Year |
Citation |
Score |
2022 |
Waman VP, Orengo C, Kleywegt GJ, Lesk AM. Three-dimensional Structure Databases of Biological Macromolecules. Methods in Molecular Biology (Clifton, N.J.). 2449: 43-91. PMID 35507259 DOI: 10.1007/978-1-0716-2095-3_3 |
0.309 |
|
2018 |
Young JY, Westbrook JD, Feng Z, Peisach E, Persikova I, Sala R, Sen S, Berrisford JM, Swaminathan GJ, Oldfield TJ, Gutmanas A, Igarashi R, Armstrong DR, Baskaran K, Chen L, ... ... Kleywegt GJ, et al. Worldwide Protein Data Bank biocuration supporting open access to high-quality 3D structural biology data. Database : the Journal of Biological Databases and Curation. 2018. PMID 29688351 DOI: 10.1093/Database/Bay002 |
0.359 |
|
2017 |
Burley SK, Berman HM, Kleywegt GJ, Markley JL, Nakamura H, Velankar S. Protein Data Bank (PDB): The Single Global Macromolecular Structure Archive. Methods in Molecular Biology (Clifton, N.J.). 1607: 627-641. PMID 28573592 DOI: 10.1007/978-1-4939-7000-1_26 |
0.362 |
|
2015 |
Sali A, Berman HM, Schwede T, Trewhella J, Kleywegt G, Burley SK, Markley J, Nakamura H, Adams P, Bonvin AM, Chiu W, Peraro MD, Di Maio F, Ferrin TE, Grünewald K, et al. Outcome of the First wwPDB Hybrid/Integrative Methods Task Force Workshop. Structure (London, England : 1993). PMID 26095030 DOI: 10.1016/J.Str.2015.05.013 |
0.507 |
|
2015 |
Gutmanas A, Adams PD, Bardiaux B, Berman HM, Case DA, Fogh RH, Güntert P, Hendrickx PM, Herrmann T, Kleywegt GJ, Kobayashi N, Lange OF, Markley JL, Montelione GT, Nilges M, et al. NMR Exchange Format: a unified and open standard for representation of NMR restraint data. Nature Structural & Molecular Biology. 22: 433-4. PMID 26036565 DOI: 10.1038/Nsmb.3041 |
0.587 |
|
2014 |
Battle G, Zardecki C, Haruki N, Kleywegt G, Berman H, Nakamura H, Conroy M. Educational Outreach and User Training at the Worldwide Protein Data Bank Acta Crystallographica Section a Foundations and Advances. 70: C1271-C1271. DOI: 10.1107/S2053273314087282 |
0.397 |
|
2014 |
Gore S, Hendrickx P, Sanz-Garcia E, Velankar S, Kleywegt G. New wwPDB validation pipelines for X-ray, NMR and 3DEM structures Acta Crystallographica Section A. 70. DOI: 10.1107/S2053273314085210 |
0.321 |
|
2013 |
Lagerstedt I, Moore WJ, Patwardhan A, Sanz-GarcÃa E, Best C, Swedlow JR, Kleywegt GJ. Web-based visualisation and analysis of 3D electron-microscopy data from EMDB and PDB. Journal of Structural Biology. 184: 173-81. PMID 24113529 DOI: 10.1016/j.jsb.2013.09.021 |
0.309 |
|
2013 |
Montelione GT, Nilges M, Bax A, Güntert P, Herrmann T, Richardson JS, Schwieters CD, Vranken WF, Vuister GW, Wishart DS, Berman HM, Kleywegt GJ, Markley JL. Recommendations of the wwPDB NMR Validation Task Force. Structure (London, England : 1993). 21: 1563-70. PMID 24010715 DOI: 10.1016/J.Str.2013.07.021 |
0.617 |
|
2013 |
Hendrickx PM, Gutmanas A, Kleywegt GJ. Vivaldi: visualization and validation of biomacromolecular NMR structures from the PDB. Proteins. 81: 583-91. PMID 23180575 DOI: 10.1002/prot.24213 |
0.304 |
|
2012 |
Berman HM, Henrick K, Kleywegt G, Nakamura H, Markley J. The Worldwide Protein Data Bank International Tables For Crystallography. DOI: 10.1107/97809553602060000896 |
0.359 |
|
2010 |
Golovin A, Henrick K, Kleywegt G. Integration of chemical information with protein sequences and 3D structures Journal of Cheminformatics. 2. DOI: 10.1186/1758-2946-2-S1-O17 |
0.343 |
|
2000 |
Chen YW, Dodson EJ, Kleywegt GJ. Does NMR mean "not for molecular replacement"? Using NMR-based search models to solve protein crystal structures. Structure (London, England : 1993). 8: R213-20. PMID 11080645 DOI: 10.1016/S0969-2126(00)00524-4 |
0.308 |
|
1997 |
Kleywegt GJ, Jones TA. Detecting folding motifs and similarities in protein structures. Methods in Enzymology. 277: 525-45. PMID 18488323 DOI: 10.1016/S0076-6879(97)77029-0 |
0.335 |
|
1997 |
Kleywegt GJ, Jones TA. Model building and refinement practice. Methods in Enzymology. 277: 208-30. PMID 18488311 DOI: 10.1016/S0076-6879(97)77013-7 |
0.309 |
|
1993 |
Kleywegt GJ, Vuister GW, Padilla A, Knegtel RMA, Boelens R, Kaptein R. Computer-Assisted Assignment of Homonuclear 3D NMR Spectra of Proteins. Application to Pike Parvalbumin III Journal of Magnetic Resonance, Series B. 102: 166-176. DOI: 10.1006/Jmrb.1993.1079 |
0.7 |
|
1991 |
Kleywegt GJ, Boelens R, Cox M, Llinás M, Kaptein R. Computer-assisted assignment of 2D 1H NMR spectra of proteins: basic algorithms and application to phoratoxin B. Journal of Biomolecular Nmr. 1: 23-47. PMID 1841687 DOI: 10.1007/Bf01874567 |
0.651 |
|
1990 |
Vuister GW, Boelens R, Padilla A, Kleywegt GJ, Kaptein R. Assignment strategies in homonuclear three-dimensional 1H NMR spectra of proteins. Biochemistry. 29: 1829-39. PMID 2331467 DOI: 10.1021/Bi00459A024 |
0.7 |
|
1990 |
Padilla A, Vuister GW, Boelens R, Kleywegt GJ, Cave A, Parello J, Kaptein R. Homonuclear three-dimensional proton NMR spectroscopy of pike parvalbumin. Comparison of short- and medium-range NOEs from 2D and 3D NMR Journal of the American Chemical Society. 112: 5024-5030. DOI: 10.1021/Ja00169A005 |
0.692 |
|
1990 |
Kleywegt GJ, Boelens R, Kaptein R. A versatile approach toward the partially automatic recognition of cross peaks in 2D 1H NMR spectra Journal of Magnetic Resonance (1969). 88: 601-608. DOI: 10.1016/0022-2364(90)90291-G |
0.665 |
|
1989 |
Kleywegt GJ, Lamerichs RMJN, Boelens R, Kaptein R. Toward automatic assignment of protein 1H NMR spectra Journal of Magnetic Resonance (1969). 85: 186-197. DOI: 10.1016/0022-2364(89)90335-1 |
0.628 |
|
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