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Loïc Salmon - Publications

Affiliations: 
2014 University of Michigan, Ann Arbor, Ann Arbor, MI 
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35 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
2023 Roy R, Geng A, Shi H, Merriman DK, Dethoff EA, Salmon L, Al-Hashimi HM. Kinetic Resolution of the Atomic 3D Structures Formed by Ground and Excited Conformational States in an RNA Dynamic Ensemble. Journal of the American Chemical Society. 145: 22964-22978. PMID 37831584 DOI: 10.1021/jacs.3c04614  0.57
2023 Sannapureddi RKR, Mohanty MK, Salmon L, Sathyamoorthy B. Conformational Plasticity of Parallel G-Quadruplex─Implications on Duplex-Quadruplex Motifs. Journal of the American Chemical Society. 145: 15370-15380. PMID 37428641 DOI: 10.1021/jacs.3c03218  0.714
2023 Nouri S, Boudet J, Dreher-Teo H, Allain FH, Glockshuber R, Salmon L, Giese C. Elongated Bacterial Pili as a Versatile Alignment Medium for NMR Spectroscopy. Angewandte Chemie (International Ed. in English). e202305120. PMID 37248171 DOI: 10.1002/anie.202305120  0.381
2019 Rocchio S, Duman R, El Omari K, Mykhaylyk V, Orr C, Yan Z, Salmon L, Wagner A, Bardwell JCA, Horowitz S. Identifying dynamic, partially occupied residues using anomalous scattering. Acta Crystallographica. Section D, Structural Biology. 75: 1084-1095. PMID 31793902 DOI: 10.1107/S2059798319014475  0.696
2019 Boudet J, Devillier JC, Wiegand T, Salmon L, Meier BH, Lipps G, Allain FH. A Small Helical Bundle Prepares Primer Synthesis by Binding Two Nucleotides that Enhance Sequence-Specific Recognition of the DNA Template. Cell. 176: 154-166.e13. PMID 30595448 DOI: 10.2210/Pdb6Gt7/Pdb  0.323
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  0.621
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  0.722
2017 Hofmann D, Salmon L, Wider G. Activity of Tumor Necrosis Factor α Is Modulated by Dynamic Conformational Rearrangements. Journal of the American Chemical Society. PMID 29192773 DOI: 10.1021/Jacs.7B05050  0.431
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  0.751
2017 Salvi N, Salmon L, Blackledge M. Dynamic descriptions of highly flexible molecules from NMR dipolar couplings: Physical basis and limitations. Journal of the American Chemical Society. PMID 28290683 DOI: 10.1021/jacs.7b01566  0.36
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  0.732
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  0.725
2016 Ahlstrom LS, Salmon L, Horowitz S, Dickson A, Brooks CL, Bardwell JC. NMR-Informed Molecular Modeling Uncovers the Conformational Landscape of Chaperone Binding with Unfolded Substrate Biophysical Journal. 110: 369a. DOI: 10.1016/J.Bpj.2015.11.1989  0.734
2015 Salmon L, Blackledge M. Investigating protein conformational energy landscapes and atomic resolution dynamics from NMR dipolar couplings: a review. Reports On Progress in Physics. Physical Society (Great Britain). 78: 126601. PMID 26517337 DOI: 10.1088/0034-4885/78/12/126601  0.315
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  0.752
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  0.69
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  0.779
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  0.628
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  0.683
2015 Salmon L, Blackledge M. Investigating protein conformational energy landscapes and atomic resolution dynamics from NMR dipolar couplings: A review Reports On Progress in Physics. 78. DOI: 10.1088/0034-4885/78/12/126601  0.314
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  0.762
2014 Ravera E, Salmon L, Fragai M, Parigi G, Al-Hashimi H, Luchinat C. Insights into domain-domain motions in proteins and RNA from solution NMR. Accounts of Chemical Research. 47: 3118-26. PMID 25148413 DOI: 10.1021/Ar5002318  0.647
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  0.729
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  0.732
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  0.677
2013 Guerry P, Salmon L, Mollica L, Ortega Roldan JL, Markwick P, van Nuland NA, McCammon JA, Blackledge M. Mapping the population of protein conformational energy sub-states from NMR dipolar couplings. Angewandte Chemie (International Ed. in English). 52: 3181-5. PMID 23371543 DOI: 10.1002/Anie.201209669  0.418
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  0.34
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  0.351
2012 Salmon L, Pierce L, Grimm A, Ortega Roldan JL, Mollica L, Jensen MR, van Nuland N, Markwick PR, McCammon JA, Blackledge M. Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics. Angewandte Chemie (International Ed. in English). 51: 6103-6. PMID 22565613 DOI: 10.1002/Anie.201202026  0.369
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  0.317
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  0.339
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  0.323
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  0.346
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  0.398
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  0.425
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