L. Kay

发表

When Are Two Heads Better than One and Why?

A. Koriat, P. Neudecker, Paul Robustelli, 2012, Science.

Observing biological dynamics at atomic resolution using NMR.

L. Kay, A. Mittermaier, 2009, Trends in biochemical sciences.

Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR

C. Dobson, L. Kay, X. Salvatella, 2004, Nature.

Multidimensional NMR Methods for Protein Structure Determination

L. Kay, J. Forman-Kay, V. Kanelis, 2001, IUBMB life.

Assignment of 1HN, 15N, 13Cα, 13CO and 13Cβ resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopy

L. Kay, C. Arrowsmith, F. Mulder, 2000 .

Propagation of dynamic changes in barnase upon binding of barstar: an NMR and computational study.

Dmitry M Korzhnev, Vladislav Yu Orekhov, Martin Billeter, 2007, Journal of molecular biology.

Variable Control of Ets-1 DNA Binding by Multiple Phosphates in an Unstructured Region

L. Kay, Gregory M Lee, L. McIntosh, 2005, Science.

Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution.

A M Gronenborn, G M Clore, L. Kay, 1990, Science.

Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins

Paul C. Driscoll, G. Marius Clore, Ad Bax, 1990 .

Methods for Measurement of Intermolecular NOEs by Multinuclear NMR Spectroscopy: Application to a Bacteriophage λ N-Peptide/boxB RNA Complex

Jack Greenblatt, Pascale Legault, Lewis E. Kay, 1997 .

Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR.

L. Kay, F. Dahlquist, F. Mulder, 2000, Biochemistry.

Structure of a AAA+ unfoldase in the process of unfolding substrate

L. Kay, J. Rubinstein, Z. A. Ripstein, 2017, bioRxiv.

Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study

L. Kay, K. Ginalski, J. Rubinstein, 2016, Proceedings of the National Academy of Sciences.

Sparsely populated folding intermediates of the Fyn SH3 domain: matching native-centric essential dynamics and experiment.

H. Chan, L. Kay, H. Kaya, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.

L. Kay, D. Yang, D. Yang, 1996, Journal of molecular biology.

Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy.

L. Kay, J. Forman-Kay, W. Choy, 2001, Journal of the American Chemical Society.

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.

T. Pawson, L. Kay, S. Shoelson, 1994, Biochemistry.

An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates.

L. Kay, D. Torchia, D. Korzhnev, 2002, Journal of the American Chemical Society.

Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy.

L. Kay, M. Tollinger, J. Forman-Kay, 2005, Journal of the American Chemical Society.

Intrinsic dynamics of an enzyme underlies catalysis

L. Kay, D. A. Bosco, E. Eisenmesser, 2005, Nature.

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

L. Kay, J. Forman-Kay, O. Zhang, 1994, Journal of biomolecular NMR.

Slow dynamics in folded and unfolded states of an SH3 domain.

L. Kay, F. Mulder, M. Tollinger, 2001, Journal of the American Chemical Society.

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

L. Kay, N. Sonenberg, R. Vernon, 2014, Nature.

A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

L. Kay, A. Bax, M. Ikura, 1990, Biochemistry.

A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin

L. Kay, A. Bax, M. Ikura, 1990 .

Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy.

L. Kay, V. Tugarinov, R. Muhandiram, 2001, Journal of molecular biology.

The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy

L. Kay, O. Millet, Rhea P. Hudson, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins

L. Kay, A. Bax, D. Torchia, 1990 .

Protein dynamics and conformational disorder in molecular recognition

L. Kay, J. Forman-Kay, T. Mittag, 2009, Journal of molecular recognition : JMR.

Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease.

L. Kay, A. Bax, D. Torchia, 1989, Biochemistry.

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.

L. Kay, F. Dahlquist, F. Mulder, 2001, Journal of the American Chemical Society.

Tracing an allosteric pathway regulating the activity of the HslV protease

L. Kay, L. Shi, Lewis E Kay, 2014, Proceedings of the National Academy of Sciences.

Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints

Jill Trewhella, Ad Bax, Alexander Grishaev, 2008, Journal of biomolecular NMR.

Magnetic resonance realization of decoherence-free quantum computation.

Daniel A Lidar, L. Kay, D. Lidar, 2003, Physical review letters.

Multiple-quantum relaxation dispersion NMR spectroscopy probing millisecond time-scale dynamics in proteins: theory and application.

Dmitry M Korzhnev, Karin Kloiber, L. Kay, 2004, Journal of the American Chemical Society.

NMR studies of protein structure and dynamics.

L. Kay, Lewis E Kay, 2005, Journal of magnetic resonance.

Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible.

M Ikura, L. Kay, A. Bax, 1992, Biochemistry.

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

L. Kay, M. Latham, 2012, PloS one.

Role of domain interactions in the aggregation of full-length immunoglobulin light chains

L. Kay, J. Kelly, G. Morgan, 2018, Proceedings of the National Academy of Sciences.

Structure of a Numb PTB domain–peptide complex suggests a basis for diverse binding specificity

Tony Pawson, Julie D. Forman-Kay, C. Jane McGlade, 1998, Nature Structural Biology.

Multiple modes of peptide recognition by the PTB domain of the cell fate determinant Numb

T Pawson, T. Pawson, L. Kay, 2000, The EMBO journal.

Protein dynamics from NMR

Lewis E. Kay, L. Kay, 1998, Nature Structural Biology.

Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein.

L. Kay, J. Forman-Kay, W. Choy, 2000, Journal of molecular biology.

Quantitative measurement of exchange dynamics in proteins via 13C relaxation dispersion of 13CHD2-labeled samples

L. Kay, E. Rennella, A. Schuetz, 2016, Journal of biomolecular NMR.

13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.

L. Kay, G. Bouvignies, A. Baldwin, 2010, Journal of the American Chemical Society.

Three-dimensional NMR experiments for the separation of side-chain correlations in proteins via the carbonyl chemical shift

L. Kay, M. Ikura, D. Muhandiram, 1992 .

NMR experiments for studies of dilute and condensed protein phases: Application to the phase-separating protein CAPRIN1.

L. Kay, J. Forman-Kay, D. Muhandiram, 2020, Journal of the American Chemical Society.

A methyl 1H double quantum CPMG experiment to study protein conformational exchange

L. Kay, Tairan Yuwen, Anusha B Gopalan, 2018, Journal of Biomolecular NMR.

A 4D TROSY-based pulse scheme for correlating 1HNi,15Ni,13Cαi,13C′i−1 chemical shifts in high molecular weight, 15N,13C, 2H labeled proteins

L. Kay, R. Konrat, D. Yang, 1999, Journal of biomolecular NMR.

Separation of NH and NH2 resonances in 1H-detected heteronuclear multiple-quantum correlation spectra

L. Kay, A. Bax, 1989 .

Sensitivity enhancement of 13C T1 measurements via polarization transfer

L. Kay, T. Jue, B. Bangerter, 1987 .

New developments in isotope labeling strategies for protein solution NMR spectroscopy.

L. Kay, N. Goto, L E Kay, 2000, Current opinion in structural biology.

Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.

L. Kay, V. Tugarinov, P. Hwang, 2004, Annual review of biochemistry.

A MULTIDIMENSIONAL NMR EXPERIMENT FOR MEASUREMENT OF THE PROTEIN DIHEDRAL ANGLE PSI BASED ON CROSS-CORRELATED RELAXATION BETWEEN 1HALPHA -13CALPHA D IPOLAR AND 13C' (CARBONYL) CHEMICAL SHIFT ANISOTROPY MECHANISMS

L. Kay, R. Konrat, Daiwen Yang, 1997 .

Methyl groups as probes of supra-molecular structure, dynamics and function

Lewis E. Kay, L. Kay, A. Ruschak, 2010, Journal of biomolecular NMR.

A Suite of Triple Resonance NMR Experiments for the Backbone Assignment of 15N, 13C, 2H Labeled Proteins with High Sensitivity

Weontae Lee, Cheryl H. Arrowsmith, Toshio Yamazaki, 1994 .

Measurement of 2H T1 and T1.rho. Relaxation Times in Uniformly 13C-Labeled and Fractionally 2H-Labeled Proteins in Solution

Brian D. Sykes, Toshio Yamazaki, Lewis E. Kay, 1995 .

Selective methyl group protonation of perdeuterated proteins.

T Pawson, T. Pawson, L. Kay, 1996, Journal of molecular biology.

Assignment of 15N, 13Cα, 13Cβ, and HN Resonances in an 15N,13C,2H Labeled 64 kDa Trp Repressor−Operator Complex Using Triple-Resonance NMR Spectroscopy and 2H-Decoupling

L. Kay, K. Gardner, C. Arrowsmith, 1996 .

Production and Incorporation of 15N, 13C, 2H (1H-δ1 Methyl) Isoleucine into Proteins for Multidimensional NMR Studies

Lewis E. Kay, Kevin H. Gardner, L. Kay, 1997 .

The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins.

L. Kay, K. Gardner, K H Gardner, 1998, Annual review of biophysics and biomolecular structure.

Solution NMR Studies of a 42 KDa Escherichia Coli Maltose Binding Protein/β-Cyclodextrin Complex: Chemical Shift Assignments and Analysis

Kalle Gehring, Lewis E. Kay, Kevin H. Gardner, 1998 .

Structure of an Intermediate State in Protein Folding and Aggregation

Michele Vendruscolo, Andrea Cavalli, Paul Robustelli, 2012, Science.

Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR.

L. Kay, M. Ikura, K. Yap, 2002, Biochemistry.

Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release.

Walid A Houry, L. Kay, W. Houry, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Comparison of 13CH3, 13CH2D, and 13CHD2 methyl labeling strategies in proteins

L. Kay, V. Tugarinov, Jason E. Ollerenshaw, 2005, Journal of biomolecular NMR.

Methyl group dynamics from relaxation of double quantum filtered NMR signals. Application to deoxycholate

L. Kay, J. Prestegard, 1987 .

Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease.

L. Kay, A. Bax, L. Nicholson, 1992, Biochemistry.

An (H)C(CO)NH-TOCSY pulse scheme for sequential assignment of protonated methyl groups in otherwise deuterated 15N, 13C-labeled proteins

L. Kay, K. Gardner, R. Konrat, 1996, Journal of biomolecular NMR.

Improved 1HN-detected triple resonance TROSY-based experiments

L. Kay, Daiwen Yang, D. Yang, 1999, Journal of biomolecular NMR.

Studying excited states of proteins by NMR spectroscopy

Frederick W. Dahlquist, Lewis E. Kay, L. Kay, 2001, Nature Structural Biology.

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

L. Kay, M. Tollinger, W. Choy, 2001, Journal of biomolecular NMR.

Ile, Leu, and Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods.

L. Kay, V. Tugarinov, Lewis E Kay, 2003, Journal of the American Chemical Society.

L. Kay, V. Tugarinov, P. Hwang, 2003, Journal of the American Chemical Society.

Side chain assignments of Ile delta 1 methyl groups in high molecular weight proteins: an application to a 46 ns tumbling molecule.

L. Kay, V. Tugarinov, 2003, Journal of the American Chemical Society.

Viscosity-dependent kinetics of protein conformational exchange: microviscosity effects and the need for a small viscogen.

Pramodh Vallurupalli, L. Kay, Lewis E Kay, 2014, The journal of physical chemistry. B.

Atomic Resolution Mechanism of Ligand Binding to a Solvent Inaccessible Cavity in T4 Lysozyme

L. Kay, N. Ahalawat, J. Mondal, 2018, bioRxiv.

Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit.

L. Kay, F. Glaser, H. Ovaa, 2017, Cell chemical biology.

Interplay of buried histidine protonation and protein stability in prion misfolding

S. Wodak, L. Kay, A. Malevanets, 2017, Scientific Reports.

Cross-validation of the structure of a transiently formed and low populated FF domain folding intermediate determined by relaxation dispersion NMR and CS-Rosetta.

L. Kay, D. Korzhnev, A. Vėlyvis, 2012, The journal of physical chemistry. B.

Solution Structure of a TBP–TAFII230 Complex Protein Mimicry of the Minor Groove Surface of the TATA Box Unwound by TBP

L. Kay, M. Ikura, Y. Nakatani, 1998, Cell.

Protein Dynamics as Studied by Solution NMR Techniques

L. Kay, L. Nicholson, D. Torchia, 1996 .

The integral membrane enzyme PagP alternates between two dynamically distinct states.

L. Kay, P. Hwang, R. Bishop, 2004, Proceedings of the National Academy of Sciences of the United States of America.

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.

L. Kay, A. Gronenborn, A. Bax, 1989, Biochemistry.

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.

S. Inouye, L. Kay, M. Ikura, 1994, Biochemistry.

An NMR Experiment for Measuring Methyl−Methyl NOEs in 13C-Labeled Proteins with High Resolution

L. Kay, K. Gardner, R. Byrd, 1998 .

A Computational Study of the Effects of 13C–13C Scalar Couplings on 13C CEST NMR Spectra: Towards Studies on a Uniformly 13C‐Labeled Protein

L. Kay, G. Bouvignies, P. Vallurupalli, 2013, Chembiochem : a European journal of chemical biology.

Four-Dimensional 13 C / 13 C-Edited Nuclear Overhauser Enhancement Spectroscopy of a Protein in Solution : Application to Interleukin 1

Marius, L. Kay, Bax, 2022 .

Protein dynamics from NMR.

L. Kay, 1998 .

A product operator description of AB and ABX spin systems

L. Kay, R. Mcclung, 1988 .

NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions.

L. Kay, K. Crowhurst, C. Kay, 1999, Journal of molecular biology.

Concurrent Increases and Decreases in Local Stability and Conformational Heterogeneity in Cu, Zn Superoxide Dismutase Variants Revealed by Temperature-Dependence of Amide Chemical Shifts.

L. Kay, Colleen M. Doyle, J. Rumfeldt, 2016, Biochemistry.

Dramatic Decrease in CEST Measurement Times Using Multi-Site Excitation.

L. Kay, G. Bouvignies, Tairan Yuwen, 2018, Chemphyschem : a European journal of chemical physics and physical chemistry.

Structural and dynamic characterization of an SH2 domain-phosphopeptide complex by NMR approaches.

L. Kay, J. Forman-Kay, A. Singer, 1995, Biochemical Society transactions.

Reversible inhibition of the ClpP protease via an N-terminal conformational switch

L. Kay, W. Houry, M. Vendruscolo, 2018, Proceedings of the National Academy of Sciences.

Three-Dimensional HMQC-NOESY, NOESY-HMQC, and NOESY-HSQC

L. Kay, R. Muhandiram, 2007 .

Specific 15N, NH correlations for residues in15 N, 13C and fractionally deuterated proteins that immediately follow methyl-containing amino acids

L. Kay, L. McIntosh, Daiwen Yang, 1997, Journal of biomolecular NMR.

Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer.

L. Kay, J. Forman-Kay, N. Farrow, 1995, Biochemistry.

Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease

L. Kay, Y. Toyama, R. Harkness, 2022, Proceedings of the National Academy of Sciences of the United States of America.

Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR

L. Kay, J. Maynes, Y. Toyama, 2021, Proceedings of the National Academy of Sciences.

NMR studies of protein structure and dynamics - a look backwards and forwards.

L. Kay, 2011, Journal of magnetic resonance.

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.

L. Kay, D. Korzhnev, H. van Ingen, 2009, The journal of physical chemistry. B.

Dipolar dynamic frequency shifts in multiple‐quantum spectra of methyl groups in proteins: correlation with side‐chain motion

L. Kay, V. Tugarinov, Jason E. Ollerenshaw, 2006, Magnetic resonance in chemistry : MRC.

A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups.

L. Kay, O. Millet, N. Skrynnikov, 2005, Journal of the American Chemical Society.

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.

L. Kay, F. Dahlquist, F. Mulder, 2001, Journal of the American Chemical Society.

A Sensitive Pulse Scheme for Measuring the Backbone Dihedral Angle ψ Based on Cross-correlation Between 13Cα-1Hα Dipolar and Carbonyl Chemical Shift Anisotropy Relaxation Interactions

L. Kay, Daiwen Yang, Kevin H. Gardner, 1998, Journal of biomolecular NMR.

NMR Studies of Protein Sidechain Dynamics

W. Gronwald, L. Kay, B. Sykes, 1998 .

Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy

L. Kay, T. Harvey, D. Kilburn, 1995 .

Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy.

L. Kay, T. Harvey, D. Kilburn, 1995, Biochemistry.

Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of Δ131Δ

L. Kay, D. Shortle, W. Choy, 2003 .

Probing Residual Interactions in Unfolded Protein States Using NMR Spin Relaxation Techniques: An Application to Δ131Δ

L. Kay, W. Choy, 2003 .

FV-162 is a novel, orally bioavailable, irreversible proteasome inhibitor with improved pharmacokinetics displaying preclinical efficacy with continuous daily dosing

A. Shamas-Din, L. Kay, S. Trudel, 2015, Cell Death and Disease.

Significantly improved resolution for noe correlations from valine and isoleucine (C(y)2) methyl groups in 15N, 13C- and 15N, 13C, 2H-labeled proteins

L. Kay, K. Gardner, C. Zwahlen, 1998 .

AX3 spin system dynamics from forbidden cross peaks in double-quantum two-dimensional NMR experiments, with application to acyl carrier protein

L. Kay, J. Prestegard, T. Holak, 1988 .

NMR PULSE SCHEMES FOR THE SEQUENCE-SPECIFIC ASSIGNMENT OF ARGININE GUANIDINO 15N AND 1H CHEMICAL SHIFTS IN PROTEINS

L. Kay, J. Forman-Kay, A. Singer, 1995 .

Probing Cooperativity of N‐Terminal Domain Orientations in the p97 Molecular Machine: Synergy Between NMR Spectroscopy and Cryo‐EM

L. Kay, J. Rubinstein, Z. A. Ripstein, 2020 .

Probing cooperativity of N-terminal domain orientations in the p97 molecular machine: synergy between NMR and cryo-EM.

L. Kay, J. Rubinstein, Z. A. Ripstein, 2020, Angewandte Chemie.

Magnetic resonance realization of decoherence-free quantum computation.

Daniel A. Lidar, L. Kay, D. Lidar, 2003, Physical review letters.

An exchange-free measure of 15N transverse relaxation: an NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange.

L. Kay, Yawen Bai, Daiwen Yang, 2007, Journal of the American Chemical Society.

Measurement of 1Hα transverse relaxation rates in proteins: application to solvent PREs

L. Kay, A. Rangadurai, Y. Toyama, 2022, Journal of Biomolecular NMR.

Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.

L. Kay, M. Vendruscolo, C. Camilloni, 2017, Physical chemistry chemical physics : PCCP.

Probing Invisible, Low-Populated States of Protein Molecules by Relaxation Dispersion NMR Spectroscopy: An Application to Protein Folding

L. Kay, D. Korzhnev, 2008 .

Protein dynamics from NMR.

L. Kay, 1998, Nature structural biology.

Spin-lattice relaxation rates of coupled spins from 2D accordion spectroscopy

L. Kay, J. Prestegard, 1988 .

Strong coupling effects in the homonuclear RELAY experiment, with applications to leucine spin systems of octanoyl-acyl carrier protein

L. Kay, J. Prestegard, Paul-James Jones, 1987 .

An HNCA Pulse Scheme for the Backbone Assignment of 15N,13C,2H-Labeled Proteins: Application to a 37-kDa Trp Repressor-DNA Complex

L. Kay, F. Dahlquist, C. Arrowsmith, 1994 .

Optimizing frequency sampling in CEST experiments

L. Kay, Nicolas Bolik-Coulon, D. Hansen, 2022, Journal of Biomolecular NMR.

Determining valine side-chain rotamer conformations in proteins from methyl 13C chemical shifts: application to the 360 kDa half-proteasome.

L. Kay, D. Hansen, D. Flemming Hansen, 2011, Journal of the American Chemical Society.

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.

A. Fersht, Patrik Lundström, L. Kay, 2007, Journal of molecular biology.

Global multi-method analysis of interaction parameters for reversibly self-associating macromolecules at high concentrations

L. Kay, Huaying Zhao, P. Schuck, 2021, Scientific Reports.

Three-Dimensional Heteronuclear NMR of 15 N-Labeled Proteins

L. Kay, A. Bax, D. Torchia, 2022 .

TROSY-based NMR evidence for a novel class of 20S proteasome inhibitors.

L. Kay, J. Rubinstein, R. Sprangers, 2008, Biochemistry.

A gradient 13C NOESY-HSQC experiment for recording NOESY spectra of 13C-labeled proteins dissolved in H2O

L. Kay, D. Muhandiram, N. Farrow, 1993 .

Revisiting dipolar relaxation of a homonuclear spin pair in the presence of a radio frequency field: a tutorial

L. Kay, Y. Toyama, 2022, Journal of Magnetic Resonance Open.

Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein

L. Kay, Y. Toyama, R. Harkness, 2021, Proceedings of the National Academy of Sciences.

Surface electrostatics dictate RNA-binding protein CAPRIN1 condensate concentration and hydrodynamic properties

L. Kay, J. Forman-Kay, A. Rangadurai, 2022, The Journal of biological chemistry.

Interaction hot spots for phase separation revealed by NMR studies of a CAPRIN1 condensed phase

L. Kay, J. Forman-Kay, Tae Hun Kim, 2021, Proceedings of the National Academy of Sciences.

Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer

L. Kay, Tairan Yuwen, A. Sekhar, 2017, Journal of Biomolecular NMR.

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

L. Kay, Tairan Yuwen, Tairan Yuwen, 2018, Journal of Biomolecular NMR.

Probing slow timescale dynamics in proteins using methyl 1H CEST

L. Kay, Rui Huang, Tairan Yuwen, 2017, Journal of Biomolecular NMR.

Longitudinal relaxation optimized amide 1H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins

L. Kay, Tairan Yuwen, Tairan Yuwen, 2017, Journal of Biomolecular NMR.

Evaluating the influence of initial magnetization conditions on extracted exchange parameters in NMR relaxation experiments: applications to CPMG and CEST

L. Kay, Tairan Yuwen, A. Sekhar, 2016, Journal of Biomolecular NMR.

Quantitative measurement of exchange dynamics in proteins via 13C relaxation dispersion of 13CHD2-labeled samples

L. Kay, E. Rennella, A. Schuetz, 2016, Journal of Biomolecular NMR.

Triple resonance-based 13Cα and 13Cβ CEST experiments for studies of ms timescale dynamics in proteins

L. Kay, Dong Long, A. Sekhar, 2014, Journal of Biomolecular NMR.

Probing slowly exchanging protein systems via 13Cα-CEST: monitoring folding of the Im7 protein

L. Kay, G. Bouvignies, Alexandar L. Hansen, 2013, Journal of Biomolecular NMR.

1H,13C-1H,1H Dipolar Cross-correlated Spin Relaxation in Methyl Groups

L. Kay, V. Tugarinov, 2004, Journal of biomolecular NMR.

A combined HNCA/HNCO experiment for 15N labeled proteins with 13C at natural abundance

L. Kay, E. Kupče, D. Muhandiram, 2003, Journal of biomolecular NMR.

Clioquinol inhibits the proteasome and displays preclinical activity in leukemia and myeloma

L. Kay, S. Trudel, R. Sprangers, 2009, Leukemia.

A methyl 1H double quantum CPMG experiment to study protein conformational exchange

L. Kay, Tairan Yuwen, P. Vallurupalli, 2018, Journal of Biomolecular NMR.

Probing non-specific interactions of Ca2+-calmodulin in E. coli lysate

L. Kay, M. Latham, 2013, Journal of Biomolecular NMR.

Determination of the Protein Backbone Dihedral Angle ψ from a Combination of NMR-Derived Cross-Correlation Spin Relaxation Rates

L. Kay, Daiwen Yang, 1998 .

Revisiting 1HN CPMG relaxation dispersion experiments: a simple modification can eliminate large artifacts

L. Kay, Tairan Yuwen, 2019, Journal of Biomolecular NMR.

An enhanced sensitivity methyl 1H triple-quantum pulse scheme for measuring diffusion constants of macromolecules

L. Kay, Jacob P. Brady, Rui Huang, 2017, Journal of Biomolecular NMR.

Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide

Tony Pawson, Julie D Forman-Kay, T. Pawson, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A

T. Pawson, L. Kay, I. Ernberg, 1999, Current Biology.

Mapping the per-residue surface electrostatic potential of CAPRIN1 along its phase-separation trajectory

L. Kay, J. Forman-Kay, A. Rangadurai, 2022, Proceedings of the National Academy of Sciences of the United States of America.

NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain.

L. Kay, A. Mittermaier, J. Forman-Kay, 2005, Biochemistry.

Assignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopy.

L. Kay, C. Arrowsmith, F. Mulder, 2000, Journal of biomolecular NMR.

Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.

P. Neudecker, A. Zarrine-Afsar, L. Kay, 2006, Biochemistry.

Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR.

L. Kay, D. Korzhnev, J. Forman-Kay, 2006, Biochemistry.

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.

P. Neudecker, L. Kay, A. Mittermaier, 2005, Journal of the American Chemical Society.

Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy.

L. Kay, A. Mittermaier, D. Korzhnev, 2005, Biochemistry.

An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.

L. Kay, Yawen Bai, W. Choy, 2005, Journal of the American Chemical Society.

Parallel acquisition of multi-dimensional spectra in protein NMR

L. Kay, E. Kupče, 2012, Journal of Biomolecular NMR.

Practical aspects of 3D heteronuclear NMR of proteins

Ad Bax, Dominique Marion, Lewis E. Kay, 1989 .

Stereospecific assignment of the NH2 resonances from the primary amides of asparagine and glutamine side chains in isotopically labeled proteins

L. Kay, L. McIntosh, E. Brun, 1997, Journal of biomolecular NMR.

CPMG relaxation dispersion NMR experiments measuring glycine 1Hα and 13Cα chemical shifts in the ‘invisible’ excited states of proteins

Patrik Lundström, L. Kay, D. Hansen, 2009, Journal of biomolecular NMR.

Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy.

L. Kay, A. Bax, M. Ikura, 1991, Biochemistry.

Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution.

L. Kay, Lewis E. Kay, 1995, Progress in biophysics and molecular biology.

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

L. Kay, 1993 .

Practical aspects of proton-carbon-carbon-proton three-dimensional correlation spectroscopy of 13C-labeled proteins

Paul C. Driscoll, G. Marius Clore, Ad Bax, 1990 .

4D NMR triple-resonance experiments for assignment of protein backbone nuclei using shared constant-time evolution periods

L. Kay, M. Friedrichs, M. Wittekind, 1992 .

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.

L. Kay, A. Bax, M. Ikura, 1991, Biochemistry.

Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G.

L. Kay, V. Tugarinov, Lewis E Kay, 2003, Journal of molecular biology.

Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view.

L. Kay, 2011, Journal of magnetic resonance.

Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states

L. Kay, D. Hansen, P. Vallurupalli, 2008, Journal of biomolecular NMR.

The A39G FF domain folds on a volcano-shaped free energy surface via separate pathways

L. Kay, Y. Toyama, P. Vallurupalli, 2021, Proceedings of the National Academy of Sciences.

Measuring Diffusion Constants of Invisible Protein Conformers by Triple-Quantum 1 H CPMG Relaxation Dispersion.

L. Kay, A. Baldwin, Tairan Yuwen, 2018, Angewandte Chemie.

Atomic resolution mechanism of ligand binding to a solvent inaccessible cavity in T4 lysozyme

Jagannath Mondal, Lewis E. Kay, Navjeet Ahalawat, 2018, bioRxiv.

Measuring hydrogen exchange rates in invisible protein excited states

L. Kay, G. Bouvignies, Dong Long, 2014, Proceedings of the National Academy of Sciences.

Measurement of histidine pKa values and tautomer populations in invisible protein states

L. Kay, Alexandar L. Hansen, 2014, Proceedings of the National Academy of Sciences.

Visualizing side chains of invisible protein conformers by solution NMR.

L. Kay, G. Bouvignies, P. Vallurupalli, 2014, Journal of molecular biology.

NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers

L. Kay, A. Sekhar, 2013, Proceedings of the National Academy of Sciences.

Probing slow chemical exchange at carbonyl sites in proteins by chemical exchange saturation transfer NMR spectroscopy.

L. Kay, P. Vallurupalli, 2013, Angewandte Chemie.

Probing slowly exchanging protein systems via 13Cα-CEST: monitoring folding of the Im7 protein

L. Kay, G. Bouvignies, Alexandar L. Hansen, 2013, Journal of Biomolecular NMR.

An R1ρ expression for a spin in chemical exchange between two sites with unequal transverse relaxation rates

L. Kay, A. Baldwin, 2013, Journal of biomolecular NMR.

Measurement of proton chemical shifts in invisible states of slowly exchanging protein systems by chemical exchange saturation transfer.

L. Kay, G. Bouvignies, 2012, The journal of physical chemistry. B.

Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1ρ: an application to αB-crystallin

L. Kay, A. Baldwin, 2012, Journal of Biomolecular NMR.

Increasing the exchange time-scale that can be probed by CPMG relaxation dispersion NMR.

L. Kay, G. Bouvignies, P. Vallurupalli, 2011, The journal of physical chemistry. B.

Solution structure of a minor and transiently formed state of a T4 lysozyme mutant

Oliver F. Lange, David Baker, Bruno E. Correia, 2011, Nature.

Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups

L. Kay, Alexandar L. Hansen, 2011, Journal of biomolecular NMR.

Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts.

P. Neudecker, L. Kay, D. Hansen, 2010, Journal of the American Chemical Society.

Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion.

P. Neudecker, L. Kay, F. Mulder, 2010, Journal of the American Chemical Society.

Selective characterization of microsecond motions in proteins by NMR relaxation.

L. Kay, Yawen Bai, D. Hansen, 2009, Journal of the American Chemical Society.

NMR spectroscopy brings invisible protein states into focus.

L. Kay, A. Baldwin, Lewis E Kay, 2009, Nature chemical biology.

Measurement of methyl group motional parameters of invisible, excited protein states by NMR spectroscopy.

L. Kay, D. Hansen, P. Vallurupalli, 2009, Journal of the American Chemical Society.

Measuring the signs of 1H(alpha) chemical shift differences between ground and excited protein states by off-resonance spin-lock R(1rho) NMR spectroscopy.

P. Neudecker, Patrik Lundström, L. Kay, 2009, Journal of the American Chemical Society.

Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.

P. Neudecker, Patrik Lundström, L. Kay, 2009, Biophysical journal.

Seeing the Invisible: Structures of Excited Protein States by Relaxation Dispersion NMR

L. Kay, P. Vallurupalli, F. D. Hansen, 2008 .

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.

L. Kay, D. Hansen, P. Vallurupalli, 2008, Journal of the American Chemical Society.

Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding.

Dmitry M Korzhnev, L. Kay, D. Korzhnev, 2008, Accounts of chemical research.

Probing structure in invisible protein states with anisotropic NMR chemical shifts.

L. Kay, D. Hansen, P. Vallurupalli, 2008, Journal of the American Chemical Society.

Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do?

P. Neudecker, Patrik Lundström, L. Kay, 2008, Journal of the American Chemical Society.

Measurement of bond vector orientations in invisible excited states of proteins

Pramodh Vallurupalli, L. Kay, E. Meirovitch, 2007, Proceedings of the National Academy of Sciences.

Fractional 13C enrichment of isolated carbons using [1-13C]- or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone Cα and side-chain methyl positions in proteins

Patrik Lundström, L. Kay, T. Carstensen, 2007, Journal of biomolecular NMR.

Complementarity of ensemble and single-molecule measures of protein motion: A relaxation dispersion NMR study of an enzyme complex

L. Kay, P. Vallurupalli, 2006, Proceedings of the National Academy of Sciences.

Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme.

Dmitry M Korzhnev, Karin Kloiber, L. Kay, 2004, Journal of the American Chemical Society.

Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.

L. Kay, F. Dahlquist, N. Skrynnikov, 2002, Journal of the American Chemical Society.

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.

L. Kay, B. Sykes, D. Corson, 1986, Biochemistry.

A ‘three‐pronged’ binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndrome

Tony Pawson, Massimo Morra, Cox Terhorst, 2002, The EMBO journal.

Assignment of Ile, Leu, and Val methyl correlations in supra-molecular systems: an application to aspartate transcarbamoylase.

L. Kay, H. K. Schachman, A. Vėlyvis, 2009, Journal of the American Chemical Society.

Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction

Shoeib Moradi, John R. Glover, Lewis E. Kay, 2013, Science.

The evolution of solution state NMR pulse sequences through the 'eyes' of triple-resonance spectroscopy.

L. Kay, 2019, Journal of magnetic resonance.

Measurement of NH-C.alpha.H coupling constants in staphylococcal nuclease by two-dimensional NMR and comparison with x-ray crystallographic results

B. Brooks, L. Kay, A. Bax, 1989 .

Structural and dynamic analysis of residual dipolar coupling data for proteins.

J H Prestegard, L. Kay, J. Prestegard, 2001, Journal of the American Chemical Society.

Field gradient techniques in NMR spectroscopy.

L. Kay, 1995, Current opinion in structural biology.

An improved 15N relaxation dispersion experiment for the measurement of millisecond time-scale dynamics in proteins.

L. Kay, D. Hansen, P. Vallurupalli, 2008, The journal of physical chemistry. B.

Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR

L. Kay, M. Bustin, Yawen Bai, 2011, Proceedings of the National Academy of Sciences.

The proteasome antechamber maintains substrates in an unfolded state

L. Kay, T. L. Religa, S. Witt, 2010, Nature.

Dynamic Regulation of Archaeal Proteasome Gate Opening As Studied by TROSY NMR

L. Kay, R. Sprangers, T. L. Religa, 2010, Science.

Quantitative dynamics and binding studies of the 20S proteasome by NMR

Lewis E. Kay, L. Kay, R. Sprangers, 2007, Nature.

Stereospecific NMR assignments of prochiral methyls, rotameric states and dynamics of valine residues in malate synthase G.

L. Kay, V. Tugarinov, 2004, Journal of the American Chemical Society.

An Isotope Labeling Strategy for Methyl TROSY Spectroscopy

L. Kay, V. Tugarinov, 2004, Journal of biomolecular NMR.

Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase g.

L. Kay, V. Tugarinov, A. Ayed, 2002, Journal of the American Chemical Society.

A robust and cost-effective method for the production of Val, Leu, Ile (δ1) methyl-protonated 15N-, 13C-, 2H-labeled proteins

L. Kay, K. Gardner, G. Mueller, 1999, Journal of biomolecular NMR.

Parallel acquisition of multi-dimensional spectra in protein NMR

L. Kay, E. Kupče, 2012, Journal of biomolecular NMR.

Detecting the "afterglow" of 13C NMR in proteins using multiple receivers.

L. Kay, R. Freeman, E. Kupče, 2010, Journal of the American Chemical Society.

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.

L. Kay, D. Muhandiram, O. Millet, 2002, Journal of the American Chemical Society.

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.

L. Kay, A. Mittermaier, D. Yang, 1998, Journal of molecular biology.

Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure

L. Kay, A. Mittermaier, J. Forman-Kay, 1999, Journal of biomolecular NMR.

NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function

L. Kay, T. Alderson, 2021, Cell.

A Gradient-Enhanced HCCH-TOCSY Experiment for Recording Side-Chain 1H and 13C Correlations in H2O Samples of Proteins

L. Kay, J. Forman-Kay, D. Muhandiram, 1993 .

Bringing dynamic molecular machines into focus by methyl-TROSY NMR.

L. Kay, Rina Rosenzweig, R. Rosenzweig, 2014, Annual review of biochemistry.

Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy

L. Kay, V. Tugarinov, V. Kanelis, 2006, Nature Protocols.

An Economical Method for Production of 2H,13CH3-Threonine for Solution NMR Studies of Large Protein Complexes: Application to the 670 kDa Proteasome

L. Kay, A. Vėlyvis, A. Ruschak, 2012, PloS one.

Solution NMR of supramolecular complexes: providing new insights into function

L. Kay, R. Sprangers, A. Vėlyvis, 2007, Nature Methods.

High-resolution four-dimensional 1H-13C NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition.

Vladislav Yu Orekhov, Ilghiz Ibraghimov, L. Kay, 2005, Journal of the American Chemical Society.

A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle

L. Kay, A. Vėlyvis, E. Rennella, 2020, Proceedings of the National Academy of Sciences.

Unveiling invisible protein states with NMR spectroscopy.

L. Kay, T. Alderson, 2019, Current opinion in structural biology.

New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy.

L. Kay, Lewis E Kay, 2016, Journal of molecular biology.

A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding

L. Kay, G. Bouvignies, 2012, Journal of biomolecular NMR.

Studying "invisible" excited protein states in slow exchange with a major state conformation.

L. Kay, G. Bouvignies, P. Vallurupalli, 2012, Journal of the American Chemical Society.

Multidimensional 2H-Based NMR Methods for Resonance Assignment, Structure Determination, and The Study of Protein Dynamics

L. Kay, K. Gardner, 2002 .

Solution NMR spectroscopy beyond 25 kDa.

L. Kay, K. Gardner, K H Gardner, 1997, Current opinion in structural biology.

Opening of a cryptic pocket in β-lactamase increases penicillinase activity

L. Kay, G. Bowman, Sukrit Singh, 2021, Proceedings of the National Academy of Sciences.

Revisiting 1HN CPMG relaxation dispersion experiments: a simple modification can eliminate large artifacts

L. Kay, Tairan Yuwen, 2019, Journal of Biomolecular NMR.

Exploring methods to expedite the recording of CEST datasets using selective pulse excitation.

L. Kay, G. Bouvignies, Tairan Yuwen, 2018, Journal of magnetic resonance.

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

L. Kay, Tairan Yuwen, 2018, Journal of biomolecular NMR.

An enhanced sensitivity methyl 1H triple-quantum pulse scheme for measuring diffusion constants of macromolecules

L. Kay, Jacob P. Brady, Rui Huang, 2017, Journal of biomolecular NMR.

Probing slow timescale dynamics in proteins using methyl 1H CEST

L. Kay, Rui Huang, Tairan Yuwen, 2017, Journal of biomolecular NMR.

Longitudinal relaxation optimized amide 1H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins

L. Kay, Tairan Yuwen, 2017, Journal of biomolecular NMR.

Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer

L. Kay, Tairan Yuwen, A. Sekhar, 2017, Journal of Biomolecular NMR.

13CHD2–CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins

L. Kay, A. Vėlyvis, Rui Huang, 2015, Journal of Biomolecular NMR.

Chi1 torsion angle dynamics in proteins from dipolar couplings.

L. Kay, A. Mittermaier, Lewis E. Kay, 2001, Journal of the American Chemical Society.

NMR Experiments for the Measurement of Carbon Relaxation Properties in Highly Enriched, Uniformly 13C,15N-Labeled Proteins: Application to 13C.alpha. Carbons

L. Kay, R. Muhandiram, T. Yamazaki, 1994 .

TROSY Triple-Resonance Four-Dimensional NMR Spectroscopy of a 46 ns Tumbling Protein

Daiwen Yang, Lewis E. Kay, L. Kay, 1999 .

αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics.

L. Kay, C. Robinson, J. Benesch, 2011, Journal of molecular biology.

Probing dynamic conformations of the high-molecular-weight αB-crystallin heat shock protein ensemble by NMR spectroscopy.

Patrick Walsh, S. Sharpe, L. Kay, 2012, Journal of the American Chemical Society.

NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond.

L. Kay, B. Reif, R. Sprangers, 2013, Angewandte Chemie.

Direct demonstration of an intramolecular SH2—phosphotyrosine interaction in the Crk protein

Tony Pawson, Toshio Yamazaki, Cyril M. Kay, 1995, Nature.

Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation

L. Kay, N. Sonenberg, R. Vernon, 2019, Science.

Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus.

L. Kay, J. Benesch, A. Baldwin, 2011, Journal of molecular biology.

Solution structure and dynamics of the outer membrane enzyme PagP by NMR

Wing-Yiu Choy, Julie D Forman-Kay, L. Kay, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Solution structure of a polypeptide dimer comprising the fourth Ca(2+)-binding site of troponin C by nuclear magnetic resonance spectroscopy.

L. Kay, C. Kay, J. Forman-Kay, 1991, Biochemistry.

Solution structure of recombinant human interleukin-6.

L. Kay, M. Stahl, H. Yu, 1997, Journal of molecular biology.

Complete 1H, 15N and 13C assignments, secondary structure, and topology of recombinant human interleukin-6

Jin Hong, L. Kay, M. Stahl, 1996, Journal of biomolecular NMR.

Changes in side-chain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein.

L. Kay, G. Varani, A. Mittermaier, 1999, Journal of molecular biology.

The ZIP5 Ectodomain Co-Localizes with PrP and May Acquire a PrP-Like Fold That Assembles into a Dimer

L. Kay, C. Arrowsmith, A. Yee, 2013, PloS one.

New Tools Provide New Insights in NMR Studies of Protein Dynamics

Lewis E. Kay, L. Kay, A. Mittermaier, 2006, Science.

Effects of maturation on the conformational free-energy landscape of SOD1

L. Kay, J. Rumfeldt, E. Meiering, 2018, Proceedings of the National Academy of Sciences.

Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways

L. Kay, G. Bouvignies, Colleen M. Doyle, 2015, eLife.

Latent and active p53 are identical in conformation

L. Kay, C. Arrowsmith, F. Mulder, 2001, Nature Structural Biology.

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.

L. Kay, J. Forman-Kay, A. Singer, 1995, Biochemistry.

Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-γ1 complexed with a high affinity binding peptide

T. Pawson, L. Kay, S. Shoelson, 1994, Cell.

Methyl TROSY: explanation and experimental verification

L. Kay, V. Tugarinov, Jason E. Ollerenshaw, 2003 .

Spectral density function mapping using 15N relaxation data exclusively

L. Kay, D. Torchia, A. Szabó, 1995, Journal of biomolecular NMR.

Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site

Mitsuhiko Ikura, Fuyuhiko Inagaki, L. Kay, 2015, Proceedings of the National Academy of Sciences.

Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination.

L. Kay, A. Bax, M. Ikura, 2007, Ciba Foundation symposium.

Quaternary dynamics and plasticity underlie small heat shock protein chaperone function

L. Kay, C. Robinson, Florian Stengel, 2010, Proceedings of the National Academy of Sciences.

Structural Coupling of SH2-Kinase Domains Links Fes and Abl Substrate Recognition and Kinase Activation

G. Superti-Furga, T. Pawson, L. Kay, 2008, Cell.

A Potential SH3 Domain-binding Site in the Crk SH2 Domain*

T. Pawson, L. Kay, G. Gish, 1996, The Journal of Biological Chemistry.

NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel

L. Kay, J. Forman-Kay, V. Kanelis, 1998 .

Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR.

L. Kay, K. Gardner, M. Rosen, 1997, Biochemistry.

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery

Zev A. Ripstein, John L. Rubinstein, Lewis E. Kay, 2019, bioRxiv.

A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin

L. Kay, G. Privé, P. Hwang, 2004, The EMBO journal.

Novel proteasome inhibitors to overcome bortezomib resistance.

L. Kay, A. Schimmer, A. Ruschak, 2011, Journal of the National Cancer Institute.

Effect of noncompetitive proteasome inhibition on bortezomib resistance.

L. Kay, S. Trudel, R. Sprangers, 2010, Journal of the National Cancer Institute.

An NMR View of Protein Dynamics in Health and Disease.

L. Kay, A. Sekhar, 2019, Annual review of biophysics.

Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation

H. Chan, L. Kay, J. Forman-Kay, 2017, Proceedings of the National Academy of Sciences.

Enhanced-Sensitivity Triple-Resonance Spectroscopy with Minimal H2O Saturation

L. Kay, T. Yamazaki, G. Xu, 1994 .

Gradient-Enhanced Triple-Resonance Three-Dimensional NMR Experiments with Improved Sensitivity

L. Kay, D. Muhandiram, 1994 .

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

L. Kay, G. Varani, L. Varani, 2000, Nature Structural Biology.

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.

L. Kay, W. Choy, G. Mueller, 2000, Journal of molecular biology.

Structure and mechanism in transcriptional antitermination by the bacteriophage lambda N protein.

J. Greenblatt, L. Kay, P. Legault, 1998, Cold Spring Harbor symposia on quantitative biology.

Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein.

Joyce Li, J. Greenblatt, L. Kay, 1998, Molecular cell.

The role of protein thermodynamics and primary structure in fibrillogenesis of variable domains from immunoglobulin light-chains.

L. Kay, J. Kelly, G. Morgan, 2019, Journal of the American Chemical Society.

L. Kay, A. Gronenborn, A. Bax, 1989, Biochemistry.

Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays.

T. Pawson, L. Kay, F. Sicheri, 2009, Journal of molecular biology.

NMR methods for the study of protein structure and dynamics.

L. Kay, L E Kay, 1997, Biochemistry and cell biology = Biochimie et biologie cellulaire.

An optimized relaxation-based coherence transfer NMR experiment for the measurement of side-chain order in methyl-protonated, highly deuterated proteins.

L. Kay, V. Tugarinov, Hechao Sun, 2011, The journal of physical chemistry. B.

Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy.

Patrik Lundström, L. Kay, D. Hansen, 2009, Journal of the American Chemical Society.

Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy.

Yawen Bai, L. Kay, Yawen Bai, 2009, Journal of molecular biology.

NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B

Yawen Bai, L. Kay, Carl Wu, 2008, Nature Structural &Molecular Biology.

Characterization of the backbone dynamics of folded and denatured states of an SH3 domain.

L. Kay, J. Forman-Kay, N. Farrow, 1997, Biochemistry.

Cotranslocational processing of the protein substrate calmodulin by an AAA+ unfoldase occurs via unfolding and refolding intermediates

L. Kay, R. Augustyniak, 2018, Proceedings of the National Academy of Sciences.

Confronting the Invisible: Assignment of Protein 1HN Chemical Shifts in Cases of Extreme Broadening.

L. Kay, Tae Hun Kim, E. Rennella, 2020, The journal of physical chemistry letters.

Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain

T. Pawson, A. Zarrine-Afsar, L. Kay, 2007, Proceedings of the National Academy of Sciences.

Self-Assembly of Human Profilin-1 Detected by Carr-Purcell-Meiboom-Gill Nuclear Magnetic Resonance (CPMG NMR) Spectroscopy.

L. Kay, E. Rennella, A. Sekhar, 2017, Biochemistry.

Stabilization of amyloidogenic immunoglobulin light chains by small molecules

Steven J Brown, L. Kay, I. Wilson, 2019, Proceedings of the National Academy of Sciences.

Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor

Mike Tyers, Xiaojing Tang, Wing-Yiu Choy, 2008, Proceedings of the National Academy of Sciences.

Structure of a AAA+ unfoldase in the process of unfolding substrate

L. Kay, J. Rubinstein, Z. A. Ripstein, 2017, bioRxiv.

Three-dimensional heteronuclear NMR of nitrogen-15 labeled proteins

Ad Bax, Dominique Marion, Lewis E. Kay, 1989 .

Measuring Solvent Hydrogen Exchange Rates by Multifrequency Excitation 15N CEST: Application to Protein Phase Separation.

L. Kay, G. Bouvignies, A. Bah, 2018, The journal of physical chemistry. B.

The RNF168 paralog RNF169 defines a new class of ubiquitylated histone reader involved in the response to DNA damage

G. Portella, D. Durocher, L. Kay, 2017, eLife.

The RNF 168 paralog RNF 169 defines a new class of ubiquitylated histone reader involved in the response to DNA damage

G. Portella, D. Durocher, L. Kay, 2017 .

The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinase

L. Kay, A. Mittermaier, Lewis E Kay, 2004, Protein science : a publication of the Protein Society.

The effects of mutations on motions of side-chains in protein L studied by 2H NMR dynamics and scalar couplings.

David Baker, D. Baker, L. Kay, 2003, Journal of molecular biology.

Model selection for the interpretation of protein side chain methyl dynamics

L. Kay, W. Choy, 2003, Journal of biomolecular NMR.

The Effects of Mutations on Motions of Side-chains in Protein L Studied by 2 H NMR Dynamics and

L. Kay, A. Mittermaier, D. Baker, 2003 .

Domain orientation in β-cyclodextrin-loaded maltose binding protein: Diffusion anisotropy measurements confirm the results of a dipolar coupling study

L. Kay, P. Hwang, N. Skrynnikov, 2001, Journal of biomolecular NMR.

Relative Orientation of Peptide Planes in Proteins Is Reflected in Carbonyl-Carbonyl Chemical Shift Anisotropy Cross-Correlated Spin Relaxation

L. Kay, R. Konrat, D. Muhandiram, 2000 .

Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity.

L. Kay, B. Sykes, L. Spyracopoulos, 1998, Journal of molecular biology.

Correlation between binding and dynamics at SH2 domain interfaces

L. Kay, S. Shoelson, J. Forman-Kay, 1998, Nature Structural Biology.

The Development of NMR Methods to Study Protein Structure and Dynamics

L. Kay, 1998 .

Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation.

L. Kay, J. Forman-Kay, D. Yang, 1997, Journal of molecular biology.

Structural, Dynamic, and Folding Studies of SH2 and SH3 Domains

L. Kay, J. Forman-Kay, N. Farrow, 1996 .

Heteronuclear NMR Studies of the Molecular Dynamics of Staphylococcal Nuclease

L. Kay, L. Nicholson, D. Torchia, 1993 .

The effects of dipolar cross correlation on 13C methyl-carbon T1, T2, and NOE measurements in macromolecules

L. Kay, D. Torchia, 1991 .

Protein dynamics and distance determination by NOE measurements

L. Kay, J. Prestegard, A. Brünger, 1988, FEBS letters.

Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP

L. Kay, Jacob P. Brady, Z. A. Ripstein, 2021, Proceedings of the National Academy of Sciences.

Exploring long-range cooperativity in the 20S proteasome core particle from Thermoplasma acidophilum using methyl-TROSY–based NMR

L. Kay, Rui Huang, Zanlin Yu, 2020, Proceedings of the National Academy of Sciences.

Membrane-dependent modulation of the mTOR activator Rheb: NMR observations of a GTPase tethered to a lipid-bilayer nanodisc.

L. Kay, M. Ikura, P. Stathopulos, 2013, Journal of the American Chemical Society.

A simple strategy for 13C,1H labeling at the Ile-γ2 methyl position in highly deuterated proteins

L. Kay, A. Vėlyvis, A. Ruschak, 2010, Journal of biomolecular NMR.

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

L. Kay, F. Dahlquist, Chun Wu, 2014, Biochemistry.

What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR.

L. Kay, F. Dahlquist, N. Skrynnikov, 2001, Journal of molecular biology.

New methods for the measurement of NHCαH coupling constants in 15N-labeled proteins

L. Kay, A. Bax, 1990 .

Heteronuclear 3D NMR and isotopic labeling of calmodulin. Towards the complete assignment of the 1H NMR spectrum.

L. Kay, A. Bax, M. Ikura, 1990, Biochemical pharmacology.

Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins. 1990.

Ad Bax, Mitsuhiko Ikura, L. Kay, 1990, Journal of magnetic resonance.

Proton-proton correlation via carbon-carbon couplings: a three-dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13

Ad Bax, Mitsuhiko Ikura, Lewis E. Kay, 1990 .

Three-dimensional NOESY-HMQC spectroscopy of a 13C-labeled protein

L. Kay, A. Bax, M. Ikura, 1990 .

Line narrowing of amide proton resonances in 2D NMR spectra of proteins

Ad Bax, Lewis E. Kay, L. Kay, 1989 .

An enhanced-sensitivity pure absorption gradient 4D 15N, 13C-edited NOESY experiment

L. Kay, D. Muhandiram, G. Xu, 1993 .

Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy

L. Kay, G. Bouvignies, D. Hansen, 2011, Journal of biomolecular NMR.

Measurement of methyl axis orientations in invisible, excited states of proteins by relaxation dispersion NMR spectroscopy.

L. Kay, A. Baldwin, D. Hansen, 2009, Journal of the American Chemical Society.

Correlation between dynamics and high affinity binding in an SH2 domain interaction.

L. Kay, J. Forman-Kay, D. Muhandiram, 1996, Biochemistry.

L. Kay, M. Latham, 2014, Journal of molecular biology.

Measuring 13Cβ chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy

Patrik Lundström, L. Kay, Hong Lin, 2009, Journal of biomolecular NMR.

Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy

Patrik Lundström, L. Kay, D. Hansen, 2009, Nature Protocols.

Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively 13C labeled samples

Patrik Lundström, L. Kay, D. Hansen, 2008, Journal of biomolecular NMR.

A single-quantum methyl 13C-relaxation dispersion experiment with improved sensitivity

Pramodh Vallurupalli, Patrik Lundström, Patrik Lundström, 2007, Journal of biomolecular NMR.

Strong coupling effects during X-pulse CPMG experiments recorded on heteronuclear ABX spin systems: artifacts and a simple solution

L. Kay, L. Scott, J. Williamson, 2007, Journal of biomolecular NMR.

Measurement of signs of chemical shift differences between ground and excited protein states: a comparison between H(S/M)QC and R1ρ methods

L. Kay, R. Konrat, D. Korzhnev, 2010, Journal of biomolecular NMR.

Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy

Lewis E. Kay, Pramodh Vallurupalli, D. Flemming Hansen, 2008, Proceedings of the National Academy of Sciences.

Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins.

L. Kay, V. Orekhov, D. Korzhnev, 2004, Journal of the American Chemical Society.

A Methyl-TROSY-Based 1 H Relaxation Dispersion Experiment for Studies of Conformational Exchange in High Molecular Weight Proteins.

L. Kay, Rui Huang, Tairan Yuwen, 2019, Angewandte Chemie.

Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.

L. Kay, V. Tugarinov, Jason E. Ollerenshaw, 2005, Journal of the American Chemical Society.

A comparative CEST NMR study of slow conformational dynamics of small GTPases complexed with GTP and GTP analogues.

L. Kay, G. Bouvignies, M. Ikura, 2013, Angewandte Chemie.

Φ-Value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy

A. Zarrine-Afsar, L. Kay, A. Davidson, 2007, Proceedings of the National Academy of Sciences.

Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme.

L. Kay, F. Dahlquist, A. Mittermaier, 2002, Journal of the American Chemical Society.

Application of methyl-TROSY NMR to test allosteric models describing effects of nucleotide binding to aspartate transcarbamoylase.

L. Kay, H. K. Schachman, A. Vėlyvis, 2009, Journal of molecular biology.

Understanding the mechanism of proteasome 20S core particle gating

L. Kay, M. Latham, A. Sekhar, 2014, Proceedings of the National Academy of Sciences.

ClpB N-terminal domain plays a regulatory role in protein disaggregation

L. Kay, A. Vėlyvis, P. Farber, 2015, Proceedings of the National Academy of Sciences.

Estimating side-chain order in [U-2H;13CH3]-labeled high molecular weight proteins from analysis of HMQC/HSQC spectra.

L. Kay, V. Tugarinov, 2013, The journal of physical chemistry. B.

Probing non-specific interactions of Ca2+-calmodulin in E. coli lysate

L. Kay, M. Latham, 2013, Journal of biomolecular NMR.

Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles

Jayashree Nagesh, L. Kay, Lewis E Kay, 2017, eLife.

High-affinity binding of the Drosophila Numb phosphotyrosine-binding domain to peptides containing a Gly-Pro-(p)Tyr motif.

T. Pawson, L. Kay, L. Cantley, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy.

L. Kay, D. Korzhnev, Soyoung Lee, 2009, Journal of molecular biology.

Sequential assignment of proline-rich regions in proteins: Application to modular binding domain complexes

Julie D. Forman-Kay, Lewis E. Kay, L. Kay, 2000, Journal of biomolecular NMR.

Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins

Julie D. Forman-Kay, Lewis E. Kay, L. Kay, 1997, Journal of biomolecular NMR.

Requirement for kinase-induced conformational change in eukaryotic initiation factor 2α (eIF2α) restricts phosphorylation of Ser51

L. Kay, F. Sicheri, A. Vėlyvis, 2011, Proceedings of the National Academy of Sciences.

Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques.

L. Kay, K. Crowhurst, F. Mulder, 2002, Journal of molecular biology.

Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopy

L. Kay, Colleen M. Doyle, J. Rumfeldt, 2016, Proceedings of the National Academy of Sciences.

Interplay of buried histidine protonation and protein stability in prion misfolding

S. Wodak, L. Kay, A. Malevanets, 2017, Scientific Reports.

ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores

L. Kay, S. Phanse, M. Babu, 2019, Communications Biology.

Practical considerations for the measurement of near-surface electrostatics based on solvent paramagnetic relaxation enhancements.

L. Kay, Y. Toyama, Atul Kaushik Rangadurai, 2023, Journal of magnetic resonance.

Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease Delta131Delta, using NMR methods with improved resolution.

L. Kay, D. Shortle, J. Forman-Kay, 1997, Journal of molecular biology.

Simultaneous Acquisition of 15N- and 13C-Edited NOE Spectra of Proteins Dissolved in H2O

L. Kay, J. Forman-Kay, D. Muhandiram, 1994 .

Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions.

L. Kay, N. Skrynnikov, Ó. Millet, 2002, Journal of the American Chemical Society.

NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel.

L. Kay, J. Forman-Kay, V. Kanelis, 1998, Biochemistry and cell biology = Biochimie et biologie cellulaire.

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

L. Kay, A. Bax, L. Nicholson, 1992 .

NMR Structure of the Bacteriophage λ N Peptide/boxB RNA Complex: Recognition of a GNRA Fold by an Arginine-Rich Motif

Jack Greenblatt, Pascale Legault, Joyce Li, 1998, Cell.

Probing the cooperativity of Thermoplasma acidophilum proteasome core particle gating by NMR spectroscopy

L. Kay, Rui Huang, Felipe Pérez, 2017, Proceedings of the National Academy of Sciences.

Measurement of Methyl 2H Quadrupolar Couplings in Oriented Proteins. How Uniform Is the Quadrupolar Coupling Constant

L. Kay, Anthony Mittermaier and, 1999 .

Removal of F1 baseline distortion and optimization of folding in multidimensional NMR spectra

L. Kay, A. Bax, M. Ikura, 1991 .

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.

L. Kay, T. L. Religa, A. Ruschak, 2011, Journal of the American Chemical Society.

Topology of an outer-membrane enzyme: Measuring oxygen and water contacts in solution NMR studies of PagP.

L. Kay, R. Prosser, F. Evanics, 2006, Journal of the American Chemical Society.

The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture.

John L Rubinstein, L. Kay, J. Rubinstein, 2011, Structure.

A Dynamic molecular basis for malfunction in disease mutants of p97/VCP

L. Kay, A. Schuetz, 2016, eLife.

Improved three-dimensional1H−13C−1H correlation spectroscopy of a13C-labeled protein using constant-time evolution

M Ikura, L. Kay, A. Bax, 1991, Journal of biomolecular NMR.

Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions

L. Kay, G. Bouvignies, A. Vėlyvis, 2018, eLife.

Conformational heterogeneity in the Hsp70 chaperone‐substrate ensemble identified from analysis of NMR‐detected titration data

L. Kay, Rina Rosenzweig, A. Sekhar, 2017, Protein science : a publication of the Protein Society.

Protein stabilization by specific binding of guanidinium to a functional arginine‐binding surface on an SH3 domain

A. Zarrine-Afsar, L. Kay, A. Mittermaier, 2006, Protein science : a publication of the Protein Society.

L Serrano, L. Kay, L. Serrano, 2000, Journal of molecular biology.

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

L. Kay, J. Forman-Kay, T. Yamazaki, 1993 .

Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy.

L. Kay, M. Tollinger, J. Forman-Kay, 2002, Journal of the American Chemical Society.

Probing allosteric interactions in homo-oligomeric molecular machines using solution NMR spectroscopy

L. Kay, Y. Toyama, Yuki Toyama, 2021, Proceedings of the National Academy of Sciences.

Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.

L. Kay, C. Deber, K. Williams, 1996, Biochemistry.

Exploiting conformational plasticity in the AAA+ protein VCP/p97 to modify function

L. Kay, A. Schütz, E. Rennella, 2017, Proceedings of the National Academy of Sciences.

Proteasome allostery as a population shift between interchanging conformers

Lewis E. Kay, L. Kay, A. Ruschak, 2012, Proceedings of the National Academy of Sciences.

Site-specific contributions to the pH dependence of protein stability

L. Kay, K. Crowhurst, M. Tollinger, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Probing Conformational Exchange in Weakly Interacting, Slowly Exchanging Protein Systems via Off-Resonance R1ρ Experiments: Application to Studies of Protein Phase Separation.

L. Kay, Jacob P. Brady, Tairan Yuwen, 2018, Journal of the American Chemical Society.

Design of amyloidogenic peptide traps

L. Kay, T. Knowles, E. Andrzejewska, 2023, bioRxiv.

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery

John L Rubinstein, Walid A Houry, L. Kay, 2019, bioRxiv.

Hsp70 biases the folding pathways of client proteins

L. Kay, G. Bouvignies, Rina Rosenzweig, 2016, Proceedings of the National Academy of Sciences.

A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium

L. Kay, J. Forman-Kay, N. Farrow, 1994, Journal of biomolecular NMR.

Crystal structure of the Sec 4 p : Sec 2 p complex in the nucleotide exchanging intermediate state

T. Pawson, L. Kay, S. Knapp, 2008 .

Methyl Groups as Probes of Structure and Dynamics in NMR Studies of High‐Molecular‐Weight Proteins

L. Kay, V. Tugarinov, Vitali Tugarinov, 2005, Chembiochem : a European journal of chemical biology.

An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR

L. Kay, A. Goldberg, A. Mittermaier, 2019, Proceedings of the National Academy of Sciences.

Characterization of conformational exchange of a histidine side chain: protonation, rotamerization, and tautomerization of His61 in plastocyanin from Anabaena variabilis.

L. Kay, D. Hansen, J. J. Led, 2008, Journal of the American Chemical Society.

Advances in Magnetic Resonance NMR studies of protein structure and dynamics

L. Kay, 2005 .

α Helix-RNA Major Groove Recognition in an HIV-1 Rev Peptide-RRE RNA Complex

L. Kay, J. Williamson, A. Frankel, 1996, Science.

A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution

Dmitry M Korzhnev, A. Fersht, L. Kay, 2010, Science.

A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase

L. Kay, H. K. Schachman, A. Vėlyvis, 2007, Proceedings of the National Academy of Sciences.

Nuclear magnetic resonance methods for high molecular weight proteins: a study involving a complex of maltose binding protein and beta-cyclodextrin.

L. Kay, 2001, Methods in enzymology.

Location of divalent ion sites in acyl carrier protein using relaxation perturbed 2D NMR

L. Kay, J. Prestegard, A. F. Frederick, 1988, FEBS letters.

A Methyl‐TROSY‐Based 1 H Relaxation Dispersion Experiment for Studies of Conformational Exchange in High Molecular Weight Proteins

L. Kay, Rui Huang, Tairan Yuwen, 2019, Angewandte Chemie.

Artifacts can emerge in spectra recorded with even the simplest of pulse schemes: an HMQC case study

L. Kay, 2019, Journal of Biomolecular NMR.

L. Kay, A. Mittermaier, D. Korzhnev, 2005, Journal of biomolecular NMR.

The measurement of heteronuclear transverse relaxation times in ax3 spin systems via polarization-transfer techniques

L. Kay, H. Schwalbe, A. Bax, 1992 .

Methyl Group Dynamics from Relaxation of Double Quantum Filtered NMR Signals: Application to Deoxycholate.

L. Kay, J. Prestegard, 1987 .

Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings

L. Kay, N. Skrynnikov, L E Kay, 2000, Journal of biomolecular NMR.

Four-dimensional carbon-13/carbon-13-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1.beta.

L. Kay, A. Gronenborn, A. Bax, 1991 .

Studies on the solution conformation of human thioredoxin using heteronuclear 15N-1H nuclear magnetic resonance spectroscopy.

L. Kay, A. Gronenborn, G. Clore, 1990, Biochemistry.

Nuclear magnetic resonance determination of metal-proton distances in a synthetic calcium binding site of rabbit skeletal troponin C.

I. Kuntz, R. Hodges, L. Kay, 1985, Biochemistry.

Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli.

L. Kay, F. Dahlquist, T. B. Morrison, 1995, Biochemistry.

Measurement of active site ionization equilibria in the 670 kDa proteasome core particle using methyl-TROSY NMR.

L. Kay, A. Vėlyvis, 2013, Journal of the American Chemical Society.

Pulse schemes for the measurement of3 JC′Cγ and3 JNCγ scalar couplings in 15N,13C uniformly labeled proteins

L. Kay, R. Konrat, D. Muhandiram, 1997 .

Relaxation rates of degenerate 1H transitions in methyl groups of proteins as reporters of side-chain dynamics.

L. Kay, V. Tugarinov, 2006, Journal of the American Chemical Society.

Quantitative 13C and 2H NMR relaxation studies of the 723-residue enzyme malate synthase G reveal a dynamic binding interface.

L. Kay, V. Tugarinov, 2005, Biochemistry.

Enhancing the Sensitivity of CPMG Relaxation Dispersion to Conformational Exchange Processes by Multiple-Quantum Spectroscopy.

L. Kay, Tairan Yuwen, P. Vallurupalli, 2016, Angewandte Chemie.

Quantifying millisecond exchange dynamics in proteins by CPMG relaxation dispersion NMR using side-chain 1H probes.

Patrik Lundström, L. Kay, A. Vėlyvis, 2012, Journal of the American Chemical Society.

Towards autonomous analysis of chemical exchange saturation transfer experiments using deep neural networks

L. Kay, D. Hansen, Tairan Yuwen, 2021, Journal of Biomolecular NMR.

Separating Dipolar and Chemical Exchange Magnetization Transfer Processes in 1 H-CEST.

L. Kay, Tairan Yuwen, A. Sekhar, 2017, Angewandte Chemie.

Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion

L. Kay, A. Sekhar, P. Vallurupalli, 2012, Proceedings of the National Academy of Sciences.

Divided-evolution-based pulse scheme for quantifying exchange processes in proteins: powerful complement to relaxation dispersion experiments.

L. Kay, G. Bouvignies, D. Hansen, 2011, Journal of the American Chemical Society.

Assessment of the Effects of Increased Relaxation Dispersion Data on the Extraction of 3-site Exchange Parameters Characterizing the Unfolding of an SH3 Domain

L. Kay, D. Korzhnev, Philipp Neudecker, 2006, Journal of biomolecular NMR.

Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain.

L. Kay, V. Orekhov, D. Korzhnev, 2005, Journal of the American Chemical Society.

Evaluating the influence of initial magnetization conditions on extracted exchange parameters in NMR relaxation experiments: applications to CPMG and CEST

L. Kay, Tairan Yuwen, A. Sekhar, 2016, Journal of biomolecular NMR.

Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.

D. Baker, A. Fersht, L. Kay, 2011, Journal of the American Chemical Society.

Probing the transition state ensemble of a protein folding reaction by pressure-dependent NMR relaxation dispersion.

L. Kay, D. Korzhnev, Yawen Bai, 2006, Journal of the American Chemical Society.

Investigating the Dynamics of Destabilized Nucleosomes Using Methyl-TROSY NMR.

L. Kay, J. Rudolph, K. Luger, 2018, Journal of the American Chemical Society.

Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy.

L. Kay, M. Akke, F. Mulder, 2006, Journal of the American Chemical Society.

Analytical description of the effect of adiabatic pulses on IS, I2S, and I3S spin systems.

L. Kay, C. Zwahlen, S. Vincent, 1998, Journal of magnetic resonance.

Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation.

L. Kay, Rina Rosenzweig, R. Rosenzweig, 2016, Journal of the American Chemical Society.

Correlation between 2H NMR side-chain order parameters and sequence conservation in globular proteins.

L. Kay, A. Mittermaier, A. Davidson, 2003, Journal of the American Chemical Society.

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

Wing-Yiu Choy, Vladislav Yu Orekhov, L. Kay, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.

L. Kay, P. Hwang, 2005, Methods in enzymology.

Line narrowing in methyl-TROSY using zero-quantum 1H-13C NMR spectroscopy.

L. Kay, V. Tugarinov, R. Sprangers, 2004, Journal of the American Chemical Society.

A pulsed field gradient isotope‐filtered 3D 13C HMQC‐NOESY experiment for extracting intermolecular NOE contacts in molecular complexes

L. Kay, C. Arrowsmith, L E Kay, 1994, FEBS letters.

A Three-Dimensional NMR Experiment for the Separation of Aliphatic Carbon Chemical Shifts via the Carbonyl Chemical Shift in 15N, 13C-Labeled Proteins

L. Kay, 1993 .

Less is more: A simple methyl-TROSY based pulse scheme offers improved sensitivity in applications to high molecular weight complexes.

L. Kay, J. Aramini, Nicolas Bolik-Coulon, 2022, Journal of magnetic resonance.

Cooperative subunit dynamics modulate p97 function

L. Kay, J. Rubinstein, Z. A. Ripstein, 2018, Proceedings of the National Academy of Sciences.

Measurement of Slow ( μ sms ) 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 T 4 Lysozyme

L. Kay, F. Dahlquist, F. Mulder, 2022 .

CommunicationThe Effects of Cross Correlation and Cross Relaxation on the Measurement of DeuteriumT1andT1ρRelaxation Times in13CH2D Spin Systems

L. Kay, Daiwen Yang, 1996 .

Mapping the conformation of a client protein through the Hsp70 functional cycle

L. Kay, G. Bouvignies, Rina Rosenzweig, 2015, Proceedings of the National Academy of Sciences.

Probing the free energy landscape of the fast-folding gpW protein by relaxation dispersion NMR.

V. Muñoz, L. Kay, A. Sekhar, 2014, Journal of the American Chemical Society.

Characterization of the hydrodynamic properties of the folding transition state of an SH3 domain by magnetization transfer NMR spectroscopy.

L. Kay, M. Tollinger, J. Forman-Kay, 2006, Biochemistry.

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.

A. Zarrine-Afsar, L. Kay, A. Davidson, 2006, Journal of molecular biology.

A suite of 2H NMR spin relaxation experiments for the measurement of RNA dynamics.

L. Kay, P. Vallurupalli, 2005, Journal of the American Chemical Society.

Kay, Lewis E.: Structure and Dynamics of Proteins – Big and Small

L. Kay, 2010 .

Estimates of methyl 13C and 1H CSA values (Δσ) in proteins from cross-correlated spin relaxation

L. Kay, R. Brüschweiler, V. Tugarinov, 2004, Journal of biomolecular NMR.

Effect of deuteration on some structural parameters of methyl groups in proteins as evaluated by residual dipolar couplings

L. Kay, A. Mittermaier, 2002, Journal of biomolecular NMR.

Separating degenerate (1)H transitions in methyl group probes for single-quantum (1)H-CPMG relaxation dispersion NMR spectroscopy.

L. Kay, V. Tugarinov, 2007, Journal of the American Chemical Society.

Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy.

L. Kay, V. Tugarinov, R. Sprangers, 2007, Journal of the American Chemical Society.

Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: Application to 15N relaxation measurements

L. Kay, V. Tugarinov, E. Kupče, 2004, Journal of biomolecular NMR.

TROSY-based HNCO pulse sequences for the measurement of 1HN-15N, 15N-13CO, 1HN-13CO, 13CO-13Cα and 1HN-13Cα dipolar couplings in 15N, 13C, 2H-labeled proteins

L. Kay, Daiwen Yang, W. Choy, 1999 .

Improved lineshape and sensitivity in the HNCO-family of triple resonance experiments

L. Kay, Daiwen Yang, 1999 .

e ffect of Noncompetitive Proteasome i nhibition on Bortezomib r esistance

L. Kay, S. Trudel, R. Sprangers, 2010 .

Mechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone.

S. Sharpe, L. Kay, W. Houry, 2016, Structure.

Flexible client-dependent cages in the assembly landscape of the periplasmic protease-chaperone DegP

L. Kay, Z. A. Ripstein, R. Harkness, 2022, bioRxiv.

A simple method for measuring signs of 1HN chemical shift differences between ground and excited protein states

L. Kay, G. Bouvignies, D. Korzhnev, 2010, Journal of biomolecular NMR.

Fractional enrichment of proteins using [2-13C]-glycerol as the carbon source facilitates measurement of excited state 13Cα chemical shifts with improved sensitivity

Patrik Lundström, L. Kay, Cecilia Andresen, 2015, Journal of biomolecular NMR.

Fractional enrichment of proteins using [2-13C]-glycerol as the carbon source facilitates measurement of excited state 13Cα chemical shifts with improved sensitivity

Patrik Lundström, L. Kay, Cecilia Andresen, 2015, Journal of Biomolecular NMR.

Defining a length scale for millisecond-timescale protein conformational exchange

L. Kay, A. Sekhar, P. Vallurupalli, 2013, Proceedings of the National Academy of Sciences.

Transiently populated intermediate functions as a branching point of the FF domain folding pathway

L. Kay, D. Korzhnev, T. L. Religa, 2012, Proceedings of the National Academy of Sciences.

Toward the solution structure of large (>30 kDa) proteins and macromolecular complexes

L. Kay, C. Arrowsmith, Weontae Lee, 1995 .

Off-resonance R1ρ relaxation outside of the fast exchange limit: An experimental study of a cavity mutant of T4 lysozyme

L. Kay, F. Dahlquist, V. Orekhov, 2003, Journal of biomolecular NMR.

Advanced isotopic labeling for the NMR investigation of challenging proteins and nucleic acids

L. Kay, J. Boisbouvier, 2018, Journal of biomolecular NMR.

13CHD2–CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins

L. Kay, A. Vėlyvis, Rui Huang, 2015, Journal of biomolecular NMR.

Optimal methyl labeling for studies of supra-molecular systems

L. Kay, T. L. Religa, 2010, Journal of biomolecular NMR.

Comparison of 13 CH 3 , 13 CH 2 D, and 13 CHD 2<

L. Kay, V. Tugarinov, Jason E. Ollerenshaw, 2005 .

Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta.

L. Kay, D. Shortle, W. Choy, 2003, Journal of the American Chemical Society.

Disrupting the α-synuclein-ESCRT interaction with a peptide inhibitor mitigates neurodegeneration in preclinical models of Parkinson’s disease

Philip M. Kim, L. Kay, K. Fujisawa, 2023, Nature communications.

An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase

L. Kay, M. Vendruscolo, J. Rubinstein, 2020, Proceedings of the National Academy of Sciences.

Correlating histone acetylation with nucleosome core particle dynamics and function.

L. Kay, Nicolas Bolik-Coulon, Tae Hun Kim, 2023, Proceedings of the National Academy of Sciences of the United States of America.

Evolution of magnetization due to asymmetric dimerization: theoretical considerations and application to aberrant oligomers formed by apoSOD1(2SH).

A. D. Bain, L. Kay, E. Meiering, 2016, Physical chemistry chemical physics : PCCP.

Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation.

Dmitry M Korzhnev, Alan R Davidson, A. Zarrine-Afsar, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone.

S. Sharpe, L. Kay, W. Houry, 2016, Structure.

Reversible inhibition of the ClpP protease via an N-terminal conformational switch

L. Kay, W. Houry, M. Vendruscolo, 2018, Proceedings of the National Academy of Sciences.

Dynamic Regulation of Archaeal Proteasome Gate Opening As Studied by TROSY NMR

L. Kay, R. Sprangers, T. L. Religa, 2010, Science.

Slow dynamics in folded and unfolded states of an SH3 domain.

L. Kay, F. Mulder, M. Tollinger, 2001, Journal of the American Chemical Society.

A pH-Dependent Conformational Switch Controls N. meningitidis ClpP Protease Function.

L. Kay, J. Rubinstein, Z. A. Ripstein, 2020, Journal of the American Chemical Society.

Structural basis for the stabilization of amyloidogenic immunoglobulin light chains by hydantoins.

L. Kay, I. Wilson, Stefano Forli, 2020, Bioorganic & medicinal chemistry letters.

The ATCUN domain as a probe of intermolecular interactions: application to calmodulin-peptide complexes.

L. Kay, M. Ikura, T. Mal, 2002, Journal of the American Chemical Society.

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

L. Kay, A. Bax, M. Ikura, 1991 .

Analyzing multi-step ligand binding reactions for oligomeric proteins by NMR: Theoretical and computational considerations.

L. Kay, Y. Toyama, R. Harkness, 2020, Journal of magnetic resonance.

An application of pulse-gradient double-quantum spin echoes to diffusion measurements on molecules with scalar-coupled spins

L. Kay, J. Prestegard, 1986 .

Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure

L. Kay, A. Mittermaier, J. Forman-Kay, 1999, Journal of biomolecular NMR.

Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy.

Patrik Lundström, L. Kay, D. Hansen, 2009, Journal of the American Chemical Society.

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.

L. Kay, A. Mittermaier, Daiwen Yang, 2001, Journal of the American Chemical Society.

An HNCO-based Pulse Scheme for the Measurement of 13Cα-1Hα One-bond Dipolar couplings in 15N, 13C Labeled Proteins

L. Kay, Daiwen Yang, N. Goto, 1998, Journal of biomolecular NMR.

NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond.

L. Kay, B. Reif, R. Sprangers, 2013, Angewandte Chemie.

Measurement of active site ionization equilibria in the 670 kDa proteasome core particle using methyl-TROSY NMR.

L. Kay, A. Vėlyvis, 2013, Journal of the American Chemical Society.

A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment

L. Kay, W. Choy, G. Mueller, 2000, Journal of Biomolecular NMR.

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.

L. Kay, T. L. Religa, A. Ruschak, 2011, Journal of the American Chemical Society.

Triple resonance-based 13Cα and 13Cβ CEST experiments for studies of ms timescale dynamics in proteins

L. Kay, Dong Long, A. Sekhar, 2014, Journal of biomolecular NMR.

NMR studies of protein structure and dynamics. 2005.

L. Kay, 2011, Journal of magnetic resonance.

Probing supramolecular structure from measurement of methyl (1)H-(13)C residual dipolar couplings.

L. Kay, R. Sprangers, 2007, Journal of the American Chemical Society.

Probing the cooperativity of Thermoplasma acidophilum proteasome core particle gating by NMR spectroscopy

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