| Year |
Citation |
Score |
| 2020 |
Lawrence C, Grishaev AV. Chemical shifts-based similarity restraints improve accuracy of RNA structures determined via NMR. Rna (New York, N.Y.). PMID 32917774 DOI: 10.1261/Rna.074617.119 |
0.379 |
|
| 2020 |
Xu X, Godoy-Ruiz R, Adipietro KA, Peralta C, Ben-Hail D, Varney KM, Cook ME, Roth BM, Wilder PT, Cleveland T, Grishaev A, Neu HM, Michel SLJ, Yu W, Beckett D, et al. Structure of the cell-binding component of the binary toxin reveals a di-heptamer macromolecular assembly. Proceedings of the National Academy of Sciences of the United States of America. PMID 31896582 DOI: 10.1073/Pnas.1919490117 |
0.354 |
|
| 2019 |
Bergonzo C, Grishaev A. Accuracy of MD solvent models in RNA structure refinement assessed via liquid-crystal NMR and spin relaxation data. Journal of Structural Biology. PMID 31279068 DOI: 10.1016/J.Jsb.2019.07.001 |
0.383 |
|
| 2019 |
Bergonzo C, Grishaev A. Maximizing accuracy of RNA structure in refinement against residual dipolar couplings. Journal of Biomolecular Nmr. PMID 31049778 DOI: 10.1007/S10858-019-00236-6 |
0.346 |
|
| 2018 |
Best RB, Zheng W, Borgia A, Buholzer K, Borgia MB, Hofmann H, Soranno A, Nettels D, Gast K, Grishaev A, Schuler B. Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water". Science (New York, N.Y.). 361. PMID 30166459 DOI: 10.1126/Science.Aar7101 |
0.323 |
|
| 2018 |
Lin X, Roy S, Jolly MK, Bocci F, Schafer NP, Tsai MY, Chen Y, He Y, Grishaev A, Weninger K, Orban J, Kulkarni P, Rangarajan G, Levine H, Onuchic JN. PAGE4 and Conformational Switching: Insights from Molecular Dynamics Simulations and Implications for Prostate Cancer. Journal of Molecular Biology. PMID 29758263 DOI: 10.1016/J.Jmb.2018.05.011 |
0.323 |
|
| 2018 |
Debnath S, Kosek D, Tagad HD, Durell SR, Appella DH, Acevedo R, Grishaev A, Dyda F, Appella E, Mazur SJ. A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity. The Journal of Biological Chemistry. PMID 29602904 DOI: 10.1074/Jbc.Ra117.001213 |
0.319 |
|
| 2017 |
Grishaev AV. Hybrid Applications of Solution Scattering to Aid Structural Biology. Advances in Experimental Medicine and Biology. 1009: 215-227. PMID 29218562 DOI: 10.1007/978-981-10-6038-0_13 |
0.373 |
|
| 2017 |
Shen Y, Roche J, Grishaev A, Bax A. Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins. Protein Science : a Publication of the Protein Society. PMID 28884933 DOI: 10.1002/Pro.3292 |
0.381 |
|
| 2017 |
Kulkarni P, Jolly MK, Jia D, Mooney SM, Bhargava A, Kagohara LT, Chen Y, Hao P, He Y, Veltri RW, Grishaev A, Weninger K, Levine H, Orban J. Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity. Proceedings of the National Academy of Sciences of the United States of America. PMID 28289210 DOI: 10.1073/Pnas.1700082114 |
0.325 |
|
| 2017 |
Zheng W, Borgia A, Grishaev A, Schuler B, Best RB. Resolving the Controversy between SAXS and FRET Measurements on Unfolded Proteins Biophysical Journal. 112: 3-5. DOI: 10.1016/J.Bpj.2016.11.1708 |
0.357 |
|
| 2016 |
Zheng W, Borgia A, Buholzer K, Grishaev A, Schuler B, Best RB. Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment. Journal of the American Chemical Society. PMID 27583687 DOI: 10.1021/Jacs.6B05443 |
0.355 |
|
| 2016 |
Borgia A, Zheng W, Buholzer K, Borgia MB, Schüler A, Hofmann H, Soranno A, Nettels D, Gast K, Grishaev A, Best RB, Schuler B. Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods. Journal of the American Chemical Society. PMID 27583570 DOI: 10.1021/Jacs.6B05917 |
0.372 |
|
| 2016 |
Deshmukh L, Schwieters CD, Grishaev A, Clore GM. Quantitative Characterization of Configurational Space Sampled by HIV-1 Nucleocapsid Using Solution NMR, X-ray Scattering and Protein Engineering. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 17: 1548-52. PMID 26946052 DOI: 10.1002/Cphc.201600212 |
0.393 |
|
| 2016 |
Deshmukh L, Schwieters CD, Grishaev A, Clore GM. Inside Back Cover: Quantitative Characterization of Configurational Space Sampled by HIV-1 Nucleocapsid Using Solution NMR, X-ray Scattering and Protein Engineering (ChemPhysChem 11/2016) Chemphyschem. 17: 1708-1708. DOI: 10.1002/Cphc.201600447 |
0.301 |
|
| 2015 |
Li F, Grishaev A, Ying J, Bax A. Side Chain Conformational Distributions of a Small Protein Derived from Model-Free Analysis of a Large Set of Residual Dipolar Couplings. Journal of the American Chemical Society. 137: 14798-811. PMID 26523828 DOI: 10.1021/Jacs.5B10072 |
0.399 |
|
| 2015 |
Venditti V, Schwieters CD, Grishaev A, Clore GM. Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering. Proceedings of the National Academy of Sciences of the United States of America. 112: 11565-70. PMID 26305976 DOI: 10.1073/Pnas.1515366112 |
0.39 |
|
| 2015 |
Gruschus JM, Jiang Z, Yap TL, Hill SA, Grishaev A, Piszczek G, Sidransky E, Lee JC. Dissociation of glucocerebrosidase dimer in solution by its co-factor, saposin C. Biochemical and Biophysical Research Communications. 457: 561-6. PMID 25600808 DOI: 10.1016/J.Bbrc.2015.01.024 |
0.309 |
|
| 2015 |
Lee JH, Li F, Grishaev A, Bax A. Quantitative residue-specific protein backbone torsion angle dynamics from concerted measurement of 3J couplings. Journal of the American Chemical Society. 137: 1432-5. PMID 25590347 DOI: 10.1021/Ja512593S |
0.35 |
|
| 2015 |
Venditti V, Tugarinov V, Schwieters CD, Grishaev A, Clore GM. Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I. Nature Communications. 6: 5960. PMID 25581904 DOI: 10.1038/Ncomms6960 |
0.388 |
|
| 2015 |
Li F, Lee JH, Grishaev A, Ying J, Bax A. High accuracy of Karplus equations for relating three-bond J couplings to protein backbone torsion angles. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 16: 572-8. PMID 25511552 DOI: 10.1002/Cphc.201402704 |
0.383 |
|
| 2015 |
Grishaev A, Li F, Ying J, Bax A. Sidechain chi1 distribution in B3 domain of protein G from extensive sets of residual dipolar couplings Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2N7J/Pdb |
0.307 |
|
| 2014 |
Maltsev AS, Grishaev A, Roche J, Zasloff M, Bax A. Improved cross validation of a static ubiquitin structure derived from high precision residual dipolar couplings measured in a drug-based liquid crystalline phase. Journal of the American Chemical Society. 136: 3752-5. PMID 24568736 DOI: 10.1021/Ja4132642 |
0.37 |
|
| 2014 |
Roche J, Louis JM, Grishaev A, Ying J, Bax A. Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion. Proceedings of the National Academy of Sciences of the United States of America. 111: 3425-30. PMID 24550514 DOI: 10.1073/Pnas.1401397111 |
0.315 |
|
| 2014 |
Roche J, Louis J, Grishaev A, Ying J, Bax A. Solution NMR structure of gp41 ectodomain monomer on a DPC micelle Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19750 |
0.336 |
|
| 2013 |
Deshmukh L, Schwieters CD, Grishaev A, Ghirlando R, Baber JL, Clore GM. Structure and dynamics of full-length HIV-1 capsid protein in solution. Journal of the American Chemical Society. 135: 16133-47. PMID 24066695 DOI: 10.1021/Ja406246Z |
0.399 |
|
| 2013 |
Ha JH, Eo Y, Grishaev A, Guo M, Smith JA, Sintim HO, Kim EH, Cheong HK, Bentley WE, Ryu KS. Crystal structures of the LsrR proteins complexed with phospho-AI-2 and two signal-interrupting analogues reveal distinct mechanisms for ligand recognition. Journal of the American Chemical Society. 135: 15526-35. PMID 24047255 DOI: 10.1021/Ja407068V |
0.355 |
|
| 2013 |
Lakomek NA, Kaufman JD, Stahl SJ, Louis JM, Grishaev A, Wingfield PT, Bax A. The Homotrimeric HIV-1 Viral Coat Protein GP41 is Highly Dynamic Biophysical Journal. 104: 384a. DOI: 10.1016/J.Bpj.2012.11.2138 |
0.372 |
|
| 2012 |
Grishaev A. Sample preparation, data collection, and preliminary data analysis in biomolecular solution X-ray scattering. Current Protocols in Protein Science. 70. PMID 23151743 DOI: 10.1002/0471140864.Ps1714S70 |
0.337 |
|
| 2012 |
Grishaev A, Anthis NJ, Clore GM. Contrast-matched small-angle X-ray scattering from a heavy-atom-labeled protein in structure determination: application to a lead-substituted calmodulin-peptide complex. Journal of the American Chemical Society. 134: 14686-9. PMID 22908850 DOI: 10.1021/Ja306359Z |
0.384 |
|
| 2012 |
Grishaev A, Ying J, Bax A. Imino hydrogen positions in nucleic acids from density functional theory validated by NMR residual dipolar couplings. Journal of the American Chemical Society. 134: 6956-9. PMID 22489834 DOI: 10.1021/Ja301775J |
0.336 |
|
| 2011 |
Ying J, Wang J, Grishaev A, Yu P, Wang YX, Bax A. Measurement of (1)H-(15)N and (1)H-(13)C residual dipolar couplings in nucleic acids from TROSY intensities. Journal of Biomolecular Nmr. 51: 89-103. PMID 21947918 DOI: 10.1007/S10858-011-9544-Y |
0.349 |
|
| 2011 |
Takayama Y, Schwieters CD, Grishaev A, Ghirlando R, Clore GM. Combined use of residual dipolar couplings and solution X-ray scattering to rapidly probe rigid-body conformational transitions in a non-phosphorylatable active-site mutant of the 128 kDa enzyme I dimer. Journal of the American Chemical Society. 133: 424-7. PMID 21162528 DOI: 10.1021/Ja109866W |
0.374 |
|
| 2011 |
Forbes JG, Wittebort RJ, Grishaev A, Tsai WL, Wang K. Elasticity of Intrinsically Disordered Nebulin Modules Biophysical Journal. 100: 61a. DOI: 10.1016/J.Bpj.2010.12.531 |
0.342 |
|
| 2010 |
Grishaev A, Guo L, Irving T, Bax A. Improved fitting of solution X-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling. Journal of the American Chemical Society. 132: 15484-6. PMID 20958032 DOI: 10.1021/Ja106173N |
0.387 |
|
| 2010 |
Schwieters CD, Suh JY, Grishaev A, Ghirlando R, Takayama Y, Clore GM. Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering. Journal of the American Chemical Society. 132: 13026-45. PMID 20731394 DOI: 10.1021/Ja105485B |
0.411 |
|
| 2010 |
Yao L, Grishaev A, Cornilescu G, Bax A. The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy. Journal of the American Chemical Society. 132: 10866-75. PMID 20681720 DOI: 10.1021/Ja103629E |
0.353 |
|
| 2010 |
Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. Structure/Function Implications in a Dynamic Complex of the Intrinsically Disordered Sic1 with the Cdc4 Subunit of an SCF Ubiquitin Ligase Structure. 18: 494-506. PMID 20399186 DOI: 10.1016/J.Str.2010.01.020 |
0.395 |
|
| 2010 |
Yao L, Grishaev A, Cornilescu G, Bax A. Site-specific backbone amide (15)N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements. Journal of the American Chemical Society. 132: 4295-309. PMID 20199098 DOI: 10.1021/Ja910186U |
0.362 |
|
| 2009 |
Battistel MD, Grishaev A, An SS, Castellino FJ, Llinás M. Solution structure and functional characterization of human plasminogen kringle 5. Biochemistry. 48: 10208-19. PMID 19821587 DOI: 10.1021/Bi901433N |
0.722 |
|
| 2009 |
Grishaev A, Yao L, Ying J, Pardi A, Bax A. Chemical shift anisotropy of imino 15N nuclei in Watson-Crick base pairs from magic angle spinning liquid crystal NMR and nuclear spin relaxation. Journal of the American Chemical Society. 131: 9490-1. PMID 19537719 DOI: 10.1021/Ja903244S |
0.346 |
|
| 2009 |
Ryabov Y, Suh JY, Grishaev A, Clore GM, Schwieters CD. Using the experimentally determined components of the overall rotational diffusion tensor to restrain molecular shape and size in NMR structure determination of globular proteins and protein-protein complexes. Journal of the American Chemical Society. 131: 9522-31. PMID 19537713 DOI: 10.1021/Ja902336C |
0.358 |
|
| 2008 |
Ozhogina OA, Grishaev A, Bominaar EL, Patthy L, Trexler M, Llinás M. NMR solution structure of the neurotrypsin Kringle domain. Biochemistry. 47: 12290-8. PMID 18956887 DOI: 10.1021/Bi800555Z |
0.605 |
|
| 2008 |
Grishaev A, Ying J, Canny MD, Pardi A, Bax A. Solution structure of tRNAVal from refinement of homology model against residual dipolar coupling and SAXS data. Journal of Biomolecular Nmr. 42: 99-109. PMID 18787959 DOI: 10.1007/S10858-008-9267-X |
0.432 |
|
| 2008 |
Comoletti D, Grishaev A, Whitten AE, Taylor P, Trewhella J. Characterization of the solution structure of a neuroligin/beta-neurexin complex. Chemico-Biological Interactions. 175: 150-5. PMID 18550038 DOI: 10.1016/J.Cbi.2008.04.040 |
0.364 |
|
| 2008 |
Parsons LM, Grishaev A, Bax A. The periplasmic domain of TolR from Haemophilus influenzae forms a dimer with a large hydrophobic groove: NMR solution structure and comparison to SAXS data. Biochemistry. 47: 3131-42. PMID 18269247 DOI: 10.1021/Bi702283X |
0.44 |
|
| 2008 |
Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A. Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. Journal of Biomolecular Nmr. 40: 95-106. PMID 18008171 DOI: 10.1007/S10858-007-9211-5 |
0.431 |
|
| 2007 |
Comoletti D, Grishaev A, Whitten AE, Tsigelny I, Taylor P, Trewhella J. Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering. Structure (London, England : 1993). 15: 693-705. PMID 17562316 DOI: 10.1016/J.Str.2007.04.010 |
0.384 |
|
| 2006 |
Ying J, Grishaev A, Bryce DL, Bax A. Chemical shift tensors of protonated base carbons in helical RNA and DNA from NMR relaxation and liquid crystal measurements. Journal of the American Chemical Society. 128: 11443-54. PMID 16939267 DOI: 10.1021/Ja061984G |
0.341 |
|
| 2006 |
Dam J, Baber J, Grishaev A, Malchiodi EL, Schuck P, Bax A, Mariuzza RA. Variable dimerization of the Ly49A natural killer cell receptor results in differential engagement of its MHC class I ligand. Journal of Molecular Biology. 362: 102-13. PMID 16899255 DOI: 10.1016/J.Jmb.2006.07.005 |
0.318 |
|
| 2006 |
Grishaev A, Ying J, Bax A. Pseudo-CSA restraints for NMR refinement of nucleic acid structure. Journal of the American Chemical Society. 128: 10010-1. PMID 16881619 DOI: 10.1021/Ja0633058 |
0.374 |
|
| 2006 |
Ying J, Grishaev A, Bax A. Carbon-13 chemical shift anisotropy in DNA bases from field dependence of solution NMR relaxation rates. Magnetic Resonance in Chemistry : Mrc. 44: 302-10. PMID 16477676 DOI: 10.1002/Mrc.1762 |
0.333 |
|
| 2005 |
Grishaev A, Wu J, Trewhella J, Bax A. Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data. Journal of the American Chemical Society. 127: 16621-8. PMID 16305251 DOI: 10.1021/Ja054342M |
0.438 |
|
| 2005 |
Bax A, Grishaev A. Weak alignment NMR: a hawk-eyed view of biomolecular structure. Current Opinion in Structural Biology. 15: 563-70. PMID 16140525 DOI: 10.1016/J.Sbi.2005.08.006 |
0.365 |
|
| 2005 |
Grishaev A, Steren CA, Wu B, Pineda-Lucena A, Arrowsmith C, Llinás M. ABACUS, a direct method for protein NMR structure computation via assembly of fragments. Proteins. 61: 36-43. PMID 16080153 DOI: 10.1002/Prot.20457 |
0.597 |
|
| 2005 |
Grishaev A, Llinás M. Protein structure elucidation from minimal NMR data: the CLOUDS approach. Methods in Enzymology. 394: 261-95. PMID 15808224 DOI: 10.1016/S0076-6879(05)94010-X |
0.593 |
|
| 2004 |
Grishaev A, Bax A. An empirical backbone-backbone hydrogen-bonding potential in proteins and its applications to NMR structure refinement and validation. Journal of the American Chemical Society. 126: 7281-92. PMID 15186165 DOI: 10.1021/Ja0319994 |
0.387 |
|
| 2004 |
Grishaev A, Llinás M. BACUS: A Bayesian protocol for the identification of protein NOESY spectra via unassigned spin systems. Journal of Biomolecular Nmr. 28: 1-10. PMID 14739635 DOI: 10.1023/B:Jnmr.0000012846.56763.F7 |
0.574 |
|
| 2002 |
Grishaev A, Llinás M. Sorting signals from protein NMR spectra: SPI, a Bayesian protocol for uncovering spin systems. Journal of Biomolecular Nmr. 24: 203-13. PMID 12522308 DOI: 10.1023/A:1021660608913 |
0.572 |
|
| 2002 |
Grishaev A, Llinas M. Protein structure elucidation from NMR proton densities. Proceedings of the National Academy of Sciences of the United States of America. 99: 6713-8. PMID 12011434 DOI: 10.1073/Pnas.042114399 |
0.561 |
|
| 2002 |
Grishaev A, Llinás M. CLOUDS, a protocol for deriving a molecular proton density via NMR. Proceedings of the National Academy of Sciences of the United States of America. 99: 6707-12. PMID 12011433 DOI: 10.1073/Pnas.082114199 |
0.613 |
|
| 1999 |
Briknarová K, Grishaev A, Bányai L, Tordai H, Patthy L, Llinás M. The second type II module from human matrix metalloproteinase 2: structure, function and dynamics. Structure (London, England : 1993). 7: 1235-45. PMID 10545322 DOI: 10.1016/S0969-2126(00)80057-X |
0.726 |
|
| 1999 |
Briknarova K, Grishaev A, Banyai L, Tordai H, Patthy L, Llinas M. The Second Type II Module From Human Matrix Metalloproteinase 2 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4510 |
0.688 |
|
| Show low-probability matches. |