Theory, Practice, and Applications of Paramagnetic Relaxation Enhancement for the Characterization of Transient Low-Population States of Biological Macromolecules and Their Complexes

NMR with Proteins and Nucleic Acids

Wüthrich, K. (1986) · Europhysics News · doi:10.1051/epn/19861701011 · Cited by 7,989

Intrinsically unstructured proteins and their functions

Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871

Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity

Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777

Relaxation Processes in a System of Two Spins

Solomon, I. (1955) · Physical Review · doi:10.1103/physrev.99.559 · Cited by 3,278

Funnels, pathways, and the energy landscape of protein folding: A synthesis

Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648

Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules

Lipari, G. (1982) · Journal of the American Chemical Society · Cited by 2,525

The Xplor-NIH NMR molecular structure determination package

Schwieters, C. D., Kuszewski, J. J., Tjandra, N., & Marius Clore, G. (2003) · Journal of Magnetic Resonance · doi:10.1016/s1090-7807(02)00014-9 · Cited by 2,369

THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective

Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210

Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium

Tjandra, N., & Bax, A. (1997) · Science · doi:10.1126/science.278.5340.1111 · Cited by 1,719

Structural chemistry and molecular biology

Rich, A., Davidson, N., & Pauling, L. C. (1968) · Medical Entomology and Zoology · Cited by 1,702

Reaction Rates by Nuclear Magnetic Resonance

McConnell, H. M. (1958) · The Journal of Chemical Physics · doi:10.1063/1.1744152 · Cited by 1,624

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher, J., Francke, C., & Postma, P. W. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00024-06 · Cited by 1,424

Proton Relaxation Times in Paramagnetic Solutions. Effects of Electron Spin Relaxation

Bloembergen, N., & Morgan, L. O. (1961) · The Journal of Chemical Physics · doi:10.1063/1.1731684 · Cited by 1,348

Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory

Berg, O. G., Winter, R. B., & Von Hippel, P. H. (1981) · Biochemistry · doi:10.1021/bi00527a028 · Cited by 1,298

Facilitated Target Location in Biological Systems

von Hippel, P. H., & Berg, O. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84994-3 · Cited by 1,030

Nuclear Magnetic Resonance Methods for Quantifying Microsecond-to-Millisecond Motions in Biological Macromolecules

Palmer, A. G., Kroenke, C. D., & Patrick Loria, J. (2001) · Methods in Enzymology · doi:10.1016/s0076-6879(01)39315-1 · Cited by 938

Nuclear Spin Relaxation in Ellipsoids Undergoing Rotational Brownian Motion

Woessner, D. E. (1962) · The Journal of Chemical Physics · doi:10.1063/1.1701390 · Cited by 904

How do site-specific DNA-binding proteins find their targets?

Halford, S. E. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh624 · Cited by 886

Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein

Bertoncini, C. W., Jung, Y.-S., Fernandez, C. O., Hoyer, W., Griesinger, C., Jovin, T. M., & Zweckstetter, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407146102 · Cited by 790

New Tools Provide New Insights in NMR Studies of Protein Dynamics

Mittermaier, A., & Kay, L. E. (2006) · Science · doi:10.1126/science.1124964 · Cited by 780

Using Xplor–NIH for NMR molecular structure determination

SCHWIETERS, C., KUSZEWSKI, J., & MARIUSCLORE, G. (2006) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2005.10.001 · Cited by 769

Methodological advances in protein NMR

Bax, A., & Grzesiek, S. (1993) · Accounts of Chemical Research · doi:10.1021/ar00028a001 · Cited by 766

Selection of DNA binding sites by regulatory proteins

Berg, O. G., & von Hippel, P. H. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90354-8 · Cited by 744

Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria

Tam, R., & Saier, M. H. (1993) · Microbiological Reviews · doi:10.1128/mmbr.57.2.320-346.1993 · Cited by 742

INHIBITORS OF HIV-1 PROTEASE: A Major Success of Structure-Assisted Drug Design

Wlodawer, A., & Vondrasek, J. (1998) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.27.1.249 · Cited by 734

Diffusion-Controlled Macromolecular Interactions

Berg, O. G., & von Hippel, P. H. (1985) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.14.060185.001023 · Cited by 726

Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations

Dedmon, M. M., Lindorff-Larsen, K., Christodoulou, J., Vendruscolo, M., & Dobson, C. M. (2005) · Journal of the American Chemical Society · doi:10.1021/ja044834j · Cited by 716

Methodological Advances in Protein NMR

Bax, A., & Grzesiek, S. (1993) · NMR of Proteins · doi:10.1007/978-1-349-12749-8_2 · Cited by 714

Crystal Structure of a Complex Between Electron Transfer Partners, Cytochrome c Peroxidase and Cytochrome c

Pelletier, H., & Kraut, J. (1992) · Science · doi:10.1126/science.1334573 · Cited by 676

TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins

Salzmann, M., Pervushin, K., Wider, G., Senn, H., & Wüthrich, K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13585 · Cited by 646

Utilization of Site-Directed Spin Labeling and High-Resolution Heteronuclear Nuclear Magnetic Resonance for Global Fold Determination of Large Proteins with Limited Nuclear Overhauser Effect Data

Battiste, J. L., & Wagner, G. (2000) · Biochemistry · doi:10.1021/bi000060h · Cited by 625

Dynamic effects of pair correlation functions on spin relaxation by translational diffusion in liquids

Hwang, L.-P., & Freed, J. H. (1975) · The Journal of Chemical Physics · doi:10.1063/1.431841 · Cited by 600

Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: kinetic measurements and conclusions

Winter, R. B., Berg, O. G., & Von Hippel, P. H. (1981) · Biochemistry · doi:10.1021/bi00527a030 · Cited by 588

Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins

Ohndorf, U.-M., Rould, M. A., He, Q., Pabo, C. O., & Lippard, S. J. (1999) · Nature · doi:10.1038/21460 · Cited by 565

Rapid, electrostatically assisted association of proteins

Schreiber, G., & Fersht, A. R. (1996) · Nature Structural Biology · doi:10.1038/nsb0596-427 · Cited by 559

Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes

Kalodimos, C. G., Biris, N., Bonvin, A. M. J. J., Levandoski, M. M., Guennuegues, M., Boelens, R., & Kaptein, R. (2004) · Science · doi:10.1126/science.1097064 · Cited by 543

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

Sprangers, R., & Kay, L. E. (2007) · Nature · doi:10.1038/nature05512 · Cited by 527

Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins

Miyashita, O., Onuchic, J. N., & Wolynes, P. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135471100 · Cited by 514

Magnetic susceptibility in paramagnetic NMR

BERTINI, I., LUCHINAT, C., & PARIGI, G. (2002) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(02)00002-x · Cited by 487

Use of dipolar 1H–15N and 1H–13C couplings in the structure determination of magnetically oriented macromolecules in solution

Tjandra, N., Omichinski, J. G., Gronenborn, A. M., Clore, G. M., & Bax, A. (1997) · Nature Structural Biology · doi:10.1038/nsb0997-732 · Cited by 481

Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis

Sharff, A. J., Rodseth, L. E., Spurlino, J. C., & Quiocho, F. A. (1992) · Biochemistry · doi:10.1021/bi00159a003 · Cited by 477

Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex

Werner, M. H., Huth, J. R., Gronenborn, A. M., & Marius Clore, G. (1995) · Cell · doi:10.1016/0092-8674(95)90532-4 · Cited by 465

High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation

Altenbach, C., Kusnetzow, A. K., Ernst, O. P., Hofmann, K. P., & Hubbell, W. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802515105 · Cited by 462

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

Farrow, N. A., Zhang, O., Forman-Kay, J. D., & Kay, L. E. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00404280 · Cited by 458

NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor

Neri, D., Billeter, M., Wider, G., & Wüthrich, K. (1992) · Science · doi:10.1126/science.1523410 · Cited by 448

Dynamic effects of pair correlation functions on spin relaxation by translational diffusion in liquids. II. Finite jumps and independent T 1 processes

Freed, J. H. (1978) · The Journal of Chemical Physics · doi:10.1063/1.436302 · Cited by 442

The crystal structure of EcoRV endonuclease and of its complexes with cognate and non-cognate DNA fragments.

Winkler, F. K., Banner, D. W., Oefner, C., Tsernoglou, D., Brown, R. S., Heathman, S. P., Bryan, R. K., Martin, P. D., Petratos, K., & Wilson, K. S. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05826.x · Cited by 441

Structures of Larger Proteins in Solution: Three- and Four-Dimensional Heteronuclear NMR Spectroscopy

Clore, G. M., & Gronenborn, A. M. (1991) · Science · doi:10.1126/science.2047852 · Cited by 436

Dipolar Couplings in Macromolecular Structure Determination

Bax, A., Kontaxis, G., & Tjandra, N. (2001) · Methods in Enzymology · doi:10.1016/s0076-6879(01)39313-8 · Cited by 418

Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR

Tang, C., Schwieters, C. D., & Clore, G. M. (2007) · Nature · doi:10.1038/nature06232 · Cited by 416

Three-dimensional solution structure of the 44kDa ectodomain of SIV gp41

Caffrey, M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.16.4572 · Cited by 410

Visualization of transient encounter complexes in protein–protein association

Tang, C., Iwahara, J., & Clore, G. M. (2006) · Nature · doi:10.1038/nature05201 · Cited by 406

HMGB proteins and gene expression

Agresti, A., & Bianchi, M. E. (2003) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(03)00023-6 · Cited by 394

NMR analysis of a 900K GroEL–GroES complex

Fiaux, J., Bertelsen, E. B., Horwich, A. L., & Wüthrich, K. (2002) · Nature · doi:10.1038/nature00860 · Cited by 386

Rotational diffusion studied by passage saturation transfer electron paramagnetic resonance

Thomas, D. D., Dalton, L. R., & Hyde, J. S. (1976) · The Journal of Chemical Physics · doi:10.1063/1.433512 · Cited by 378

Detecting transient intermediates in macromolecular binding by paramagnetic NMR

Iwahara, J., & Clore, G. M. (2006) · Nature · doi:10.1038/nature04673 · Cited by 370

Addition of the keto functional group to the genetic code of Escherichia coli

Wang, L., Zhang, Z., Brock, A., & Schultz, P. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0234824100 · Cited by 356

Hydrogen exchange methods to study protein folding

KRISHNA, M. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.005 · Cited by 348

Ribosome Loading onto the mRNA Cap Is Driven by Conformational Coupling between eIF4G and eIF4E

Gross, J. D., Moerke, N. J., von der Haar, T., Lugovskoy, A. A., Sachs, A. B., McCarthy, J. E. G., & Wagner, G. (2003) · Cell · doi:10.1016/s0092-8674(03)00975-9 · Cited by 346

Determination of Three-Dimensional Structures of Proteins and Nucleic Acids in Solution by Nuclear Magnetic Resonance Spectroscop

Clore, G. M., & Gronenborn, A. M. (1989) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238909086962 · Cited by 339

Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor

Quiocho, F. A., Spurlino, J. C., & Rodseth, L. E. (1997) · Structure · doi:10.1016/s0969-2126(97)00253-0 · Cited by 338

Ensemble Approach for NMR Structure Refinement against1H Paramagnetic Relaxation Enhancement Data Arising from a Flexible Paramagnetic Group Attached to a Macromolecule

Iwahara, J., Schwieters, C. D., & Clore, G. M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja031580d · Cited by 328

Nuclear relaxation in macromolecules by paramagnetic ions: a novel mechanism

Gueron, M. (1975) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(75)90029-3 · Cited by 327

Protein topology determines binding mechanism

Levy, Y., Wolynes, P. G., & Onuchic, J. N. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2534828100 · Cited by 324

Kinetic studies of protein–protein interactions

Schreiber, G. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00287-7 · Cited by 323

Measurement of Residual Dipolar Couplings of Macromolecules Aligned in the Nematic Phase of a Colloidal Suspension of Rod-Shaped Viruses

Clore, G. M., Starich, M. R., & Gronenborn, A. M. (1998) · Journal of the American Chemical Society · doi:10.1021/ja982592f · Cited by 316

Rational design of faster associating and tighter binding protein complexes.

Schreiber, G., Selzer, T., & Albeck, S. (2000) · Nature Structural Biology · doi:10.1038/76744 · Cited by 299

Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. paramagnetic relaxation enhancement by nitroxide spin labels

Gillespie, J. R., & Shortle, D. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0954 · Cited by 296

Brownian Dynamics of Cytochrome c and Cytochrome c Peroxidase Association

Northrup, S. H., Boles, J. O., & Reynolds, J. C. L. (1988) · Science · doi:10.1126/science.2838904 · Cited by 290

Time-averaged nuclear overhauser effect distance restraints applied to tendamistat

Torda, A. E., Scheek, R. M., & van Gunsteren, W. F. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90157-h · Cited by 284

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

Korzhnev, D. M., & Kay, L. E. (2008) · Accounts of Chemical Research · doi:10.1021/ar700189y · Cited by 268

Practical aspects of 1H transverse paramagnetic relaxation enhancement measurements on macromolecules

Iwahara, J., Tang, C., & Marius Clore, G. (2007) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2006.10.003 · Cited by 266

Time-dependent distance restraints in molecular dynamics simulations

Torda, A., Scheek, R., & van Gunsteren, W. V. (1989) · Chemical Physics Letters · doi:10.1016/0009-2614(89)87249-5 · Cited by 251

Four-Dimensional NMR Spectroscopy of a 723-Residue Protein: Chemical Shift Assignments and Secondary Structure of Malate Synthase G

Tugarinov, V., Muhandiram, R., Ayed, A., & Kay, L. E. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0205636 · Cited by 249

Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR

Volkov, A. N., Worrall, J. A. R., Holtzmann, E., & Ubbink, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603551103 · Cited by 248

NMR Structure of Mistic, a Membrane-Integrating Protein for Membrane Protein Expression

Roosild, T. P., Greenwald, J., Vega, M., Castronovo, S., Riek, R., & Choe, S. (2005) · Science · doi:10.1126/science.1106392 · Cited by 247

Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. distance restraints from paramagnetic relaxation and calculation of an ensemble of structures

Gillespie, J. R., & Shortle, D. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0953 · Cited by 246

R-factor, Free R, and Complete Cross-Validation for Dipolar Coupling Refinement of NMR Structures

Clore, G. M., & Garrett, D. S. (1999) · Journal of the American Chemical Society · doi:10.1021/ja991789k · Cited by 244

New methods of structure refinement for macromolecular structure determination by NMR

Clore, G. M., & Gronenborn, A. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5891 · Cited by 227

Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement

Clore, G. M., Tang, C., & Iwahara, J. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.08.013 · Cited by 226

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

Tugarinov, V., Choy, W.-Y., Orekhov, V. Y., & Kay, L. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407792102 · Cited by 223

Protein Sliding along DNA: Dynamics and Structural Characterization

Givaty, O., & Levy, Y. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.11.016 · Cited by 220

Identification of Protein Surfaces by NMR Measurements with a Paramagnetic Gd(III) Chelate

Pintacuda, G., & Otting, G. (2002) · Journal of the American Chemical Society · doi:10.1021/ja016985h · Cited by 216

Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr.

Gronenborn, A. M., Clore, G. M., Garrett, D. S., Seok, Y., & Peterkofsky, A. (1999) · Nature Structural Biology · doi:10.1038/5854 · Cited by 212

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

Sprangers, R., Gribun, A., Hwang, P. M., Houry, W. A., & Kay, L. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507370102 · Cited by 209

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

Vallurupalli, P., Hansen, D. F., & Kay, L. E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804221105 · Cited by 205

How Much Backbone Motion in Ubiquitin Is Required To Account for Dipolar Coupling Data Measured in Multiple Alignment Media as Assessed by Independent Cross-Validation?

Clore, G. M., & Schwieters, C. D. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0386804 · Cited by 200

Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar 1 1Edited by B. Honig

Vijayakumar, M., Wong, K.-Y., Schreiber, G., Fersht, A. R., Szabo, A., & Zhou, H.-X. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1747 · Cited by 199

Theory and Practice of Electron Transfer within Protein−Protein Complexes: Application to the Multidomain Binding of Cytochrome c by Cytochrome c Peroxidase

Nocek, J. M., Zhou, J. S., De Forest, S., Priyadarshy, S., Beratan, D. N., Onuchic, J. N., & Hoffman, B. M. (1996) · Chemical Reviews · doi:10.1021/cr9500444 · Cited by 198

Structure of a DNA Glycosylase Searching for Lesions

Banerjee, A., Santos, W. L., & Verdine, G. L. (2006) · Science · doi:10.1126/science.1120288 · Cited by 193

Recent advances in FRET: distance determination in protein–DNA complexes

Hillisch, A., Lorenz, M., & Diekmann, S. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00190-1 · Cited by 192

Methods and Applications of Site-Directed Spin Labeling EPR Spectroscopy

Klug, C. S., & Feix, J. B. (2008) · Methods in Cell Biology · doi:10.1016/s0091-679x(07)84020-9 · Cited by 189

NMR structural and kinetic characterization of a homeodomain diffusing and hopping on nonspecific DNA

Iwahara, J., Zweckstetter, M., & Clore, G. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605868103 · Cited by 189

Accurate and rapid docking of protein–protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization

Clore, G. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.9021 · Cited by 180

Biomolecular diffusional association

Gabdoulline, R. R., & Wade, R. C. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00311-1 · Cited by 179

Internal Coordinates for Molecular Dynamics and Minimization in Structure Determination and Refinement

Schwieters, C. D., & Clore, G. M. (2001) · Journal of Magnetic Resonance · doi:10.1006/jmre.2001.2413 · Cited by 177

Design, Synthesis, and Evaluation of a Lanthanide Chelating Protein Probe: CLaNP-5 Yields Predictable Paramagnetic Effects Independent of Environment

Keizers, P. H. J., Saragliadis, A., Hiruma, Y., Overhand, M., & Ubbink, M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8054832 · Cited by 177

Structural Characterization of Proteins with an Attached ATCUN Motif by Paramagnetic Relaxation Enhancement NMR Spectroscopy

Donaldson, L. W., Skrynnikov, N. R., Choy, W.-Y., Muhandiram, D. R., Sarkar, B., Forman-Kay, J. D., & Kay, L. E. (2001) · Journal of the American Chemical Society · doi:10.1021/ja011241p · Cited by 175

Biological Magnetic Resonance

(1978) · Biological Magnetic Resonance · doi:10.1007/978-1-4615-6534-5 · Cited by 173

Structure of BamHI Bound to Nonspecific DNA

Viadiu, H., & Aggarwal, A. K. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80329-9 · Cited by 172

Characterization of Enzyme Motions by Solution NMR Relaxation Dispersion

Loria, J. P., Berlow, R. B., & Watt, E. D. (2008) · Accounts of Chemical Research · doi:10.1021/ar700132n · Cited by 170

TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution

Riek, R., Pervushin, K., & Wüthrich, K. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01665-0 · Cited by 168

Site-Directed Parallel Spin-Labeling and Paramagnetic Relaxation Enhancement in Structure Determination of Membrane Proteins by Solution NMR Spectroscopy

Liang, B., Bushweller, J. H., & Tamm, L. K. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0574825 · Cited by 167

Molecular Basis for Synergistic Transcriptional Activation by Oct1 and Sox2 Revealed from the Solution Structure of the 42-kDa Oct1·Sox2·Hoxb1-DNA Ternary Transcription Factor Complex

Williams, D. C., Cai, M., & Clore, G. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309790200 · Cited by 164

Impact of Transverse Relaxation Optimized Spectroscopy (TROSY) on NMR as a technique in structural biology

Pervushin, K. (2000) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500003619 · Cited by 163

Solution Structure of the 30 kDa N-Terminal Domain of Enzyme I of the Escherichia coli Phosphoenolpyruvate:Sugar Phosphotransferase System by Multidimensional NMR

Garrett, D. S., Seok, Y., Liao, D., Peterkofsky, A., Gronenborn, A. M., & Clore, G. M. (1997) · Biochemistry · doi:10.1021/bi962924y · Cited by 153

Structural Basis for SRY-dependent 46-X,Y Sex Reversal: Modulation of DNA Bending by a Naturally Occurring Point Mutation

Murphy, E. C., Zhurkin, V. B., Louis, J. M., Cornilescu, G., & Clore, G. M. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4977 · Cited by 146

Mapping Long-range Contacts in a Highly Unfolded Protein

Lietzow, M. A., Jamin, M., Dyson, H. J., & Wright, P. E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00847-1 · Cited by 143

Comparison of X-ray and NMR structures for the Antennapedia homeodomain–DNA complex

Fraenkel, E., & Pabo, C. O. (1998) · Nature Structural & Molecular Biology · doi:10.1038/1382 · Cited by 141

Conformation-dependent cleavage of staphylococcal nuclease with a disulfide-linked iron chelate.

Ermácora, M. R., Delfino, J. M., Cuenoud, B. M., Schepartz, A., & Fox, R. O. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.14.6383 · Cited by 140

Spin-label study of hemoglobin conformations in solution.

Ogawa, S., & McConnell, H. M. (1967) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.58.1.19 · Cited by 140

Structural Basis of ARNT PAS-B Dimerization: Use of a Common Beta-sheet Interface for Hetero- and Homodimerization

Card, P. B., Erbel, P. J. A., & Gardner, K. H. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.043 · Cited by 140

Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease

Tang, C., Louis, J. M., Aniana, A., Suh, J., & Clore, G. M. (2008) · Nature · doi:10.1038/nature07342 · Cited by 138

Multi-conformational peptide dynamics derived from NMR data: A new search algorithm and its application to antamanide

Brüschweiler, R., Blackledge, M. J., & Ernst, R. R. (1991) · Journal of Biomolecular NMR · doi:10.1007/bf01874565 · Cited by 138

Amplitudes of Protein Backbone Dynamics and Correlated Motions in a Small α/β Protein: Correspondence of Dipolar Coupling and Heteronuclear Relaxation Measurements

Clore, G. M., & Schwieters, C. D. (2004) · Biochemistry · doi:10.1021/bi049357w · Cited by 136

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.

Varani, G., Varani, L., Gunderson, S., Mattaj, I. W., Kay, L. E., & Neuhaus, D. (2000) · Nature Structural Biology · doi:10.1038/74101 · Cited by 135

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

Evenäs, J., Tugarinov, V., Skrynnikov, N. R., Goto, N. K., Muhandiram, R., & Kay, L. E. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4695 · Cited by 135

A New Method To Detect Long-Range Protein−RNA Contacts: NMR Detection of Electron−Proton Relaxation Induced by Nitroxide Spin-Labeled RNA

Ramos, A., & Varani, G. (1998) · Journal of the American Chemical Society · doi:10.1021/ja982496e · Cited by 133

Paramagnetism-Based NMR Restraints Provide Maximum Allowed Probabilities for the Different Conformations of Partially Independent Protein Domains

Bertini, I., Gupta, Y. K., Luchinat, C., Parigi, G., Peana, M., Sgheri, L., & Yuan, J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0726613 · Cited by 133

Membrane Protein–Lipid Interactions in Mixed Micelles Studied by NMR Spectroscopy with the Use of Paramagnetic Reagents

Hilty, C., Wider, G., Fernández, C. F., & Kurt Wüthrich, A. (2004) · ChemBioChem · doi:10.1002/cbic.200300815 · Cited by 128

Diffusional Encounter of Barnase and Barstar

Spaar, A., Dammer, C., Gabdoulline, R. R., Wade, R. C., & Helms, V. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.075507 · Cited by 125

Conformational Variability of Solution Nucelar Magnetic Resonance Structures

Bonvin, A. M. J. J., & Brünger, A. T. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0360 · Cited by 116

2D Chemical exchange NMR spectroscopy by proton-detected heteronuclear correlation

Montelione, G. T., & Wagner, G. H. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00190a072 · Cited by 116

Improved Structural Characterizations of the drkN SH3 Domain Unfolded State Suggest a Compact Ensemble with Native-like and Non-native Structure

Marsh, J. A., Neale, C., Jack, F. E., Choy, W., Lee, A. Y., Crowhurst, K. A., & Forman-Kay, J. D. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.01.038 · Cited by 116

New insights into the mechanism of protein–protein association

Selzer, T., & Schreiber, G. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.1139 · Cited by 115

Direct NMR observation of a substrate protein bound to the chaperonin GroEL

Horst, R., Bertelsen, E. B., Fiaux, J., Wider, G., Horwich, A. L., & Wüthrich, K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505642102 · Cited by 113

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

Millet, Ó., Hudson, R. D. A., & Kay, L. E. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2134311100 · Cited by 112

Simple Energy Landscape Model for the Kinetics of Functional Transitions in Proteins

Miyashita, O., Wolynes, P. G., & Onuchic, J. N. (2005) · The Journal of Physical Chemistry B · doi:10.1021/jp046736q · Cited by 111

Incorporation of an EDTA-metal complex at a rationally selected site within a protein: application to EDTA-iron DNA affinity cleaving with catabolite gene activator protein (CAP) and Cro

Ebright, Y. W., Chen, Y., Pendergrast, P. S., & Ebright, R. H. (1992) · Biochemistry · doi:10.1021/bi00159a004 · Cited by 109

Spin-label-induced nuclear relaxation. Distances between bound saccharides, histidine-15, and tryptophan-123 on lysozyme in solution

Wien, R. W., Morrisett, J. D., & McConnell, H. M. (1972) · Biochemistry · doi:10.1021/bi00770a008 · Cited by 107

Concordance of Residual Dipolar Couplings, Backbone Order Parameters and Crystallographic B-factors for a Small α/β Protein: A Unified Picture of High Probability, Fast Atomic Motions in Proteins

Clore, G. M., & Schwieters, C. D. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.11.042 · Cited by 106

The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex

Gewirth, D. T., & Sigler, P. B. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb0595-386 · Cited by 105

Replica exchange simulations of transient encounter complexes in protein–protein association

Kim, Y. C., Tang, C., Clore, G. M., & Hummer, G. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802460105 · Cited by 104

Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein.

Louis, J. M., Nashed, N. T., Parris, K. D., Kimmel, A. R., & JERINA, D. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.7970 · Cited by 102

Magnetic Resonance Realization of Decoherence-Free Quantum Computation

Ollerenshaw, J. E., Lidar, D. A., & Kay, L. E. (2003) · Physical Review Letters · doi:10.1103/physrevlett.91.217904 · Cited by 102

Dynamics in a Pure Encounter Complex of Two Proteins Studied by Solution Scattering and Paramagnetic NMR Spectroscopy

Xu, X., Reinle, W., Hannemann, F., Konarev, P. V., Svergun, D. I., Bernhardt, R., & Ubbink, M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja7101357 · Cited by 99

Global jumping and domain-specific intersegment transfer between DNA cognate sites of the multidomain transcription factor Oct-1

Doucleff, M., & Clore, G. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805050105 · Cited by 99

A Physical Picture of Atomic Motions within the Dickerson DNA Dodecamer in Solution Derived from Joint Ensemble Refinement against NMR and Large-Angle X-ray Scattering Data

Schwieters, C. D., & Clore, G. M. (2007) · Biochemistry · doi:10.1021/bi061943x · Cited by 99

Multivalent Mechanism of Membrane Insertion by the FYVE Domain

Kutateladze, T. G., Capelluto, D. G. S., Ferguson, C. G., Cheever, M. L., Kutateladze, A. G., Prestwich, G. D., & Overduin, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309007200 · Cited by 94

Intrinsically disordered γ-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure

Song, J., Guo, L., Muradov, H., Artemyev, N. O., Ruoho, A. E., & Markley, J. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709558105 · Cited by 94

Formation of Native and Non-native Interactions in Ensembles of Denatured ACBP Molecules from Paramagnetic Relaxation Enhancement Studies

Kristjánsdóttir, S., Lindorff‐Larsen, K., Fieber, W., Dobson, C. M., Vendruscolo, M., & Poulsen, F. M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.01.009 · Cited by 91

Protein global fold determination using site‐directed spin and isotope labeling

Gaponenko, V., Howarth, J. W., Gasmi-Seabrook, G. M. C., Yuan, J., Columbus, L. M., Hubbell, W. L., & Rosevear, P. R. (2000) · Protein Science · doi:10.1110/ps.9.2.302 · Cited by 90

Line Narrowing in Methyl-TROSY Using Zero-Quantum 1H-13C NMR Spectroscopy

Tugarinov, V., Sprangers, R., & Kay, L. E. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039732s · Cited by 82

Role of Electrostatic Interactions in Transient Encounter Complexes in Protein−Protein Association Investigated by Paramagnetic Relaxation Enhancement

Suh, J., Tang, C., & Clore, G. M. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0760978 · Cited by 81

Visualization of Transient Ultra-Weak Protein Self-Association in Solution Using Paramagnetic Relaxation Enhancement

Tang, C., Ghirlando, R., & Clore, G. M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja710493m · Cited by 80

Characterization of Nonspecific Protein−DNA Interactions by 1H Paramagnetic Relaxation Enhancement

Iwahara, J., Schwieters, C. D., & Clore, G. M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja046246b · Cited by 80

How to get from A to B: strategies for analysing protein motion on DNA

Halford, S. E., & Szczelkun, M. D. (2002) · European Biophysics Journal · doi:10.1007/s00249-002-0224-4 · Cited by 78

Long‐Range‐Distance NMR Effects in a Protein Labeled with a Lanthanide–DOTA Chelate

Vlasie, M. D., Comuzzi, C., van den Nieuwendijk, A. M. C. H., Prudêncio, M., Overhand, M., & Ubbink, M. (2006) · Chemistry - A European Journal · doi:10.1002/chem.200600916 · Cited by 75

Localization of Fe2+ at an RTGR sequence within a DNA duplex explains preferential cleavage by Fe2+ and H2O211Edited by M. F. Summers

Rai, P., Cole, T. D., Wemmer, D. E., & Linn, S. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5010 · Cited by 73

HIV-I protease: Maturation, enzyme specificity, and drug resistance

Louis, J. M., Webert, I. T., Tőzsér, J., Clore, G. M., & Gronenborn, A. M. (2000) · Advances in pharmacology · doi:10.1016/s1054-3589(00)49025-3 · Cited by 71

Visualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancement

Clore, G. M. (2008) · Molecular BioSystems · doi:10.1039/b810232e · Cited by 70

Enhancement of Association Rates by Nonspecific Binding to DNA and Cell Membranes

Zhou, H., & Szabó, A. (2004) · Physical Review Letters · doi:10.1103/physrevlett.93.178101 · Cited by 68

Protein Folding Pathways Studied by Pulsed- and Native-State Hydrogen Exchange

Bai, Y. (2006) · Chemical Reviews · doi:10.1021/cr040432i · Cited by 67

Solution Structure of the Phosphoryl Transfer Complex between the Cytoplasmic A Domain of the Mannitol Transporter IIMannitol and HPr of the Escherichia coliPhosphotransferase System

Cornilescu, G., Lee, B. R., Cornilescu, C. C., Wang, G., Peterkofsky, A., & Clore, G. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207314200 · Cited by 66

A Transient Precursor of the HIV-1 Protease

Wondrak, E. M., Nashed, N. T., Haber, M. T., Jerina, D. M., & Louis, J. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4477 · Cited by 65

Reweighted atomic densities to represent ensembles of NMR structures*

Schwieters, C. D., & Clore, G. M. (2002) · Journal of Biomolecular NMR · doi:10.1023/a:1019875223132 · Cited by 63

Proteolytic Processing of HIV-1 Protease Precursor, Kinetics and Mechanism

Louis, J. M., Wondrak, E. M., Kimmel, A. R., Wingfield, P. T., & Nashed, N. T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23437 · Cited by 61

Direct-Detected13C NMR to Investigate the Iron(III) Hemophore HasA

Caillet‐Saguy, C., Delepierre, M., Lecroisey, A., Bertini, I., Piccioli, M., & Turano, P. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054902h · Cited by 60

Studies of slow conformational equilibria in macromolecules by exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experiment

Wider, G., Neri, D., & Kurt Wüthrich, A. (1991) · Journal of Biomolecular NMR · doi:10.1007/bf01874572 · Cited by 60

Solution NMR Structure of the 48-kDa IIAMannose-HPr Complex of the Escherichia coli Mannose Phosphotransferase System

Williams, D. C., Cai, M., Suh, J.-Y., Peterkofsky, A., & Clore, G. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501986200 · Cited by 59

Distance mapping of protein‐binding sites using spin‐labeled oligosaccharide ligands

Jain, N. U., Venot, A. P., Umemoto, K., Leffler, H., & Prestegard, J. H. (2001) · Protein Science · doi:10.1110/ps.17401 · Cited by 52

Dynamics in the Transient Complex of Plastocyanin−CytochromeffromProchlorothrixhollandica

Hulsker, R., Baranova, M. V., Bullerjahn, G. S., & Ubbink, M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja077453p · Cited by 51

Identifying long-range structure in the intrinsically unstructured transactivation domain of p53

Vise, P., Baral, B., Stancik, A., Lowry, D. F., & Daughdrill, G. W. (2007) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21364 · Cited by 47

NMR Structural Characterization of Substrates Bound to N-Acetylglucosaminyltransferase V

Macnaughtan, M. A., Kamar, M., Álvarez-Manilla, G., Venot, A. P., Glushka, J., Pierce, J. M., & Prestegard, J. H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.015 · Cited by 40

Introduction to Protein Structure

Meisenberg, G., & Simmons, W. H. (2012) · Elsevier eBooks · doi:10.1016/b978-0-323-07155-0.00002-2 · Cited by 40

Mapping protein–protein interaction by 13C′-detected heteronuclear NMR spectroscopy

Bertini, I., Felli, I. C., Gonnelli, L., Pierattelli, R., Spyranti, Z., & Spyroulias, G. A. (2006) · Journal of Biomolecular NMR · doi:10.1007/s10858-006-9068-z · Cited by 36

Determination of the Three-Dimensional Structure of the Mrf2−DNA Complex Using Paramagnetic Spin Labeling

Cai, S., Zhu, L., Zhang, Z., & Chen, Y. (2007) · Biochemistry · doi:10.1021/bi061738h · Cited by 36

High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment

Rumpel, S., Becker, S., & Zweckstetter, M. (2007) · Journal of Biomolecular NMR · doi:10.1007/s10858-007-9204-4 · Cited by 32

Nuclear spin relaxation in paramagnetic systems (S = 1) in the slow-motion regime for the electron spin. IV. Motional anisotropy and noncoinciding dipole-dipole and zero-field splitting tensors

Benetis, N.-P., & Kowalewski, J. (1985) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(85)90372-5 · Cited by 31

Mobility of TOAC spin-labelled peptides binding to the Src SH3 domain studied by paramagnetic NMR

Lindfors, H. E., de Koning, P. E., Drijfhout, J. W., Venezia, B., & Ubbink, M. (2008) · Journal of Biomolecular NMR · doi:10.1007/s10858-008-9248-0 · Cited by 21

NMR Study of Repair Mechanism of DNA Photolyase by FAD-induced Paramagnetic Relaxation Enhancement

Ueda, T., Kato, A., Ogawa, Y., Torizawa, T., Kuramitsu, S., Iwai, S., Terasawa, H., & Shimada, I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409942200 · Cited by 19

High stability of the hinge region in the membrane-active peptide helix of zervamicin: paramagnetic relaxation enhancement studies

Shenkarev, Z. O., Paramonov, A. S., Balashova, T. A., Yakimenko, Z. A., Baru, M. B., Mustaeva, L. G., Raap, J., Ovchinnikova, T. V., & Arseniev, A. S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.115 · Cited by 14

Protonless 13C direct detection NMR: Characterization of the 37 kDa trimeric protein CutA1

Bertini, I., Jiménez, B., Pierattelli, R., Wedd, A. G., & Xiao, Z. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21577 · Cited by 14

Structural disorder of monomeric α-synuclein persists in mammalian cells

Theillet, F.-X., Binolfi, A., Bekei, B., Martorana, A., Rose, H. M., Stuiver, M., Verzini, S., Lorenz, D., van Rossum, M., Goldfarb, D., et al. (2016) · Nature · doi:10.1038/nature16531 · Cited by 868

An introduction to NMR-based approaches for measuring protein dynamics

Kleckner, I. R., & Foster, M. P. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.10.012 · Cited by 561

Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

Oroz, J., Chang, B. J., Wysoczanski, P., Lee, C.-T., Pérez-Lara, Á., Chakraborty, P., Hofele, R. V., Baker, J. D., Blair, L. J., Biernat, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06880-0 · Cited by 100

Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition

Liu, Z., Gong, Z., Jiang, W.-X., Yang, J., Zhu, W.-K., Guo, D.-C., Zhang, W.-P., Liu, M.-L., & Tang, C. (2015) · eLife · doi:10.7554/elife.05767 · Cited by 60

Molecular Structure of Cu(II)-Bound Amyloid-β Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer’s Disease

Abelein, A., Ciofi-Baffoni, S., Mörman, C., Kumar, R., Giachetti, A., Piccioli, M., & Biverstål, H. (2022) · JACS Au · doi:10.1021/jacsau.2c00438 · Cited by 52