava Ram","first_name":"Niraghatam","full_name":"Bhargava Ram, Niraghatam"},{"first_name":"Marcos","full_name":"Atala, Marcos","last_name":"Atala"},{"last_name":"Shvetsov-Shilovski","first_name":"Nikolay I","full_name":"Shvetsov-Shilovski, Nikolay I"},{"first_name":"Aaron","full_name":"von Conta, Aaron","last_name":"von Conta"},{"full_name":"Baykusheva, Denitsa Rangelova","first_name":"Denitsa Rangelova","id":"71b4d059-2a03-11ee-914d-dfa3beed6530","last_name":"Baykusheva"},{"last_name":"Lein","full_name":"Lein, Manfred","first_name":"Manfred"},{"full_name":"Wörner, Hans Jakob","first_name":"Hans Jakob","last_name":"Wörner"}],"date_published":"2017-06-15T00:00:00Z","pmid":1,"article_number":"15651","date_created":"2023-08-10T06:36:09Z","intvolume":"         8","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry","Multidisciplinary"],"extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","publication_identifier":{"eissn":["2041-1723"]},"quality_controlled":"1","month":"06","article_type":"original","volume":8},{"publisher":"American Chemical Society","year":"2017","language":[{"iso":"eng"}],"doi":"10.1021/acscentsci.7b00392","type":"journal_article","oa":1,"_id":"10369","author":[{"last_name":"Simunovic","full_name":"Simunovic, Mijo","first_name":"Mijo"},{"last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela"},{"last_name":"Henderson","first_name":"J. Michael","full_name":"Henderson, J. Michael"},{"last_name":"Lee","full_name":"Lee, Ka Yee C.","first_name":"Ka Yee C."},{"first_name":"Gregory A.","full_name":"Voth, Gregory A.","last_name":"Voth"}],"date_published":"2017-11-21T00:00:00Z","pmid":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_created":"2021-11-29T08:49:50Z","keyword":["general chemical engineering","general chemistry"],"intvolume":"         3","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","ddc":["540"],"extern":"1","article_processing_charge":"No","file_date_updated":"2021-11-29T09:00:40Z","quality_controlled":"1","publication_identifier":{"eissn":["2374-7951"],"issn":["2374-7943"]},"month":"11","article_type":"original","volume":3,"date_updated":"2021-11-29T09:28:06Z","license":"https://creativecommons.org/licenses/by/4.0/","status":"public","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."}],"publication_status":"published","page":"1246-1253","oa_version":"Published Version","day":"21","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"citation":{"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>.","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.","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.","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>","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>.","short":"M. Simunovic, A. Šarić, J.M. Henderson, K.Y.C. Lee, G.A. Voth, ACS Central Science 3 (2017) 1246–1253.","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>"},"has_accepted_license":"1","issue":"12","scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://pubs.acs.org/doi/10.1021/acscentsci.7b00392"}],"external_id":{"pmid":["29296664"]},"title":"Long-range organization of membrane-curving proteins","file":[{"file_name":"2017_ACSCentSci_Simunovic.pdf","file_size":2635263,"file_id":"10371","date_created":"2021-11-29T09:00:40Z","checksum":"1cf3e5e5342f2d728f47560acc3ec560","success":1,"date_updated":"2021-11-29T09:00:40Z","creator":"cchlebak","access_level":"open_access","content_type":"application/pdf","relation":"main_file"}],"publication":"ACS Central Science"},{"date_created":"2021-11-29T09:29:31Z","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).","pmid":1,"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","ddc":["540"],"article_processing_charge":"No","extern":"1","intvolume":"         8","keyword":["general chemistry"],"month":"08","publication_identifier":{"issn":["2041-6520"],"eissn":["2041-6539"]},"quality_controlled":"1","volume":8,"article_type":"original","doi":"10.1039/c7sc01965c","language":[{"iso":"eng"}],"year":"2017","publisher":"Royal Society of Chemistry","type":"journal_article","author":[{"first_name":"Georg","full_name":"Meisl, Georg","last_name":"Meisl"},{"last_name":"Rajah","full_name":"Rajah, Luke","first_name":"Luke"},{"first_name":"Samuel A. I.","full_name":"Cohen, Samuel A. I.","last_name":"Cohen"},{"last_name":"Pfammatter","full_name":"Pfammatter, Manuela","first_name":"Manuela"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela"},{"first_name":"Erik","full_name":"Hellstrand, Erik","last_name":"Hellstrand"},{"full_name":"Buell, Alexander K.","first_name":"Alexander K.","last_name":"Buell"},{"last_name":"Aguzzi","full_name":"Aguzzi, Adriano","first_name":"Adriano"},{"last_name":"Linse","first_name":"Sara","full_name":"Linse, Sara"},{"last_name":"Vendruscolo","first_name":"Michele","full_name":"Vendruscolo, Michele"},{"last_name":"Dobson","first_name":"Christopher M.","full_name":"Dobson, Christopher M."},{"full_name":"Knowles, Tuomas P. J.","first_name":"Tuomas P. J.","last_name":"Knowles"}],"_id":"10374","oa":1,"date_published":"2017-08-31T00:00:00Z","citation":{"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>","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>.","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.","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.","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>","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.","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>."},"scopus_import":"1","issue":"10","main_file_link":[{"url":"https://pubs.rsc.org/en/content/articlelanding/2017/SC/C7SC01965C","open_access":"1"}],"publication":"Chemical Science","title":"Scaling behaviour and rate-determining steps in filamentous self-assembly","external_id":{"pmid":["29147538"]},"date_updated":"2021-11-29T10:00:00Z","status":"public","license":"https://creativecommons.org/licenses/by-nc/3.0/","day":"31","tmp":{"name":"Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)","image":"/images/cc_by_nc.png","short":"CC BY-NC (3.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/3.0/legalcode"},"page":"7087-7097","oa_version":"Published Version","publication_status":"published","abstract":[{"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.","lang":"eng"}]},{"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","article_processing_charge":"No","extern":"1","intvolume":"        13","keyword":["condensed matter physics","general chemistry"],"date_created":"2021-11-29T10:00:39Z","acknowledgement":"This work was supported by the Netherlands Organisation for Scientific Research (NWO/OCW), as part of the Frontiers of Nanoscience program.","pmid":1,"article_type":"original","volume":13,"month":"06","publication_identifier":{"eissn":["1744-6848"],"issn":["1744-683X"]},"quality_controlled":"1","type":"journal_article","doi":"10.1039/c7sm00433h","language":[{"iso":"eng"}],"year":"2017","publisher":"Royal Society of Chemistry","date_published":"2017-06-15T00:00:00Z","author":[{"last_name":"Vahid","full_name":"Vahid, Afshin","first_name":"Afshin"},{"full_name":"Šarić, Anđela","first_name":"Anđela","orcid":"0000-0002-7854-2139","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b"},{"full_name":"Idema, Timon","first_name":"Timon","last_name":"Idema"}],"_id":"10375","oa":1,"scopus_import":"1","issue":"28","arxiv":1,"citation":{"short":"A. Vahid, A. Šarić, T. Idema, Soft Matter 13 (2017) 4924–4930.","ista":"Vahid A, Šarić A, Idema T. 2017. Curvature variation controls particle aggregation on fluid vesicles. Soft Matter. 13(28), 4924–4930.","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>.","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>","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>","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>.","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."},"publication":"Soft Matter","title":"Curvature variation controls particle aggregation on fluid vesicles","external_id":{"arxiv":["1703.00776"],"pmid":["28677712"]},"main_file_link":[{"open_access":"1","url":"https://pubs.rsc.org/en/content/articlelanding/2017/SM/C7SM00433H"}],"status":"public","license":"https://creativecommons.org/licenses/by/3.0/","date_updated":"2021-11-29T10:33:36Z","day":"15","tmp":{"image":"/images/cc_by.png","short":"CC BY (3.0)","name":"Creative Commons Attribution 3.0 Unported (CC BY 3.0)","legal_code_url":"https://creativecommons.org/licenses/by/3.0/legalcode"},"publication_status":"published","oa_version":"Published Version","page":"4924-4930","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"}]},{"type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1038/ncomms13874","publisher":"Springer Nature","year":"2016","date_published":"2016-12-22T00:00:00Z","author":[{"first_name":"Robert A.H.","full_name":"van de Ven, Robert A.H.","last_name":"van de Ven"},{"full_name":"de Groot, Jolien S.","first_name":"Jolien S.","last_name":"de Groot"},{"first_name":"Danielle","full_name":"Park, Danielle","last_name":"Park"},{"last_name":"van Domselaar","first_name":"Robert","full_name":"van Domselaar, Robert"},{"last_name":"de Jong","full_name":"de Jong, Danielle","first_name":"Danielle"},{"last_name":"Szuhai","full_name":"Szuhai, Karoly","first_name":"Karoly"},{"first_name":"Elsken","full_name":"van der Wall, Elsken","last_name":"van der Wall"},{"first_name":"Oscar M.","full_name":"Rueda, Oscar M.","last_name":"Rueda"},{"first_name":"H. Raza","full_name":"Ali, H. Raza","last_name":"Ali"},{"first_name":"Carlos","full_name":"Caldas, Carlos","last_name":"Caldas"},{"full_name":"van Diest, Paul J.","first_name":"Paul J.","last_name":"van Diest"},{"orcid":"0000-0002-2111-992X","last_name":"HETZER","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","first_name":"Martin W","full_name":"HETZER, Martin W"},{"first_name":"Erik","full_name":"Sahai, Erik","last_name":"Sahai"},{"last_name":"Derksen","first_name":"Patrick W.B.","full_name":"Derksen, Patrick W.B."}],"oa":1,"_id":"11072","article_processing_charge":"No","extern":"1","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"intvolume":"         7","article_number":"13874","date_created":"2022-04-07T07:48:34Z","pmid":1,"volume":7,"article_type":"original","month":"12","quality_controlled":"1","publication_identifier":{"issn":["2041-1723"]},"status":"public","date_updated":"2022-07-18T08:34:32Z","oa_version":"Published Version","publication_status":"published","day":"22","abstract":[{"lang":"eng","text":"Spatiotemporal activation of RhoA and actomyosin contraction underpins cellular adhesion and division. Loss of cell–cell adhesion and chromosomal instability are cardinal events that drive tumour progression. Here, we show that p120-catenin (p120) not only controls cell–cell adhesion, but also acts as a critical regulator of cytokinesis. We find that p120 regulates actomyosin contractility through concomitant binding to RhoA and the centralspindlin component MKLP1, independent of cadherin association. In anaphase, p120 is enriched at the cleavage furrow where it binds MKLP1 to spatially control RhoA GTPase cycling. Binding of p120 to MKLP1 during cytokinesis depends on the N-terminal coiled-coil domain of p120 isoform 1A. Importantly, clinical data show that loss of p120 expression is a common event in breast cancer that strongly correlates with multinucleation and adverse patient survival. In summary, our study identifies p120 loss as a driver event of chromosomal instability in cancer.\r\n"}],"scopus_import":"1","citation":{"ieee":"R. A. H. van de Ven <i>et al.</i>, “p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis,” <i>Nature Communications</i>, vol. 7. Springer Nature, 2016.","chicago":"Ven, Robert A.H. van de, Jolien S. de Groot, Danielle Park, Robert van Domselaar, Danielle de Jong, Karoly Szuhai, Elsken van der Wall, et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” <i>Nature Communications</i>. Springer Nature, 2016. <a href=\"https://doi.org/10.1038/ncomms13874\">https://doi.org/10.1038/ncomms13874</a>.","ama":"van de Ven RAH, de Groot JS, Park D, et al. p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. <i>Nature Communications</i>. 2016;7. doi:<a href=\"https://doi.org/10.1038/ncomms13874\">10.1038/ncomms13874</a>","mla":"van de Ven, Robert A. H., et al. “P120-Catenin Prevents Multinucleation through Control of MKLP1-Dependent RhoA Activity during Cytokinesis.” <i>Nature Communications</i>, vol. 7, 13874, Springer Nature, 2016, doi:<a href=\"https://doi.org/10.1038/ncomms13874\">10.1038/ncomms13874</a>.","short":"R.A.H. van de Ven, J.S. de Groot, D. Park, R. van Domselaar, D. de Jong, K. Szuhai, E. van der Wall, O.M. Rueda, H.R. Ali, C. Caldas, P.J. van Diest, M. Hetzer, E. Sahai, P.W.B. Derksen, Nature Communications 7 (2016).","apa":"van de Ven, R. A. H., de Groot, J. S., Park, D., van Domselaar, R., de Jong, D., Szuhai, K., … Derksen, P. W. B. (2016). p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/ncomms13874\">https://doi.org/10.1038/ncomms13874</a>","ista":"van de Ven RAH, de Groot JS, Park D, van Domselaar R, de Jong D, Szuhai K, van der Wall E, Rueda OM, Ali HR, Caldas C, van Diest PJ, Hetzer M, Sahai E, Derksen PWB. 2016. p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis. Nature Communications. 7, 13874."},"publication":"Nature Communications","related_material":{"link":[{"url":"https://doi.org/10.1038/ncomms16030","relation":"erratum"}]},"external_id":{"pmid":["28004812"]},"title":"p120-catenin prevents multinucleation through control of MKLP1-dependent RhoA activity during cytokinesis","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/ncomms13874"}]},{"year":"2016","publisher":"Royal Society of Chemistry","date_updated":"2021-01-12T08:19:23Z","doi":"10.1039/c6cc04484k","language":[{"iso":"eng"}],"type":"journal_article","status":"public","_id":"8455","author":[{"first_name":"Vilius","full_name":"Kurauskas, Vilius","last_name":"Kurauskas"},{"full_name":"Crublet, Elodie","first_name":"Elodie","last_name":"Crublet"},{"last_name":"Macek","first_name":"Pavel","full_name":"Macek, Pavel"},{"full_name":"Kerfah, Rime","first_name":"Rime","last_name":"Kerfah"},{"full_name":"Gauto, Diego F.","first_name":"Diego F.","last_name":"Gauto"},{"full_name":"Boisbouvier, Jérôme","first_name":"Jérôme","last_name":"Boisbouvier"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul"}],"abstract":[{"lang":"eng","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."}],"day":"04","page":"9558-9561","date_published":"2016-07-04T00:00:00Z","publication_status":"published","oa_version":"None","citation":{"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>.","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>","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.","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>","short":"V. Kurauskas, E. Crublet, P. Macek, R. Kerfah, D.F. Gauto, J. Boisbouvier, P. Schanda, Chemical Communications 52 (2016) 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>."},"date_created":"2020-09-18T10:07:29Z","intvolume":"        52","keyword":["Materials Chemistry","Electronic","Optical and Magnetic Materials","General Chemistry","Surfaces","Coatings and Films","Metals and Alloys","Ceramics and Composites","Catalysis"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","issue":"61","extern":"1","publication_identifier":{"issn":["1359-7345","1364-548X"]},"quality_controlled":"1","month":"07","title":"Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3labelling: Application to the 50S ribosome subunit","volume":52,"article_type":"original","publication":"Chemical Communications"},{"_id":"13390","author":[{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn","full_name":"Klajn, Rafal","first_name":"Rafal"}],"publication_status":"published","page":"420-421","date_published":"2016-03-08T00:00:00Z","oa_version":"None","day":"08","publisher":"Springer Nature","date_updated":"2023-08-07T12:49:01Z","year":"2016","language":[{"iso":"eng"}],"doi":"10.1007/s11426-016-5573-4","type":"journal_article","status":"public","quality_controlled":"1","publication_identifier":{"issn":["1674-7291"],"eissn":["1869-1870"]},"month":"03","article_type":"original","volume":59,"title":"Borrowing titania’s photoinduced electrons for molecular switching","publication":"Science China Chemistry","citation":{"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>.","short":"R. Klajn, Science China Chemistry 59 (2016) 420–421.","ista":"Klajn R. 2016. Borrowing titania’s photoinduced electrons for molecular switching. Science China Chemistry. 59(4), 420–421.","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>","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>","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."},"date_created":"2023-08-01T09:43:33Z","keyword":["General Chemistry"],"intvolume":"        59","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","extern":"1","issue":"4","scopus_import":"1"},{"issue":"1","scopus_import":"1","citation":{"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.","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>.","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>","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>","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>.","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.","short":"N. Amdursky, P.K. Kundu, J. Ahrens, D. Huppert, R. Klajn, ChemPlusChem 81 (2016) 44–48."},"publication":"ChemPlusChem","external_id":{"pmid":["31968727"]},"title":"Noncovalent interactions with proteins modify the physicochemical properties of a molecular switch","status":"public","date_updated":"2023-08-07T12:51:56Z","page":"44-48","publication_status":"published","oa_version":"None","day":"01","abstract":[{"lang":"eng","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."}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","extern":"1","keyword":["General Chemistry"],"intvolume":"        81","date_created":"2023-08-01T09:43:46Z","pmid":1,"volume":81,"article_type":"original","month":"01","quality_controlled":"1","publication_identifier":{"eissn":["2192-6506"]},"type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1002/cplu.201500417","publisher":"Wiley","year":"2016","date_published":"2016-01-01T00:00:00Z","author":[{"last_name":"Amdursky","full_name":"Amdursky, Nadav","first_name":"Nadav"},{"first_name":"Pintu K.","full_name":"Kundu, Pintu K.","last_name":"Kundu"},{"first_name":"Johannes","full_name":"Ahrens, Johannes","last_name":"Ahrens"},{"last_name":"Huppert","first_name":"Dan","full_name":"Huppert, Dan"},{"first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn"}],"_id":"13391"},{"year":"2016","publisher":"Elsevier","doi":"10.1016/j.crci.2015.12.004","language":[{"iso":"eng"}],"type":"journal_article","_id":"9019","oa":1,"author":[{"last_name":"Bakail","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E","orcid":"0000-0002-9592-1587","full_name":"Bakail, May M","first_name":"May M"},{"full_name":"Ochsenbein, Francoise","first_name":"Francoise","last_name":"Ochsenbein"}],"date_published":"2016-02-06T00:00:00Z","date_created":"2021-01-19T11:11:54Z","intvolume":"        19","keyword":["General Chemistry","General Chemical Engineering"],"file_date_updated":"2021-01-22T12:36:52Z","article_processing_charge":"No","ddc":["570"],"extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["1631-0748"]},"quality_controlled":"1","month":"02","volume":19,"article_type":"original","date_updated":"2023-02-23T13:46:55Z","license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","status":"public","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."},{"lang":"fre","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."}],"tmp":{"image":"/images/cc_by_nc_nd.png","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode"},"day":"06","oa_version":"Published Version","page":"19-27","publication_status":"published","citation":{"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>.","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.","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>","short":"M.M. Bakail, F. Ochsenbein, Comptes Rendus Chimie 19 (2016) 19–27.","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.","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>.","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>"},"has_accepted_license":"1","issue":"1-2","title":"Targeting protein–protein interactions, a wide open field for drug design","file":[{"success":1,"date_updated":"2021-01-22T12:36:52Z","file_id":"9035","checksum":"c262814ffdbfe95900256ab9ff42cdf5","date_created":"2021-01-22T12:36:52Z","file_size":2045260,"file_name":"2016_ComptesRendueChimie_Bakail.pdf","content_type":"application/pdf","relation":"main_file","access_level":"open_access","creator":"dernst"}],"publication":"Comptes Rendus Chimie"},{"author":[{"full_name":"Moyses, Henrique","first_name":"Henrique","last_name":"Moyses"},{"last_name":"Palacci","id":"8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d","orcid":"0000-0002-7253-9465","full_name":"Palacci, Jérémie A","first_name":"Jérémie A"},{"first_name":"Stefano","full_name":"Sacanna, Stefano","last_name":"Sacanna"},{"last_name":"Grier","first_name":"David G.","full_name":"Grier, David G."}],"_id":"9052","oa":1,"date_published":"2016-08-14T00:00:00Z","doi":"10.1039/c6sm01163b","language":[{"iso":"eng"}],"year":"2016","publisher":"Royal Society of Chemistry ","type":"journal_article","month":"08","publication_identifier":{"eissn":["1744-6848"],"issn":["1744-683X"]},"quality_controlled":"1","volume":12,"article_type":"original","date_created":"2021-02-01T13:44:15Z","pmid":1,"user_id":"D865714E-FA4E-11E9-B85B-F5C5E5697425","article_processing_charge":"No","extern":"1","intvolume":"        12","keyword":["General Chemistry","Condensed Matter Physics"],"day":"14","page":"6357-6364","oa_version":"Preprint","publication_status":"published","abstract":[{"lang":"eng","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."}],"date_updated":"2023-02-23T13:47:40Z","status":"public","main_file_link":[{"url":"https://arxiv.org/abs/1609.01497","open_access":"1"}],"publication":"Soft Matter","title":"Trochoidal trajectories of self-propelled Janus particles in a diverging laser beam","external_id":{"pmid":["27338294"],"arxiv":["1609.01497"]},"arxiv":1,"citation":{"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.","short":"H. Moyses, J.A. Palacci, S. Sacanna, D.G. Grier, Soft Matter 12 (2016) 6357–6364.","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.","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>."},"scopus_import":"1","issue":"30"}]