| Year |
Citation |
Score |
| 2024 |
Harkness RW, Zhao H, Toyama Y, Schuck P, Kay LE. Exploring Host-Guest Interactions within a 600 kDa DegP Protease Cage Complex Using Hydrodynamics Measurements and Methyl-TROSY NMR. Journal of the American Chemical Society. 146: 8242-8259. PMID 38477967 DOI: 10.1021/jacs.3c13247 |
0.343 |
|
| 2023 |
Rennella E, Sahtoe DD, Baker D, Kay LE. Exploiting conformational dynamics to modulate the function of designed proteins. Proceedings of the National Academy of Sciences of the United States of America. 120: e2303149120. PMID 37094170 DOI: 10.1073/pnas.2303149120 |
0.303 |
|
| 2022 |
Toyama Y, Rangadurai AK, Kay LE. Measurement of H transverse relaxation rates in proteins: application to solvent PREs. Journal of Biomolecular Nmr. PMID 36018482 DOI: 10.1007/s10858-022-00401-4 |
0.314 |
|
| 2021 |
Toyama Y, Kay LE. Probing allosteric interactions in homo-oligomeric molecular machines using solution NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34893543 DOI: 10.1073/pnas.2116325118 |
0.302 |
|
| 2021 |
Tiwari VP, Toyama Y, De D, Kay LE, Vallurupalli P. The A39G FF domain folds on a volcano-shaped free energy surface via separate pathways. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34764225 DOI: 10.1073/pnas.2115113118 |
0.301 |
|
| 2020 |
Conicella AE, Huang R, Ripstein ZA, Nguyen A, Wang E, Löhr T, Schuck P, Vendruscolo M, Rubinstein JL, Kay LE. An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase. Proceedings of the National Academy of Sciences of the United States of America. PMID 33028677 DOI: 10.1073/pnas.2013920117 |
0.301 |
|
| 2020 |
Huang R, Ripstein ZA, Rubinstein JL, Kay LE. Probing cooperativity of N-terminal domain orientations in the p97 molecular machine: synergy between NMR and cryo-EM. Angewandte Chemie (International Ed. in English). PMID 32857889 DOI: 10.1002/Anie.202009767 |
0.453 |
|
| 2020 |
Harkness RW, Toyama Y, Kay LE. Analyzing multi-step ligand binding reactions for oligomeric proteins by NMR: Theoretical and computational considerations. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 318: 106802. PMID 32818875 DOI: 10.1016/J.Jmr.2020.106802 |
0.366 |
|
| 2020 |
Yan NL, Santos-Martins D, Rennella E, Sanchez BB, Chen JS, Kay LE, Wilson IA, Morgan GJ, Forli S, Kelly JW. Structural basis for the stabilization of amyloidogenic immunoglobulin light chains by hydantoins. Bioorganic & Medicinal Chemistry Letters. 30: 127356. PMID 32631553 DOI: 10.1016/J.Bmcl.2020.127356 |
0.351 |
|
| 2020 |
Abramov G, Velyvis A, Rennella E, Wong LE, Kay LE. A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle. Proceedings of the National Academy of Sciences of the United States of America. PMID 32457157 DOI: 10.1073/Pnas.2004317117 |
0.379 |
|
| 2020 |
Wong LE, Kim TH, Rennella E, Vallurupalli P, Kay LE. Confronting the Invisible: Assignment of Protein H Chemical Shifts in Cases of Extreme Broadening. The Journal of Physical Chemistry Letters. PMID 32286073 DOI: 10.1021/Acs.Jpclett.0C00747 |
0.402 |
|
| 2020 |
Vahidi S, Ripstein ZA, Juravsky JB, Rennella E, Goldberg AL, Mittermaier AK, Rubinstein JL, Kay LE. An allosteric switch regulates ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR. Proceedings of the National Academy of Sciences of the United States of America. PMID 32123115 DOI: 10.1073/Pnas.1921630117 |
0.666 |
|
| 2020 |
Rennella E, Huang R, Yu Z, Kay LE. Exploring long-range cooperativity in the 20S proteasome core particle from using methyl-TROSY-based NMR. Proceedings of the National Academy of Sciences of the United States of America. PMID 32094174 DOI: 10.1073/Pnas.1920770117 |
0.495 |
|
| 2020 |
Ripstein ZA, Vahidi S, Houry WA, Rubinstein JL, Kay LE. A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. Elife. 9. PMID 31916936 DOI: 10.7554/Elife.52158 |
0.344 |
|
| 2020 |
Wong LE, Kim TH, Muhandiram DR, Forman-Kay JD, Kay LE. NMR experiments for studies of dilute and condensed protein phases: Application to the phase-separating protein CAPRIN1. Journal of the American Chemical Society. PMID 31898464 DOI: 10.1021/Jacs.9B12208 |
0.347 |
|
| 2019 |
Alderson TR, Kay LE. Unveiling invisible protein states with NMR spectroscopy. Current Opinion in Structural Biology. 60: 39-49. PMID 31835059 DOI: 10.1016/J.Sbi.2019.10.008 |
0.433 |
|
| 2019 |
Yuwen T, Kay LE. Revisiting H CPMG relaxation dispersion experiments: a simple modification can eliminate large artifacts. Journal of Biomolecular Nmr. PMID 31646421 DOI: 10.1007/S10858-019-00276-Y |
0.403 |
|
| 2019 |
Rennella E, Morgan GJ, Yan N, Kelly JW, Kay LE. The role of protein thermodynamics and primary structure in fibrillogenesis of variable domains from immunoglobulin light-chains. Journal of the American Chemical Society. PMID 31364359 DOI: 10.1021/Jacs.9B05499 |
0.333 |
|
| 2019 |
Kay LE. The evolution of solution state NMR pulse sequences through the 'eyes' of triple-resonance spectroscopy. Journal of Magnetic Resonance (San Diego, Calif. : 1997). PMID 31324584 DOI: 10.1016/J.Jmr.2019.07.035 |
0.35 |
|
| 2019 |
Morgan GJ, Yan NL, Mortenson DE, Rennella E, Blundon JM, Gwin RM, Lin CY, Stanfield RL, Brown SJ, Rosen H, Spicer TP, Fernandez-Vega V, Merlini G, Kay LE, Wilson IA, et al. Stabilization of amyloidogenic immunoglobulin light chains by small molecules. Proceedings of the National Academy of Sciences of the United States of America. PMID 30971495 DOI: 10.1073/Pnas.1817567116 |
0.332 |
|
| 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 |
0.402 |
|
| 2019 |
Yuwen T, Huang R, Vallurupalli P, Kay LE. A Methyl-TROSY Based ¹H Relaxation Dispersion Experiment for Studies of Conformational Exchange in High Molecular Weight Proteins. Angewandte Chemie (International Ed. in English). PMID 30847985 DOI: 10.1002/Anie.201900241 |
0.544 |
|
| 2019 |
Kay L. NMR Why Bother Biophysical Journal. 116: 297a. DOI: 10.1016/J.Bpj.2018.11.1605 |
0.386 |
|
| 2018 |
Rennella E, Morgan GJ, Kelly JW, Kay LE. Role of domain interactions in the aggregation of full-length immunoglobulin light chains. Proceedings of the National Academy of Sciences of the United States of America. PMID 30598439 DOI: 10.1073/Pnas.1817538116 |
0.355 |
|
| 2018 |
Huang R, Ripstein ZA, Rubinstein JL, Kay LE. Cooperative subunit dynamics modulate p97 function. Proceedings of the National Academy of Sciences of the United States of America. PMID 30584095 DOI: 10.1073/Pnas.1815495116 |
0.456 |
|
| 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 |
0.454 |
|
| 2018 |
Gopalan AB, Yuwen T, Kay LE, Vallurupalli P. A methyl H double quantum CPMG experiment to study protein conformational exchange. Journal of Biomolecular Nmr. PMID 30276607 DOI: 10.1007/S10858-018-0208-Z |
0.372 |
|
| 2018 |
Yuwen T, Bah A, Brady JP, Ferrage F, Bouvignies G, Kay LE. Measuring Solvent Hydrogen Exchange Rates by Multi-Frequency Excitation N CEST. The Journal of Physical Chemistry. B. PMID 30179470 DOI: 10.1021/Acs.Jpcb.8B06820 |
0.415 |
|
| 2018 |
Boisbouvier J, Kay LE. Advanced isotopic labeling for the NMR investigation of challenging proteins and nucleic acids. Journal of Biomolecular Nmr. PMID 30043256 DOI: 10.1007/S10858-018-0199-9 |
0.364 |
|
| 2018 |
Vahidi S, Ripstein ZA, Bonomi M, Yuwen T, Mabanglo MF, Juravsky JB, Rizzolo K, Velyvis A, Houry WA, Vendruscolo M, Rubinstein JL, Kay LE. Reversible inhibition of the ClpP protease via an N-terminal conformational switch. Proceedings of the National Academy of Sciences of the United States of America. PMID 29941580 DOI: 10.1073/Pnas.1805125115 |
0.442 |
|
| 2018 |
Mondal J, Ahalawat N, Pandit S, Kay LE, Vallurupalli P. Atomic resolution mechanism of ligand binding to a solvent inaccessible cavity in T4 lysozyme. Plos Computational Biology. 14: e1006180. PMID 29775455 DOI: 10.1371/Journal.Pcbi.1006180 |
0.358 |
|
| 2018 |
Yuwen T, Bouvignies G, Kay LE. Exploring methods to expedite the recording of CEST datasets using selective pulse excitation. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 292: 1-7. PMID 29753980 DOI: 10.1016/J.Jmr.2018.04.013 |
0.357 |
|
| 2018 |
Augustyniak R, Kay LE. Cotranslocational processing of the protein substrate calmodulin by an AAA+ unfoldase occurs via unfolding and refolding intermediates. Proceedings of the National Academy of Sciences of the United States of America. PMID 29735657 DOI: 10.1073/Pnas.1721811115 |
0.421 |
|
| 2018 |
Yuwen T, Kay LE, Bouvignies G. Dramatic Decrease in CEST Measurement Times Using Multi-site Excitation. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 29663694 DOI: 10.1002/Cphc.201800249 |
0.359 |
|
| 2018 |
Kitevski-LeBlanc JL, Yuwen T, Dyer PN, Rudolph J, Luger K, Kay LE. Investigating the Dynamics of Destabilized Nucleosomes Using Methyl-TROSY NMR. Journal of the American Chemical Society. PMID 29589929 DOI: 10.1021/Jacs.8B00931 |
0.364 |
|
| 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 |
0.345 |
|
| 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 |
0.388 |
|
| 2018 |
Yuwen T, Kay LE. A new class of CEST experiment based on selecting different magnetization components at the start and end of the CEST relaxation element: an application to 1H CEST. Journal of Biomolecular Nmr. PMID 29352366 DOI: 10.1007/S10858-017-0161-2 |
0.377 |
|
| 2018 |
Yuwen T, Brady JP, Kay LE. Probing conformational exchange in weakly interacting, slowly exchanging protein systems via off-resonance R1ρ experiments: Application to studies of protein phase separation. Journal of the American Chemical Society. PMID 29303268 DOI: 10.1021/Jacs.7B09576 |
0.475 |
|
| 2017 |
Huang R, Pérez F, Kay LE. Probing the cooperativity of Thermoplasma acidophilum proteasome core particle gating by NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. PMID 29087330 DOI: 10.1073/Pnas.1712297114 |
0.506 |
|
| 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 |
0.491 |
|
| 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 |
0.406 |
|
| 2017 |
Schütz AK, Rennella E, Kay LE. Exploiting conformational plasticity in the AAA+ protein VCP/p97 to modify function. Proceedings of the National Academy of Sciences of the United States of America. PMID 28760999 DOI: 10.1073/Pnas.1707974114 |
0.361 |
|
| 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 |
0.459 |
|
| 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 |
0.401 |
|
| 2017 |
Yuwen T, Huang R, Kay LE. Probing slow timescale dynamics in proteins using methyl (1)H CEST. Journal of Biomolecular Nmr. PMID 28647789 DOI: 10.1007/S10858-017-0121-X |
0.526 |
|
| 2017 |
Malevanets A, Chong PA, Hansen DF, Rizk P, Sun Y, Lin H, Muhandiram R, Chakrabartty A, Kay LE, Forman-Kay JD, Wodak SJ. Interplay of buried histidine protonation and protein stability in prion misfolding. Scientific Reports. 7: 882. PMID 28408762 DOI: 10.1038/S41598-017-00954-7 |
0.383 |
|
| 2017 |
Kitevski-LeBlanc J, Fradet-Turcotte A, Kukic P, Wilson MD, Portella G, Yuwen T, Panier S, Duan S, Canny MD, van Ingen H, Arrowsmith CH, Rubinstein JL, Vendruscolo M, Durocher D, Kay LE. The RNF168 paralog RNF169 defines a new class of ubiquitylated-histone reader involved in the response to DNA damage. Elife. 6. PMID 28406400 DOI: 10.7554/Elife.23872 |
0.31 |
|
| 2017 |
Ripstein ZA, Huang R, Augustyniak R, Kay LE, Rubinstein JL. Structure of a AAA+ unfoldase in the process of unfolding substrate. Elife. 6. PMID 28390173 DOI: 10.7554/Elife.25754 |
0.485 |
|
| 2017 |
Yuwen T, Kay LE. Longitudinal relaxation optimized amide (1)H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins. Journal of Biomolecular Nmr. PMID 28357518 DOI: 10.1007/S10858-017-0104-Y |
0.436 |
|
| 2017 |
Chojnacki M, Mansour W, Hameed DS, Singh RK, El Oualid F, Rosenzweig R, Nakasone MA, Yu Z, Glaser F, Kay LE, Fushman D, Ovaa H, Glickman MH. Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit. Cell Chemical Biology. PMID 28330605 DOI: 10.1016/J.Chembiol.2017.02.013 |
0.338 |
|
| 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 |
0.401 |
|
| 2017 |
Borkar AN, Vallurupalli P, Camilloni C, Kay LE, Vendruscolo M. Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop. Physical Chemistry Chemical Physics : Pccp. PMID 28067358 DOI: 10.1039/C6Cp08313G |
0.315 |
|
| 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 |
0.394 |
|
| 2017 |
Ripstein ZA, Huang R, Augustyniak R, Kay LE, Rubinstein JL. Author response: Structure of a AAA+ unfoldase in the process of unfolding substrate Elife. DOI: 10.7554/Elife.25754.026 |
0.386 |
|
| 2016 |
Vallurupalli P, Chakrabarti N, Pomès R, Kay LE. Atomistic picture of conformational exchange in a T4 lysozyme cavity mutant: an experiment-guided molecular dynamics study. Chemical Science. 7: 3602-3613. PMID 30008994 DOI: 10.1039/C5Sc03886C |
0.436 |
|
| 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 |
0.41 |
|
| 2016 |
Schuetz AK, Kay LE. A Dynamic molecular basis for malfunction in disease mutants of p97/VCP. Elife. 5. PMID 27828775 DOI: 10.7554/Elife.20143 |
0.347 |
|
| 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 |
0.377 |
|
| 2016 |
Yuwen T, Vallurupalli P, Kay LE. Enhancing the Sensitivity of CPMG Relaxation Dispersion to Conformational Exchange Processes by Multiple-Quantum Spectroscopy. Angewandte Chemie (International Ed. in English). PMID 27527986 DOI: 10.1002/Anie.201605843 |
0.431 |
|
| 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 |
0.339 |
|
| 2016 |
Huang R, Ripstein ZA, Augustyniak R, Lazniewski M, Ginalski K, Kay LE, Rubinstein JL. Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study. Proceedings of the National Academy of Sciences of the United States of America. PMID 27402735 DOI: 10.1073/Pnas.1603980113 |
0.528 |
|
| 2016 |
Chan SW, Yau J, Ing C, Liu K, Farber P, Won A, Bhandari V, Kara-Yacoubian N, Seraphim TV, Chakrabarti N, Kay LE, Yip CM, Pomès R, Sharpe S, Houry WA. Mechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone. Structure (London, England : 1993). PMID 27265850 DOI: 10.1016/J.Str.2016.05.002 |
0.355 |
|
| 2016 |
Rennella E, Schuetz AK, Kay LE. Quantitative measurement of exchange dynamics in proteins via (13)C relaxation dispersion of (13)CHD2-labeled samples. Journal of Biomolecular Nmr. PMID 27251650 DOI: 10.1007/S10858-016-0038-9 |
0.449 |
|
| 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 |
0.446 |
|
| 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 |
0.365 |
|
| 2015 |
Kay LE. New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy. Journal of Molecular Biology. PMID 26707200 DOI: 10.1016/J.Jmb.2015.11.028 |
0.435 |
|
| 2015 |
Rosenzweig R, Kay LE. Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation. Journal of the American Chemical Society. PMID 26651836 DOI: 10.1021/Jacs.5B11346 |
0.423 |
|
| 2015 |
Rosenzweig R, Farber P, Velyvis A, Rennella E, Latham MP, Kay LE. ClpB N-terminal domain plays a regulatory role in protein disaggregation. Proceedings of the National Academy of Sciences of the United States of America. PMID 26621746 DOI: 10.1073/Pnas.1512783112 |
0.751 |
|
| 2015 |
Rennella E, Huang R, Velyvis A, Kay LE. (13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins. Journal of Biomolecular Nmr. 63: 187-99. PMID 26271302 DOI: 10.1007/S10858-015-9974-Z |
0.58 |
|
| 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 |
0.423 |
|
| 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 |
0.397 |
|
| 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 |
0.354 |
|
| 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 |
0.354 |
|
| 2015 |
Ahlner A, Andresen C, Khan SN, Kay LE, Lundström P. Fractional enrichment of proteins using [2-(13)C]-glycerol as the carbon source facilitates measurement of excited state (13)Cα chemical shifts with improved sensitivity. Journal of Biomolecular Nmr. 62: 341-51. PMID 25990019 DOI: 10.1007/S10858-015-9948-1 |
0.453 |
|
| 2015 |
Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD. Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. Nature. 519: 106-9. PMID 25533957 DOI: 10.1038/Nature13999 |
0.344 |
|
| 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 |
0.326 |
|
| 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 |
0.37 |
|
| 2014 |
Latham MP, Kay LE. A similar in vitro and in cell lysate folding intermediate for the FF domain. Journal of Molecular Biology. 426: 3214-20. PMID 25083919 DOI: 10.1016/J.Jmb.2014.07.019 |
0.753 |
|
| 2014 |
Rosenzweig R, Kay LE. Bringing dynamic molecular machines into focus by methyl-TROSY NMR. Annual Review of Biochemistry. 83: 291-315. PMID 24905784 DOI: 10.1146/Annurev-Biochem-060713-035829 |
0.344 |
|
| 2014 |
Long D, Bouvignies G, Kay LE. Measuring hydrogen exchange rates in invisible protein excited states. Proceedings of the National Academy of Sciences of the United States of America. 111: 8820-5. PMID 24889628 DOI: 10.1073/Pnas.1405011111 |
0.417 |
|
| 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 |
0.429 |
|
| 2014 |
Hansen AL, Kay LE. Measurement of histidine pKa values and tautomer populations in invisible protein states. Proceedings of the National Academy of Sciences of the United States of America. 111: E1705-12. PMID 24733918 DOI: 10.1073/Pnas.1400577111 |
0.476 |
|
| 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 |
0.751 |
|
| 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 |
0.705 |
|
| 2014 |
Kay LE, Frydman L. A special "JMR Perspectives" issue: foresights in biomolecular solution-state NMR spectroscopy - from spin gymnastics to structure and dynamics. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 1-2. PMID 24656075 DOI: 10.1016/J.Jmr.2014.01.010 |
0.387 |
|
| 2014 |
Shi L, Kay LE. Tracing an allosteric pathway regulating the activity of the HslV protease. Proceedings of the National Academy of Sciences of the United States of America. 111: 2140-5. PMID 24469799 DOI: 10.1073/Pnas.1318476111 |
0.416 |
|
| 2014 |
Wang X, Vallurupalli P, Vu A, Lee K, Sun S, Bai WJ, Wu C, Zhou H, Shea JE, Kay LE, Dahlquist FW. The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity. Biochemistry. 53: 855-61. PMID 24444349 DOI: 10.1021/Bi4012379 |
0.357 |
|
| 2014 |
Bouvignies G, Vallurupalli P, Kay LE. Visualizing side chains of invisible protein conformers by solution NMR. Journal of Molecular Biology. 426: 763-74. PMID 24211467 DOI: 10.1016/J.Jmb.2013.10.041 |
0.497 |
|
| 2014 |
Bouvignies G, Vallurupalli P, Kay L. Aliphatic 13C Chemical Shift Assignments For the Unfolded State of the Fyn SH3 Domain G48A Mutant Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19590 |
0.338 |
|
| 2013 |
Pocanschi CL, Ehsani S, Mehrabian M, Wille H, Reginold W, Trimble WS, Wang H, Yee A, Arrowsmith CH, Bozóky Z, Kay LE, Forman-Kay JD, Rini JM, Schmitt-Ulms G. The ZIP5 ectodomain co-localizes with PrP and may acquire a PrP-like fold that assembles into a dimer. Plos One. 8: e72446. PMID 24039764 DOI: 10.1371/Journal.Pone.0072446 |
0.37 |
|
| 2013 |
Long D, Marshall CB, Bouvignies G, Mazhab-Jafari MT, Smith MJ, Ikura M, Kay LE. A comparative CEST NMR study of slow conformational dynamics of small GTPases complexed with GTP and GTP analogues. Angewandte Chemie (International Ed. in English). 52: 10771-4. PMID 24039022 DOI: 10.1002/Anie.201305434 |
0.373 |
|
| 2013 |
Mainz A, Religa TL, Sprangers R, Linser R, Kay LE, Reif B. NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond. Angewandte Chemie (International Ed. in English). 52: 8746-51. PMID 23873792 DOI: 10.1002/Anie.201301215 |
0.403 |
|
| 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 |
0.443 |
|
| 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 |
0.441 |
|
| 2013 |
Velyvis A, Kay LE. Measurement of active site ionization equilibria in the 670 kDa proteasome core particle using methyl-TROSY NMR. Journal of the American Chemical Society. 135: 9259-62. PMID 23800213 DOI: 10.1021/Ja403091C |
0.334 |
|
| 2013 |
Vallurupalli P, Bouvignies G, Kay LE. A computational study of the effects of (13) C-(13) C scalar couplings on (13) C CEST NMR spectra: towards studies on a uniformly (13) C-labeled protein. Chembiochem : a European Journal of Chemical Biology. 14: 1709-13. PMID 23784752 DOI: 10.1002/Cbic.201300230 |
0.422 |
|
| 2013 |
Tugarinov V, Kay LE. Estimating side-chain order in [U-2H;13CH3]-labeled high molecular weight proteins from analysis of HMQC/HSQC spectra. The Journal of Physical Chemistry. B. 117: 3571-7. PMID 23458382 DOI: 10.1021/Jp401088C |
0.41 |
|
| 2013 |
Vallurupalli P, Kay LE. Probing slow chemical exchange at carbonyl sites in proteins by chemical exchange saturation transfer NMR spectroscopy. Angewandte Chemie (International Ed. in English). 52: 4156-9. PMID 23450751 DOI: 10.1002/Anie.201209118 |
0.388 |
|
| 2013 |
Mazhab-Jafari MT, Marshall CB, Stathopulos PB, Kobashigawa Y, Stambolic V, Kay LE, Inagaki F, Ikura M. Membrane-dependent modulation of the mTOR activator Rheb: NMR observations of a GTPase tethered to a lipid-bilayer nanodisc. Journal of the American Chemical Society. 135: 3367-70. PMID 23409921 DOI: 10.1021/Ja312508W |
0.311 |
|
| 2013 |
Rosenzweig R, Moradi S, Zarrine-Afsar A, Glover JR, Kay LE. Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. Science (New York, N.Y.). 339: 1080-3. PMID 23393091 DOI: 10.1126/Science.1233066 |
0.405 |
|
| 2013 |
Hansen AL, Bouvignies G, Kay LE. Probing slowly exchanging protein systems via ¹³Cα-CEST: monitoring folding of the Im7 protein. Journal of Biomolecular Nmr. 55: 279-89. PMID 23386228 DOI: 10.1007/S10858-013-9711-4 |
0.425 |
|
| 2013 |
Baldwin AJ, Kay LE. An R(1Ï) expression for a spin in chemical exchange between two sites with unequal transverse relaxation rates. Journal of Biomolecular Nmr. 55: 211-8. PMID 23340732 DOI: 10.1007/S10858-012-9694-6 |
0.332 |
|
| 2013 |
Latham MP, Kay LE. Probing non-specific interactions of Ca²âº-calmodulin in E. coli lysate. Journal of Biomolecular Nmr. 55: 239-47. PMID 23324860 DOI: 10.1007/S10858-013-9705-2 |
0.733 |
|
| 2013 |
Mainz A, Religa TL, Sprangers R, Linser R, Kay LE, Reif B. NMR-Spektroskopie an löslichen Proteinkomplexen mit Molekulargewicht im Mega-Dalton-Bereich Angewandte Chemie. 125: 8909-8914. DOI: 10.1002/Ange.201301215 |
0.385 |
|
| 2012 |
Bouvignies G, Kay LE. Measurement of proton chemical shifts in invisible states of slowly exchanging protein systems by chemical exchange saturation transfer. The Journal of Physical Chemistry. B. 116: 14311-7. PMID 23194058 DOI: 10.1021/Jp311109U |
0.438 |
|
| 2012 |
Ruschak AM, Kay LE. Proteasome allostery as a population shift between interchanging conformers. Proceedings of the National Academy of Sciences of the United States of America. 109: E3454-62. PMID 23150576 DOI: 10.1073/Pnas.1213640109 |
0.378 |
|
| 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 |
0.434 |
|
| 2012 |
Latham MP, Kay LE. Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. coli lysate. Plos One. 7: e48226. PMID 23118958 DOI: 10.1371/Journal.Pone.0048226 |
0.747 |
|
| 2012 |
Velyvis A, Ruschak AM, Kay LE. An economical method for production of (2)H, (13)CH3-threonine for solution NMR studies of large protein complexes: application to the 670 kDa proteasome. Plos One. 7: e43725. PMID 22984438 DOI: 10.1371/Journal.Pone.0043725 |
0.447 |
|
| 2012 |
Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, ... ... Kay LE, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/Nsmb.2371 |
0.742 |
|
| 2012 |
Baldwin AJ, Walsh P, Hansen DF, Hilton GR, Benesch JL, Sharpe S, Kay LE. Probing dynamic conformations of the high-molecular-weight αB-crystallin heat shock protein ensemble by NMR spectroscopy. Journal of the American Chemical Society. 134: 15343-50. PMID 22916679 DOI: 10.1021/Ja307874R |
0.457 |
|
| 2012 |
Baldwin AJ, Kay LE. Structural biology: Dynamic binding. Nature. 488: 165-6. PMID 22874961 DOI: 10.1038/488165A |
0.407 |
|
| 2012 |
KupÄe E, Kay LE. Parallel acquisition of multi-dimensional spectra in protein NMR. Journal of Biomolecular Nmr. 54: 1-7. PMID 22802131 DOI: 10.1007/S10858-012-9646-1 |
0.379 |
|
| 2012 |
Bouvignies G, Kay LE. A 2D ¹³C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding. Journal of Biomolecular Nmr. 53: 303-10. PMID 22689067 DOI: 10.1007/S10858-012-9640-7 |
0.474 |
|
| 2012 |
Korzhnev DM, Religa TL, Kay LE. Transiently populated intermediate functions as a branching point of the FF domain folding pathway. Proceedings of the National Academy of Sciences of the United States of America. 109: 17777-82. PMID 22647611 DOI: 10.1073/Pnas.1201799109 |
0.427 |
|
| 2012 |
Vallurupalli P, Bouvignies G, Kay LE. Studying "invisible" excited protein states in slow exchange with a major state conformation. Journal of the American Chemical Society. 134: 8148-61. PMID 22554188 DOI: 10.1021/Ja3001419 |
0.403 |
|
| 2012 |
Neudecker P, Robustelli P, Cavalli A, Walsh P, Lundström P, Zarrine-Afsar A, Sharpe S, Vendruscolo M, Kay LE. Structure of an intermediate state in protein folding and aggregation. Science (New York, N.Y.). 336: 362-6. PMID 22517863 DOI: 10.1126/Science.1214203 |
0.376 |
|
| 2012 |
Baldwin AJ, Kay LE. Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R(1Ï): an application to αB-crystallin. Journal of Biomolecular Nmr. 53: 1-12. PMID 22476760 DOI: 10.1007/S10858-012-9617-6 |
0.421 |
|
| 2012 |
Hansen AL, Lundström P, Velyvis A, Kay LE. Quantifying millisecond exchange dynamics in proteins by CPMG relaxation dispersion NMR using side-chain 1H probes. Journal of the American Chemical Society. 134: 3178-89. PMID 22300166 DOI: 10.1021/Ja210711V |
0.464 |
|
| 2012 |
Barette J, Velyvis A, Religa TL, Korzhnev DM, Kay LE. Cross-validation of the structure of a transiently formed and low populated FF domain folding intermediate determined by relaxation dispersion NMR and CS-Rosetta. The Journal of Physical Chemistry. B. 116: 6637-44. PMID 22148426 DOI: 10.1021/Jp209974F |
0.41 |
|
| 2012 |
Yang D, Kay LE. Improved 1HN-detected triple resonance TROSY-based experiments. Journal of Biomolecular Nmr. 13: 3-10. PMID 21080259 DOI: 10.1023/A:1008329230975 |
0.371 |
|
| 2012 |
Konrat R, Yang D, Kay LE. A 4D TROSY-based pulse scheme for correlating 1HNi,15Ni,13Calphai,13C'i-1 chemical shifts in high molecular weight, 15N,13C, 2H labeled proteins. Journal of Biomolecular Nmr. 15: 309-13. PMID 20703855 DOI: 10.1023/A:1008310617047 |
0.423 |
|
| 2012 |
Muhandiram DR, Johnson PE, Yang D, Zhang O, McIntosh LP, Kay LE. Specific (15)N, NH correlations for residues in(15) N, (13)C and fractionally deuterated proteins that immediately follow methyl-containing amino acids. Journal of Biomolecular Nmr. 10: 283-8. PMID 20700832 DOI: 10.1023/A:1018301818803 |
0.424 |
|
| 2012 |
McIntosh LP, Brun E, Kay LE. Stereospecific assignment of the NH2 resonances from the primary amides of asparagine and glutamine side chains in isotopically labeled proteins. Journal of Biomolecular Nmr. 9: 306-12. PMID 20680662 DOI: 10.1023/A:1018635110491 |
0.421 |
|
| 2012 |
Kay L. Seeing the Invisible by Solution NMR Biophysical Journal. 102: 42a. DOI: 10.1016/J.Bpj.2011.11.261 |
0.402 |
|
| 2011 |
Baldwin AJ, Lioe H, Hilton GR, Baker LA, Rubinstein JL, Kay LE, Benesch JL. The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture. Structure (London, England : 1993). 19: 1855-63. PMID 22153508 DOI: 10.1016/J.Str.2011.09.015 |
0.314 |
|
| 2011 |
Kay LE. NMR studies of protein structure and dynamics. 2005. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 213: 477-91. PMID 22152364 DOI: 10.1016/j.jmr.2011.09.009 |
0.319 |
|
| 2011 |
Kay LE, Ikura M, Tschudin R, Bax A. Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins. 1990. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 213: 423-41. PMID 22152361 DOI: 10.1016/J.Jmr.2011.09.004 |
0.551 |
|
| 2011 |
Vallurupalli P, Bouvignies G, Kay LE. Increasing the exchange time-scale that can be probed by CPMG relaxation dispersion NMR. The Journal of Physical Chemistry. B. 115: 14891-900. PMID 22077866 DOI: 10.1021/Jp209610V |
0.426 |
|
| 2011 |
Sun H, Kay LE, Tugarinov V. An optimized relaxation-based coherence transfer NMR experiment for the measurement of side-chain order in methyl-protonated, highly deuterated proteins. The Journal of Physical Chemistry. B. 115: 14878-84. PMID 22040035 DOI: 10.1021/Jp209049K |
0.424 |
|
| 2011 |
Kay LE. NMR studies of protein structure and dynamics - a look backwards and forwards. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 213: 492-4. PMID 21885309 DOI: 10.1016/J.Jmr.2011.08.010 |
0.411 |
|
| 2011 |
Bouvignies G, Vallurupalli P, Hansen DF, Correia BE, Lange O, Bah A, Vernon RM, Dahlquist FW, Baker D, Kay LE. Solution structure of a minor and transiently formed state of a T4 lysozyme mutant. Nature. 477: 111-4. PMID 21857680 DOI: 10.1038/Nature10349 |
0.385 |
|
| 2011 |
Baldwin AJ, Hilton GR, Lioe H, Bagnéris C, Benesch JL, Kay LE. Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus. Journal of Molecular Biology. 413: 310-20. PMID 21839749 DOI: 10.1016/J.Jmb.2011.07.017 |
0.414 |
|
| 2011 |
Baldwin AJ, Lioe H, Robinson CV, Kay LE, Benesch JL. αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics. Journal of Molecular Biology. 413: 297-309. PMID 21839090 DOI: 10.1016/J.Jmb.2011.07.016 |
0.384 |
|
| 2011 |
Kato H, van Ingen H, Zhou BR, Feng H, Bustin M, Kay LE, Bai Y. Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR. Proceedings of the National Academy of Sciences of the United States of America. 108: 12283-8. PMID 21730181 DOI: 10.1073/Pnas.1105848108 |
0.36 |
|
| 2011 |
Hansen AL, Kay LE. Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups. Journal of Biomolecular Nmr. 50: 347-55. PMID 21681650 DOI: 10.1007/S10858-011-9520-6 |
0.459 |
|
| 2011 |
Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE. Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study. Journal of the American Chemical Society. 133: 10974-82. PMID 21639149 DOI: 10.1021/Ja203686T |
0.425 |
|
| 2011 |
Religa TL, Ruschak AM, Rosenzweig R, Kay LE. Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: applications to the proteasome and to the ClpP protease. Journal of the American Chemical Society. 133: 9063-8. PMID 21557628 DOI: 10.1021/Ja202259A |
0.462 |
|
| 2011 |
Hansen DF, Kay LE. Determining valine side-chain rotamer conformations in proteins from methyl 13C chemical shifts: application to the 360 kDa half-proteasome. Journal of the American Chemical Society. 133: 8272-81. PMID 21545099 DOI: 10.1021/Ja2014532 |
0.427 |
|
| 2011 |
Kay LE. Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 210: 159-70. PMID 21458338 DOI: 10.1016/J.Jmr.2011.03.008 |
0.406 |
|
| 2011 |
Bouvignies G, Vallurupalli P, Cordes MH, Hansen DF, Kay LE. Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy. Journal of Biomolecular Nmr. 50: 13-8. PMID 21424227 DOI: 10.1007/S10858-011-9498-0 |
0.411 |
|
| 2011 |
Bouvignies G, Hansen DF, Vallurupalli P, Kay LE. Divided-evolution-based pulse scheme for quantifying exchange processes in proteins: powerful complement to relaxation dispersion experiments. Journal of the American Chemical Society. 133: 1935-45. PMID 21244030 DOI: 10.1021/Ja109589Y |
0.415 |
|
| 2011 |
Neudecker P, Robustelli P, Cavalli A, Vendruscolo M, Kay L. Folding Intermediate of the Fyn SH3 A39V/N53P/V55L from NMR Relaxation Dispersion Experiments Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17149 |
0.329 |
|
| 2010 |
KupÄe Ä’, Kay LE, Freeman R. Detecting the "afterglow" of 13C NMR in proteins using multiple receivers. Journal of the American Chemical Society. 132: 18008-11. PMID 21126087 DOI: 10.1021/Ja1080025 |
0.407 |
|
| 2010 |
Ruschak AM, Velyvis A, Kay LE. A simple strategy for ¹³C, ¹H labeling at the Ile-γ2 methyl position in highly deuterated proteins. Journal of Biomolecular Nmr. 48: 129-35. PMID 20949307 DOI: 10.1007/S10858-010-9449-1 |
0.368 |
|
| 2010 |
Ruschak AM, Religa TL, Breuer S, Witt S, Kay LE. The proteasome antechamber maintains substrates in an unfolded state. Nature. 467: 868-71. PMID 20944750 DOI: 10.1038/Nature09444 |
0.385 |
|
| 2010 |
Korzhnev DM, Religa TL, Banachewicz W, Fersht AR, Kay LE. A transient and low-populated protein-folding intermediate at atomic resolution. Science (New York, N.Y.). 329: 1312-6. PMID 20829478 DOI: 10.1126/Science.1191723 |
0.456 |
|
| 2010 |
Baldwin AJ, Religa TL, Hansen DF, Bouvignies G, Kay LE. 13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics. Journal of the American Chemical Society. 132: 10992-5. PMID 20698653 DOI: 10.1021/Ja104578N |
0.421 |
|
| 2010 |
Hansen DF, Neudecker P, Kay LE. Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts. Journal of the American Chemical Society. 132: 7589-91. PMID 20465253 DOI: 10.1021/Ja102090Z |
0.434 |
|
| 2010 |
Bouvignies G, Korzhnev DM, Neudecker P, Hansen DF, Cordes MH, Kay LE. A simple method for measuring signs of (1)H (N) chemical shift differences between ground and excited protein states. Journal of Biomolecular Nmr. 47: 135-41. PMID 20428928 DOI: 10.1007/S10858-010-9418-8 |
0.461 |
|
| 2010 |
Religa TL, Kay LE. Optimal methyl labeling for studies of supra-molecular systems. Journal of Biomolecular Nmr. 47: 163-9. PMID 20422256 DOI: 10.1007/S10858-010-9419-7 |
0.307 |
|
| 2010 |
Religa TL, Sprangers R, Kay LE. Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR. Science (New York, N.Y.). 328: 98-102. PMID 20360109 DOI: 10.1126/Science.1184991 |
0.387 |
|
| 2010 |
Stengel F, Baldwin AJ, Painter AJ, Jaya N, Basha E, Kay LE, Vierling E, Robinson CV, Benesch JL. Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. Proceedings of the National Academy of Sciences of the United States of America. 107: 2007-12. PMID 20133845 DOI: 10.1073/Pnas.0910126107 |
0.385 |
|
| 2010 |
Auer R, Hansen DF, Neudecker P, Korzhnev DM, Muhandiram DR, Konrat R, Kay LE. Measurement of signs of chemical shift differences between ground and excited protein states: a comparison between H(S/M)QC and R1rho methods. Journal of Biomolecular Nmr. 46: 205-16. PMID 20033258 DOI: 10.1007/S10858-009-9394-Z |
0.425 |
|
| 2010 |
Hansen DF, Neudecker P, Vallurupalli P, Mulder FA, Kay LE. Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion. Journal of the American Chemical Society. 132: 42-3. PMID 20000605 DOI: 10.1021/Ja909294N |
0.721 |
|
| 2010 |
Ruschak AM, Kay LE. Methyl groups as probes of supra-molecular structure, dynamics and function. Journal of Biomolecular Nmr. 46: 75-87. PMID 19784810 DOI: 10.1007/S10858-009-9376-1 |
0.407 |
|
| 2010 |
Mittag T, Kay LE, Forman-Kay JD. Protein dynamics and conformational disorder in molecular recognition. Journal of Molecular Recognition : Jmr. 23: 105-16. PMID 19585546 DOI: 10.1002/Jmr.961 |
0.388 |
|
| 2009 |
Lundström P, Vallurupalli P, Hansen DF, Kay LE. Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy. Nature Protocols. 4: 1641-8. PMID 19876024 DOI: 10.1038/Nprot.2009.118 |
0.477 |
|
| 2009 |
Velyvis A, Schachman HK, Kay LE. Assignment of Ile, Leu, and Val methyl correlations in supra-molecular systems: an application to aspartate transcarbamoylase. Journal of the American Chemical Society. 131: 16534-43. PMID 19860411 DOI: 10.1021/Ja906978R |
0.404 |
|
| 2009 |
Mittermaier AK, Kay LE. Observing biological dynamics at atomic resolution using NMR. Trends in Biochemical Sciences. 34: 601-11. PMID 19846313 DOI: 10.1016/J.Tibs.2009.07.004 |
0.672 |
|
| 2009 |
Hansen DF, Feng H, Zhou Z, Bai Y, Kay LE. Selective characterization of microsecond motions in proteins by NMR relaxation. Journal of the American Chemical Society. 131: 16257-65. PMID 19842628 DOI: 10.1021/Ja906842S |
0.406 |
|
| 2009 |
Baldwin AJ, Kay LE. NMR spectroscopy brings invisible protein states into focus. Nature Chemical Biology. 5: 808-14. PMID 19841630 DOI: 10.1038/Nchembio.238 |
0.425 |
|
| 2009 |
Murphy JM, Hansen DF, Wiesner S, Muhandiram DR, Borg M, Smith MJ, Sicheri F, Kay LE, Forman-Kay JD, Pawson T. Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays. Journal of Molecular Biology. 393: 409-24. PMID 19715701 DOI: 10.1016/J.Jmb.2009.08.049 |
0.36 |
|
| 2009 |
Hansen DF, Vallurupalli P, Kay LE. Measurement of methyl group motional parameters of invisible, excited protein states by NMR spectroscopy. Journal of the American Chemical Society. 131: 12745-54. PMID 19685870 DOI: 10.1021/Ja903897E |
0.446 |
|
| 2009 |
Baldwin AJ, Hansen DF, Vallurupalli P, Kay LE. Measurement of methyl axis orientations in invisible, excited states of proteins by relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 131: 11939-48. PMID 19627152 DOI: 10.1021/Ja903896P |
0.47 |
|
| 2009 |
Auer R, Neudecker P, Muhandiram DR, Lundström P, Hansen DF, Konrat R, Kay LE. Measuring the signs of 1H(alpha) chemical shift differences between ground and excited protein states by off-resonance spin-lock R(1rho) NMR spectroscopy. Journal of the American Chemical Society. 131: 10832-3. PMID 19606858 DOI: 10.1021/Ja904315M |
0.431 |
|
| 2009 |
van Ingen H, Korzhnev DM, Kay LE. An analysis of the effects of 1HN-(1)HN dipolar couplings on the measurement of amide bond vector orientations in invisible protein states by relaxation dispersion NMR. The Journal of Physical Chemistry. B. 113: 9968-77. PMID 19569643 DOI: 10.1021/Jp902793Y |
0.406 |
|
| 2009 |
Lundström P, Lin H, Kay LE. Measuring 13Cbeta chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy. Journal of Biomolecular Nmr. 44: 139-55. PMID 19448976 DOI: 10.1007/S10858-009-9321-3 |
0.431 |
|
| 2009 |
Hansen DF, Zhou Z, Feng H, Miller Jenkins LM, Bai Y, Kay LE. Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy. Journal of Molecular Biology. 387: 1-9. PMID 19385041 DOI: 10.1016/J.Jmb.2009.01.009 |
0.304 |
|
| 2009 |
Vallurupalli P, Hansen DF, Lundström P, Kay LE. CPMG relaxation dispersion NMR experiments measuring glycine 1H alpha and 13C alpha chemical shifts in the 'invisible' excited states of proteins. Journal of Biomolecular Nmr. 45: 45-55. PMID 19319480 DOI: 10.1007/S10858-009-9310-6 |
0.389 |
|
| 2009 |
Velyvis A, Schachman HK, Kay LE. Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase. Journal of Molecular Biology. 387: 540-7. PMID 19302799 DOI: 10.1016/J.Jmb.2009.01.066 |
0.407 |
|
| 2009 |
Neudecker P, Lundström P, Kay LE. Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding. Biophysical Journal. 96: 2045-54. PMID 19289032 DOI: 10.1016/J.Bpj.2008.12.3907 |
0.457 |
|
| 2009 |
Lundström P, Hansen DF, Vallurupalli P, Kay LE. Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 131: 1915-26. PMID 19152327 DOI: 10.1021/Ja807796A |
0.499 |
|
| 2009 |
Korzhnev DM, Bezsonova I, Lee S, Chalikian TV, Kay LE. Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy. Journal of Molecular Biology. 386: 391-405. PMID 19111555 DOI: 10.1016/J.Jmb.2008.11.055 |
0.433 |
|
| 2008 |
Mittag T, Orlicky S, Choy WY, Tang X, Lin H, Sicheri F, Kay LE, Tyers M, Forman-Kay JD. Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. Proceedings of the National Academy of Sciences of the United States of America. 105: 17772-7. PMID 19008353 DOI: 10.1073/Pnas.0809222105 |
0.338 |
|
| 2008 |
Lundström P, Hansen DF, Kay LE. Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples. Journal of Biomolecular Nmr. 42: 35-47. PMID 18762869 DOI: 10.1007/S10858-008-9260-4 |
0.425 |
|
| 2008 |
Vallurupalli P, Hansen DF, Kay LE. Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 105: 11766-71. PMID 18701719 DOI: 10.1073/Pnas.0804221105 |
0.483 |
|
| 2008 |
Zhou Z, Feng H, Hansen DF, Kato H, Luk E, Freedberg DI, Kay LE, Wu C, Bai Y. NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B. Nature Structural & Molecular Biology. 15: 868-9. PMID 18641662 DOI: 10.1038/Nsmb.1465 |
0.326 |
|
| 2008 |
Hansen DF, Vallurupalli P, Kay LE. Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states. Journal of Biomolecular Nmr. 41: 113-20. PMID 18574698 DOI: 10.1007/S10858-008-9251-5 |
0.418 |
|
| 2008 |
Sprangers R, Li X, Mao X, Rubinstein JL, Schimmer AD, Kay LE. TROSY-based NMR evidence for a novel class of 20S proteasome inhibitors. Biochemistry. 47: 6727-34. PMID 18540636 DOI: 10.1021/Bi8005913 |
0.345 |
|
| 2008 |
Hass MA, Hansen DF, Christensen HE, Led JJ, Kay LE. Characterization of conformational exchange of a histidine side chain: protonation, rotamerization, and tautomerization of His61 in plastocyanin from Anabaena variabilis. Journal of the American Chemical Society. 130: 8460-70. PMID 18540585 DOI: 10.1021/Ja801330H |
0.466 |
|
| 2008 |
Hansen DF, Vallurupalli P, Kay LE. Quantifying two-bond 1HN-13CO and one-bond 1H(alpha)-13C(alpha) dipolar couplings of invisible protein states by spin-state selective relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 130: 8397-405. PMID 18528998 DOI: 10.1021/Ja801005N |
0.448 |
|
| 2008 |
Korzhnev DM, Kay LE. Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding. Accounts of Chemical Research. 41: 442-51. PMID 18275162 DOI: 10.1021/Ar700189Y |
0.483 |
|
| 2008 |
Vallurupalli P, Hansen DF, Kay LE. Probing structure in invisible protein states with anisotropic NMR chemical shifts. Journal of the American Chemical Society. 130: 2734-5. PMID 18257570 DOI: 10.1021/Ja710817G |
0.44 |
|
| 2008 |
Hansen DF, Vallurupalli P, Lundström P, Neudecker P, Kay LE. Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do? Journal of the American Chemical Society. 130: 2667-75. PMID 18237174 DOI: 10.1021/Ja078337P |
0.465 |
|
| 2008 |
Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A. Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. Journal of Biomolecular Nmr. 40: 95-106. PMID 18008171 DOI: 10.1007/S10858-007-9211-5 |
0.568 |
|
| 2008 |
Hansen DF, Vallurupalli P, Kay LE. An improved 15N relaxation dispersion experiment for the measurement of millisecond time-scale dynamics in proteins. The Journal of Physical Chemistry. B. 112: 5898-904. PMID 18001083 DOI: 10.1021/Jp074793O |
0.373 |
|
| 2007 |
Vallurupalli P, Hansen DF, Stollar E, Meirovitch E, Kay LE. Measurement of bond vector orientations in invisible excited states of proteins. Proceedings of the National Academy of Sciences of the United States of America. 104: 18473-7. PMID 18006656 DOI: 10.1073/Pnas.0708296104 |
0.469 |
|
| 2007 |
Sprangers R, Kay LE. Probing supramolecular structure from measurement of methyl (1)H-(13)C residual dipolar couplings. Journal of the American Chemical Society. 129: 12668-9. PMID 17910459 DOI: 10.1021/Ja075846I |
0.43 |
|
| 2007 |
Neudecker P, Zarrine-Afsar A, Davidson AR, Kay LE. Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 104: 15717-22. PMID 17898173 DOI: 10.1073/Pnas.0705097104 |
0.424 |
|
| 2007 |
Sprangers R, Velyvis A, Kay LE. Solution NMR of supramolecular complexes: providing new insights into function. Nature Methods. 4: 697-703. PMID 17762877 DOI: 10.1038/Nmeth1080 |
0.389 |
|
| 2007 |
Murphy JM, Korzhnev DM, Ceccarelli DF, Briant DJ, Zarrine-Afsar A, Sicheri F, Kay LE, Pawson T. Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain. Proceedings of the National Academy of Sciences of the United States of America. 104: 14336-41. PMID 17726107 DOI: 10.1073/Pnas.0703012104 |
0.372 |
|
| 2007 |
Hansen DF, Yang D, Feng H, Zhou Z, Wiesner S, Bai Y, Kay LE. An exchange-free measure of 15N transverse relaxation: an NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange. Journal of the American Chemical Society. 129: 11468-79. PMID 17722922 DOI: 10.1021/ja072717t |
0.311 |
|
| 2007 |
Korzhnev DM, Religa TL, Lundström P, Fersht AR, Kay LE. The folding pathway of an FF domain: characterization of an on-pathway intermediate state under folding conditions by (15)N, (13)C(alpha) and (13)C-methyl relaxation dispersion and (1)H/(2)H-exchange NMR spectroscopy. Journal of Molecular Biology. 372: 497-512. PMID 17689561 DOI: 10.1016/J.Jmb.2007.06.012 |
0.476 |
|
| 2007 |
Tugarinov V, Kay LE. Separating degenerate (1)H transitions in methyl group probes for single-quantum (1)H-CPMG relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 129: 9514-21. PMID 17628064 DOI: 10.1021/Ja0726456 |
0.459 |
|
| 2007 |
Lundström P, Teilum K, Carstensen T, Bezsonova I, Wiesner S, Hansen DF, Religa TL, Akke M, Kay LE. Fractional 13C enrichment of isolated carbons using [1-13C]- or [2- 13C]-glucose facilitates the accurate measurement of dynamics at backbone Calpha and side-chain methyl positions in proteins. Journal of Biomolecular Nmr. 38: 199-212. PMID 17554498 DOI: 10.1007/S10858-007-9158-6 |
0.66 |
|
| 2007 |
Velyvis A, Yang YR, Schachman HK, Kay LE. A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase. Proceedings of the National Academy of Sciences of the United States of America. 104: 8815-20. PMID 17502625 DOI: 10.1073/Pnas.0703347104 |
0.358 |
|
| 2007 |
Lundström P, Vallurupalli P, Religa TL, Dahlquist FW, Kay LE. A single-quantum methyl 13C-relaxation dispersion experiment with improved sensitivity. Journal of Biomolecular Nmr. 38: 79-88. PMID 17464570 DOI: 10.1007/S10858-007-9149-7 |
0.41 |
|
| 2007 |
Vallurupalli P, Scott L, Williamson JR, Kay LE. Strong coupling effects during X-pulse CPMG experiments recorded on heteronuclear ABX spin systems: artifacts and a simple solution. Journal of Biomolecular Nmr. 38: 41-6. PMID 17334825 DOI: 10.1007/S10858-006-9139-1 |
0.389 |
|
| 2007 |
Zhuravleva A, Korzhnev DM, Nolde SB, Kay LE, Arseniev AS, Billeter M, Orekhov VY. Propagation of dynamic changes in barnase upon binding of barstar: an NMR and computational study. Journal of Molecular Biology. 367: 1079-92. PMID 17306298 DOI: 10.1016/J.Jmb.2007.01.051 |
0.421 |
|
| 2007 |
Tugarinov V, Sprangers R, Kay LE. Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy. Journal of the American Chemical Society. 129: 1743-50. PMID 17249677 DOI: 10.1021/Ja067827Z |
0.46 |
|
| 2007 |
Sprangers R, Kay LE. Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature. 445: 618-22. PMID 17237764 DOI: 10.1038/Nature05512 |
0.42 |
|
| 2007 |
Kay LE. Seeing the Invisible by Solution NMR Spectroscopy The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A39-E |
0.332 |
|
| 2006 |
Tugarinov V, Kanelis V, Kay LE. Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy. Nature Protocols. 1: 749-54. PMID 17406304 DOI: 10.1038/Nprot.2006.101 |
0.444 |
|
| 2006 |
Neudecker P, Zarrine-Afsar A, Choy WY, Muhandiram DR, Davidson AR, Kay LE. Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy. Journal of Molecular Biology. 363: 958-76. PMID 16989862 DOI: 10.1016/J.Jmb.2006.08.047 |
0.403 |
|
| 2006 |
Tugarinov V, Kay LE. A 2H NMR relaxation experiment for the measurement of the time scale of methyl side-chain dynamics in large proteins. Journal of the American Chemical Society. 128: 12484-9. PMID 16984199 DOI: 10.1021/Ja063071S |
0.465 |
|
| 2006 |
Korzhnev DM, Neudecker P, Zarrine-Afsar A, Davidson AR, Kay LE. Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states. Biochemistry. 45: 10175-83. PMID 16922492 DOI: 10.1021/Bi0611560 |
0.378 |
|
| 2006 |
Vallurupalli P, Kay LE. Complementarity of ensemble and single-molecule measures of protein motion: a relaxation dispersion NMR study of an enzyme complex. Proceedings of the National Academy of Sciences of the United States of America. 103: 11910-5. PMID 16880391 DOI: 10.1073/Pnas.0602310103 |
0.438 |
|
| 2006 |
Vallurupalli P, Scott L, Hennig M, Williamson JR, Kay LE. New RNA labeling methods offer dramatic sensitivity enhancements in 2H NMR relaxation spectra. Journal of the American Chemical Society. 128: 9346-7. PMID 16848466 DOI: 10.1021/Ja0632512 |
0.38 |
|
| 2006 |
Tugarinov V, Ollerenshaw JE, Kay LE. Dipolar dynamic frequency shifts in multiple-quantum spectra of methyl groups in proteins: correlation with side-chain motion. Magnetic Resonance in Chemistry : Mrc. 44: S122-9. PMID 16826549 DOI: 10.1002/Mrc.1819 |
0.402 |
|
| 2006 |
Evanics F, Hwang PM, Cheng Y, Kay LE, Prosser RS. Topology of an outer-membrane enzyme: Measuring oxygen and water contacts in solution NMR studies of PagP. Journal of the American Chemical Society. 128: 8256-64. PMID 16787090 DOI: 10.1021/Ja0610075 |
0.35 |
|
| 2006 |
Tugarinov V, Kay LE. Relaxation rates of degenerate 1H transitions in methyl groups of proteins as reporters of side-chain dynamics. Journal of the American Chemical Society. 128: 7299-308. PMID 16734484 DOI: 10.1021/Ja060817D |
0.45 |
|
| 2006 |
Tollinger M, Neale C, Kay LE, Forman-Kay JD. Characterization of the hydrodynamic properties of the folding transition state of an SH3 domain by magnetization transfer NMR spectroscopy. Biochemistry. 45: 6434-45. PMID 16700554 DOI: 10.1021/Bi060268O |
0.405 |
|
| 2006 |
Brath U, Akke M, Yang D, Kay LE, Mulder FA. Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 128: 5718-27. PMID 16637639 DOI: 10.1021/Ja0570279 |
0.804 |
|
| 2006 |
Mittermaier A, Kay LE. New tools provide new insights in NMR studies of protein dynamics. Science (New York, N.Y.). 312: 224-8. PMID 16614210 DOI: 10.1126/Science.1124964 |
0.689 |
|
| 2006 |
Korzhnev DM, Bezsonova I, Evanics F, Taulier N, Zhou Z, Bai Y, Chalikian TV, Prosser RS, Kay LE. Probing the transition state ensemble of a protein folding reaction by pressure-dependent NMR relaxation dispersion. Journal of the American Chemical Society. 128: 5262-9. PMID 16608362 DOI: 10.1021/Ja0601540 |
0.376 |
|
| 2006 |
Bezsonova I, Korzhnev DM, Prosser RS, Forman-Kay JD, Kay LE. Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR. Biochemistry. 45: 4711-9. PMID 16605239 DOI: 10.1021/Bi060177R |
0.44 |
|
| 2006 |
Neudecker P, Korzhnev DM, Kay LE. Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domain. Journal of Biomolecular Nmr. 34: 129-35. PMID 16604422 DOI: 10.1007/S10858-006-0001-2 |
0.39 |
|
| 2006 |
Zarrine-Afsar A, Mittermaier A, Kay LE, Davidson AR. Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain. Protein Science : a Publication of the Protein Society. 15: 162-70. PMID 16373478 DOI: 10.1110/Ps.051829106 |
0.665 |
|
| 2005 |
Tugarinov V, Kay LE. Quantitative 13C and 2H NMR relaxation studies of the 723-residue enzyme malate synthase G reveal a dynamic binding interface. Biochemistry. 44: 15970-7. PMID 16331956 DOI: 10.1021/Bi0519809 |
0.45 |
|
| 2005 |
Mittermaier A, Korzhnev DM, Kay LE. Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy. Biochemistry. 44: 15430-6. PMID 16300390 DOI: 10.1021/Bi051771O |
0.699 |
|
| 2005 |
Eisenmesser EZ, Millet O, Labeikovsky W, Korzhnev DM, Wolf-Watz M, Bosco DA, Skalicky JJ, Kay LE, Kern D. Intrinsic dynamics of an enzyme underlies catalysis. Nature. 438: 117-21. PMID 16267559 DOI: 10.1038/Nature04105 |
0.38 |
|
| 2005 |
Sprangers R, Gribun A, Hwang PM, Houry WA, Kay LE. Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. Proceedings of the National Academy of Sciences of the United States of America. 102: 16678-83. PMID 16263929 DOI: 10.1073/Pnas.0507370102 |
0.398 |
|
| 2005 |
Korzhnev DM, Neudecker P, Mittermaier A, Orekhov VY, Kay LE. Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant. Journal of the American Chemical Society. 127: 15602-11. PMID 16262426 DOI: 10.1021/Ja054550E |
0.72 |
|
| 2005 |
Ollerenshaw JE, Tugarinov V, Skrynnikov NR, Kay LE. Comparison of 13CH3, 13CH2D, and 13CHD2 methyl labeling strategies in proteins. Journal of Biomolecular Nmr. 33: 25-41. PMID 16222555 DOI: 10.1007/S10858-005-2614-2 |
0.656 |
|
| 2005 |
Tugarinov V, Kay LE. Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins. Chembiochem : a European Journal of Chemical Biology. 6: 1567-77. PMID 16075427 DOI: 10.1002/Cbic.200500110 |
0.39 |
|
| 2005 |
Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, Kay LE, McIntosh LP, Graves BJ. Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. Science (New York, N.Y.). 309: 142-5. PMID 15994560 DOI: 10.1126/Science.1111915 |
0.311 |
|
| 2005 |
Tollinger M, Kay LE, Forman-Kay JD. Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy. Journal of the American Chemical Society. 127: 8904-5. PMID 15969539 DOI: 10.1021/Ja051942C |
0.429 |
|
| 2005 |
Korzhnev DM, Mittermaier AK, Kay LE. Cross-correlated spin relaxation effects in methyl 1H CPMG-based relaxation dispersion experiments: complications and a simple solution. Journal of Biomolecular Nmr. 31: 337-42. PMID 15929000 DOI: 10.1007/S10858-005-2468-7 |
0.676 |
|
| 2005 |
Tugarinov V, Ollerenshaw JE, Kay LE. Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme. Journal of the American Chemical Society. 127: 8214-25. PMID 15926851 DOI: 10.1021/Ja0508830 |
0.424 |
|
| 2005 |
Vallurupalli P, Kay LE. A suite of 2H NMR spin relaxation experiments for the measurement of RNA dynamics. Journal of the American Chemical Society. 127: 6893-901. PMID 15869313 DOI: 10.1021/Ja0427799 |
0.381 |
|
| 2005 |
Choy WY, Zhou Z, Bai Y, Kay LE. An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562. Journal of the American Chemical Society. 127: 5066-72. PMID 15810841 DOI: 10.1021/Ja042560U |
0.431 |
|
| 2005 |
Hwang PM, Kay LE. Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP. Methods in Enzymology. 394: 335-50. PMID 15808227 DOI: 10.1016/S0076-6879(05)94013-5 |
0.457 |
|
| 2005 |
Kay LE. NMR studies of protein structure and dynamics. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 173: 193-207. PMID 15780912 DOI: 10.1016/J.Jmr.2004.11.021 |
0.455 |
|
| 2005 |
Xu J, Millet O, Kay LE, Skrynnikov NR. A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups. Journal of the American Chemical Society. 127: 3220-9. PMID 15740163 DOI: 10.1021/Ja040215Z |
0.667 |
|
| 2005 |
Tugarinov V, Kay LE, Ibraghimov I, Orekhov VY. High-resolution four-dimensional 1H-13C NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition. Journal of the American Chemical Society. 127: 2767-75. PMID 15725035 DOI: 10.1021/Ja044032O |
0.368 |
|
| 2005 |
Korzhnev DM, Orekhov VY, Kay LE. Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain. Journal of the American Chemical Society. 127: 713-21. PMID 15643897 DOI: 10.1021/Ja0446855 |
0.416 |
|
| 2005 |
Finerty PJ, Mittermaier AK, Muhandiram R, Kay LE, Forman-Kay JD. NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain. Biochemistry. 44: 694-703. PMID 15641795 DOI: 10.1021/Bi048641K |
0.67 |
|
| 2005 |
Tugarinov V, Choy WY, Orekhov VY, Kay LE. Solution NMR-derived global fold of a monomeric 82-kDa enzyme. Proceedings of the National Academy of Sciences of the United States of America. 102: 622-7. PMID 15637152 DOI: 10.1073/Pnas.0407792102 |
0.445 |
|
| 2004 |
Tugarinov V, Choy WY, Kupce E, Kay LE. Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: application to (15)N relaxation measurements. Journal of Biomolecular Nmr. 30: 347-52. PMID 15756461 DOI: 10.1007/S10858-005-1549-Y |
0.413 |
|
| 2004 |
Tugarinov V, Scheurer C, Brüschweiler R, Kay LE. Estimates of methyl 13C and 1H CSA values (Deltasigma) in proteins from cross-correlated spin relaxation. Journal of Biomolecular Nmr. 30: 397-406. PMID 15630560 DOI: 10.1007/S10858-004-4349-X |
0.413 |
|
| 2004 |
Ollerenshaw JE, Kaya H, Chan HS, Kay LE. Sparsely populated folding intermediates of the Fyn SH3 domain: matching native-centric essential dynamics and experiment. Proceedings of the National Academy of Sciences of the United States of America. 101: 14748-53. PMID 15469926 DOI: 10.1073/Pnas.0404436101 |
0.441 |
|
| 2004 |
Tugarinov V, Kay LE. Stereospecific NMR assignments of prochiral methyls, rotameric states and dynamics of valine residues in malate synthase G. Journal of the American Chemical Society. 126: 9827-36. PMID 15291587 DOI: 10.1021/Ja048738U |
0.437 |
|
| 2004 |
Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE. Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature. 430: 586-90. PMID 15282609 DOI: 10.1038/Nature02655 |
0.447 |
|
| 2004 |
Ahn VE, Lo EI, Engel CK, Chen L, Hwang PM, Kay LE, Bishop RE, Privé GG. A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin. The Embo Journal. 23: 2931-41. PMID 15272304 DOI: 10.1038/Sj.Emboj.7600320 |
0.305 |
|
| 2004 |
Tugarinov V, Kay LE. 1H,13C-1H,1H dipolar cross-correlated spin relaxation in methyl groups. Journal of Biomolecular Nmr. 29: 369-76. PMID 15213435 DOI: 10.1023/B:Jnmr.0000032562.07475.7F |
0.41 |
|
| 2004 |
Hwang PM, Bishop RE, Kay LE. The integral membrane enzyme PagP alternates between two dynamically distinct states. Proceedings of the National Academy of Sciences of the United States of America. 101: 9618-23. PMID 15210985 DOI: 10.1073/Pnas.0402324101 |
0.379 |
|
| 2004 |
Tugarinov V, Hwang PM, Kay LE. Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annual Review of Biochemistry. 73: 107-46. PMID 15189138 DOI: 10.1146/Annurev.Biochem.73.011303.074004 |
0.434 |
|
| 2004 |
Korzhnev DM, Kloiber K, Kay LE. Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application. Journal of the American Chemical Society. 126: 7320-9. PMID 15186169 DOI: 10.1021/Ja049968B |
0.419 |
|
| 2004 |
Di Nardo AA, Korzhnev DM, Stogios PJ, Zarrine-Afsar A, Kay LE, Davidson AR. Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation. Proceedings of the National Academy of Sciences of the United States of America. 101: 7954-9. PMID 15148398 DOI: 10.1073/Pnas.0400550101 |
0.411 |
|
| 2004 |
Tugarinov V, Sprangers R, Kay LE. Line narrowing in methyl-TROSY using zero-quantum 1H-13C NMR spectroscopy. Journal of the American Chemical Society. 126: 4921-5. PMID 15080697 DOI: 10.1021/Ja039732S |
0.405 |
|
| 2004 |
Mittermaier A, Kay LE. The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinase. Protein Science : a Publication of the Protein Society. 13: 1088-99. PMID 15044737 DOI: 10.1110/Ps.03502504 |
0.685 |
|
| 2004 |
Korzhnev DM, Kloiber K, Kanelis V, Tugarinov V, Kay LE. Probing Slow Dynamics in High Molecular Weight Proteins by Methyl-TROSY NMR Spectroscopy: Application to a 723-Residue Enzyme Journal of the American Chemical Society. 126: 3964-3973. PMID 15038751 DOI: 10.1021/Ja039587I |
0.427 |
|
| 2004 |
Orekhov VY, Korzhnev DM, Kay LE. Double- and Zero-Quantum NMR Relaxation Dispersion Experiments Sampling Millisecond Time Scale Dynamics in Proteins Journal of the American Chemical Society. 126: 1886-1891. PMID 14871121 DOI: 10.1021/Ja038620Y |
0.42 |
|
| 2004 |
Tugarinov V, Kay LE. An isotope labeling strategy for methyl TROSY spectroscopy Journal of Biomolecular Nmr. 28: 165-172. PMID 14755160 DOI: 10.1023/B:Jnmr.0000013824.93994.1F |
0.409 |
|
| 2004 |
Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE. Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. Journal of the American Chemical Society. 125: 10420-8. PMID 12926967 DOI: 10.1021/Ja030153X |
0.459 |
|
| 2004 |
Choy WY, Kay LE. Model selection for the interpretation of protein side chain methyl dynamics. Journal of Biomolecular Nmr. 25: 325-33. PMID 12766394 DOI: 10.1023/A:1023065310430 |
0.36 |
|
| 2003 |
Mittermaier A, Davidson AR, Kay LE. Correlation between 2H NMR side-chain order parameters and sequence conservation in globular proteins. Journal of the American Chemical Society. 125: 9004-5. PMID 15369343 DOI: 10.1021/Ja034856Q |
0.694 |
|
| 2003 |
Tugarinov V, Kay LE. Ile, Leu, and Val Methyl Assignments of the 723-Residue Malate Synthase G Using a New Labeling Strategy and Novel NMR Methods Journal of the American Chemical Society. 125: 13868-13878. PMID 14599227 DOI: 10.1021/Ja030345S |
0.428 |
|
| 2003 |
Millet O, Hudson RP, Kay LE. The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 100: 12700-5. PMID 14530390 DOI: 10.1073/Pnas.2134311100 |
0.419 |
|
| 2003 |
Choy WY, Kay LE. Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta. Journal of the American Chemical Society. 125: 11988-92. PMID 14505420 DOI: 10.1021/Ja035705Q |
0.382 |
|
| 2003 |
Kupce E, Muhandiram DR, Kay LE. A combined HNCA/HNCO experiment for 15N labeled proteins with 13C at natural abundance Journal of Biomolecular Nmr. 27: 175-179. PMID 12913414 DOI: 10.1023/A:1024985219764 |
0.397 |
|
| 2003 |
Millet O, Mittermaier A, Baker D, Kay LE. The effects of mutations on motions of side-chains in protein L studied by 2H NMR dynamics and scalar couplings. Journal of Molecular Biology. 329: 551-63. PMID 12767834 DOI: 10.1016/S0022-2836(03)00471-6 |
0.698 |
|
| 2003 |
Korzhnev DM, Orekhov VY, Dahlquist FW, Kay LE. Off-resonance R1rho relaxation outside of the fast exchange limit: an experimental study of a cavity mutant of T4 lysozyme. Journal of Biomolecular Nmr. 26: 39-48. PMID 12766401 DOI: 10.1023/A:1023039902737 |
0.419 |
|
| 2003 |
Tugarinov V, Kay LE. Side chain assignments of Ile delta 1 methyl groups in high molecular weight proteins: an application to a 46 ns tumbling molecule. Journal of the American Chemical Society. 125: 5701-6. PMID 12733908 DOI: 10.1021/Ja021452+ |
0.426 |
|
| 2003 |
Tollinger M, Crowhurst KA, Kay LE, Forman-Kay JD. Site-specific contributions to the pH dependence of protein stability. Proceedings of the National Academy of Sciences of the United States of America. 100: 4545-50. PMID 12671071 DOI: 10.1073/Pnas.0736600100 |
0.365 |
|
| 2003 |
Tugarinov V, Kay LE. Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G. Journal of Molecular Biology. 327: 1121-33. PMID 12662935 DOI: 10.1016/S0022-2836(03)00238-9 |
0.415 |
|
| 2003 |
Choy WY, Shortle D, Kay LE. Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta. Journal of the American Chemical Society. 125: 1748-58. PMID 12580600 DOI: 10.1021/Ja021179B |
0.521 |
|
| 2003 |
Ollerenshaw JE, Tugarinov V, Kay LE. Methyl TROSY: explanation and experimental verification Magnetic Resonance in Chemistry. 41: 843-852. DOI: 10.1002/Mrc.1256 |
0.454 |
|
| 2002 |
Mittermaier T, Mulder F, Dahlquist R, Kay LE. Studying Protein-Excited States by Nmr. Thescientificworldjournal. 2: 45-46. PMID 29973797 DOI: 10.1100/tsw.2002.23 |
0.661 |
|
| 2002 |
Mal TK, Ikura M, Kay LE. The ATCUN domain as a probe of intermolecular interactions: application to calmodulin-peptide complexes. Journal of the American Chemical Society. 124: 14002-3. PMID 12440892 DOI: 10.1021/Ja028109P |
0.326 |
|
| 2002 |
Mal TK, Skrynnikov NR, Yap KL, Kay LE, Ikura M. Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR. Biochemistry. 41: 12899-906. PMID 12390014 DOI: 10.1021/Bi0264162 |
0.633 |
|
| 2002 |
Donaldson LW, Gish G, Pawson T, Kay LE, Forman-Kay JD. Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide. Proceedings of the National Academy of Sciences of the United States of America. 99: 14053-8. PMID 12384576 DOI: 10.1073/Pnas.212518799 |
0.346 |
|
| 2002 |
Skrynnikov NR, Dahlquist FW, Kay LE. Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments. Journal of the American Chemical Society. 124: 12352-60. PMID 12371879 DOI: 10.1021/Ja0207089 |
0.685 |
|
| 2002 |
Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE. An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates. Journal of the American Chemical Society. 124: 10743-53. PMID 12207529 DOI: 10.1021/Ja0204776 |
0.674 |
|
| 2002 |
Tugarinov V, Muhandiram R, Ayed A, Kay LE. Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase g. Journal of the American Chemical Society. 124: 10025-35. PMID 12188667 DOI: 10.1021/Ja0205636 |
0.468 |
|
| 2002 |
Mittermaier A, Kay LE. Effect of deuteration on some structural parameters of methyl groups in proteins as evaluated by residual dipolar couplings. Journal of Biomolecular Nmr. 23: 35-45. PMID 12061716 DOI: 10.1023/A:1015368803552 |
0.69 |
|
| 2002 |
Skrynnikov NR, Millet O, Kay LE. Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions. Journal of the American Chemical Society. 124: 6449-60. PMID 12033876 DOI: 10.1021/Ja012498Q |
0.691 |
|
| 2002 |
Millet O, Muhandiram DR, Skrynnikov NR, Kay LE. Deuterium spin probes of side-chain dynamics in proteins. 1. Measurement of five relaxation rates per deuteron in (13)C-labeled and fractionally (2)H-enriched proteins in solution. Journal of the American Chemical Society. 124: 6439-48. PMID 12033875 DOI: 10.1021/Ja012497Y |
0.721 |
|
| 2002 |
Tollinger M, Forman-Kay JD, Kay LE. Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy. Journal of the American Chemical Society. 124: 5714-7. PMID 12010044 DOI: 10.1021/Ja020066P |
0.476 |
|
| 2002 |
Kanelis V, Forman-Kay JD, Kay LE. Multidimensional NMR methods for protein structure determination Iubmb Life. 52: 291-302. PMID 11895078 DOI: 10.1080/152165401317291147 |
0.442 |
|
| 2002 |
Mulder FA, Hon B, Mittermaier A, Dahlquist FW, Kay LE. Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 124: 1443-51. PMID 11841314 DOI: 10.1021/Ja0119806 |
0.796 |
|
| 2002 |
Choy WY, Mulder FA, Crowhurst KA, Muhandiram DR, Millett IS, Doniach S, Forman-Kay JD, Kay LE. Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques. Journal of Molecular Biology. 316: 101-12. PMID 11829506 DOI: 10.1006/Jmbi.2001.5328 |
0.678 |
|
| 2002 |
Hwang PM, Li C, Morra M, Lillywhite J, Muhandiram DR, Gertler F, Terhorst C, Kay LE, Pawson T, Forman-Kay JD, Li SC. A 'three-pronged' binding mechanism for the SAP/SH2D1A SH2 domain: Structural basis and relevance to the XLP syndrome Embo Journal. 21: 314-323. PMID 11823424 DOI: 10.1093/Emboj/21.3.314 |
0.367 |
|
| 2001 |
Tollinger M, Skrynnikov NR, Mulder FA, Forman-Kay JD, Kay LE. Slow dynamics in folded and unfolded states of an SH3 domain. Journal of the American Chemical Society. 123: 11341-52. PMID 11707108 DOI: 10.1021/Ja011300Z |
0.8 |
|
| 2001 |
Choy WY, Tollinger M, Mueller GA, Kay LE. Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein. Journal of Biomolecular Nmr. 21: 31-40. PMID 11693566 DOI: 10.1023/A:1011933020122 |
0.463 |
|
| 2001 |
Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE. Studying excited states of proteins by NMR spectroscopy. Nature Structural Biology. 8: 932-5. PMID 11685237 DOI: 10.1038/Nsb1101-932 |
0.788 |
|
| 2001 |
Donaldson LW, Skrynnikov NR, Choy WY, Muhandiram DR, Sarkar B, Forman-Kay JD, Kay LE. Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy. Journal of the American Chemical Society. 123: 9843-7. PMID 11583547 DOI: 10.1021/Ja011241P |
0.692 |
|
| 2001 |
Ayed A, Mulder FAA, Yi GS, Lu Y, Kay LE, Arrowsmith CH. Latent and active p53 are identical in conformation Nature Structural Biology. 8: 756-760. PMID 11524676 DOI: 10.1038/Nsb0901-756 |
0.343 |
|
| 2001 |
Kay LE. Nuclear magnetic resonance methods for high molecular weight proteins: a study involving a complex of maltose binding protein and beta-cyclodextrin. Methods in Enzymology. 339: 174-203. PMID 11462811 DOI: 10.1016/S0076-6879(01)39314-X |
0.353 |
|
| 2001 |
Skrynnikov NR, Mulder FA, Hon B, Dahlquist FW, Kay LE. Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 4556-66. PMID 11457242 DOI: 10.1021/Ja004179P |
0.803 |
|
| 2001 |
Evenäs J, Mittermaier A, Yang D, Kay LE. Measurement of (13)C(alpha)-(13)C(beta) dipolar couplings in (15)N,(13)C,(2)H-labeled proteins: application to domain orientation in maltose binding protein. Journal of the American Chemical Society. 123: 2858-64. PMID 11456973 DOI: 10.1021/Ja003833Y |
0.699 |
|
| 2001 |
Tolman JR, Al-Hashimi HM, Kay LE, Prestegard JH. Structural and dynamic analysis of residual dipolar coupling data for proteins. Journal of the American Chemical Society. 123: 1416-24. PMID 11456715 DOI: 10.1021/Ja002500Y |
0.821 |
|
| 2001 |
Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE. Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 967-75. PMID 11456632 DOI: 10.1021/Ja003447G |
0.81 |
|
| 2001 |
Mittermaier A, Kay LE. Chi1 torsion angle dynamics in proteins from dipolar couplings. Journal of the American Chemical Society. 123: 6892-903. PMID 11448195 DOI: 10.1021/Ja010595D |
0.695 |
|
| 2001 |
Hwang PM, Skrynnikov NR, Kay LE. Domain orientation in beta-cyclodextrin-loaded maltose binding protein: diffusion anisotropy measurements confirm the results of a dipolar coupling study. Journal of Biomolecular Nmr. 20: 83-8. PMID 11430759 DOI: 10.1023/A:1011226512421 |
0.684 |
|
| 2001 |
Evenäs J, Tugarinov V, Skrynnikov NR, Goto NK, Muhandiram R, Kay LE. Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy. Journal of Molecular Biology. 309: 961-74. PMID 11399072 DOI: 10.1006/Jmbi.2001.4695 |
0.811 |
|
| 2001 |
Goto NK, Skrynnikov NR, Dahlquist FW, Kay LE. What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR. Journal of Molecular Biology. 308: 745-64. PMID 11350172 DOI: 10.1006/Jmbi.2001.4614 |
0.795 |
|
| 2001 |
Evenas J, Tugarinov V, Skrynnikov N, Goto N, Muhandiram R, Kay L. Backbone 1H,13C and 15N chemical shift assignment for the maltotriose-bound state of 2H,13C,15N-labeled maltodextrin-binding protein Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4987 |
0.688 |
|
| 2000 |
Skrynnikov NR, Kay LE. Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings. Journal of Biomolecular Nmr. 18: 239-52. PMID 11142514 DOI: 10.1023/A:1026501101716 |
0.671 |
|
| 2000 |
Mueller GA, Choy WY, Skrynnikov NR, Kay LE. A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment. Journal of Biomolecular Nmr. 18: 183-8. PMID 11142508 DOI: 10.1023/A:1026788430236 |
0.705 |
|
| 2000 |
Mulder FAA, Ayed A, Yang D, Arrowsmith CH, Kay LE. Assignment of 1H(N), 15N, 13C(α), 13CO and 13C(β) resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopy Journal of Biomolecular Nmr. 18: 173-176. PMID 11101222 DOI: 10.1023/A:1008317825976 |
0.394 |
|
| 2000 |
Goto NK, Kay LE. New developments in isotope labeling strategies for protein solution NMR spectroscopy. Current Opinion in Structural Biology. 10: 585-92. PMID 11042458 DOI: 10.1016/S0959-440X(00)00135-4 |
0.732 |
|
| 2000 |
Mulder FA, Hon B, Muhandiram DR, Dahlquist FW, Kay LE. Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR. Biochemistry. 39: 12614-22. PMID 11027141 DOI: 10.1021/Bi001351T |
0.721 |
|
| 2000 |
Mueller GA, Choy WY, Yang D, Forman-Kay JD, Venters RA, Kay LE. Global folds of proteins with low densities of NOEs using residual dipolar couplings: Application to the 370-residue maltodextrin-binding protein Journal of Molecular Biology. 300: 197-212. PMID 10864509 DOI: 10.1006/Jmbi.2000.3842 |
0.468 |
|
| 2000 |
Kanelis V, Donaldson L, Muhandiram DR, Rotin D, Forman-Kay JD, Kay LE. Sequential assignment of proline-rich regions in proteins: application to modular binding domain complexes. Journal of Biomolecular Nmr. 16: 253-9. PMID 10805132 DOI: 10.1023/A:1008355012528 |
0.421 |
|
| 2000 |
Kortemme T, Kelly MJ, Kay LE, Forman-Kay J, Serrano L. Similarities between the spectrin SH3 domain denatured state and its folding transition state. Journal of Molecular Biology. 297: 1217-29. PMID 10764585 DOI: 10.1006/Jmbi.2000.3618 |
0.446 |
|
| 2000 |
Zwahlen C, Li SC, Kay LE, Pawson T, Forman-Kay JD. Multiple modes of peptide recognition by the PTB domain of the cell fate determinant Numb Embo Journal. 19: 1505-1515. PMID 10747019 DOI: 10.1093/Emboj/19.7.1505 |
0.346 |
|
| 2000 |
Varani L, Gunderson SI, Mattaj IW, Kay LE, Neuhaus D, Varani G. The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein. Nature Structural Biology. 7: 329-35. PMID 10742179 DOI: 10.1038/74101 |
0.34 |
|
| 2000 |
Skrynnikov NR, Goto NK, Yang D, Choy WY, Tolman JR, Mueller GA, Kay LE. Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin. Journal of Molecular Biology. 295: 1265-73. PMID 10653702 DOI: 10.1006/Jmbi.1999.3430 |
0.831 |
|
| 2000 |
Skrynnikov NR, Konrat R, Muhandiram DR, Kay LE. Relative orientation of peptide planes in proteins is reflected in carbonyl - Carbonyl chemical shift anisotropy cross-correlated spin relaxation Journal of the American Chemical Society. 122: 7059-7071. DOI: 10.1021/Ja0000201 |
0.676 |
|
| 1999 |
Mittermaier A, Kay LE, Forman-Kay JD. Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure. Journal of Biomolecular Nmr. 13: 181-5. PMID 20700817 DOI: 10.1023/A:1008387715167 |
0.651 |
|
| 1999 |
Li SC, Gish G, Yang D, Coffey AJ, Forman-Kay JD, Ernberg I, Kay LE, Pawson T. Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2DIA Current Biology. 9: 1355-1362. PMID 10607564 DOI: 10.1016/S0960-9822(00)80080-9 |
0.365 |
|
| 1999 |
Mittermaier A, Varani L, Muhandiram DR, Kay LE, Varani G. Changes in side-chain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein. Journal of Molecular Biology. 294: 967-79. PMID 10588900 DOI: 10.1006/Jmbi.1999.3311 |
0.655 |
|
| 1999 |
Goto NK, Gardner KH, Mueller GA, Willis RC, Kay LE. A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins. Journal of Biomolecular Nmr. 13: 369-74. PMID 10383198 DOI: 10.1023/A:1008393201236 |
0.76 |
|
| 1999 |
Mok YK, Kay CM, Kay LE, Forman-Kay J. NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions Journal of Molecular Biology. 289: 619-638. PMID 10356333 DOI: 10.1006/Jmbi.1999.2769 |
0.411 |
|
| 1999 |
Zwahlen C, Li S, Vincent S, Mcglade C, Kay L, Pawson T, Forman-Kay J. dNumb PTB Domain Complexed with a Phosphotyrosine Peptide, NMR, Ensemble of Structures. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4263 |
0.331 |
|
| 1999 |
Yang D, Kay LE. Improved lineshape and sensitivity in the HNCO-family of triple resonance experiments Journal of Biomolecular Nmr. 14: 273-276. DOI: 10.1023/A:1008381929212 |
0.407 |
|
| 1999 |
Yang D, Venters RA, Mueller GA, Choy W, Kay LE. Journal of Biomolecular Nmr. 14: 333-343. DOI: 10.1023/A:1008314803561 |
0.432 |
|
| 1999 |
Mittermaier A, Kay LE. Measurement of methyl 2H quadrupolar couplings in oriented proteins. How uniform is the quadrupolar coupling constant? Journal of the American Chemical Society. 121: 10608-10613. DOI: 10.1021/Ja9925047 |
0.673 |
|
| 1999 |
Yang D, Mok YK, Muhandiram DR, Forman-Kay JD, Kay LE. 1H-13C dipole-dipole cross-correlated spin relaxation as a probe of dynamics in unfolded proteins: Application to the DrkN SH3 domain [14] Journal of the American Chemical Society. 121: 3555-3556. DOI: 10.1021/Ja9900914 |
0.434 |
|
| 1999 |
Yang D, Kay LE. TROSY Triple-Resonance Four-Dimensional NMR Spectroscopy of a 46 ns Tumbling Protein Journal of the American Chemical Society. 121: 2571-2575. DOI: 10.1021/Ja984056T |
0.419 |
|
| 1998 |
Yang D, Tolman JR, Goto NK, Kay LE. An HNCO-based Pulse Scheme for the Measurement of 13Cα-1Hα One-bond Dipolar couplings in 15N, 13C Labeled Proteins. Journal of Biomolecular Nmr. 12: 325-32. PMID 21136327 DOI: 10.1023/A:1008223017233 |
0.819 |
|
| 1998 |
Yang D, Gardner KH, Kay LE. A Sensitive Pulse Scheme for Measuring the Backbone Dihedral Angle psi Based on Cross-correlation Between (13)C (alpha)- (1)Halpha Dipolar and Carbonyl Chemical Shift Anisotropy Relaxation Interactions. Journal of Biomolecular Nmr. 11: 213-20. PMID 20700829 DOI: 10.1023/A:1008284315816 |
0.583 |
|
| 1998 |
Kanelis V, Farrow NA, Kay LE, Rotin D, Forman-Kay JD. NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 76: 341-50. PMID 9923703 DOI: 10.1139/Bcb-76-2-3-341 |
0.408 |
|
| 1998 |
Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M. Solution structure of a TBP-TAF(II)230 complex: Protein mimicry of the minor groove surface of the TATA box unwound by TBP Cell. 94: 573-583. PMID 9741622 DOI: 10.1016/S0092-8674(00)81599-8 |
0.311 |
|
| 1998 |
Shan X, Gardner KH, Muhandiram DR, Kay LE, Arrowsmith CH. Subunit-specific backbone NMR assignments of a 64 kDa trp repressor/DNA complex: a role for N-terminal residues in tandem binding. Journal of Biomolecular Nmr. 11: 307-18. PMID 9691278 DOI: 10.1023/A:1008257803130 |
0.626 |
|
| 1998 |
Kay LE. Protein dynamics from NMR. Nature Structural Biology. 513-7. PMID 9665181 DOI: 10.1139/Bcb-76-2-3-145 |
0.376 |
|
| 1998 |
Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J. Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein. Molecular Cell. 1: 265-75. PMID 9659923 DOI: 10.1016/S1097-2765(00)80027-1 |
0.347 |
|
| 1998 |
Gardner KH, Kay LE. The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annual Review of Biophysics and Biomolecular Structure. 27: 357-406. PMID 9646872 DOI: 10.1146/Annurev.Biophys.27.1.357 |
0.645 |
|
| 1998 |
Gagné SM, Tsuda S, Spyracopoulos L, Kay LE, Sykes BD. Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity. Journal of Molecular Biology. 278: 667-86. PMID 9600847 DOI: 10.1006/Jmbi.1998.1723 |
0.563 |
|
| 1998 |
Legault P, Li J, Mogridge J, Kay LE, Greenblatt J. NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif. Cell. 93: 289-99. PMID 9568720 DOI: 10.1016/S0092-8674(00)81579-2 |
0.374 |
|
| 1998 |
Yang D, Mittermaier A, Mok YK, Kay LE. A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk. Journal of Molecular Biology. 276: 939-54. PMID 9566198 DOI: 10.1006/Jmbi.1997.1588 |
0.715 |
|
| 1998 |
Kay LE, Muhandiram DR, Wolf G, Shoelson SE, Forman-Kay JD. Correlation between binding and dynamics at SH2 domain interfaces. Nature Structural Biology. 5: 156-63. PMID 9461082 DOI: 10.1038/Nsb0298-156 |
0.426 |
|
| 1998 |
Yang D, Kay LE. Determination of the Protein Backbone Dihedral Angle ψ from a Combination of NMR-Derived Cross-Correlation Spin Relaxation Rates Journal of the American Chemical Society. 120: 9880-9887. DOI: 10.1021/Ja981873K |
0.446 |
|
| 1998 |
Zwahlen C, Gardner KH, Sarma SP, Horita DA, Byrd RA, Kay LE. An NMR experiment for measuring methyl-methyl NOEs in 13C-labeled proteins with high resolution Journal of the American Chemical Society. 120: 7617-7625. DOI: 10.1021/Ja981205Z |
0.642 |
|
| 1998 |
Zwahlen C, Vincent SJF, Gardner KH, Kay LE. Significantly improved resolution for noe correlations from valine and isoleucine (C(y)2) methyl groups in 15N, 13C- and 15N, 13C, 2H-labeled proteins Journal of the American Chemical Society. 120: 4825-4831. DOI: 10.1021/Ja9742601 |
0.613 |
|
| 1997 |
Yang D, Mok YK, Forman-Kay JD, Farrow NA, Kay LE. Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation Journal of Molecular Biology. 272: 790-803. PMID 9368658 DOI: 10.1006/Jmbi.1997.1285 |
0.408 |
|
| 1997 |
Kay LE, Gardner KH. Solution NMR spectroscopy beyond 25 kDa. Current Opinion in Structural Biology. 7: 722-31. PMID 9345633 DOI: 10.1016/S0959-440X(97)80084-X |
0.612 |
|
| 1997 |
Zhang O, Kay LE, Shortle D, Forman-Kay JD. Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease Δ131Δ, using NMR methods with improved resolution Journal of Molecular Biology. 272: 9-20. PMID 9299333 DOI: 10.1006/Jmbi.1997.1219 |
0.441 |
|
| 1997 |
Konrat R, Muhandiram DR, Farrow NA, Kay LE. Pulse schemes for the measurement of 3JC'C gamma and 3JNC gamma scalar couplings in 15N,13C uniformly labeled proteins. Journal of Biomolecular Nmr. 9: 409-22. PMID 9255945 DOI: 10.1023/A:1018354712430 |
0.395 |
|
| 1997 |
Li SC, Songyang Z, Vincent SJ, Zwahlen C, Wiley S, Cantley L, Kay LE, Forman-Kay J, Pawson T. High-affinity binding of the Drosophila Numb phosphotyrosine-binding domain to peptides containing a Gly-Pro-(p)Tyr motif. Proceedings of the National Academy of Sciences of the United States of America. 94: 7204-9. PMID 9207069 DOI: 10.1073/Pnas.94.14.7204 |
0.338 |
|
| 1997 |
Kay LE. NMR methods for the study of protein structure and dynamics. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 75: 1-15. PMID 9192068 DOI: 10.1139/O97-023 |
0.433 |
|
| 1997 |
Xu GY, Yu HA, Hong J, Stahl M, McDonagh T, Kay LE, Cumming DA. Solution structure of recombinant human interleukin-6. Journal of Molecular Biology. 268: 468-81. PMID 9159484 DOI: 10.1006/Jmbi.1997.0933 |
0.389 |
|
| 1997 |
Zhang O, Forman-Kay JD, Shortle D, Kay LE. Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins Journal of Biomolecular Nmr. 9: 181-200. PMID 9090132 DOI: 10.1023/A:1018658305040 |
0.481 |
|
| 1997 |
Gardner KH, Rosen MK, Kay LE. Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. Biochemistry. 36: 1389-401. PMID 9063887 DOI: 10.1021/Bi9624806 |
0.735 |
|
| 1997 |
Farrow NA, Zhang O, Forman-Kay JD, Kay LE. Characterization of the backbone dynamics of folded and denatured states of an SH3 domain Biochemistry. 36: 2390-2402. PMID 9054544 DOI: 10.1021/Bi962548H |
0.416 |
|
| 1997 |
Rao NS, Legault P, Muhandiram DR, Greenblatt J, Battiste JL, Williamson JR, Kay LE. NMR pulse schemes for the sequential assignment of arginine side-chain H epsilon protons. Journal of Magnetic Resonance. Series B. 113: 272-6. PMID 8995846 DOI: 10.1006/Jmrb.1996.0188 |
0.345 |
|
| 1997 |
Yang D, Konrat R, Kay LE. A Multidimensional NMR Experiment for Measurement of the Protein Dihedral Angle ψ Based on Cross-Correlated Relaxation between1Hα−13CαDipolar and13C‘ (Carbonyl) Chemical Shift Anisotropy Mechanisms Journal of the American Chemical Society. 119: 11938-11940. DOI: 10.1021/Ja972329Z |
0.433 |
|
| 1997 |
Gardner KH, Kay LE. Production and incorporation of 15N, 13C, 2H (1H-δ1 methyl) isoleucine into proteins for multidimensional NMR studies Journal of the American Chemical Society. 119: 7599-7600. DOI: 10.1021/Ja9706514 |
0.585 |
|
| 1997 |
Zwahlen C, Legault P, Vincent SJF, Greenblatt J, Konrat R, Kay LE. Methods for Measurement of Intermolecular NOEs by Multinuclear NMR Spectroscopy: Application to a Bacteriophage λ N-Peptide/boxBRNA Complex Journal of the American Chemical Society. 119: 6711-6721. DOI: 10.1021/Ja970224Q |
0.407 |
|
| 1996 |
Gardner KH, Konrat R, Rosen MK, Kay LE. An (H)C(CO)NH-TOCSY pulse scheme for sequential assignment of protonated methyl groups in otherwise deuterated (15)N, (13)C-labeled proteins. Journal of Biomolecular Nmr. 8: 351-6. PMID 20686885 DOI: 10.1007/Bf00410333 |
0.708 |
|
| 1996 |
Rosen MK, Gardner KH, Willis RC, Parris WE, Pawson T, Kay LE. Selective methyl group protonation of perdeuterated proteins. Journal of Molecular Biology. 263: 627-36. PMID 8947563 DOI: 10.1006/Jmbi.1996.0603 |
0.73 |
|
| 1996 |
Xu G, Hong J, McDonagh T, Stahl M, Kay LE, Seehra J, Cumming DA. Complete 1H, 15N and 13C assignments, secondary structure, and topology of recombinant human interleukin-6. Journal of Biomolecular Nmr. 8: 123-135. PMID 8914271 DOI: 10.1007/Bf00211159 |
0.376 |
|
| 1996 |
Yang D, Kay LE. Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding. Journal of Molecular Biology. 263: 369-82. PMID 8913313 DOI: 10.1006/Jmbi.1996.0581 |
0.363 |
|
| 1996 |
Anafi M, Rosen MK, Gish GD, Kay LE, Pawson T. A potential SH3 domain-binding site in the Crk SH2 domain. The Journal of Biological Chemistry. 271: 21365-74. PMID 8702917 DOI: 10.1074/Jbc.271.35.21365 |
0.558 |
|
| 1996 |
McEvoy MM, Muhandiram DR, Kay LE, Dahlquist FW. Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. Biochemistry. 35: 5633-40. PMID 8639521 DOI: 10.1021/Bi952707H |
0.431 |
|
| 1996 |
Williams KA, Farrow NA, Deber CM, Kay LE. Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR Biochemistry. 35: 5145-5157. PMID 8611498 DOI: 10.1021/Bi952897W |
0.442 |
|
| 1996 |
Kay LE. Field gradient techniques in NMR spectroscopy. Current Opinion in Structural Biology. 5: 674-81. PMID 8574704 DOI: 10.1016/0959-440X(95)80061-1 |
0.36 |
|
| 1996 |
Kay LE, Muhandiram DR, Farrow NA, Aubin Y, Forman-Kay JD. Correlation between dynamics and high affinity binding in an SH2 domain interaction Biochemistry. 35: 361-368. PMID 8555205 DOI: 10.1021/Bi9522312 |
0.436 |
|
| 1996 |
Shan X, Gardner KH, Muhandiram DR, Rao NS, Arrowsmith CH, Kay LE. Assignment of 15N, 13C(α), 13C(β), and HN resonances in an 15N,13C,2H labeled 64 kDa trp repressor-operator complex using triple-resonance NMR spectroscopy and 2H-decoupling Journal of the American Chemical Society. 118: 6570-6579. DOI: 10.1021/Ja960627A |
0.588 |
|
| 1995 |
Pascal SM, Singer AU, Yamazaki T, Kay LE, Forman-Kay JD. Structural and dynamic characterization of an SH2 domain-phosphopeptide complex by NMR approaches Biochemical Society Transactions. 23: 729-733. PMID 8654826 DOI: 10.1042/Bst0230729 |
0.373 |
|
| 1995 |
Farrow NA, Zhang O, Szabo A, Torchia DA, Kay LE. Spectral density function mapping using 15N relaxation data exclusively. Journal of Biomolecular Nmr. 6: 153-62. PMID 8589604 DOI: 10.1007/Bf00211779 |
0.376 |
|
| 1995 |
Farrow NA, Zhang O, Forman-Kay JD, Kay LE. Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer. Biochemistry. 34: 868-78. PMID 7827045 DOI: 10.1021/Bi00003A021 |
0.437 |
|
| 1995 |
Rosen MK, Yamazaki T, Gish GD, Kay CM, Pawson T, Kay LE. Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein. Nature. 374: 477-9. PMID 7700361 DOI: 10.1038/374477A0 |
0.587 |
|
| 1995 |
McEvoy MM, Zhou H, Roth AF, Lowry DF, Morrison TB, Kay LE, Dahlquist FW. Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli. Biochemistry. 34: 13871-80. PMID 7577981 DOI: 10.1021/Bi00042A019 |
0.422 |
|
| 1995 |
Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay JD. Structural and Dynamic Characterization of the Phosphotyrosine Binding Region of a Src Homology 2 Domain-Phosphopeptide Complex by NMR Relaxation, Proton Exchange, and Chemical Shift Approaches Biochemistry. 34: 11353-11362. PMID 7547863 DOI: 10.1021/Bi00036A008 |
0.47 |
|
| 1995 |
Xu G, Ong E, Gilkes NR, Kilburn DG, Muhandiram DR, Harris-Brandts M, Carver JP, Kay LE, Harvey TS. Solution Structure of a Cellulose-Binding Domain from Cellulomonas fimi by Nuclear Magnetic Resonance Spectroscopy Biochemistry. 34: 6993-7009. DOI: 10.2210/Pdb1Exg/Pdb |
0.404 |
|
| 1995 |
Muhandiram DR, Yamazaki T, Sykes BD, Kay LE. Measurement of 2H T1 and T1.rho. Relaxation Times in Uniformly 13C-Labeled and Fractionally 2H-Labeled Proteins in Solution Journal of the American Chemical Society. 117: 11536-11544. DOI: 10.1021/Ja00151A018 |
0.525 |
|
| 1995 |
Yamazaki T, Pascal SM, Singer AU, Forman-Kay JD, Kay LE. NMR Pulse Schemes for the Sequence-Specific Assignment of Arginine Guanidino 15N and 1H Chemical Shifts in Proteins Journal of the American Chemical Society. 117: 3556-3564. DOI: 10.1021/Ja00117A025 |
0.388 |
|
| 1995 |
Arrowsmith CH, Lee W, Revington M, Yamazaki T, Kay LE. Toward the solution structure of large (>30 kDa) proteins and macromolecular complexes Techniques in Protein Chemistry. 6: 503-510. DOI: 10.1016/S1080-8914(06)80061-X |
0.421 |
|
| 1994 |
Pascal SM, Singer AU, Gish G, Yamazaki T, Shoelson SE, Pawson T, Kay LE, Forman-Kay JD. Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide. Cell. 77: 461-72. PMID 8181064 DOI: 10.1016/0092-8674(94)90160-0 |
0.381 |
|
| 1994 |
Bagby S, Harvey TS, Kay LE, Eagle SG, Inouye S, Ikura M. Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S. 1H, 15N, and 13C assignments and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy. Biochemistry. 33: 2409-21. PMID 8117701 DOI: 10.1021/Bi00175A009 |
0.469 |
|
| 1994 |
Lee W, Revington MJ, Arrowsmith C, Kay LE. A pulsed field gradient isotope-filtered 3D 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes Febs Letters. 350: 87-90. PMID 8062930 DOI: 10.1016/0014-5793(94)00740-3 |
0.348 |
|
| 1994 |
Farrow NA, Zhang O, Forman-Kay JD, Kay LE. A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium Journal of Biomolecular Nmr. 4: 727-734. PMID 7919956 DOI: 10.1007/Bf00404280 |
0.358 |
|
| 1994 |
Zhang O, Kay LE, Olivier JP, Forman-Kay JD. Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques Journal of Biomolecular Nmr. 4: 845-858. PMID 7812156 DOI: 10.1007/BF00398413 |
0.326 |
|
| 1994 |
Farrow NA, Muhandiram R, Singer AU, Pascal SM, Kay CM, Gish G, Shoelson SE, Pawson T, Forman-Kay JD, Kay LE. Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry. 33: 5984-6003. PMID 7514039 DOI: 10.1021/Bi00185A040 |
0.412 |
|
| 1994 |
Yamazaki T, Lee W, Arrowsmith CH, Muhandiram DR, Kay LE. A Suite of Triple Resonance NMR Experiments for the Backbone Assignment of 15N, 13C, 2H Labeled Proteins with High Sensitivity Journal of the American Chemical Society. 116: 11655-11666. DOI: 10.1021/Ja00105A005 |
0.444 |
|
| 1994 |
Yamazaki T, Muhandiram R, Kay LE. NMR Experiments for the Measurement of Carbon Relaxation Properties in Highly Enriched, Uniformly 13C,15N-Labeled Proteins: Application to 13C.alpha. Carbons Journal of the American Chemical Society. 116: 8266-8278. DOI: 10.1021/Ja00097A037 |
0.371 |
|
| 1994 |
Yamazaki T, Lee W, Revington M, Mattiello DL, Dahlquist FW, Arrowsmith CH, Kay LE. An HNCA pulse scheme for the backbone assignment of 15N,13C,2H-labeled proteins: Application to a 37-kDa Trp repressor-DNA complex Journal of the American Chemical Society. 116: 6464-6465. DOI: 10.1021/Ja00093A069 |
0.376 |
|
| 1994 |
Muhandiram DR, Kay LE. Gradient-Enhanced Triple-Resonance Three-Dimensional NMR Experiments with Improved Sensitivity Journal of Magnetic Resonance, Series B. 103: 203-216. DOI: 10.1006/Jmrb.1994.1032 |
0.349 |
|
| 1994 |
Pascal S, Muhandiram D, Yamazaki T, Formankay J, Kay L. Simultaneous Acquisition of 15N- and 13C-Edited NOE Spectra of Proteins Dissolved in H2O Journal of Magnetic Resonance, Series B. 103: 197-201. DOI: 10.1006/Jmrb.1994.1031 |
0.396 |
|
| 1993 |
Yamazaki T, Forman-Kay JD, Kay LE. Two-dimensional NMR experiments for correlating carbon-13.beta. and proton.delta./.epsilon. chemical shifts of aromatic residues in 13C-labeled proteins via scalar couplings Journal of the American Chemical Society. 115: 11054-11055. DOI: 10.1021/Ja00076A099 |
0.421 |
|
| 1993 |
Kay LE. Pulsed-field gradient-enhanced three-dimensional NMR experiment for correlating 13C.alpha./.beta., 13C', and 1H.alpha. chemical shifts in uniformly carbon-13-labeled proteins dissolved in water Journal of the American Chemical Society. 115: 2055-2057. DOI: 10.1021/Ja00058A072 |
0.361 |
|
| 1993 |
Muhandiram DR, Xu GY, Kay LE. An enhanced-sensitivity pure absorption gradient 4D 15N, 13C-edited NOESY experiment Journal of Biomolecular Nmr. 3: 463-470. DOI: 10.1007/Bf00176011 |
0.328 |
|
| 1993 |
Muhandiram D, Farrow N, Xu G, Smallcombe S, Kay L. A Gradient 13C NOESY-HSQC Experiment for Recording NOESY Spectra of 13C-Labeled Proteins Dissolved in H2O Journal of Magnetic Resonance, Series B. 102: 317-321. DOI: 10.1006/Jmrb.1993.1102 |
0.381 |
|
| 1993 |
Kay L, Xu G, Singer A, Muhandiram D, Formankay J. A Gradient-Enhanced HCCH-TOCSY Experiment for Recording Side-Chain 1H and 13C Correlations in H2O Samples of Proteins Journal of Magnetic Resonance, Series B. 101: 333-337. DOI: 10.1006/Jmrb.1993.1053 |
0.38 |
|
| 1993 |
Gorlach M, Wittekind M, Farmer B, Kay L, Mueller L. Measurement of 3JHNα Vicinal Coupling Constants in Proteins Journal of Magnetic Resonance, Series B. 101: 194-197. DOI: 10.1006/Jmrb.1993.1031 |
0.354 |
|
| 1993 |
Kay L. A Three-Dimensional NMR Experiment for the Separation of Aliphatic Carbon Chemical Shifts via the Carbonyl Chemical Shift in 15N, 13C-Labeled Proteins Journal of Magnetic Resonance, Series B. 101: 110-113. DOI: 10.1006/Jmrb.1993.1018 |
0.41 |
|
| 1992 |
Barbato G, Ikura M, Kay LE, Pastor RW, Bax A. Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry. 31: 5269-78. PMID 1606151 DOI: 10.1021/Bi00138A005 |
0.562 |
|
| 1992 |
Nicholson LK, Kay LE, Baldisseri DM, Arango J, Young PE, Bax A, Torchia DA. Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease. Biochemistry. 31: 5253-63. PMID 1606149 DOI: 10.1021/Bi00138A003 |
0.584 |
|
| 1992 |
Kay LE, Nicholson LK, Delaglio F, Bax A, Torchia DA. Pulse sequences for removal of the effects of cross correlation between dipolar and chemical-shift anisotropy relaxation mechanisms on the measurement of heteronuclear T1 and T2 values in proteins Journal of Magnetic Resonance (1969). 97: 359-375. DOI: 10.1016/0022-2364(92)90320-7 |
0.509 |
|
| 1992 |
Kay LE, Ikura M, Grey A, Muhandiram D. Three-dimensional NMR experiments for the separation of side-chain correlations in proteins via the carbonyl chemical shift Journal of Magnetic Resonance (1969). 99: 652-659. DOI: 10.1016/0022-2364(92)90223-T |
0.411 |
|
| 1992 |
Kay LE, Wittekind M, McCoy MA, Friedrichs MS, Mueller L. 4D NMR triple-resonance experiments for assignment of protein backbone nuclei using shared constant-time evolution periods Journal of Magnetic Resonance (1969). 98: 443-450. DOI: 10.1016/0022-2364(92)90146-X |
0.401 |
|
| 1992 |
Kay LE, Bull TE, Nicholson LK, Griesinger C, Schwalbe H, Bax A, Torchia DA. The measurement of heteronuclear transverse relaxation times in ax3 spin systems via polarization-transfer techniques Journal of Magnetic Resonance (1969). 100: 538-558. DOI: 10.1016/0022-2364(92)90058-F |
0.523 |
|
| 1991 |
Ikura M, Kay LE, Krinks M, Bax A. Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix. Biochemistry. 30: 5498-504. PMID 2036419 DOI: 10.1021/Bi00236A024 |
0.555 |
|
| 1991 |
Kay LE, Forman-Kay JD, McCubbin WD, Kay CM. Solution structure of a polypeptide dimer comprising the fourth Ca(2+)-binding site of troponin C by nuclear magnetic resonance spectroscopy. Biochemistry. 30: 4323-33. PMID 2021624 DOI: 10.1021/Bi00231A031 |
0.41 |
|
| 1991 |
Clore GM, Kay LE, Bax A, Gronenborn AM. Four-dimensional 13C/13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1 beta. Biochemistry. 30: 12-8. PMID 1988012 DOI: 10.1021/Bi00215A002 |
0.579 |
|
| 1991 |
Ikura M, Spera S, Barbato G, Kay LE, Krinks M, Bax A. Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. Biochemistry. 30: 9216-28. PMID 1909892 DOI: 10.1021/Bi00102A013 |
0.615 |
|
| 1991 |
Ikura M, Kay LE, Bax A. Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution. Journal of Biomolecular Nmr. 1: 299-304. PMID 1841700 DOI: 10.1007/Bf01875522 |
0.578 |
|
| 1991 |
Bax A, Ikura M, Kay LE, Barbato G, Spera S. Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination. Ciba Foundation Symposium. 161: 108-19; discussion 1. PMID 1814691 |
0.536 |
|
| 1991 |
Bax A, Ikura M, Kay LE, Zhu G. Removal of F1 baseline distortion and optimization of folding in multidimensional NMR spectra Journal of Magnetic Resonance (1969). 91: 174-178. DOI: 10.1016/0022-2364(91)90422-P |
0.477 |
|
| 1991 |
Kay LE, Ikura M, Bax A. The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins Journal of Magnetic Resonance (1969). 91: 84-92. DOI: 10.1016/0022-2364(91)90410-U |
0.617 |
|
| 1991 |
Kay LE, Ikura M, Zhu G, Bax A. Four-dimensional heteronuclear triple-resonance NMR of isotopically enriched proteins for sequential assignment of backbone atoms Journal of Magnetic Resonance (1969). 91: 422-428. DOI: 10.1016/0022-2364(91)90208-B |
0.522 |
|
| 1991 |
Kay LE, Torchia DA. The effects of dipolar cross correlation on 13C methyl-carbon T1, T2, and NOE measurements in macromolecules Journal of Magnetic Resonance (1969). 95: 536-547. DOI: 10.1016/0022-2364(91)90167-R |
0.368 |
|
| 1990 |
Kay LE, Clore GM, Bax A, Gronenborn AM. Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution. Science (New York, N.Y.). 249: 411-4. PMID 2377896 DOI: 10.1126/Science.2377896 |
0.594 |
|
| 1990 |
Ikura M, Kay LE, Bax A. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry. 29: 4659-67. PMID 2372549 DOI: 10.1021/Bi00471A022 |
0.602 |
|
| 1990 |
Ikura M, Marion D, Kay LE, Shih H, Krinks M, Klee CB, Bax A. Heteronuclear 3D NMR and isotopic labeling of calmodulin. Towards the complete assignment of the 1H NMR spectrum. Biochemical Pharmacology. 40: 153-60. PMID 2372304 DOI: 10.1016/0006-2952(90)90190-V |
0.556 |
|
| 1990 |
Forman-Kay JD, Gronenborn AM, Kay LE, Wingfield PT, Marius Clore G. Studies on the solution conformation of human thioredoxin using heteronuclear15N-1H nuclear magnetic resonance spectroscopy Biochemistry. 29: 1566-1572. PMID 2334715 DOI: 10.1021/bi00458a030 |
0.322 |
|
| 1990 |
Clore GM, Szabo A, Bax A, Kay LE, Driscoll PC, Gronenborn AM. Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins Journal of the American Chemical Society. 112: 4989-4991. DOI: 10.1021/Ja00168A070 |
0.505 |
|
| 1990 |
Kay LE, Ikura M, Bax A. Proton-proton correlation via carbon-carbon couplings: a three-dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13 Journal of the American Chemical Society. 112: 888-889. DOI: 10.1021/Ja00158A070 |
0.506 |
|
| 1990 |
Bax A, Clore G, Driscoll PC, Gronenborn AM, Ikura M, Kay LE. Practical aspects of proton-carbon-carbon-proton three-dimensional correlation spectroscopy of 13C-labeled proteins Journal of Magnetic Resonance (1969). 87: 620-627. DOI: 10.1016/0022-2364(90)90320-9 |
0.579 |
|
| 1990 |
Bax A, Ikura M, Kay LE, Torchia DA, Tschudin R. Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins Journal of Magnetic Resonance (1969). 86: 304-318. DOI: 10.1016/0022-2364(90)90262-8 |
0.569 |
|
| 1990 |
Ikura M, Kay LE, Tschudin R, Bax A. Three-dimensional NOESY-HMQC spectroscopy of a 13C-labeled protein Journal of Magnetic Resonance (1969). 86: 204-209. DOI: 10.1016/0022-2364(90)90227-Z |
0.58 |
|
| 1990 |
Kay LE, Bax A. New methods for the measurement of NHCαH coupling constants in 15N-labeled proteins Journal of Magnetic Resonance (1969). 86: 110-126. DOI: 10.1016/0022-2364(90)90215-U |
0.561 |
|
| 1989 |
Kay LE, Torchia DA, Bax A. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry. 28: 8972-9. PMID 2690953 DOI: 10.1021/Bi00449A003 |
0.6 |
|
| 1989 |
Marion D, Driscoll PC, Kay LE, Wingfield PT, Bax A, Gronenborn AM, Clore GM. Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta. Biochemistry. 28: 6150-6. PMID 2675964 DOI: 10.1021/Bi00441A004 |
0.576 |
|
| 1989 |
Kay LE, Brooks B, Sparks SW, Torchia DA, Bax A. Measurement of NH-C.alpha.H coupling constants in staphylococcal nuclease by two-dimensional NMR and comparison with x-ray crystallographic results Journal of the American Chemical Society. 111: 5488-5490. DOI: 10.1021/Ja00196A078 |
0.523 |
|
| 1989 |
Marion D, Kay LE, Sparks SW, Torchia DA, Bax A. Three-dimensional heteronuclear NMR of nitrogen-15 labeled proteins Journal of the American Chemical Society. 111: 1515-1517. DOI: 10.1021/Ja00186A066 |
0.54 |
|
| 1989 |
Bax A, Kay LE, Sparks SW, Torchia DA. Line narrowing of amide proton resonances in 2D NMR spectra of proteins Journal of the American Chemical Society. 111: 408-409. DOI: 10.1021/Ja00183A082 |
0.526 |
|
| 1989 |
Kay LE, Bax A. Separation of NH and NH2 resonances in 1H-detected heteronuclear multiple-quantum correlation spectra Journal of Magnetic Resonance (1969). 84: 598-603. DOI: 10.1016/0022-2364(89)90125-X |
0.486 |
|
| 1989 |
Kay LE, Marion D, Bax A. Practical aspects of 3D heteronuclear NMR of proteins Journal of Magnetic Resonance (1969). 84: 72-84. DOI: 10.1016/0022-2364(89)90006-1 |
0.479 |
|
| 1988 |
Frederick AF, Kay LE, Prestegard JH. Location of divalent ion sites in acyl carrier protein using relaxation perturbed 2D NMR. Febs Letters. 238: 43-8. PMID 3049158 DOI: 10.1016/0014-5793(88)80222-9 |
0.506 |
|
| 1988 |
LeMaster DM, Kay LE, Brünger AT, Prestegard JH. Protein dynamics and distance determination by NOE measurements. Febs Letters. 236: 71-6. PMID 2841170 DOI: 10.1016/0014-5793(88)80287-4 |
0.508 |
|
| 1988 |
Kay LE, Holak T, Prestegard J. AX3 spin system dynamics from forbidden cross peaks in double-quantum two-dimensional NMR experiments, with application to acyl carrier protein Journal of Magnetic Resonance (1969). 76: 30-40. DOI: 10.1016/0022-2364(88)90198-9 |
0.538 |
|
| 1988 |
Kay LE, Prestegard JH. Simultaneous measurement of 13C multiplicities and 1H and 13C chemical shifts Journal of Magnetic Resonance (1969). 78: 172-177. DOI: 10.1016/0022-2364(88)90170-9 |
0.533 |
|
| 1988 |
Kay LE, Prestegard J. Spin-lattice relaxation rates of coupled spins from 2D accordion spectroscopy Journal of Magnetic Resonance (1969). 77: 599-605. DOI: 10.1016/0022-2364(88)90021-2 |
0.44 |
|
| 1988 |
Kay LE, Thomson DS, Prestegard JH. Extraction of1H1H and1H13C dipolar couplings from spectra acquired in inhomogeneous magnetic fields Magnetic Resonance in Chemistry. 26: 860-866. DOI: 10.1002/mrc.1260261010 |
0.462 |
|
| 1987 |
Kay LE, Prestegard JH. Methyl group dynamics from relaxation of double quantum filtered NMR signals. Application to deoxycholate Journal of the American Chemical Society. 109: 3829-3835. DOI: 10.1021/Ja00247A002 |
0.509 |
|
| 1987 |
Kay LE, Jones P, Prestegard J. Strong coupling effects in the homonuclear RELAY experiment, with applications to leucine spin systems of octanoyl-acyl carrier protein Journal of Magnetic Resonance (1969). 72: 392-396. DOI: 10.1016/0022-2364(87)90307-6 |
0.483 |
|
| 1987 |
KAY LE, PRESTEGARD JH. ChemInform Abstract: Methyl Group Dynamics from Relaxation of Double Quantum Filtered NMR Signals: Application to Deoxycholate. Cheminform. 18. DOI: 10.1002/chin.198743043 |
0.448 |
|
| 1986 |
Corson DC, Williams TC, Kay LE, Sykes BD. 1H NMR spectroscopic studies of calcium-binding proteins. 1. Stepwise proteolysis of the C-terminal alpha-helix of a helix-loop-helix metal-binding domain. Biochemistry. 25: 1817-26. PMID 3707912 DOI: 10.1021/Bi00355A055 |
0.58 |
|
| 1986 |
Kay LE, Holak TA, Johnson BA, Armitage IM, Prestegard JH. Second-order effects in two-dimensional cross-relaxation spectra of proteins: investigation of glycine spin systems Journal of the American Chemical Society. 108: 4242-4244. DOI: 10.1021/Ja00274A076 |
0.542 |
|
| 1986 |
Kay LE, Prestegard J. An application of pulse-gradient double-quantum spin echoes to diffusion measurements on molecules with scalar-coupled spins Journal of Magnetic Resonance (1969). 67: 103-113. DOI: 10.1016/0022-2364(86)90413-0 |
0.439 |
|
| 1986 |
Kay LE, Scarsdale JN, Hare DR, Prestegard JH. Simulation of two-dimensional cross-relaxation spectra in strongly coupled spin systems Journal of Magnetic Resonance (1969). 68: 515-525. DOI: 10.1016/0022-2364(86)90340-9 |
0.475 |
|
| 1985 |
Gariépy J, Kay LE, Kuntz ID, Sykes BD, Hodges RS. Nuclear magnetic resonance determination of metal-proton distances in a synthetic calcium binding site of rabbit skeletal troponin C Biochemistry. 24: 544-550. PMID 2983759 DOI: 10.1021/Bi00323A045 |
0.546 |
|
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