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Ashok Sekhar, Ph.D. - Publications

Affiliations: 
2011 University of Wisconsin, Madison, Madison, WI 
Area:
Protein folding in the cell and Biomolecular spectroscopy
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49 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
2024 Jain S, Sekhar A. Transient excited states of the metamorphic protein Mad2 and their implications for function. Proteins. PMID 38221646 DOI: 10.1002/prot.26667  0.318
2023 Kumar A, Madhurima K, Naganathan AN, Vallurupalli P, Sekhar A. Probing excited state Hα chemical shifts in intrinsically disordered proteins with a triple resonance-based CEST experiment: Application to a disorder-to-order switch. Methods (San Diego, Calif.). PMID 37607621 DOI: 10.1016/j.ymeth.2023.08.009  0.333
2022 Jain S, Sekhar A. Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy. Journal of Magnetic Resonance Open. 100034. PMID 35586549 DOI: 10.1016/j.jmro.2022.100034  0.357
2022 Rajendran D, Mitra S, Oikawa H, Madhurima K, Sekhar A, Takahashi S, Naganathan AN. Quantification of Entropic Excluded Volume Effects Driving Crowding-Induced Collapse and Folding of a Disordered Protein. The Journal of Physical Chemistry Letters. 13: 3112-3120. PMID 35357183 DOI: 10.1021/acs.jpclett.2c00316  0.317
2021 Madhurima K, Nandi B, Sekhar A. Metamorphic proteins: the Janus proteins of structural biology. Open Biology. 11: 210012. PMID 33878950 DOI: 10.1098/rsob.210012  0.384
2019 Kumar A, Narayanan V, Sekhar A. Characterizing Post-Translational Modifications and Their Effects on Protein Conformation Using NMR Spectroscopy. Biochemistry. PMID 31682116 DOI: 10.1021/Acs.Biochem.9B00827  0.458
2019 Munshi S, Subramanian S, Ramesh S, Golla H, Kalivarathan D, Kulkarni M, Campos Prieto LA, Sekhar A, Naganathan AN. Engineering Order and Cooperativity in a Disordered Protein. Biochemistry. PMID 31002232 DOI: 10.1021/Acs.Biochem.9B00182  0.443
2019 Sekhar A, Kay LE. An NMR View of Protein Dynamics in Health and Disease. Annual Review of Biophysics. PMID 30901260 DOI: 10.1146/Annurev-Biophys-052118-115647  0.372
2018 Yuwen T, Sekhar A, Baldwin AJ, Vallurupalli P, Kay LE. Measuring Diffusion Constants of Invisible Protein Conformers by Triple-Quantum ¹H CPMG Relaxation Dispersion. Angewandte Chemie (International Ed. in English). PMID 30370966 DOI: 10.1002/Anie.201810868  0.442
2018 Culik RM, Sekhar A, Nagesh J, Deol H, Rumfeldt JAO, Meiering EM, Kay LE. Effects of maturation on the conformational free-energy landscape of SOD1. Proceedings of the National Academy of Sciences of the United States of America. PMID 29483249 DOI: 10.1073/Pnas.1721022115  0.384
2018 Sekhar A, Velyvis A, Zoltsman G, Rosenzweig R, Bouvignies G, Kay LE. Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions. Elife. 7. PMID 29460778 DOI: 10.7554/Elife.32764  0.406
2017 Rajasekaran N, Sekhar A, Naganathan AN. A Universal Pattern in the Percolation and Dissipation of Protein Structural Perturbations. The Journal of Physical Chemistry Letters. PMID 28910120 DOI: 10.1021/Acs.Jpclett.7B02021  0.472
2017 Brady JP, Farber PJ, Sekhar A, Lin YH, Huang R, Bah A, Nott TJ, Chan HS, Baldwin AJ, Forman-Kay JD, Kay LE. Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation. Proceedings of the National Academy of Sciences of the United States of America. PMID 28894006 DOI: 10.1073/Pnas.1706197114  0.416
2017 Sekhar A, Nagesh J, Rosenzweig R, Kay LE. Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data. Protein Science : a Publication of the Protein Society. PMID 28833766 DOI: 10.1002/Pro.3276  0.434
2017 Huang R, Brady JP, Sekhar A, Yuwen T, Kay LE. An enhanced sensitivity methyl (1)H triple-quantum pulse scheme for measuring diffusion constants of macromolecules. Journal of Biomolecular Nmr. PMID 28717997 DOI: 10.1007/S10858-017-0122-9  0.301
2017 Rosenzweig R, Sekhar A, Nagesh J, Kay LE. Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles. Elife. 6. PMID 28708484 DOI: 10.7554/Elife.28030  0.453
2017 Valluruapalli P, Sekhar A, Yuwen T, Kay LE. Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer. Journal of Biomolecular Nmr. PMID 28317074 DOI: 10.1007/S10858-017-0099-4  0.38
2017 Rennella E, Sekhar A, Kay LE. Self-Assembly of Human Profilin-1 Detected by CPMG NMR Spectroscopy. Biochemistry. PMID 28052669 DOI: 10.1021/Acs.Biochem.6B01263  0.414
2017 Rosenzweig R, Sekhar A, Nagesh J, Kay LE. Author response: Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles Elife. DOI: 10.7554/Elife.28030.025  0.31
2016 Yuwen T, Sekhar A, Kay LE. Separating Dipolar and Chemical Exchange Magnetization Transfer Processes in (1) H-CEST. Angewandte Chemie (International Ed. in English). PMID 28035783 DOI: 10.1002/Anie.201610759  0.412
2016 Sekhar A, Rumfeldt JA, Broom HR, Doyle CM, Sobering RE, Meiering EM, Kay LE. Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. PMID 27791136 DOI: 10.1073/Pnas.1611418113  0.394
2016 Yuwen T, Sekhar A, Kay LE. Evaluating the influence of initial magnetization conditions on extracted exchange parameters in NMR relaxation experiments: applications to CPMG and CEST. Journal of Biomolecular Nmr. PMID 27473413 DOI: 10.1007/S10858-016-0045-X  0.325
2016 Sekhar A, Rosenzweig R, Bouvignies G, Kay LE. Hsp70 biases the folding pathways of client proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 27140645 DOI: 10.1073/Pnas.1601846113  0.523
2016 Doyle CM, Rumfeldt JA, Broom HR, Sekhar A, Kay LE, Meiering EM. Concurrent Increases and Decreases in Local Stability and Conformational Heterogeneity in Cu, Zn Superoxide Dismutase Variants Revealed by Temperature-Dependence of Amide Chemical Shifts. Biochemistry. PMID 26849066 DOI: 10.1021/Acs.Biochem.5B01133  0.404
2015 Sekhar A, Rosenzweig R, Bouvignies G, Kay LE. Mapping the conformation of a client protein through the Hsp70 functional cycle. Proceedings of the National Academy of Sciences of the United States of America. 112: 10395-400. PMID 26240333 DOI: 10.1073/Pnas.1508504112  0.482
2015 Lee JH, Zhang D, Hughes C, Okuno Y, Sekhar A, Cavagnero S. Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone. Proceedings of the National Academy of Sciences of the United States of America. 112: E4206-15. PMID 26195753 DOI: 10.1073/Pnas.1505173112  0.704
2015 Long D, Delaglio F, Sekhar A, Kay LE. Probing Invisible, Excited Protein States by Non-Uniformly Sampled Pseudo-4D CEST Spectroscopy. Angewandte Chemie (International Ed. in English). 54: 10507-11. PMID 26178142 DOI: 10.1002/Anie.201504070  0.365
2015 Sekhar A, Bain AD, Rumfeldt JA, Meiering EM, Kay LE. Evolution of magnetization due to asymmetric dimerization: theoretical considerations and application to aberrant oligomers formed by apoSOD1(2SH). Physical Chemistry Chemical Physics : Pccp. PMID 26156673 DOI: 10.1039/C5Cp03044G  0.314
2015 Sekhar A, Rumfeldt JA, Broom HR, Doyle CM, Bouvignies G, Meiering EM, Kay LE. Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways. Elife. 4. PMID 26099300 DOI: 10.7554/Elife.07296  0.399
2015 Kay L, Sekhar A, Rumfeldt J, Broom H, Doyle C, Meiering E. Backbone and sidechain 1H, 13C and 15N chemical shifts for human superoxide dismutase (hSOD1) lacking bound metal and the intrasubunit disulfide bond Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26570  0.34
2015 Lee JH, Zhang D, Hughes C, Okuno Y, Sekhar A, Cavagnero S. Backbone chemical shift assignments for the folded/unfolded drkN SH3 protein at pH 7.2 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25501  0.658
2015 Lee JH, Zhang D, Hughes C, Okuno Y, Sekhar A, Cavagnero S. Backbone chemical shift assignments for the folded/unfolded drkN SH3 protein in the presence of DnaK chaperone at pH 7.2 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25500  0.666
2014 Long D, Sekhar A, Kay LE. Triple resonance-based ¹³C(α) and ¹³C(β) CEST experiments for studies of ms timescale dynamics in proteins. Journal of Biomolecular Nmr. 60: 203-8. PMID 25348177 DOI: 10.1007/S10858-014-9868-5  0.352
2014 Sanchez-Medina C, Sekhar A, Vallurupalli P, Cerminara M, Muñoz V, Kay LE. Probing the free energy landscape of the fast-folding gpW protein by relaxation dispersion NMR. Journal of the American Chemical Society. 136: 7444-51. PMID 24805164 DOI: 10.1021/Ja502705Y  0.477
2014 Sekhar A, Latham MP, Vallurupalli P, Kay LE. Viscosity-dependent kinetics of protein conformational exchange: microviscosity effects and the need for a small viscogen. The Journal of Physical Chemistry. B. 118: 4546-51. PMID 24707961 DOI: 10.1021/Jp501583T  0.462
2014 Latham MP, Sekhar A, Kay LE. Understanding the mechanism of proteasome 20S core particle gating. Proceedings of the National Academy of Sciences of the United States of America. 111: 5532-7. PMID 24706783 DOI: 10.1073/Pnas.1322079111  0.318
2013 Sekhar A, Kay LE. NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers. Proceedings of the National Academy of Sciences of the United States of America. 110: 12867-74. PMID 23868852 DOI: 10.1073/Pnas.1305688110  0.439
2013 Sekhar A, Vallurupalli P, Kay LE. Defining a length scale for millisecond-timescale protein conformational exchange. Proceedings of the National Academy of Sciences of the United States of America. 110: 11391-6. PMID 23801755 DOI: 10.1073/Pnas.1303273110  0.436
2013 Lee JH, Sekhar A, Zhang D, Santiago M, Lam HN, Cavagnero S. Interaction of RNase HD and Sh3 Proteins with DnaK Molecular Chaperone Biophysical Journal. 104: 570a. DOI: 10.1016/J.Bpj.2012.11.3166  0.69
2012 Sekhar A, Vallurupalli P, Kay LE. Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion. Proceedings of the National Academy of Sciences of the United States of America. 109: 19268-73. PMID 23129654 DOI: 10.1073/Pnas.1212036109  0.499
2012 Sekhar A, Lam HN, Cavagnero S. Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system. Protein Science : a Publication of the Protein Society. 21: 1489-502. PMID 22886941 DOI: 10.1002/Pro.2139  0.672
2012 Sekhar A, Santiago M, Lam HN, Lee JH, Cavagnero S. Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery. Protein Science : a Publication of the Protein Society. 21: 1042-55. PMID 22549943 DOI: 10.1002/Pro.2087  0.678
2011 Lee JH, Sekhar A, Cavagnero S. 1H-Detected 13C photo-CIDNP as a sensitivity enhancement tool in solution NMR. Journal of the American Chemical Society. 133: 8062-5. PMID 21548581 DOI: 10.1021/Ja111613C  0.654
2010 Fedyukina DV, Rajagopalan S, Sekhar A, Fulmer EC, Eun YJ, Cavagnero S. Contribution of long-range interactions to the secondary structure of an unfolded globin. Biophysical Journal. 99: L37-9. PMID 20816043 DOI: 10.1016/J.Bpj.2010.06.038  0.658
2009 Sekhar A, Cavagnero S. EPIC- and CHANCE-HSQC: two 15N-photo-CIDNP-enhanced pulse sequences for the sensitive detection of solvent-exposed tryptophan. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 200: 207-13. PMID 19643649 DOI: 10.1016/J.Jmr.2009.07.001  0.634
2009 Sekhar A, Cavagnero S. 1H photo-CIDNP enhancements in heteronuclear correlation NMR spectroscopy. The Journal of Physical Chemistry. B. 113: 8310-8. PMID 19462951 DOI: 10.1021/Jp901000Z  0.645
2009 Sekhar A, Cavagnero S. 1H photo-CIDNP enhancements in heteronuclear correlation NMR spectroscopy (Journal of Physical Chemistry B (2009) 113B (8310)) Journal of Physical Chemistry B. 113: 10548. DOI: 10.1021/jp905605u  0.554
2009 Santiago M, Sekhar A, Cavagnero S. Experimental Studies on Protein Folding in the Presence of the Hsp70 Chaperone System Biophysical Journal. 96: 81a. DOI: 10.1016/J.Bpj.2008.12.321  0.675
2008 Eun YJ, Kurt N, Sekhar A, Cavagnero S. Thermodynamic and kinetic characterization of apoHmpH, a fast-folding bacterial globin. Journal of Molecular Biology. 376: 879-97. PMID 18187151 DOI: 10.1016/J.Jmb.2007.11.038  0.677
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