The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

NMR with Proteins and Nucleic Acids

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

NMR of Proteins and Nucleic Acids

(2006) · Nuclear Magnetic Resonance · doi:10.1039/9781847555236-00336 · Cited by 5,863

A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants

States, D. J., Haberkorn, R. A., & Ruben, D. J. (1982) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(82)90279-7 · Cited by 2,573

Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR

Grzesiek, S., & Bax, A. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00042a003 · Cited by 1,022

Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

Wüthrich, K., Billeter, M., & Braun, W. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80144-2 · Cited by 1,002

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

Ikura, M., Kay, L. E., & Bax, A. (1990) · Biochemistry · doi:10.1021/bi00471a022 · Cited by 918

Methodological advances in protein NMR

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

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

A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams

Garrett, D. S., Powers, R., Gronenborn, A. M., & Clore, G. M. (1991) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(91)90341-p · Cited by 682

1H1H correlation via isotropic mixing of 13C magnetization, a new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins

Bax, A., Clore, G. M., & Gronenborn, A. M. (1990) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(90)90202-k · Cited by 584

The CCPN data model for NMR spectroscopy: Development of a software pipeline

Vranken, W. F., Boucher, W., Stevens, T. J., Fogh, R. H., Pajon, A., Llinas, M., Ulrich, E. L., Markley, J. L., Ionides, J., & Laue, E. D. (2005) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.20449 · Cited by 3,209

NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy

Lee, W., Tonelli, M., & Markley, J. L. (2015) · Bioinformatics · doi:10.1093/bioinformatics/btu830 · Cited by 2,045

Automated NMR Structure Calculation With CYANA

Güntert, P. (2004) · Protein NMR Techniques · doi:10.1385/1-59259-809-9:353 · Cited by 1,351

NMR characterization of the full‐length recombinant murine prion protein, m PrP(23–231)

Riek, R., Hornemann, S., Wider, G., Glockshuber, R., & Wüthrich, K. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00920-4 · Cited by 722

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

Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis

Czabotar, P. E., Westphal, D., Dewson, G., Ma, S., Hockings, C., Fairlie, W. D., Lee, E. F., Yao, S., Robin, A. Y., Smith, B. J., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.031 · Cited by 573

Small-Molecule Inhibition of the Interaction between the Translation Initiation Factors eIF4E and eIF4G

Moerke, N. J., Aktas, H., Chen, H., Cantel, S., Reibarkh, M. Y., Fahmy, A., Gross, J. D., Degterev, A., Yuan, J., Chorev, M., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.046 · Cited by 572

Principles for designing ideal protein structures

Koga, N., Tatsumi-Koga, R., Liu, G., Xiao, R., Acton, T. B., Montelione, G. T., & Baker, D. (2012) · Nature · doi:10.1038/nature11600 · Cited by 564

Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase.

Salim, K., Bottomley, M. J., Querfurth, E., Zvelebil, M. J., Gout, I., Scaife, R., Margolis, R. L., Gigg, R., Smith, C. I., Driscoll, P. C., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01014.x · Cited by 558

CcpNmr AnalysisAssign: a flexible platform for integrated NMR analysis

Skinner, S. P., Fogh, R. H., Boucher, W., Ragan, T. J., Mureddu, L. G., & Vuister, G. W. (2016) · Journal of Biomolecular NMR · doi:10.1007/s10858-016-0060-y · Cited by 513

Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS

Herrmann, T., Güntert, P., & Wüthrich, K. (2002) · Journal of Biomolecular NMR · doi:10.1023/a:1021614115432 · Cited by 481

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

Structure of translation factor elF4E bound to m7GDP and interaction with 4E-binding protein

Matsuo, H., Li, H., McGuire, A. M., Fletcher, C. M., Gingras, A.-C., Sonenberg, N., & Wagner, G. (1997) · Nature Structural Biology · doi:10.1038/nsb0997-717 · Cited by 377

Drosophila PIWI associates with chromatin and interacts directly with HP1a

Brower-Toland, B., Findley, S. D., Jiang, L., Liu, L., Yin, H., Dus, M., Zhou, P., Elgin, S. C. R., & Lin, H. (2007) · Genes & Development · doi:10.1101/gad.1564307 · Cited by 350

Structure and function of the complex formed by the tuberculosis virulence factors CFP‐10 and ESAT‐6

Renshaw, P. S., Lightbody, K. L., Veverka, V., Muskett, F. W., Kelly, G., Frenkiel, T. A., Gordon, S. V., Hewinson, R. G., Burke, B., Norman, J., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600732 · Cited by 334

Mars - robust automatic backbone assignment of proteins

Jung, Y.-S., & Zweckstetter, M. (2004) · Journal of Biomolecular NMR · doi:10.1023/b:jnmr.0000042954.99056.ad · Cited by 311

Structural insights into the U-box, a domain associated with multi-ubiquitination

Ohi, M. D., Vander Kooi, C. W., Rosenberg, J. A., Chazin, W. J., & Gould, K. L. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb906 · Cited by 295

Architecture of the mitochondrial calcium uniporter

Oxenoid, K., Dong, Y., Cao, C., Cui, T., Sancak, Y., Markhard, A. L., Grabarek, Z., Kong, L., Liu, Z., Ouyang, B., et al. (2016) · Nature · doi:10.1038/nature17656 · Cited by 294

Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A

Bochkareva, E., Kaustov, L., Ayed, A., Yi, G.-S., Lu, Y., Pineda-Lucena, A., Liao, J. C. C., Okorokov, A. L., Milner, J., Arrowsmith, C. H., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504614102 · Cited by 275

Development of α-Helical Calpain Probes by Mimicking a Natural Protein–Protein Interaction

Jo, H., Meinhardt, N., Wu, Y., Kulkarni, S., Hu, X., Low, K. E., Davies, P. L., DeGrado, W. F., & Greenbaum, D. C. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307599z · Cited by 261

The Major Birch Allergen, Bet v 1, Shows Affinity for a Broad Spectrum of Physiological Ligands

Mogensen, J. E., Wimmer, R., Larsen, J. N., Spangfort, M. D., & Otzen, D. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202065200 · Cited by 254

Interpreting protein chemical shift data

Wishart, D. S. (2011) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2010.07.004 · Cited by 252

The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation

Bottomley (2001) · Nature Structural Biology · doi:10.1038/89675 · Cited by 224

Chemical and structural studies provide a mechanistic basis for recognition of the MYC G-quadruplex

Calabrese, D. R., Chen, X., Leon, E. C., Gaikwad, S. M., Phyo, Z., Hewitt, W. M., Alden, S., Hilimire, T. A., He, F., Michalowski, A. M., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06315-w · Cited by 172

Structure–Activity Studies in a Family of β‐Hairpin Protein Epitope Mimetic Inhibitors of the p53–HDM2 Protein–Protein Interaction

Fasan, R., Dias, R. L. A., Moehle, K., Zerbe, O., Obrecht, D., Mittl, P. R. E., Grütter, M. G., & Robinson, J. A. (2006) · ChemBioChem · doi:10.1002/cbic.200500452 · Cited by 129

Snapshots and ensembles of BTK and cIAP1 protein degrader ternary complexes

Schiemer, J., Horst, R., Meng, Y., Montgomery, J. I., Xu, Y., Feng, X., Borzilleri, K., Uccello, D. P., Leverett, C., Brown, S., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-020-00686-2 · Cited by 113

Structural Basis for the Versatile Interactions of Smad7 with Regulator WW Domains in TGF-β Pathways

Aragón, E., Goerner, N., Xi, Q., Gomes, T., Gao, S., Massagué, J., & Macias, M. J. (2012) · Structure · doi:10.1016/j.str.2012.07.014 · Cited by 99

Stabilization of Neurotoxic Soluble β-Sheet-Rich Conformations of the Alzheimer's Disease Amyloid-β Peptide

Tew, D. J., Bottomley, S. P., Smith, D. P., Ciccotosto, G. D., Babon, J., Hinds, M. G., Masters, C. L., Cappai, R., & Barnham, K. J. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.119909 · Cited by 93

Cyclization of the Antimicrobial Peptide Gomesin with Native Chemical Ligation: Influences on Stability and Bioactivity

Chan, L. Y., Zhang, V. M., Huang, Y., Waters, N. C., Bansal, P. S., Craik, D. J., & Daly, N. L. (2013) · ChemBioChem · doi:10.1002/cbic.201300034 · Cited by 88

Molecular Analysis of the Interaction between the Hematopoietic Master Transcription Factors GATA-1 and PU.1

Liew, C. W., Rand, K. D., Simpson, R. J. Y., Yung, W. W., Mansfield, R. E., Crossley, M., Proetorius-Ibba, M., Nerlov, C., Poulsen, F. M., & Mackay, J. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602830200 · Cited by 63

VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins

Swarbrick, J. D., Shaw, D. J., Chhabra, S., Ghai, R., Valkov, E., Norwood, S. J., Seaman, M. N. J., & Collins, B. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020420 · Cited by 59

Automatic structure-based NMR methyl resonance assignment in large proteins

Pritišanac, I., Würz, J. M., Alderson, T. R., & Güntert, P. (2019) · Nature Communications · doi:10.1038/s41467-019-12837-8 · Cited by 46

Structural and Functional Comparison of the RING Domains of Two p53 E3 Ligases, Mdm2 and Pirh2

Shloush, J., Vlassov, J. E., Engson, I., Duan, S., Saridakis, V., Dhe-paganon, S., Raught, B., Sheng, Y., & Arrowsmith, C. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.157669 · Cited by 42

HIV-1 fusion inhibitors targeting the membrane-proximal external region of Env spikes

Xiao, T., Frey, G., Fu, Q., Lavine, C. L., Scott, D. A., Seaman, M. S., Chou, J. J., & Chen, B. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0496-y · Cited by 38

Structure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum

Olson, L. J., Orsi, R., Alculumbre, S. G., Peterson, F. C., Stigliano, I. D., Parodi, A. J., D'Alessio, C., & Dahms, N. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.450239 · Cited by 24

The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection

Vieira, M. F. M., Hernandez, G., Zhong, Q., Arbesú, M., Veloso, T., Gomes, T., Martins, M. L., Monteiro, H., Frazão, C., Frankel, G., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-05856-9 · Cited by 14