| Year |
Citation |
Score |
| 2020 |
Mureddu LG, Ragan TJ, Brooksbank EJ, Vuister GW. CcpNmr AnalysisScreen, a new software programme with dedicated automated analysis tools for fragment-based drug discovery by NMR. Journal of Biomolecular Nmr. PMID 32638146 DOI: 10.1007/s10858-020-00321-1 |
0.311 |
|
| 2019 |
Berman HM, Adams PD, Bonvin AA, Burley SK, Carragher B, Chiu W, DiMaio F, Ferrin TE, Gabanyi MJ, Goddard TD, Griffin PR, Haas J, Hanke CA, Hoch JC, Hummer G, ... ... Vuister GW, et al. Federating Structural Models and Data: Outcomes from A Workshop on Archiving Integrative Structures. Structure (London, England : 1993). PMID 31780431 DOI: 10.1016/J.Str.2019.11.002 |
0.301 |
|
| 2019 |
Mureddu L, Vuister GW. Simple high-resolution NMR spectroscopy as a tool in molecular biology. The Febs Journal. PMID 30706658 DOI: 10.1111/febs.14771 |
0.401 |
|
| 2017 |
Skinner SP, Fogh RH, Boucher W, Ragan TJ, Mureddu LG, Vuister GW. Erratum to: CcpNmr AnalysisAssign: a flexible platform for integrated NMR analysis. Journal of Biomolecular Nmr. PMID 28421403 DOI: 10.1007/s10858-017-0102-0 |
0.327 |
|
| 2016 |
Skinner SP, Fogh RH, Boucher W, Ragan TJ, Mureddu LG, Vuister GW. CcpNmr AnalysisAssign: a flexible platform for integrated NMR analysis. Journal of Biomolecular Nmr. PMID 27663422 DOI: 10.1007/s10858-016-0060-y |
0.311 |
|
| 2015 |
Rosato A, Vranken W, Fogh RH, Ragan TJ, Tejero R, Pederson K, Lee HW, Prestegard JH, Yee A, Wu B, Lemak A, Houliston S, Arrowsmith CH, Kennedy M, Acton TB, ... ... Vuister GW, et al. The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013. Journal of Biomolecular Nmr. PMID 26071966 DOI: 10.1007/S10858-015-9953-4 |
0.391 |
|
| 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, ... ... Vuister GW, 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 |
0.608 |
|
| 2015 |
Ragan TJ, Fogh RH, Tejero R, Vranken W, Montelione GT, Rosato A, Vuister GW. Analysis of the structural quality of the CASD-NMR 2013 entries. Journal of Biomolecular Nmr. PMID 26032236 DOI: 10.1007/S10858-015-9949-0 |
0.369 |
|
| 2015 |
Skinner SP, Goult BT, Fogh RH, Boucher W, Stevens TJ, Laue ED, Vuister GW. Structure calculation, refinement and validation using CcpNmr Analysis. Acta Crystallographica. Section D, Biological Crystallography. 71: 154-61. PMID 25615869 DOI: 10.1107/S1399004714026662 |
0.399 |
|
| 2015 |
Vranken WF, Vuister GW, Bonvin AM. NMR-based modeling and refinement of protein 3D structures. Methods in Molecular Biology (Clifton, N.J.). 1215: 351-80. PMID 25330971 DOI: 10.1007/978-1-4939-1465-4_16 |
0.619 |
|
| 2014 |
Vuister GW, Fogh RH, Hendrickx PM, Doreleijers JF, Gutmanas A. An overview of tools for the validation of protein NMR structures. Journal of Biomolecular Nmr. 58: 259-85. PMID 23877928 DOI: 10.1007/s10858-013-9750-x |
0.414 |
|
| 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 |
0.698 |
|
| 2012 |
Cilia E, Vuister GW, Lenaerts T. Accurate prediction of the dynamical changes within the second PDZ domain of PTP1e. Plos Computational Biology. 8: e1002794. PMID 23209399 DOI: 10.1371/journal.pcbi.1002794 |
0.304 |
|
| 2012 |
Doreleijers JF, Sousa da Silva AW, Krieger E, Nabuurs SB, Spronk CA, Stevens TJ, Vranken WF, Vriend G, Vuister GW. CING: an integrated residue-based structure validation program suite. Journal of Biomolecular Nmr. 54: 267-83. PMID 22986687 DOI: 10.1007/S10858-012-9669-7 |
0.361 |
|
| 2012 |
Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, ... ... Vuister GW, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/Nsmb.2371 |
0.717 |
|
| 2012 |
Breukels V, Touw WG, Vuister GW. NMR structure note: solution structure of Ca²⁺ binding domain 2B of the third isoform of the Na⁺/Ca²⁺ exchanger. Journal of Biomolecular Nmr. 54: 115-21. PMID 22806131 DOI: 10.1007/s10858-012-9654-1 |
0.351 |
|
| 2012 |
Rosato A, Aramini JM, Arrowsmith C, Bagaria A, Baker D, Cavalli A, Doreleijers JF, Eletsky A, Giachetti A, Guerry P, Gutmanas A, Güntert P, He Y, Herrmann T, Huang YJ, ... ... Vuister GW, et al. Blind testing of routine, fully automated determination of protein structures from NMR data. Structure (London, England : 1993). 20: 227-36. PMID 22325772 DOI: 10.1016/J.Str.2012.01.002 |
0.633 |
|
| 2012 |
Doreleijers JF, Vranken WF, Schulte C, Markley JL, Ulrich EL, Vriend G, Vuister GW. NRG-CING: integrated validation reports of remediated experimental biomolecular NMR data and coordinates in wwPDB. Nucleic Acids Research. 40: D519-24. PMID 22139937 DOI: 10.1093/Nar/Gkr1134 |
0.397 |
|
| 2012 |
Wassenaar TA, van Dijk M, Loureiro-Ferreira N, van der Schot G, de Vries SJ, Schmitz C, van der Zwan J, Boelens R, Giachetti A, Ferella L, Rosato A, Bertini I, Herrmann T, Jonker HRA, Bagaria A, ... ... Vuister GW, et al. WeNMR: Structural Biology on the Grid Journal of Grid Computing. 10: 743-767. DOI: 10.1007/s10723-012-9246-z |
0.575 |
|
| 2011 |
Breukels V, Konijnenberg A, Nabuurs SM, Doreleijers JF, Kovalevskaya NV, Vuister GW. Overview on the use of NMR to examine protein structure. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit17.5. PMID 21488042 DOI: 10.1002/0471140864.ps1705s64 |
0.439 |
|
| 2009 |
Doreleijers JF, Vranken WF, Schulte C, Lin J, Wedell JR, Penkett CJ, Vuister GW, Vriend G, Markley JL, Ulrich EL. The NMR restraints grid at BMRB for 5,266 protein and nucleic acid PDB entries. Journal of Biomolecular Nmr. 45: 389-96. PMID 19809795 DOI: 10.1007/S10858-009-9378-Z |
0.385 |
|
| 2009 |
Rosato A, Bagaria A, Baker D, Bardiaux B, Cavalli A, Doreleijers JF, Giachetti A, Guerry P, Güntert P, Herrmann T, Huang YJ, Jonker HR, Mao B, Malliavin TE, Montelione GT, ... ... Vuister GW, et al. CASD-NMR: critical assessment of automated structure determination by NMR. Nature Methods. 6: 625-6. PMID 19718014 DOI: 10.1038/Nmeth0909-625 |
0.635 |
|
| 2007 |
Gianni S, Geierhaas CD, Calosci N, Jemth P, Vuister GW, Travaglini-Allocatelli C, Vendruscolo M, Brunori M. A PDZ domain recapitulates a unifying mechanism for protein folding. Proceedings of the National Academy of Sciences of the United States of America. 104: 128-33. PMID 17179214 DOI: 10.1073/Pnas.0602770104 |
0.338 |
|
| 2007 |
Spronk C, Vuister G, Sargent F. Solution structure of the E. coli Tat proofreading chaperone protein NapD Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Jsx/Pdb |
0.306 |
|
| 2006 |
Gianni S, Walma T, Arcovito A, Calosci N, Bellelli A, Engström A, Travaglini-Allocatelli C, Brunori M, Jemth P, Vuister GW. Demonstration of long-range interactions in a PDZ domain by NMR, kinetics, and protein engineering. Structure (London, England : 1993). 14: 1801-9. PMID 17161370 DOI: 10.1016/j.str.2006.10.010 |
0.357 |
|
| 2006 |
van Ingen H, Vuister GW, Wijmenga S, Tessari M. CEESY: characterizing the conformation of unobservable protein states. Journal of the American Chemical Society. 128: 3856-7. PMID 16551062 DOI: 10.1021/ja0568749 |
0.364 |
|
| 2006 |
van Ingen H, Baltussen MA, Aelen J, Vuister GW. Role of structural and dynamical plasticity in Sin3: the free PAH2 domain is a folded module in mSin3B. Journal of Molecular Biology. 358: 485-97. PMID 16519900 DOI: 10.1016/j.jmb.2006.01.100 |
0.311 |
|
| 2006 |
Nabuurs SB, Spronk CA, Vuister GW, Vriend G. Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. Plos Computational Biology. 2: e9. PMID 16462939 DOI: 10.1371/Journal.Pcbi.0020009 |
0.384 |
|
| 2005 |
Nabuurs SB, Krieger E, Spronk CA, Nederveen AJ, Vriend G, Vuister GW. Definition of a new information-based per-residue quality parameter. Journal of Biomolecular Nmr. 33: 123-34. PMID 16258830 DOI: 10.1007/S10858-005-2826-5 |
0.322 |
|
| 2004 |
Kloks CP, Tessari M, Vuister GW, Hilbers CW. Cold shock domain of the human Y-box protein YB-1. Backbone dynamics and equilibrium between the native state and a partially unfolded state. Biochemistry. 43: 10237-46. PMID 15287751 DOI: 10.1021/bi049524s |
0.362 |
|
| 2004 |
Nabuurs SB, Nederveen AJ, Vranken W, Doreleijers JF, Bonvin AM, Vuister GW, Vriend G, Spronk CA. DRESS: a database of REfined solution NMR structures. Proteins. 55: 483-6. PMID 15103611 DOI: 10.1002/Prot.20118 |
0.598 |
|
| 2004 |
Spronk CAEM, Nabuurs SB, Krieger E, Vriend G, Vuister GW. Validation of protein structures derived by NMR spectroscopy Progress in Nuclear Magnetic Resonance Spectroscopy. 45: 315-337. DOI: 10.1016/J.Pnmrs.2004.08.003 |
0.4 |
|
| 2004 |
Nabuurs SB, Spronk CAEM, Vriend G, Vuister GW. Concepts and tools for NMR restraint analysis and validation Concepts in Magnetic Resonance Part a: Bridging Education and Research. 22: 90-105. DOI: 10.1002/Cmr.A.20016 |
0.387 |
|
| 2003 |
Nabuurs SB, Spronk CA, Krieger E, Maassen H, Vriend G, Vuister GW. Quantitative evaluation of experimental NMR restraints. Journal of the American Chemical Society. 125: 12026-34. PMID 14505424 DOI: 10.1021/Ja035440F |
0.363 |
|
| 2003 |
Wingens M, Walma T, van Ingen H, Stortelers C, van Leeuwen JE, van Zoelen EJ, Vuister GW. Structural analysis of an epidermal growth factor/transforming growth factor-alpha chimera with unique ErbB binding specificity. The Journal of Biological Chemistry. 278: 39114-23. PMID 12869572 DOI: 10.1074/jbc.M305603200 |
0.338 |
|
| 2003 |
Spronk CA, Nabuurs SB, Bonvin AM, Krieger E, Vuister GW, Vriend G. The precision of NMR structure ensembles revisited. Journal of Biomolecular Nmr. 25: 225-34. PMID 12652134 DOI: 10.1023/A:1022819716110 |
0.57 |
|
| 2003 |
Ingen Hv, Tessari M, Vuister G. Complete 1H Chemical Shift Assignment of a 24-residue Sin Interacting Domain of hMad1 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5457 |
0.316 |
|
| 2002 |
van Ingen H, Tessari M, Vuister GW. A 3D doubly sensitivity enhanced X-filtered TOCSY-TOCSY experiment. Journal of Biomolecular Nmr. 24: 155-60. PMID 12495032 DOI: 10.1023/A:1020975705237 |
0.344 |
|
| 2002 |
van Ingen H, Vuister GW, Tessari M. A two-dimensional artifact from asynchronous decoupling. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 156: 258-61. PMID 12165261 DOI: 10.1006/jmre.2002.2564 |
0.337 |
|
| 2002 |
Spronk CA, Linge JP, Hilbers CW, Vuister GW. Improving the quality of protein structures derived by NMR spectroscopy. Journal of Biomolecular Nmr. 22: 281-9. PMID 11991356 DOI: 10.1023/A:1014971029663 |
0.401 |
|
| 2002 |
Walma T, Spronk CA, Tessari M, Aelen J, Schepens J, Hendriks W, Vuister GW. Structure, dynamics and binding characteristics of the second PDZ domain of PTP-BL. Journal of Molecular Biology. 316: 1101-10. PMID 11884147 DOI: 10.1006/jmbi.2002.5402 |
0.341 |
|
| 2002 |
Kloks CP, Spronk CA, Lasonder E, Hoffmann A, Vuister GW, Grzesiek S, Hilbers CW. The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1. Journal of Molecular Biology. 316: 317-26. PMID 11851341 DOI: 10.1006/jmbi.2001.5334 |
0.31 |
|
| 2000 |
Spronk CA, Tessari M, Kaan AM, Jansen JF, Vermeulen M, Stunnenberg HG, Vuister GW. The Mad1-Sin3B interaction involves a novel helical fold. Nature Structural Biology. 7: 1100-4. PMID 11101889 DOI: 10.1038/81944 |
0.333 |
|
| 2000 |
Tessari M, Vuister GW. A novel experiment for the quantitative measurement of CSA(1H(N))/CSA(15N) cross-correlated relaxation in 15N-labeled proteins. Journal of Biomolecular Nmr. 16: 171-4. PMID 10723996 DOI: 10.1023/A:1008347012429 |
0.317 |
|
| 1999 |
Whitehead B, Tessari M, Carotenuto A, van Bergen en Henegouwen PM, Vuister GW. The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins. Biochemistry. 38: 11271-7. PMID 10471276 DOI: 10.1021/bi990922i |
0.366 |
|
| 1999 |
Carotenuto A, Tessari M, Whitehead B, Aelen JM, van Bergen en Henegouwen PM, Vuister GW. Sequence-specific 1H, 13C and 15N assignment and secondary structure of the apo EH2 domain of mouse Eps15. Journal of Biomolecular Nmr. 14: 97-8. PMID 10382315 DOI: 10.1023/A:1008394326526 |
0.323 |
|
| 1999 |
Rubinstenn G, Vuister GW, Zwanenburg N, Hellingwerf KJ, Boelens R, Kaptein R. NMR experiments for the study of photointermediates: application to the photoactive yellow protein. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 137: 443-7. PMID 10089180 DOI: 10.1006/Jmre.1999.1705 |
0.75 |
|
| 1998 |
Kloks CP, Hoffmann A, Omichinski JG, Vuister GW, Hilbers CW, Grzesiek S. Resonance assignment and secondary structure of the cold shock domain of the human YB-1 protein. Journal of Biomolecular Nmr. 12: 463-4. PMID 9835056 DOI: 10.1023/A:1008309216938 |
0.38 |
|
| 1998 |
Düx P, Rubinstenn G, Vuister GW, Boelens R, Mulder FA, Hård K, Hoff WD, Kroon AR, Crielaard W, Hellingwerf KJ, Kaptein R. Solution structure and backbone dynamics of the photoactive yellow protein. Biochemistry. 37: 12689-99. PMID 9737845 DOI: 10.1021/Bi9806652 |
0.791 |
|
| 1998 |
Rubinstenn G, Vuister GW, Mulder FA, Düx PE, Boelens R, Hellingwerf KJ, Kaptein R. Structural and dynamic changes of photoactive yellow protein during its photocycle in solution. Nature Structural Biology. 5: 568-70. PMID 9665170 DOI: 10.1038/823 |
0.777 |
|
| 1997 |
Düx P, Whitehead B, Boelens R, Kaptein R, Vuister GW. Measurement of (15)N- (1)H coupling constants in uniformly (15)N-labeled proteins: Application to the photoactive yellow protein. Journal of Biomolecular Nmr. 10: 301-6. PMID 20700833 DOI: 10.1023/A:1018393225804 |
0.746 |
|
| 1997 |
Whitehead B, Tessari M, Düx P, Boelens R, Kaptein R, Vuister GW. A 15n-filtered 2D 1H TOCSY experiment for assignment of aromatic ring resonances and selective identification of tyrosine ring resonances in proteins: Description and application to Photoactive Yellow Protein. Journal of Biomolecular Nmr. 9: 313-6. PMID 20680663 DOI: 10.1023/A:1018687127330 |
0.744 |
|
| 1997 |
Tessari M, Gentile LN, Taylor SJ, Shalloway DI, Nicholson LK, Vuister GW. Heteronuclear NMR studies of the combined Src homology domains 2 and 3 of pp60 c-Src: effects of phosphopeptide binding. Biochemistry. 36: 14561-71. PMID 9398174 DOI: 10.1021/Bi9712044 |
0.368 |
|
| 1997 |
Tessari M, Vis H, Boelens R, Kaptein R, Vuister GW. Quantitative measurement of relaxation interference effects between 1H(N) CSA and 1H-15N dipolar interaction: Correlation with secondary structure Journal of the American Chemical Society. 119: 8985-8990. DOI: 10.1021/Ja970573K |
0.744 |
|
| 1997 |
Tessari M, Mulder FA, Boelens R, Vuister GW. Determination of Amide Proton CSA in15N-Labeled Proteins Using1H CSA/15N–1H Dipolar and15N CSA/15N–1H Dipolar Cross-Correlation Rates Journal of Magnetic Resonance. 127: 128-133. DOI: 10.1006/Jmre.1997.1199 |
0.749 |
|
| 1997 |
Düx P, Whitehead B, Boelens R, Kaptein R, Vuister GW. Measurement of 15N-1H coupling constants in uniformly 15N-labeled proteins: Application to the photoactive yellow protein Journal of Biomolecular Nmr. 10: 301-306. |
0.584 |
|
| 1995 |
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. Journal of Biomolecular Nmr. 6: 277-93. PMID 8520220 DOI: 10.1007/BF00197809 |
0.417 |
|
| 1994 |
Vuister GW, Kim SJ, Wu C, Bax A. NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors. Biochemistry. 33: 10-6. PMID 8286326 DOI: 10.1021/Bi00167A002 |
0.521 |
|
| 1994 |
Garrett DS, Kuszewski J, Hancock TJ, Lodi PJ, Vuister GW, Gronenborn AM, Clore GM. The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR. Journal of Magnetic Resonance. Series B. 104: 99-103. PMID 8025816 DOI: 10.1006/Jmrb.1994.1061 |
0.375 |
|
| 1994 |
Vuister GW, Bax A. Measurement of four-bond HN-H alpha J-couplings in staphylococcal nuclease. Journal of Biomolecular Nmr. 4: 193-200. PMID 8019134 DOI: 10.1007/BF00175247 |
0.493 |
|
| 1994 |
Wang AC, Lodi PJ, Qin J, Vuister GW, Gronenborn AM, Clore GM. An efficient triple-resonance experiment for proton-directed sequential backbone assignment of medium-sized proteins. Journal of Magnetic Resonance. Series B. 105: 196-8. PMID 7952935 DOI: 10.1006/Jmrb.1994.1123 |
0.354 |
|
| 1994 |
Bax A, Vuister GW, Grzesiek S, Delaglio F, Wang AC, Tschudin R, Zhu G. Measurement of homo- and heteronuclear J couplings from quantitative J correlation. Methods in Enzymology. 239: 79-105. PMID 7830604 DOI: 10.1016/S0076-6879(94)39004-5 |
0.507 |
|
| 1994 |
Bax A, Delaglio F, Grzesiek S, Vuister GW. Resonance assignment of methionine methyl groups and chi 3 angular information from long-range proton-carbon and carbon-carbon J correlation in a calmodulin-peptide complex. Journal of Biomolecular Nmr. 4: 787-97. PMID 7812153 DOI: 10.1007/BF00398409 |
0.518 |
|
| 1994 |
Vuister GW, Kim SJ, Orosz A, Marquardt J, Wu C, Bax A. Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor. Nature Structural Biology. 1: 605-14. PMID 7634100 DOI: 10.2210/Pdb1Hks/Pdb |
0.489 |
|
| 1994 |
Vuister GW, Kim SJ, Wu C, Bax A. 2D and 3D NMR study of phenylalanine residues in proteins by reverse isotopic labeling Journal of the American Chemical Society. 116: 9206-9210. DOI: 10.1021/Ja00099A041 |
0.605 |
|
| 1993 |
Vuister GW, Delaglio F, Bax A. The use of 1JC alpha H alpha coupling constants as a probe for protein backbone conformation. Journal of Biomolecular Nmr. 3: 67-80. PMID 8448436 DOI: 10.1007/BF00242476 |
0.485 |
|
| 1993 |
Grzesiek S, Vuister GW, Bax A. A simple and sensitive experiment for measurement of JCC couplings between backbone carbonyl and methyl carbons in isotopically enriched proteins. Journal of Biomolecular Nmr. 3: 487-93. PMID 8400833 DOI: 10.1007/BF00176014 |
0.538 |
|
| 1993 |
Vuister GW, Yamazaki T, Torchia DA, Bax A. Measurement of two- and three-bond 13C-1H J couplings to the C delta carbons of leucine residues in staphylococcal nuclease. Journal of Biomolecular Nmr. 3: 297-306. PMID 8358233 DOI: 10.1007/Bf00212516 |
0.51 |
|
| 1993 |
Vuister GW, Bax A. Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HNH.alpha.) coupling constants in 15N-enriched proteins Journal of the American Chemical Society. 115: 7772-7777. DOI: 10.1021/JA00070A024 |
0.543 |
|
| 1993 |
Vuister GW, Wang AC, Bax A. Measurement of three-bond nitrogen-carbon J couplings in proteins uniformly enriched in nitrogen-15 and carbon-13 Journal of the American Chemical Society. 115: 5334-5335. DOI: 10.1021/JA00065A071 |
0.459 |
|
| 1993 |
Ikura M, Grzesiek S, Vuister G, Klee CB, Bax A. Flexibility of the calmodulin central helix is key to its function. Journal of Inorganic Biochemistry. 51: 56. DOI: 10.1016/0162-0134(93)85092-M |
0.428 |
|
| 1993 |
Vuister GW, Bax A. Measurement of Two- and Three-Bond Proton to Methyl-Carbon J Couplings in Proteins Uniformly Enriched with 13C Journal of Magnetic Resonance, Series B. 102: 228-231. DOI: 10.1006/jmrb.1993.1089 |
0.426 |
|
| 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 |
0.8 |
|
| 1993 |
Vuister GW, Clore GM, Gronenborn AM, Powers R, Garrett DS, Tschudin R, Bax A. Increased Resolution and Improved Spectral Quality in Four-Dimensional 13C/13C-Separated HMQC-NOESY-HMQC Spectra Using Pulsed Field Gradients Journal of Magnetic Resonance, Series B. 101: 210-213. DOI: 10.1006/Jmrb.1993.1035 |
0.47 |
|
| 1993 |
Vuister GW, Wang AC, Bax A. Measurement of three-bond nitrogen-carbon J couplings in proteins uniformly enriched in15N and13C Journal of the American Chemical Society. 115: 5334-5335. |
0.407 |
|
| 1993 |
Vuister GW, Bax A. Quantitative J correlation: A new approach for measuring homonuclear three-bond J(HNHα) coupling constants in 15N-enriched proteins Journal of the American Chemical Society. 115: 7772-7777. |
0.428 |
|
| 1992 |
Vuister GW, Bax A. Measurement of two-bond JCOH alpha coupling constants in proteins uniformly enriched with 13C. Journal of Biomolecular Nmr. 2: 401-5. PMID 1511238 DOI: 10.1007/BF01874818 |
0.485 |
|
| 1992 |
de Waard P, Leeflang BR, Vliegenthart JF, Boelens R, Vuister GW, Kaptein R. Application of 2D and 3D NMR experiments to the conformational study of a diantennary oligosaccharide. Journal of Biomolecular Nmr. 2: 211-26. PMID 1392566 DOI: 10.1007/Bf01875317 |
0.754 |
|
| 1992 |
Vuister GW, Delaglio F, Bax A. An empirical correlation between 1JC.alpha.H.alpha. and protein backbone conformation Journal of the American Chemical Society. 114: 9674-9675. DOI: 10.1021/JA00050A066 |
0.478 |
|
| 1992 |
Vuister GW, Ruff-Cabello J, van Zijl PCM. Gradient-enhanced multiple-quantum filter (ge-MQF). A simple way to obtain single-scan phase-sensitive HMQC spectra Journal of Magnetic Resonance (1969). 100: 215-220. DOI: 10.1016/0022-2364(92)90381-G |
0.374 |
|
| 1992 |
Moonen CTW, Van Gelderen P, Vuister GW, Van Zijl PCM. Gradient-enhanced exchange spectroscopy Journal of Magnetic Resonance (1969). 97: 419-425. DOI: 10.1016/0022-2364(92)90327-4 |
0.309 |
|
| 1992 |
Vuister GW, Bax A. Resolution enhancement and spectral editing of uniformly 13C-enriched proteins by homonuclear broadband 13C decoupling Journal of Magnetic Resonance (1969). 98: 428-435. DOI: 10.1016/0022-2364(92)90144-V |
0.475 |
|
| 1992 |
Vuister GW, Boelens R, Kaptein R, Burgering M, van Zijl PCM. Gradient-enhanced 3D NOESY-HMQC spectroscopy Journal of Biomolecular Nmr. 2: 301-305. DOI: 10.1007/Bf01875323 |
0.731 |
|
| 1991 |
Vuister GW, Boelens R, Padilla A, Kaptein R. Statistical analysis of double NOE transfer pathways in proteins as measured in 3D NOE-NOE spectroscopy. Journal of Biomolecular Nmr. 1: 421-38. PMID 1841709 DOI: 10.1007/Bf02192864 |
0.781 |
|
| 1991 |
Vuister GW, Boelens R, Kaptein R, Hurd RE, John B, Van Zijl PCM. Gradient-enhanced HMQC and HSQC spectroscopy. Applications to 15N-labeled Mnt repressor Journal of the American Chemical Society. 113: 9688-9690. DOI: 10.1021/Ja00025A053 |
0.714 |
|
| 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 |
0.809 |
|
| 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 |
0.8 |
|
| 1990 |
De Waard P, Boelens R, Vuister GW, Vliegenthart JFG. Structural studies by 1HX13C two-dimensional and three-dimensional HMQC-NOE at natural abundance on complex carbohydrates Journal of the American Chemical Society. 112: 3232-3234. DOI: 10.1021/Ja00164A066 |
0.585 |
|
| 1990 |
De Waard P, Boelens R, Vuister GW, Vliegenthart JFG. Structural studies by proton/carbon-13 two-dimensional and three-dimensional HMQC-NOE at natural abundance on complex carbohydrates Journal of the American Chemical Society. 112: 3232-3234. DOI: 10.1021/ja00164a066 |
0.594 |
|
| 1990 |
Breg JN, Boelens R, Vuister GW, Kaptein R. 3D NOE-NOE spectroscopy of proteins. Observation of sequential 3D NOE cross peaks in arc repressor Journal of Magnetic Resonance (1969). 87: 646-651. DOI: 10.1016/0022-2364(90)90324-3 |
0.766 |
|
| 1990 |
Padilla A, Vuister GW, Boelens R, Kleywegt GJ, Cavé A, Parello J, Kaptein R. Homonuclear three-dimensional 1H 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. |
0.32 |
|
| 1989 |
Boelens R, Vuister GW, Koning TMG, Kaptein R. Observation of spin diffusion in biomolecules by three-dimensional NOE-NOE spectroscopy Journal of the American Chemical Society®. 111: 8525-8526. DOI: 10.1021/Ja00204A039 |
0.715 |
|
| 1989 |
Vuister GW, De Waard P, Boelens R, Vliegenthart JFG, Kaptein R. The use of 3D NMR in structural studies of oligosaccharides Journal of the American Chemical Society. 111: 772-774. DOI: 10.1021/Ja00184A078 |
0.747 |
|
| 1989 |
Vuister GW, De Waard P, Boelens R, Vliegenthart JFG, Kaptein R. The use of three-dimensional NMR in structural studies of oligosaccharides Journal of the American Chemical Society. 111: 772-774. DOI: 10.1021/ja00184a078 |
0.74 |
|
| 1989 |
VUISTER GW, DE WAARD P, BOELENS R, VLIEGENTHART JFG, KAPTEIN R. ChemInform Abstract: The Use of 3D NMR in Structural Studies of Oligosaccharides Cheminform. 20. DOI: 10.1002/chin.198919060 |
0.752 |
|
| 1988 |
Endo T, Oya M, Kaptein R, Vuister GW, Kihara H, Mohri N, Tanaka S, Ohno M. Proton NMR resonance assignments and surface accessibility of tryptophan residues of a dimeric phospholipase A2 from Trimeresurus flavoviridis. Febs Letters. 230: 57-60. PMID 3350151 DOI: 10.1016/0014-5793(88)80641-0 |
0.632 |
|
| 1988 |
Vuister GW, Boelens R, Kaptein R. Nonselective three-dimensional nmr spectroscopy. The 3D NOE-HOHAHA experiment Journal of Magnetic Resonance (1969). 80: 176-185. DOI: 10.1016/0022-2364(88)90072-8 |
0.765 |
|
| 1988 |
Mayo KH, Schussheim A, Vuister GW, Boelens R, Kaptein R, Engelhard M, Hess B. Mobility and solvent exposure of aromatic residues in bacteriorhodopsin investigated by 1H-NMR and photo-CIDNP-NMR spectroscopy Febs Letters. 235: 163-168. DOI: 10.1016/0014-5793(88)81255-9 |
0.763 |
|
| 1987 |
Vuister GW, Boelens R. Three-dimensional J-resolved NMR spectroscopy Journal of Magnetic Resonance (1969). 73: 328-333. DOI: 10.1016/0022-2364(87)90205-8 |
0.673 |
|
| 1987 |
KEMMINK J, VUISTER GW, BOELENS R, DIJKSTRA K, KAPTEIN R. ChemInform Abstract: Nuclear Spin Coherence Transfer in Photochemical Reactions. Cheminform. 18. DOI: 10.1002/chin.198702055 |
0.682 |
|
| 1986 |
Kemmink J, Vuister GW, Boelens R, Dijkstra K, Kaptein R. Nuclear spin coherence transfer in photochemical reactions Journal of the American Chemical Society. 108: 5631-5633. DOI: 10.1021/Ja00278A048 |
0.733 |
|
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