Loïc Salmon - Publications

Affiliations: 
2014 University of Michigan, Ann Arbor, Ann Arbor, MI 

27 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2018 Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JCA. Reply to 'Misreading chaperone-substrate complexes from random noise'. Nature Structural & Molecular Biology. PMID 30297780 DOI: 10.1038/s41594-018-0145-2  0.6
2018 Salmon L, Ahlstrom LS, Bardwell JCA, Horowitz S. Selecting Conformational Ensembles Using Residual Electron and Anomalous Density (READ). Methods in Molecular Biology (Clifton, N.J.). 1764: 491-504. PMID 29605935 DOI: 10.1007/978-1-4939-7759-8_31  0.6
2017 Salmon L, Stull F, Sayle S, Cato C, Akgül Ş, Foit L, Ahlstrom LS, Eisenmesser EZ, Al-Hashimi HM, Bardwell JCA, Horowitz S. The Mechanism of HdeA Unfolding and Chaperone Activation. Journal of Molecular Biology. PMID 29138002 DOI: 10.1016/j.jmb.2017.11.002  0.6
2016 Salmon L, Ahlstrom LS, Horowitz S, Dickson A, Brooks CL, Bardwell JC. Capturing a dynamic chaperone-substrate interaction using NMR-informed molecular modeling. Journal of the American Chemical Society. PMID 27415450 DOI: 10.1021/jacs.6b02382  0.6
2016 Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JC. Visualizing chaperone-assisted protein folding. Nature Structural & Molecular Biology. PMID 27239796 DOI: 10.1038/nsmb.3237  0.6
2015 Swanson MD, Boudreaux DM, Salmon L, Chugh J, Winter HC, Meagher JL, André S, Murphy PV, Oscarson S, Roy R, King S, Kaplan MH, Goldstein IJ, Tarbet EB, Hurst BL, et al. Engineering a Therapeutic Lectin by Uncoupling Mitogenicity from Antiviral Activity. Cell. 163: 746-58. PMID 26496612 DOI: 10.1016/j.cell.2015.09.056  0.6
2015 Andrałojć W, Ravera E, Salmon L, Parigi G, Al-Hashimi HM, Luchinat C. Inter-helical conformational preferences of HIV-1 TAR-RNA from maximum occurrence analysis of NMR data and molecular dynamics simulations. Physical Chemistry Chemical Physics : Pccp. PMID 26360616 DOI: 10.1039/c5cp03993b  0.6
2015 Salmon L, Giambaşu GM, Nikolova EN, Petzold K, Bhattacharya A, Case DA, Al-Hashimi HM. Modulating RNA Alignment Using Directional Dynamic Kinks: Application in Determining an Atomic-Resolution Ensemble for a Hairpin using NMR Residual Dipolar Couplings. Journal of the American Chemical Society. PMID 26306428 DOI: 10.1021/jacs.5b07229  0.6
2015 Dahl JU, Koldewey P, Salmon L, Horowitz S, Bardwell JC, Jakob U. HdeB functions as an acid-protective chaperone in bacteria. The Journal of Biological Chemistry. 290: 9950. PMID 25888567 DOI: 10.1074/jbc.A114.612986  0.6
2015 Dahl JU, Koldewey P, Salmon L, Horowitz S, Bardwell JC, Jakob U. HdeB functions as an acid-protective chaperone in bacteria. The Journal of Biological Chemistry. 290: 65-75. PMID 25391835 DOI: 10.1074/jbc.M114.612986  0.6
2014 Dickson A, Mustoe AM, Salmon L, Brooks CL. Efficient in silico exploration of RNA interhelical conformations using Euler angles and WExplore. Nucleic Acids Research. 42: 12126-37. PMID 25294827 DOI: 10.1093/nar/gku799  0.6
2014 Yang S, Salmon L, Al-Hashimi HM. Measuring similarity between dynamic ensembles of biomolecules. Nature Methods. 11: 552-4. PMID 24705474 DOI: 10.1038/nmeth.2921  0.6
2014 Salmon L, Yang S, Al-Hashimi HM. Advances in the determination of nucleic acid conformational ensembles. Annual Review of Physical Chemistry. 65: 293-316. PMID 24364917 DOI: 10.1146/annurev-physchem-040412-110059  0.6
2013 Salmon L, Bascom G, Andricioaei I, Al-Hashimi HM. A general method for constructing atomic-resolution RNA ensembles using NMR residual dipolar couplings: the basis for interhelical motions revealed. Journal of the American Chemical Society. 135: 5457-66. PMID 23473378 DOI: 10.1021/ja400920w  0.6
2012 Ozenne V, Schneider R, Yao M, Huang JR, Salmon L, Zweckstetter M, Jensen MR, Blackledge M. Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution. Journal of the American Chemical Society. 134: 15138-48. PMID 22901047 DOI: 10.1021/ja306905s  0.6
2012 Salmon L, Jensen MR, Bernadó P, Blackledge M. Measurement and analysis of NMR residual dipolar couplings for the study of intrinsically disordered proteins. Methods in Molecular Biology (Clifton, N.J.). 895: 115-25. PMID 22760316 DOI: 10.1007/978-1-61779-927-3_9  0.6
2012 Ozenne V, Bauer F, Salmon L, Huang JR, Jensen MR, Segard S, Bernadó P, Charavay C, Blackledge M. Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables. Bioinformatics (Oxford, England). 28: 1463-70. PMID 22613562 DOI: 10.1093/bioinformatics/bts172  0.6
2012 Schneider R, Huang JR, Yao M, Communie G, Ozenne V, Mollica L, Salmon L, Jensen MR, Blackledge M. Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy. Molecular Biosystems. 8: 58-68. PMID 21874206 DOI: 10.1039/c1mb05291h  0.6
2011 Jensen MR, Ortega-Roldan JL, Salmon L, van Nuland N, Blackledge M. Characterizing weak protein-protein complexes by NMR residual dipolar couplings. European Biophysics Journal : Ebj. 40: 1371-81. PMID 21710303 DOI: 10.1007/s00249-011-0720-5  0.6
2011 Jensen MR, Communie G, Ribeiro EA, Martinez N, Desfosses A, Salmon L, Mollica L, Gabel F, Jamin M, Longhi S, Ruigrok RW, Blackledge M. Intrinsic disorder in measles virus nucleocapsids. Proceedings of the National Academy of Sciences of the United States of America. 108: 9839-44. PMID 21613569 DOI: 10.1073/pnas.1103270108  0.6
2011 Salmon L, Ortega Roldan JL, Lescop E, Licinio A, van Nuland N, Jensen MR, Blackledge M. Structure, dynamics, and kinetics of weak protein-protein complexes from NMR spin relaxation measurements of titrated solutions. Angewandte Chemie (International Ed. in English). 50: 3755-9. PMID 21425222 DOI: 10.1002/anie.201100310  0.6
2011 Salmon L, Bouvignies G, Markwick P, Blackledge M. Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scales. Biochemistry. 50: 2735-47. PMID 21388216 DOI: 10.1021/bi200177v  0.6
2010 Salmon L, Nodet G, Ozenne V, Yin G, Jensen MR, Zweckstetter M, Blackledge M. NMR characterization of long-range order in intrinsically disordered proteins. Journal of the American Chemical Society. 132: 8407-18. PMID 20499903 DOI: 10.1021/ja101645g  0.6
2010 Jensen MR, Salmon L, Nodet G, Blackledge M. Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts. Journal of the American Chemical Society. 132: 1270-2. PMID 20063887 DOI: 10.1021/ja909973n  0.6
2009 Markwick PR, Bouvignies G, Salmon L, McCammon JA, Nilges M, Blackledge M. Toward a unified representation of protein structural dynamics in solution. Journal of the American Chemical Society. 131: 16968-75. PMID 19919148 DOI: 10.1021/ja907476w  0.6
2009 Nodet G, Salmon L, Ozenne V, Meier S, Jensen MR, Blackledge M. Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings. Journal of the American Chemical Society. 131: 17908-18. PMID 19908838 DOI: 10.1021/ja9069024  0.6
2008 Hus JC, Salmon L, Bouvignies G, Lotze J, Blackledge M, Brüschweiler R. 16-fold degeneracy of peptide plane orientations from residual dipolar couplings: analytical treatment and implications for protein structure determination. Journal of the American Chemical Society. 130: 15927-37. PMID 18959402 DOI: 10.1021/ja804274s  0.6
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