Year |
Citation |
Score |
2021 |
Pustovalova Y, Delaglio F, Craft DL, Arthanari H, Bax A, Billeter M, Bostock MJ, Dashti H, Hansen DF, Hyberts SG, Johnson BA, Kazimierczuk K, Lu H, Maciejewski M, Miljenović TM, et al. NUScon: a community-driven platform for quantitative evaluation of nonuniform sampling in NMR. Magnetic Resonance (Gottingen, Germany). 2: 843-861. PMID 37905225 DOI: 10.5194/mr-2-843-2021 |
0.366 |
|
2021 |
Robertson AJ, Ying J, Bax A. Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis. Magnetic Resonance (Gottingen, Germany). 2: 129-138. PMID 37904772 DOI: 10.5194/mr-2-129-2021 |
0.302 |
|
2020 |
Bax A, Chiliveri SC, Louis JM. Concentration-dependent structural transition of the HIV-1 gp41 MPER peptide into α-helical trimers. Angewandte Chemie (International Ed. in English). PMID 32916024 DOI: 10.1002/anie.202008804 |
0.311 |
|
2020 |
Alderson TR, Ying J, Bax A, Benesch JLP, Baldwin AJ. Conditional disorder in small heat-shock proteins. Journal of Molecular Biology. PMID 32081587 DOI: 10.1016/J.Jmb.2020.02.003 |
0.337 |
|
2020 |
Barnes CA, Shen Y, Ying J, Bax A. Modulating the Stiffness of the Myosin VI Single α-Helical Domain. Biophysical Journal. PMID 32049057 DOI: 10.1016/J.Bpj.2020.01.003 |
0.337 |
|
2019 |
Bax A, Ramanujan V, Charlier C. Observation and kinetic characterization of transient Schiff base intermediates by CEST NMR. Angewandte Chemie (International Ed. in English). PMID 31449352 DOI: 10.1002/anie.201908416 |
0.341 |
|
2019 |
Barnes CA, Robertson AJ, Louis JM, Anfinrud P, Bax A. Observation of β-Amyloid Peptide Oligomerization by Pressure-Jump NMR Spectroscopy. Journal of the American Chemical Society. PMID 31432672 DOI: 10.1021/jacs.9b06970 |
0.308 |
|
2019 |
Ying J, Barnes CA, Louis JM, Bax A. Importance of time-ordered non-uniform sampling of multi-dimensional NMR spectra of Aβ peptide under aggregating conditions. Journal of Biomolecular Nmr. PMID 31407200 DOI: 10.1007/S10858-019-00235-7 |
0.318 |
|
2019 |
Barnes CA, Shen Y, Ying J, Takagi Y, Torchia DA, Sellers JR, Bax A. Remarkable rigidity of the single α-helical domain of myosin-VI revealed by NMR spectroscopy. Journal of the American Chemical Society. PMID 31117653 DOI: 10.1021/Jacs.9B03116 |
0.365 |
|
2019 |
Courtney JM, Charlier C, Bax A. Structural Characterization of a Ubiquitin Folding Intermediate by Pressure-Jump NMR Biophysical Journal. 116: 338a. DOI: 10.1016/J.BPJ.2018.11.1841 |
0.307 |
|
2018 |
Natarajan K, Jiang J, May NA, Mage MG, Boyd LF, McShan AC, Sgourakis NG, Bax A, Margulies DH. The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling. Frontiers in Immunology. 9: 1657. PMID 30065727 DOI: 10.3389/Fimmu.2018.01657 |
0.77 |
|
2018 |
Marchant J, Bax A, Summers MF. Accurate Measurement of Residual Dipolar Couplings in Large RNAs by Variable Flip Angle NMR. Journal of the American Chemical Society. PMID 29757635 DOI: 10.1021/Jacs.8B03298 |
0.662 |
|
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 |
0.365 |
|
2017 |
Natarajan K, McShan AC, Jiang J, Kumirov VK, Wang R, Zhao H, Schuck P, Tilahun ME, Boyd LF, Ying J, Bax A, Margulies DH, Sgourakis NG. An allosteric site in the T-cell receptor Cβ domain plays a critical signalling role. Nature Communications. 8: 15260. PMID 28508865 DOI: 10.1038/Ncomms15260 |
0.779 |
|
2016 |
Louis JM, Baber JL, Ghirlando R, Aniana A, Bax A, Roche J. Insights into the Conformation of the Membrane Proximal Regions Critical to the Trimerization of the HIV-1 gp41 Ectodomain Bound to Dodecyl Phosphocholine Micelles. Plos One. 11: e0160597. PMID 27513582 DOI: 10.1371/Journal.Pone.0160597 |
0.308 |
|
2016 |
Lee JH, Ying J, Bax A. Nuclear Magnetic Resonance Observation of α-Synuclein Membrane Interaction by Monitoring the Acetylation Reactivity of Its Lysine Side Chains. Biochemistry. 55: 4949-59. PMID 27455358 DOI: 10.1021/Acs.Biochem.6B00637 |
0.347 |
|
2016 |
Roche J, Ying J, Shen Y, Torchia DA, Bax A. ARTSY-J: Convenient and precise measurement of (3)JHNHα couplings in medium-size proteins from TROSY-HSQC spectra. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 268: 73-81. PMID 27179455 DOI: 10.1016/J.Jmr.2016.05.001 |
0.405 |
|
2016 |
Li J, Wang Y, Chen J, Liu Z, Bax A, Yao L. Observation of α-Helical Hydrogen-Bond Cooperativity in an Intact Protein. Journal of the American Chemical Society. 138: 1824-7. PMID 26853186 DOI: 10.1021/Jacs.5B13140 |
0.368 |
|
2016 |
Roche J, Shen Y, Lee JH, Ying J, Bax A. Monomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil. Biochemistry. 55: 762-75. PMID 26780756 DOI: 10.1021/Acs.Biochem.5B01259 |
0.309 |
|
2016 |
Roche J, Ying J, Bax A. Accurate measurement of (3)J(HNHα) couplings in small or disordered proteins from WATERGATE-optimized TROSY spectra. Journal of Biomolecular Nmr. 64: 1-7. PMID 26660434 DOI: 10.1007/S10858-015-0004-Y |
0.395 |
|
2016 |
Lee JH, Ying J, Bax A. Quantitative evaluation of positive ϕ angle propensity in flexible regions of proteins from three-bond J couplings. Physical Chemistry Chemical Physics : Pccp. 18: 5759-70. PMID 26415896 DOI: 10.1039/C5Cp04542H |
0.383 |
|
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 |
0.37 |
|
2015 |
Sgourakis NG, May NA, Boyd LF, Ying J, Bax A, Margulies DH. A Novel MHC-I Surface Targeted for Binding by the MCMV m06 Immunoevasin Revealed by Solution NMR. The Journal of Biological Chemistry. 290: 28857-68. PMID 26463211 DOI: 10.1074/Jbc.M115.689661 |
0.626 |
|
2015 |
Mantsyzov AB, Shen Y, Lee JH, Hummer G, Bax A. MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data. Journal of Biomolecular Nmr. 63: 85-95. PMID 26219516 DOI: 10.1007/S10858-015-9971-2 |
0.34 |
|
2015 |
Shen Y, Bax A. Homology modeling of larger proteins guided by chemical shifts. Nature Methods. 12: 747-50. PMID 26053889 DOI: 10.1038/Nmeth.3437 |
0.361 |
|
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 |
0.397 |
|
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 |
0.392 |
|
2015 |
Shen Y, Bax A. Protein structural information derived from NMR chemical shift with the neural network program TALOS-N. Methods in Molecular Biology (Clifton, N.J.). 1260: 17-32. PMID 25502373 DOI: 10.1007/978-1-4939-2239-0_2 |
0.388 |
|
2015 |
Roche J, Louis JM, Bax A. Conformation of inhibitor-free HIV-1 protease derived from NMR spectroscopy in a weakly oriented solution. Chembiochem : a European Journal of Chemical Biology. 16: 214-8. PMID 25470009 DOI: 10.1002/Cbic.201402585 |
0.318 |
|
2015 |
Roche J, Louis JM, Bax A. Solution Conformation of the Unbound HIV-1 Protease Derived from Residual Dipolar Couplings Measured at Ambient and High-Pressure Conditions Biophysical Journal. 108: 203a. DOI: 10.1016/J.Bpj.2014.11.1122 |
0.328 |
|
2014 |
Ying J, Li F, Lee JH, Bax A. ¹³Cα decoupling during direct observation of carbonyl resonances in solution NMR of isotopically enriched proteins. Journal of Biomolecular Nmr. 60: 15-21. PMID 25129622 DOI: 10.1007/S10858-014-9853-Z |
0.419 |
|
2014 |
Sgourakis NG, Natarajan K, Ying J, Vogeli B, Boyd LF, Margulies DH, Bax A. The structure of mouse cytomegalovirus m04 protein obtained from sparse NMR data reveals a conserved fold of the m02-m06 viral immune modulator family. Structure (London, England : 1993). 22: 1263-1273. PMID 25126960 DOI: 10.1016/J.Str.2014.05.018 |
0.609 |
|
2014 |
Mantsyzov AB, Maltsev AS, Ying J, Shen Y, Hummer G, Bax A. A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein. Protein Science : a Publication of the Protein Society. 23: 1275-90. PMID 24976112 DOI: 10.1002/Pro.2511 |
0.36 |
|
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 |
0.403 |
|
2014 |
Ying J, Roche J, Bax A. Homonuclear decoupling for enhancing resolution and sensitivity in NOE and RDC measurements of peptides and proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 97-102. PMID 24360766 DOI: 10.1016/J.Jmr.2013.11.006 |
0.438 |
|
2014 |
Lorieau JL, Louis JM, Schwieters CD, Bax A. Influenza Membrane Fusion as Viewed from the Structure and Dynamics of the Full-Length Hemagglutinin Fusion Domain Biophysical Journal. 106: 707a. DOI: 10.1016/j.bpj.2013.11.3925 |
0.713 |
|
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 |
0.625 |
|
2013 |
Roche J, Ying J, Maltsev AS, Bax A. Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of α-synuclein. Chembiochem : a European Journal of Chemical Biology. 14: 1754-61. PMID 23813793 DOI: 10.1002/Cbic.201300244 |
0.344 |
|
2013 |
Shen Y, Bax A. Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. Journal of Biomolecular Nmr. 56: 227-41. PMID 23728592 DOI: 10.1007/S10858-013-9741-Y |
0.324 |
|
2013 |
Lorieau JL, Maltsev AS, Louis JM, Bax A. Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles. Journal of Biomolecular Nmr. 55: 369-77. PMID 23508769 DOI: 10.1007/S10858-013-9720-3 |
0.714 |
|
2013 |
Lorieau JL, Louis JM, Bax A. The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics. Biopolymers. 99: 189-95. PMID 23015412 DOI: 10.1002/Bip.22102 |
0.71 |
|
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 |
0.359 |
|
2013 |
Maltsev A, Ying J, Shen Y, Bax A. Alpha-Synuclein, an Intrinsically Unstructured Protein. How Interesting Can It Be? Biophysical Journal. 104: 5a. DOI: 10.1016/J.Bpj.2012.11.051 |
0.39 |
|
2012 |
Lorieau JL, Louis JM, Schwieters CD, Bax A. pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR. Proceedings of the National Academy of Sciences of the United States of America. 109: 19994-9. PMID 23169643 DOI: 10.1073/Pnas.1213801109 |
0.693 |
|
2012 |
Maltsev AS, Ying J, Bax A. Deuterium isotope shifts for backbone ¹H, ¹⁵N and ¹³C nuclei in intrinsically disordered protein α-synuclein. Journal of Biomolecular Nmr. 54: 181-91. PMID 22960996 DOI: 10.1007/S10858-012-9666-X |
0.416 |
|
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, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/Nsmb.2371 |
0.744 |
|
2012 |
Maltsev AS, Ying J, Bax A. Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding properties. Biochemistry. 51: 5004-13. PMID 22694188 DOI: 10.1021/Bi300642H |
0.377 |
|
2012 |
Lakomek NA, Ying J, Bax A. Measurement of ¹⁵N relaxation rates in perdeuterated proteins by TROSY-based methods. Journal of Biomolecular Nmr. 53: 209-21. PMID 22689066 DOI: 10.1007/S10858-012-9626-5 |
0.316 |
|
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 |
0.316 |
|
2012 |
Shen Y, Bax A. Identification of helix capping and b-turn motifs from NMR chemical shifts. Journal of Biomolecular Nmr. 52: 211-32. PMID 22314702 DOI: 10.1007/S10858-012-9602-0 |
0.371 |
|
2012 |
Lorieau J, Louis J, Schwieters C, Bax A. Conformational ensemble for the G8A mutant of the influenza hemagglutinin fusion peptide Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr18617 |
0.688 |
|
2011 |
Kay LE, Ikura M, Tschudin R, Bax A. Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins. 1990. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 213: 423-41. PMID 22152361 DOI: 10.1016/J.Jmr.2011.09.004 |
0.547 |
|
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 |
0.41 |
|
2011 |
Bax A. Triple resonance three-dimensional protein NMR: before it became a black box. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 213: 442-5. PMID 21885307 DOI: 10.1016/j.jmr.2011.08.003 |
0.385 |
|
2011 |
Lorieau JL, Louis JM, Bax A. Whole-body rocking motion of a fusion peptide in lipid bilayers from size-dispersed 15N NMR relaxation. Journal of the American Chemical Society. 133: 14184-7. PMID 21848255 DOI: 10.1021/Ja2045309 |
0.7 |
|
2011 |
Trigo-Mouriño P, Navarro-Vázquez A, Ying J, Gil RR, Bax A. Structural discrimination in small molecules by accurate measurement of long-range proton-carbon NMR residual dipolar couplings. Angewandte Chemie (International Ed. in English). 50: 7576-80. PMID 21751308 DOI: 10.1002/Anie.201101739 |
0.356 |
|
2011 |
Sgourakis NG, Lange OF, DiMaio F, André I, Fitzkee NC, Rossi P, Montelione GT, Bax A, Baker D. Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings. Journal of the American Chemical Society. 133: 6288-98. PMID 21466200 DOI: 10.1021/Ja111318M |
0.696 |
|
2011 |
Lorieau JL, Louis JM, Bax A. Helical hairpin structure of influenza hemagglutinin fusion peptide stabilized by charge-dipole interactions between the N-terminal amino group and the second helix. Journal of the American Chemical Society. 133: 2824-7. PMID 21319795 DOI: 10.1021/Ja1099775 |
0.739 |
|
2011 |
Fitzkee NC, Torchia DA, Bax A. Measuring rapid hydrogen exchange in the homodimeric 36 kDa HIV-1 integrase catalytic core domain. Protein Science : a Publication of the Protein Society. 20: 500-12. PMID 21213249 DOI: 10.1002/Pro.582 |
0.373 |
|
2010 |
Fitzkee NC, Bax A. Facile measurement of ¹H-¹5N residual dipolar couplings in larger perdeuterated proteins. Journal of Biomolecular Nmr. 48: 65-70. PMID 20694505 DOI: 10.1007/s10858-010-9441-9 |
0.361 |
|
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 |
0.691 |
|
2010 |
Shen Y, Bax A. SPARTA+: a modest improvement in empirical NMR chemical shift prediction by means of an artificial neural network. Journal of Biomolecular Nmr. 48: 13-22. PMID 20628786 DOI: 10.1007/S10858-010-9433-9 |
0.367 |
|
2010 |
Tolbert BS, Miyazaki Y, Barton S, Kinde B, Starck P, Singh R, Bax A, Case DA, Summers MF. Major groove width variations in RNA structures determined by NMR and impact of 13C residual chemical shift anisotropy and 1H-13C residual dipolar coupling on refinement. Journal of Biomolecular Nmr. 47: 205-19. PMID 20549304 DOI: 10.1007/S10858-010-9424-X |
0.713 |
|
2010 |
Lorieau JL, Louis JM, Bax A. The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface. Proceedings of the National Academy of Sciences of the United States of America. 107: 11341-6. PMID 20534508 DOI: 10.1073/Pnas.1006142107 |
0.736 |
|
2010 |
Fitzkee NC, Masse JE, Shen Y, Davies DR, Bax A. Solution conformation and dynamics of the HIV-1 integrase core domain. The Journal of Biological Chemistry. 285: 18072-84. PMID 20363759 DOI: 10.1074/Jbc.M110.113407 |
0.342 |
|
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 |
0.688 |
|
2010 |
Shen Y, Bax A. Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts. Journal of Biomolecular Nmr. 46: 199-204. PMID 20041279 DOI: 10.1007/S10858-009-9395-Y |
0.359 |
|
2010 |
Shen Y, Bryan PN, He Y, Orban J, Baker D, Bax A. De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds. Protein Science : a Publication of the Protein Society. 19: 349-56. PMID 19998407 DOI: 10.1002/Pro.303 |
0.467 |
|
2010 |
Tolbert B, Summers M, Miyazaki Y, Barton S, Kinde B, Stark P, Singh R, Bax A, Case D. RDC and RCSA refinement of an A-form RNA: Improvements in Major Groove Width Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Kyd/Pdb |
0.619 |
|
2010 |
Lorieau J, Louis J, Bax A. The hemagglutinin fusion peptide (H1 subtype) at pH 7.4 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16907 |
0.695 |
|
2009 |
Shen Y, Delaglio F, Cornilescu G, Bax A. TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. Journal of Biomolecular Nmr. 44: 213-23. PMID 19548092 DOI: 10.1007/S10858-009-9333-Z |
0.67 |
|
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 |
0.38 |
|
2009 |
Yao L, Ying J, Bax A. Improved accuracy of 15N-1H scalar and residual dipolar couplings from gradient-enhanced IPAP-HSQC experiments on protonated proteins. Journal of Biomolecular Nmr. 43: 161-70. PMID 19205898 DOI: 10.1007/S10858-009-9299-X |
0.388 |
|
2009 |
Shen Y, Vernon R, Baker D, Bax A. De novo protein structure generation from incomplete chemical shift assignments. Journal of Biomolecular Nmr. 43: 63-78. PMID 19034676 DOI: 10.1007/S10858-008-9288-5 |
0.48 |
|
2008 |
Yao L, Vögeli B, Ying J, Bax A. NMR determination of amide N-H equilibrium bond length from concerted dipolar coupling measurements. Journal of the American Chemical Society. 130: 16518-20. PMID 19049453 DOI: 10.1021/Ja805654F |
0.351 |
|
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 |
0.368 |
|
2008 |
Lorieau J, Yao L, Bax A. Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins. Journal of the American Chemical Society. 130: 7536-7. PMID 18498162 DOI: 10.1021/Ja801729F |
0.727 |
|
2008 |
Vögeli B, Yao L, Bax A. Protein backbone motions viewed by intraresidue and sequential HN-Halpha residual dipolar couplings. Journal of Biomolecular Nmr. 41: 17-28. PMID 18458825 DOI: 10.1007/S10858-008-9237-3 |
0.414 |
|
2008 |
Yao L, Vögeli B, Torchia DA, Bax A. Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis. The Journal of Physical Chemistry. B. 112: 6045-56. PMID 18358021 DOI: 10.1021/Jp0772124 |
0.412 |
|
2008 |
Shen Y, Lange O, Delaglio F, Rossi P, Aramini JM, Liu G, Eletsky A, Wu Y, Singarapu KK, Lemak A, Ignatchenko A, Arrowsmith CH, Szyperski T, Montelione GT, Baker D, Bax A, et al. Consistent blind protein structure generation from NMR chemical shift data. Proceedings of the National Academy of Sciences of the United States of America. 105: 4685-90. PMID 18326625 DOI: 10.1073/Pnas.0800256105 |
0.51 |
|
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 |
0.375 |
|
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 |
0.541 |
|
2007 |
Yao L, Bax A. Modulating protein alignment in a liquid-crystalline medium through conservative mutagenesis. Journal of the American Chemical Society. 129: 11326-7. PMID 17718572 DOI: 10.1021/Ja073937+ |
0.366 |
|
2007 |
Ying J, Grishaev A, Latham MP, Pardi A, Bax A. Magnetic field induced residual dipolar couplings of imino groups in nucleic acids from measurements at a single magnetic field. Journal of Biomolecular Nmr. 39: 91-6. PMID 17680332 DOI: 10.1007/S10858-007-9181-7 |
0.715 |
|
2007 |
Shen Y, Bax A. Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology. Journal of Biomolecular Nmr. 38: 289-302. PMID 17610132 DOI: 10.1007/S10858-007-9166-6 |
0.405 |
|
2007 |
Vögeli B, Ying J, Grishaev A, Bax A. Limits on variations in protein backbone dynamics from precise measurements of scalar couplings. Journal of the American Chemical Society. 129: 9377-85. PMID 17608477 DOI: 10.1021/Ja070324O |
0.421 |
|
2007 |
Ying J, Chill JH, Louis JM, Bax A. Mixed-time parallel evolution in multiple quantum NMR experiments: sensitivity and resolution enhancement in heteronuclear NMR. Journal of Biomolecular Nmr. 37: 195-204. PMID 17245527 DOI: 10.1007/S10858-006-9120-Z |
0.396 |
|
2007 |
Bax A, Torchia DA. Structural biology: molecular machinery in action. Nature. 445: 609. PMID 17237759 DOI: 10.1038/Nature05566 |
0.309 |
|
2006 |
Chill JH, Louis JM, Baber JL, Bax A. Measurement of 15N relaxation in the detergent-solubilized tetrameric KcsA potassium channel. Journal of Biomolecular Nmr. 36: 123-36. PMID 17013683 DOI: 10.1007/s10858-006-9071-4 |
0.35 |
|
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 |
0.612 |
|
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 |
0.415 |
|
2006 |
Ying J, Bax A. 2'-hydroxyl proton positions in helical RNA from simultaneously measured heteronuclear scalar couplings and NOEs. Journal of the American Chemical Society. 128: 8372-3. PMID 16802782 DOI: 10.1021/Ja0606226 |
0.318 |
|
2006 |
Chill JH, Louis JM, Miller C, Bax A. NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Science : a Publication of the Protein Society. 15: 684-98. PMID 16522799 DOI: 10.1110/Ps.051954706 |
0.359 |
|
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 |
0.394 |
|
2005 |
Jaroniec CP, Kaufman JD, Stahl SJ, Viard M, Blumenthal R, Wingfield PT, Bax A. Structure and dynamics of micelle-associated human immunodeficiency virus gp41 fusion domain. Biochemistry. 44: 16167-80. PMID 16331977 DOI: 10.1021/Bi051672A |
0.676 |
|
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 |
0.359 |
|
2005 |
Wu Z, Delaglio F, Wyatt K, Wistow G, Bax A. Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR. Protein Science : a Publication of the Protein Society. 14: 3101-14. PMID 16260758 DOI: 10.1110/Ps.051635205 |
0.653 |
|
2005 |
Maderia M, Wu J, Bax A, Shenoy S, O'Keefe B, Marquez VE, Barchi JJ. Engineering DNA topology with locked nucleosides: a structural study. Nucleosides, Nucleotides & Nucleic Acids. 24: 687-90. PMID 16248015 DOI: 10.1081/Ncn-200060256 |
0.342 |
|
2005 |
Ulmer TS, Bax A. Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants. The Journal of Biological Chemistry. 280: 43179-87. PMID 16166095 DOI: 10.1074/jbc.M507624200 |
0.322 |
|
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 |
0.352 |
|
2005 |
Bryce DL, Grishaev A, Bax A. Measurement of ribose carbon chemical shift tensors for A-form RNA by liquid crystal NMR spectroscopy. Journal of the American Chemical Society. 127: 7387-96. PMID 15898787 DOI: 10.1021/Ja051039C |
0.629 |
|
2005 |
Jaroniec CP, Boisbouvier J, Tworowska I, Nikonowicz EP, Bax A. Accurate measurement of 15N-13C residual dipolar couplings in nucleic acids. Journal of Biomolecular Nmr. 31: 231-41. PMID 15803396 DOI: 10.1007/S10858-005-0646-2 |
0.685 |
|
2005 |
Miclet E, Boisbouvier J, Bax A. Measurement of eight scalar and dipolar couplings for methine-methylene pairs in proteins and nucleic acids. Journal of Biomolecular Nmr. 31: 201-16. PMID 15803394 DOI: 10.1007/s10858-005-0175-z |
0.407 |
|
2005 |
Wu Z, Maderia M, Barchi JJ, Marquez VE, Bax A. Changes in DNA bending induced by restricting nucleotide ring pucker studied by weak alignment NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 102: 24-8. PMID 15618396 DOI: 10.1073/Pnas.0408498102 |
0.657 |
|
2005 |
Ulmer TS, Bax A, Cole NB, Nussbaum RL. Structure and dynamics of micelle-bound human alpha-synuclein. The Journal of Biological Chemistry. 280: 9595-603. PMID 15615727 DOI: 10.1074/jbc.M411805200 |
0.314 |
|
2004 |
Bryce DL, Bax A. Erratum: Application of correlated residual dipolar couplings to the determination of the molecular alignment tensor magnitude of oriented proteins and nucleic acids. Journal of Biomolecular Nmr. 29: 219. PMID 20859787 DOI: 10.1023/B:Jnmr.0000019275.08261.18 |
0.631 |
|
2004 |
Boisbouvier J, Bryce DL, O'neil-Cabello E, Nikonowicz EP, Bax A. Resolution-optimized NMR measurement of (1)D(CH), (1)D(CC) and (2)D(CH) residual dipolar couplings in nucleic acid bases. Journal of Biomolecular Nmr. 30: 287-301. PMID 15756460 DOI: 10.1007/S10858-005-1846-5 |
0.563 |
|
2004 |
Jaroniec CP, Ulmer TS, Bax A. Quantitative J correlation methods for the accurate measurement of 13C'-13Calpha dipolar couplings in proteins. Journal of Biomolecular Nmr. 30: 181-94. PMID 15666562 DOI: 10.1023/B:Jnmr.0000048946.71249.2F |
0.659 |
|
2004 |
O'Neil-Cabello E, Wu Z, Bryce DL, Nikonowicz EP, Bax A. Enhanced spectral resolution in RNA HCP spectra for measurement of (3)J(C2'P) and (3)J(C4'P) couplings and (31)P chemical shift changes upon weak alignment. Journal of Biomolecular Nmr. 30: 61-70. PMID 15452435 DOI: 10.1023/B:Jnmr.0000042952.66982.38 |
0.738 |
|
2004 |
Bryce DL, Boisbouvier J, Bax A. Experimental and theoretical determination of nucleic acid magnetic susceptibility: importance for the study of dynamics by field-induced residual dipolar couplings. Journal of the American Chemical Society. 126: 10820-1. PMID 15339148 DOI: 10.1021/Ja047179O |
0.577 |
|
2004 |
Miclet E, Williams Jr DC, Clore GM, Bryce DL, Boisbouvier J, Bax A. Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic acids. Journal of the American Chemical Society. 126: 10560-70. PMID 15327312 DOI: 10.1021/Ja047904V |
0.633 |
|
2004 |
Chou JJ, Baber JL, Bax A. Characterization of phospholipid mixed micelles by translational diffusion. Journal of Biomolecular Nmr. 29: 299-308. PMID 15213428 DOI: 10.1023/B:JNMR.0000032560.43738.6a |
0.56 |
|
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 |
0.336 |
|
2004 |
Lukin JA, Kontaxis G, Simplaceanu V, Yuan Y, Bax A, Ho C. Backbone resonance assignments of human adult hemoglobin in the carbonmonoxy form. Journal of Biomolecular Nmr. 28: 203-4. PMID 14755170 DOI: 10.1023/B:Jnmr.0000013816.64039.6F |
0.349 |
|
2004 |
Bryce DL, Bax A. Application of correlated residual dipolar couplings to the determination of the molecular alignment tensor magnitude of oriented proteins and nucleic acids. Journal of Biomolecular Nmr. 28: 273-87. PMID 14752260 DOI: 10.1023/B:JNMR.0000013701.16162.0c |
0.592 |
|
2004 |
O'Neil-Cabello E, Bryce DL, Nikonowicz EP, Bax A. Measurement of five dipolar couplings from a single 3D NMR multiplet applied to the study of RNA dynamics. Journal of the American Chemical Society. 126: 66-7. PMID 14709062 DOI: 10.1021/Ja038314K |
0.616 |
|
2003 |
Ulmer TS, Ramirez BE, Delaglio F, Bax A. Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy. Journal of the American Chemical Society. 125: 9179-91. PMID 15369375 DOI: 10.1021/ja0350684 |
0.389 |
|
2003 |
Miclet E, O'Neil-Cabello E, Nikonowicz EP, Live D, Bax A. 1H-1H dipolar couplings provide a unique probe of RNA backbone structure. Journal of the American Chemical Society. 125: 15740-1. PMID 14677953 DOI: 10.1021/Ja0388212 |
0.415 |
|
2003 |
Boisbouvier J, Delaglio F, Bax A. Direct observation of dipolar couplings between distant protons in weakly aligned nucleic acids. Proceedings of the National Academy of Sciences of the United States of America. 100: 11333-8. PMID 12972645 DOI: 10.1073/pnas.1534664100 |
0.358 |
|
2003 |
Boisbouvier J, Wu Z, Ono A, Kainosho M, Bax A. Rotational diffusion tensor of nucleic acids from 13C NMR relaxation. Journal of Biomolecular Nmr. 27: 133-42. PMID 12913409 DOI: 10.1023/A:1024931619957 |
0.644 |
|
2003 |
Chou JJ, Case DA, Bax A. Insights into the mobility of methyl-bearing side chains in proteins from (3)J(CC) and (3)J(CN) couplings. Journal of the American Chemical Society. 125: 8959-66. PMID 12862493 DOI: 10.1021/Ja029972S |
0.638 |
|
2003 |
Wu Z, Delaglio F, Tjandra N, Zhurkin VB, Bax A. Overall structure and sugar dynamics of a DNA dodecamer from homo- and heteronuclear dipolar couplings and 31P chemical shift anisotropy. Journal of Biomolecular Nmr. 26: 297-315. PMID 12815257 DOI: 10.1023/A:1024047103398 |
0.684 |
|
2002 |
Boisbouvier J, Bax A. Long-range magnetization transfer between uncoupled nuclei by dipole-dipole cross-correlated relaxation: a precise probe of beta-sheet geometry in proteins. Journal of the American Chemical Society. 124: 11038-45. PMID 12224951 DOI: 10.1021/Ja020511G |
0.389 |
|
2002 |
Koenig BW, Kontaxis G, Mitchell DC, Louis JM, Litman BJ, Bax A. Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings. Journal of Molecular Biology. 322: 441-61. PMID 12217702 DOI: 10.1016/S0022-2836(02)00745-3 |
0.402 |
|
2002 |
Wu Z, Bax A. Measurement of long-range 1H-1H dipolar couplings in weakly aligned proteins. Journal of the American Chemical Society. 124: 9672-3. PMID 12175202 DOI: 10.1021/Ja026845N |
0.661 |
|
2002 |
Zweckstetter M, Bax A. Evaluation of uncertainty in alignment tensors obtained from dipolar couplings. Journal of Biomolecular Nmr. 23: 127-37. PMID 12153038 DOI: 10.1023/A:1016316415261 |
0.337 |
|
2002 |
Chou JJ, Kaufman JD, Stahl SJ, Wingfield PT, Bax A. Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel. Journal of the American Chemical Society. 124: 2450-1. PMID 11890789 DOI: 10.1021/Ja017875D |
0.622 |
|
2001 |
Chou JJ, Gaemers S, Howder B, Louis JM, Bax A. A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles. Journal of Biomolecular Nmr. 21: 377-82. PMID 11824758 DOI: 10.1023/A:1013336502594 |
0.586 |
|
2001 |
Chou JJ, Li S, Klee CB, Bax A. Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains. Nature Structural Biology. 8: 990-7. PMID 11685248 DOI: 10.1038/nsb1101-990 |
0.58 |
|
2001 |
Wu Z, Bax A. Measurement of homonuclear proton couplings based on cross-peak nulling in CT-COSY. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 151: 242-52. PMID 11531346 DOI: 10.1006/Jmre.2001.2358 |
0.647 |
|
2001 |
Wu Z, Tjandra N, Bax A. 31P chemical shift anisotropy as an aid in determining nucleic acid structure in liquid crystals. Journal of the American Chemical Society. 123: 3617-8. PMID 11472143 DOI: 10.1021/Ja015650X |
0.604 |
|
2001 |
Bax A, Kontaxis G, Tjandra N. Dipolar couplings in macromolecular structure determination Methods in Enzymology. 339: 127-174. PMID 11462810 DOI: 10.1016/S0076-6879(01)39313-8 |
0.315 |
|
2001 |
Chou JJ, Bax A. Protein side-chain rotamers from dipolar couplings in a liquid crystalline phase. Journal of the American Chemical Society. 123: 3844-5. PMID 11457127 DOI: 10.1021/Ja015660Y |
0.522 |
|
2001 |
Kontaxis G, Bax A. Multiplet component separation for measurement of methyl 13C-1H dipolar couplings in weakly aligned proteins. Journal of Biomolecular Nmr. 20: 77-82. PMID 11430758 DOI: 10.1023/A:1011280529850 |
0.379 |
|
2001 |
Wu Z, Tjandra N, Bax A. Measurement of 1H3'-31P dipolar couplings in a DNA oligonucleotide by constant-time NOESY difference spectroscopy. Journal of Biomolecular Nmr. 19: 367-70. PMID 11370783 DOI: 10.1023/A:1011292803363 |
0.664 |
|
2001 |
Wu Z, Ono A, Kainosho M, Bax A. H...N hydrogen bond lengths in double stranded DNA from internucleotide dipolar couplings. Journal of Biomolecular Nmr. 19: 361-5. PMID 11370782 DOI: 10.1023/A:1011250219293 |
0.65 |
|
2001 |
Delaglio F, Wu Z, Bax A. Measurement of homonuclear proton couplings from regular 2D COSY spectra. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 149: 276-81. PMID 11318630 DOI: 10.1006/Jmre.2001.2297 |
0.654 |
|
2001 |
Ramirez BE, Voloshin ON, Camerini-Otero RD, Bax A. Solution structure of DinI provides insight into its mode of RecA inactivation. Protein Science : a Publication of the Protein Society. 9: 2161-9. PMID 11152126 DOI: 10.1110/PS.9.11.2161 |
0.339 |
|
2001 |
Wüthrich K, Bax A, Billeter M, Kaptein R, Palmer AG, Sykes BD, Wagner G. Letter from the Editor-in-Chief Journal of Biomolecular Nmr. 19: 1. DOI: 10.1023/A:1008382926453 |
0.324 |
|
2000 |
Chou JJ, Li S, Bax A. Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings. Journal of Biomolecular Nmr. 18: 217-27. PMID 11142512 DOI: 10.1023/A:1026563923774 |
0.589 |
|
2000 |
Chou JJ, Delaglio F, Bax A. Measurement of one-bond 15N-13C' dipolar couplings in medium sized proteins. Journal of Biomolecular Nmr. 18: 101-5. PMID 11101214 DOI: 10.1023/A:1008358318863 |
0.609 |
|
2000 |
Koenig BW, Mitchell DC, König S, Grzesiek S, Litman BJ, Bax A. Measurement of dipolar couplings in a transducin peptide fragment weakly bound to oriented photo-activated rhodopsin Journal of Biomolecular Nmr. 16: 121-125. PMID 10723991 DOI: 10.1023/A:1008378523816 |
0.362 |
|
2000 |
Kontaxis G, Clore GM, Bax A. Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 143: 184-96. PMID 10698659 DOI: 10.1006/JMRE.1999.1979 |
0.383 |
|
2000 |
Delaglio F, Kontaxis G, Bax A. Protein Structure Determination Using Molecular Fragment Replacement and NMR Dipolar Couplings Journal of the American Chemical Society. 122: 2142-2143. DOI: 10.1021/JA993603N |
0.381 |
|
2000 |
Cornilescu G, Bax A. Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase Journal of the American Chemical Society. 122: 10143-10154. DOI: 10.1021/ja0016194 |
0.698 |
|
2000 |
Tjandra N, Tate SI, Ono A, Kainosho M, Bax A. The NMR structure of a DNA dodecamer in an aqueous dilute liquid crystalline phase Journal of the American Chemical Society. 122: 6190-6200. DOI: 10.1021/Ja000324N |
0.432 |
|
2000 |
Zweckstetter M, Bax A. Prediction of Sterically Induced Alignment in a Dilute Liquid Crystalline Phase: Aid to Protein Structure Determination by NMR Journal of the American Chemical Society. 122: 3791-3792. DOI: 10.1021/JA0000908 |
0.323 |
|
1999 |
Cordier F, Rogowski M, Grzesiek S, Bax A. Observation of through-hydrogen-bond 2hJHC' in a perdeuterated protein. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 140: 510-2. PMID 10497060 DOI: 10.1006/JMRE.1999.1899 |
0.327 |
|
1999 |
Wang YX, Jacob J, Cordier F, Wingfield P, Stahl SJ, Lee-Huang S, Torchia D, Grzesiek S, Bax A. Measurement of (3h)J(NC') connectivities across hydrogen bonds in a 30 kDa protein Journal of Biomolecular Nmr. 14: 181-184. PMID 10427744 DOI: 10.1023/A:1008346517302 |
0.394 |
|
1999 |
Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. Journal of Biomolecular Nmr. 13: 289-302. PMID 10212987 DOI: 10.1023/A:1008392405740 |
0.686 |
|
1999 |
Ottiger M, Bax A. Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values. Journal of Biomolecular Nmr. 13: 187-91. PMID 10070759 DOI: 10.1023/A:1008395916985 |
0.349 |
|
1999 |
Ottiger M, Bax A. Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules. Journal of Biomolecular Nmr. 12: 361-72. PMID 9835045 DOI: 10.1023/A:1008366116644 |
0.35 |
|
1999 |
Cornilescu G, Marquardt JL, Ottiger M, Bax A. Ubiquitin Nmr Structure Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb1D3Z/Pdb |
0.671 |
|
1999 |
Cornilescu G, Ramirez BE, Frank MK, Clore GM, Gronenborn AM, Bax A. Correlation between (3h)J(NC')' and hydrogen bond length in proteins Journal of the American Chemical Society. 121: 6275-6279. DOI: 10.1021/Ja9909024 |
0.667 |
|
1999 |
Cornilescu G, Hu JS, Bax A. Identification of the hydrogen bonding network in a protein by scalar couplings Journal of the American Chemical Society. 121: 2949-2950. DOI: 10.1021/Ja9902221 |
0.629 |
|
1999 |
Koenig BW, Hu J, Ottiger M, Bose S, Hendler RW, Bax A. NMR Measurement of Dipolar Couplings in Proteins Aligned by Transient Binding to Purple Membrane Fragments Journal of the American Chemical Society. 121: 1385-1386. DOI: 10.1021/JA9837856 |
0.38 |
|
1998 |
Ottiger M, Delaglio F, Marquardt JL, Tjandra N, Bax A. Measurement of Dipolar Couplings for Methylene and Methyl Sites in Weakly Oriented Macromolecules and Their Use in Structure Determination Journal of Magnetic Resonance. 134: 365-369. PMID 9761712 DOI: 10.1006/Jmre.1998.1546 |
0.395 |
|
1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy. European Journal of Biochemistry / Febs. 256: 1-15. PMID 9746340 DOI: 10.1046/J.1432-1327.1998.2560001.X |
0.465 |
|
1998 |
Clore GM, Murphy EC, Gronenborn AM, Bax A. Determination of Three-Bond 1H3′-31P Couplings in Nucleic Acids and Protein-Nucleic Acid Complexes by Quantitative J Correlation Spectroscopy Journal of Magnetic Resonance. 134: 164-167. PMID 9740744 DOI: 10.1006/Jmre.1998.1513 |
0.356 |
|
1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy. Journal of Biomolecular Nmr. 12: 1-23. PMID 9729785 DOI: 10.1023/A:1008290618449 |
0.528 |
|
1998 |
Hu JS, Bax A. Measurement of three-bond, 13C'-13C beta J couplings in human ubiquitin by a triple resonance, E. COSY-type NMR technique. Journal of Biomolecular Nmr. 11: 199-203. PMID 9679294 DOI: 10.1023/A:1008241904271 |
0.335 |
|
1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids. Journal of Molecular Biology. 280: 933-52. PMID 9671561 DOI: 10.1006/Jmbi.1998.1852 |
0.459 |
|
1998 |
Bewley CA, Gustafson KR, Boyd MR, Covell DG, Bax A, Clore GM, Gronenborn AM. Solution structure of cyanovirin-N, a potent HIV-inactivating protein Nature Structural Biology. 5: 571-578. PMID 9665171 DOI: 10.1038/828 |
0.339 |
|
1998 |
Clore GM, Gronenborn AM, Bax A. A Robust Method for Determining the Magnitude of the Fully Asymmetric Alignment Tensor of Oriented Macromolecules in the Absence of Structural Information Journal of Magnetic Resonance. 133: 216-221. PMID 9654491 DOI: 10.1006/Jmre.1998.1419 |
0.392 |
|
1998 |
Ottiger M, Delaglio F, Bax A. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 131: 373-8. PMID 9571116 DOI: 10.1006/JMRE.1998.1361 |
0.379 |
|
1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids (IUPAC Recommendations 1998) Pure and Applied Chemistry. 70: 117-142. DOI: 10.1351/Pac199870010117 |
0.517 |
|
1998 |
Ottiger M, Bax A. Determination of Relative N−HN, N−C‘, Cα−C‘, and Cα−HαEffective Bond Lengths in a Protein by NMR in a Dilute Liquid Crystalline Phase Journal of the American Chemical Society. 120: 12334-12341. DOI: 10.1021/JA9826791 |
0.381 |
|
1998 |
Ramirez BE, Bax A. Modulation of the alignment tensor of macromolecules dissolved in a dilute liquid crystalline medium [19] Journal of the American Chemical Society. 120: 9106-9107. DOI: 10.1021/ja982310b |
0.394 |
|
1998 |
Cornilescu G, Marquardt JL, Ottiger M, Bax A. Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase Journal of the American Chemical Society. 120: 6836-6837. DOI: 10.1021/Ja9812610 |
0.648 |
|
1998 |
Wang YX, Marquardt JL, Wingfield P, Stahl SJ, Lee-Huang S, Torchia D, Bax A. Simultaneous measurement of 1H-15N, 1H-13C', and 15N-13C' dipolar couplings in a perdeuterated 30 kDa protein dissolved in a dilute liquid crystalline phase [20] Journal of the American Chemical Society. 120: 7385-7386. DOI: 10.1021/Ja980862O |
0.371 |
|
1997 |
Tjandra N, Bax A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium Science. 278: 1111-1114. PMID 9353189 DOI: 10.1126/Science.278.5340.1111 |
0.422 |
|
1997 |
Tjandra N, Omichinski JG, Gronenborn AM, Marius Clore G, Bax A. Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution Nature Structural Biology. 4: 732-738. PMID 9303001 DOI: 10.1038/Nsb0997-732 |
0.377 |
|
1997 |
Liwang AC, Bax A. Solution NMR characterization of hydrogen bonds in a protein by indirect measurement of deuterium quadrupole couplings. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 127: 54-64. PMID 9245630 DOI: 10.1006/Jmre.1997.1187 |
0.394 |
|
1997 |
Hu JS, Bax A. Chi 1 angle information from a simple two-dimensional NMR experiment that identifies trans 3JNC gamma couplings in isotopically enriched proteins. Journal of Biomolecular Nmr. 9: 323-8. PMID 9204558 DOI: 10.1023/A:1018691228238 |
0.412 |
|
1997 |
Grzesiek S, Bax A, Hu JS, Kaufman J, Palmer I, Stahl SJ, Tjandra N, Wingfield PT. Refined solution structure and backbone dynamics of HIV-1 Nef. Protein Science : a Publication of the Protein Society. 6: 1248-63. PMID 9194185 DOI: 10.1002/Pro.5560060613 |
0.383 |
|
1997 |
Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM. Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy Nature Structural Biology. 4: 443-449. PMID 9187651 DOI: 10.1038/Nsb0697-443 |
0.351 |
|
1997 |
Tjandra N, Bax A. Measurement of Dipolar Contributions to 1JCH Splittings from Magnetic-Field Dependence of J Modulation in Two-Dimensional NMR Spectra Journal of Magnetic Resonance. 124: 512-515. PMID 9169226 DOI: 10.1006/Jmre.1996.1088 |
0.41 |
|
1997 |
Grzesiek S, Bax A. A three-dimensional NMR experiment with improved sensitivity for carbonyl-carbonyl J correlation in proteins. Journal of Biomolecular Nmr. 9: 207-11. PMID 9090134 DOI: 10.1023/A:1018614505948 |
0.374 |
|
1997 |
Tjandra N, Bax A. Large variations in 13Cα chemical shift anisotropy in proteins correlate with secondary structure Journal of the American Chemical Society. 119: 9576-9577. DOI: 10.1021/Ja9721374 |
0.373 |
|
1997 |
Ottiger M, Tjandra N, Bax A. Magnetic field dependent amide 15N chemical shifts in a Protein-DNA complex resulting from magnetic ordering in solution Journal of the American Chemical Society. 119: 9825-9830. DOI: 10.1021/Ja971639E |
0.359 |
|
1997 |
Tjandra N, Bax A. Solution NMR measurement of amide proton chemical shift anisotropy in 15N-enriched proteins. Correlation with hydrogen bond length Journal of the American Chemical Society. 119: 8076-8082. DOI: 10.1021/Ja970876E |
0.388 |
|
1997 |
Ottiger M, Bax A. An Empirical Correlation between Amide Deuterium Isotope Effects on13CαChemical Shifts and Protein Backbone Conformation Journal of the American Chemical Society. 119: 8070-8075. DOI: 10.1021/JA9707466 |
0.36 |
|
1997 |
Hu J, Bax A. Determination of φ and χ1Angles in Proteins from13C−13C Three-BondJCouplings Measured by Three-Dimensional Heteronuclear NMR. How Planar Is the Peptide Bond? Journal of the American Chemical Society. 119: 6360-6368. DOI: 10.1021/JA970067V |
0.395 |
|
1997 |
Hu J, Grzesiek S, Bax A. Two-Dimensional NMR Methods for Determining χ1Angles of Aromatic Residues in Proteins from Three-BondJC‘CγandJNCγCouplings Journal of the American Chemical Society. 119: 1803-1804. DOI: 10.1021/JA963625Z |
0.371 |
|
1996 |
Tjandra N, Wingfield P, Stahl S, Bax A. Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation measurements at two magnetic fields Journal of Biomolecular Nmr. 8: 273-284. PMID 8953218 DOI: 10.1007/Bf00410326 |
0.341 |
|
1996 |
Grzesiek S, Bax A, Clore GM, Gronenborn AM, Hu JS, Kaufman J, Palmer I, Stahl SJ, Wingfield PT. The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nature Structural Biology. 3: 340-5. PMID 8599760 DOI: 10.1038/Nsb0496-340 |
0.312 |
|
1996 |
Grzesiek S, Bax A. Spin-locked multiple quantum coherence for signal enhancement in heteronuclear multidimensional NMR experiments. Journal of Biomolecular Nmr. 6: 335-9. PMID 8520225 DOI: 10.1007/BF00197815 |
0.377 |
|
1996 |
LiWang AC, Bax A. Equilibrium Protium/Deuterium Fractionation of Backbone Amides in U−13C/15N Labeled Human Ubiquitin by Triple Resonance NMR Journal of the American Chemical Society. 118: 12864-12865. DOI: 10.1021/Ja9630553 |
0.346 |
|
1996 |
Tjandra N, Szabo A, Bax A. Protein backbone dynamics and 15N chemical shift anisotropy from quantitative measurement of relaxation interference effects Journal of the American Chemical Society. 118: 6986-6991. DOI: 10.1021/Ja960510M |
0.383 |
|
1996 |
Tjandra N, Grzesiek S, Bax A. Magnetic field dependence of nitrogen-proton J splittings in 15N-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling Journal of the American Chemical Society. 118: 6264-6272. DOI: 10.1021/Ja960106N |
0.394 |
|
1996 |
Wang AC, Bax A. Determination of the Backbone Dihedral Angles φ in Human Ubiquitin from Reparametrized Empirical Karplus Equations Journal of the American Chemical Society. 118: 2483-2494. DOI: 10.1021/JA9535524 |
0.361 |
|
1996 |
Bax A. Learning modern protein NMR Structure. 4: 351-352. DOI: 10.1016/S0969-2126(96)00038-X |
0.43 |
|
1996 |
Bax A, Farley KA, Walker GS. Increased HMBC Sensitivity for Correlating Poorly Resolved Proton Multiplets to Carbon-13 Using Selective or Semi-selective Pulses Journal of Magnetic Resonance, Series A. 119: 134-138. DOI: 10.1006/JMRA.1996.0063 |
0.38 |
|
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 |
0.529 |
|
1995 |
Kuboniwa H, Grzesiek S, Delaglio F, Bax A. Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. Journal of Biomolecular Nmr. 4: 871-8. PMID 7812158 DOI: 10.1007/BF00398416 |
0.375 |
|
1995 |
Wang AC, Grzesiek S, Tschudin R, Lodi PJ, Bax A. Sequential backbone assignment of isotopically enriched proteins in D2O by deuterium-decoupled HA(CA)N and HA(CACO)N. Journal of Biomolecular Nmr. 5: 376-82. PMID 7647557 DOI: 10.1007/BF00182281 |
0.386 |
|
1995 |
Tjandra N, Kuboniwa H, Ren H, Bax A. Rotational Dynamics of Calcium‐Free Calmodulin Studied by 15N‐NMR Relaxation Measurements European Journal of Biochemistry. 230: 1014-1024. PMID 7601131 DOI: 10.1111/J.1432-1033.1995.1014G.X |
0.37 |
|
1995 |
Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. Solution structure of calcium-free calmodulin. Nature Structural Biology. 2: 768-76. PMID 7552748 DOI: 10.1038/Nsb0995-768 |
0.329 |
|
1995 |
Anglister J, Ren H, Klee CB, Bax A. NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide. Febs Letters. 375: 108-12. PMID 7498455 DOI: 10.1016/0014-5793(95)01192-H |
0.342 |
|
1995 |
Grzesiek S, Bax A. Audio-Frequency NMR in a Nutating Frame. Application to the Assignment of Phenylalanine Residues in Isotopically Enriched Proteins Journal of the American Chemical Society. 117: 6527-6531. DOI: 10.1021/JA00129A016 |
0.401 |
|
1995 |
Grzesiek S, Kuboniwa H, Hinck AP, Bax A. Multiple-Quantum Line Narrowing for Measurement of H.alpha.-H.beta. J Couplings in Isotopically Enriched Proteins Journal of the American Chemical Society. 117: 5312-5315. DOI: 10.1021/Ja00124A014 |
0.329 |
|
1995 |
Wang AC, Bax A. Reparametrization of the Karplus Relation for 3J(H.alpha.-N) and 3J(HN-C') in Peptides from Uniformly 13C/15N-Enriched Human Ubiquitin Journal of the American Chemical Society. 117: 1810-1813. DOI: 10.1021/JA00111A021 |
0.381 |
|
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 |
0.611 |
|
1994 |
Anglister J, Grzesiek S, Wang AC, Ren H, Klee CB, Bax A. 1H, 13C, 15N nuclear magnetic resonance backbone assignments and secondary structure of human calcineurin B. Biochemistry. 33: 3540-7. PMID 8142351 DOI: 10.1021/Bi00178A010 |
0.402 |
|
1994 |
Grzesiek S, Bax A. Measurement of amide proton exchange rates and NOEs with water in 13C/15N-enriched calcineurin B. Journal of Biomolecular Nmr. 3: 627-38. PMID 8111229 DOI: 10.1007/BF00198368 |
0.4 |
|
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 |
0.614 |
|
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 |
0.623 |
|
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 |
0.632 |
|
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 |
0.583 |
|
1994 |
Grzesiek S, Bax A. Interference between Dipolar and Quadrupolar Interactions in the Slow Tumbling Limit: A Source of Line Shift and Relaxation in 2H-Labeled Compounds Journal of the American Chemical Society. 116: 10196-10201. DOI: 10.1021/JA00101A045 |
0.353 |
|
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 |
0.675 |
|
1994 |
Zhu G, Live D, Bax A. Analysis of Sugar Puckers and Glycosidic Torsion Angles in a DNA G-Tetrad Structure by Heteronuclear Three-Bond J Couplings Journal of the American Chemical Society. 116: 8370-8371. DOI: 10.1021/ja00097a056 |
0.302 |
|
1994 |
Bax A. Multidimensional nuclear magnetic resonance methods for protein studies Current Opinion in Structural Biology. 4: 738-744. DOI: 10.1016/S0959-440X(94)90173-2 |
0.363 |
|
1994 |
Zhu G, Renwick A, Bax A. Measurement of Two- and Three-Bond 1H-13C J-Couplings from Quantitative Heteronuclear J Correlation for Molecules with Overlapping 1H Resonances, Using t1 Noise Reduction Journal of Magnetic Resonance, Series A. 110: 257-261. DOI: 10.1006/jmra.1994.1214 |
0.364 |
|
1993 |
Grzesiek S, Bax A. Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. Journal of Biomolecular Nmr. 3: 185-204. PMID 8477186 DOI: 10.1007/BF00178261 |
0.39 |
|
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 |
0.59 |
|
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 |
0.647 |
|
1993 |
Anglister J, Grzesiek S, Ren H, Klee CB, Bax A. Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS. Journal of Biomolecular Nmr. 3: 121-6. PMID 8383554 DOI: 10.1007/Bf00242480 |
0.365 |
|
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 |
0.638 |
|
1993 |
Grzesiek S, Bax A. The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements Journal of the American Chemical Society. 115: 12593-12594. DOI: 10.1021/JA00079A052 |
0.311 |
|
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 |
0.642 |
|
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 |
0.58 |
|
1993 |
Grzesiek S, Anglister J, Ren H, Bax A. Carbon-13 line narrowing by deuterium decoupling in deuterium/carbon-13/nitrogen-15 enriched proteins. Application to triple resonance 4D J connectivity of sequential amides Journal of the American Chemical Society. 115: 4369-4370. DOI: 10.1021/Ja00063A068 |
0.43 |
|
1993 |
Clore G, Bax A, Ikura M, Gronenborn AM. Structure of calmodulin-target peptide complexes Current Opinion in Structural Biology. 3: 838-845. DOI: 10.1016/0959-440X(93)90146-C |
0.314 |
|
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 |
0.54 |
|
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 |
0.576 |
|
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 |
0.595 |
|
1993 |
Grzesiek S, Anglister J, Bax A. Correlation of Backbone Amide and Aliphatic Side-Chain Resonances in 13C/15N-Enriched Proteins by Isotropic Mixing of 13C Magnetization Journal of Magnetic Resonance, Series B. 101: 114-119. DOI: 10.1006/jmrb.1993.1019 |
0.355 |
|
1993 |
Zhu G, Bax A. Measurement of Long-Range 1H-13C Coupling Constants from Quantitative 2D Heteronuclear Multiple-Quantum Correlation Spectra Journal of Magnetic Resonance, Series A. 104: 353-357. DOI: 10.1006/jmra.1993.1235 |
0.376 |
|
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. |
0.554 |
|
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. |
0.57 |
|
1992 |
Spera S, Ikura M, Bax A. Measurement of the exchange rates of rapidly exchanging amide protons: application to the study of calmodulin and its complex with a myosin light chain kinase fragment. Journal of Biomolecular Nmr. 1: 155-65. PMID 1668721 DOI: 10.1007/BF01877227 |
0.373 |
|
1992 |
Bax A, Ikura M. An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins. Journal of Biomolecular Nmr. 1: 99-104. PMID 1668719 DOI: 10.1007/BF01874573 |
0.392 |
|
1992 |
Clore GM, Bax A, Gronenborn AM. Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy. Journal of Biomolecular Nmr. 1: 13-22. PMID 1668718 DOI: 10.1007/Bf01874566 |
0.381 |
|
1992 |
Barbato G, Ikura M, Kay LE, Pastor RW, Bax A. Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry. 31: 5269-78. PMID 1606151 DOI: 10.1021/Bi00138A005 |
0.517 |
|
1992 |
Nicholson LK, Kay LE, Baldisseri DM, Arango J, Young PE, Bax A, Torchia DA. Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease. Biochemistry. 31: 5253-63. PMID 1606149 DOI: 10.1021/Bi00138A003 |
0.541 |
|
1992 |
Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science (New York, N.Y.). 256: 632-8. PMID 1585175 DOI: 10.1126/Science.1585175 |
0.33 |
|
1992 |
Grzesiek S, Döbeli H, Gentz R, Garotta G, Labhardt AM, Bax A. 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma. Biochemistry. 31: 8180-90. PMID 1525157 DOI: 10.1021/BI00150A009 |
0.312 |
|
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 |
0.602 |
|
1992 |
Ikura M, Barbato G, Klee CB, Bax A. Solution structure of calmodulin and its complex with a myosin light chain kinase fragment. Cell Calcium. 13: 391-400. PMID 1505004 DOI: 10.1016/0143-4160(92)90052-T |
0.32 |
|
1992 |
Blake PR, Lee B, Summers MF, Adams MW, Park JB, Zhou ZH, Bax A. Quantitative measurement of small through-hydrogen-bond and 'through-space' 1H-113Cd and 1H-199Hg J couplings in metal-substituted rubredoxin from Pyrococcus furiosus. Journal of Biomolecular Nmr. 2: 527-33. PMID 1422158 DOI: 10.1007/Bf02192814 |
0.678 |
|
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 |
0.577 |
|
1992 |
Bax A, Max D, Zax D. Measurement of long-range 13C-13C J couplings in a 20-kDa protein-peptide complex Journal of the American Chemical Society. 114: 6923-6925. DOI: 10.1021/Ja00043A052 |
0.343 |
|
1992 |
Grzesiek S, Bax A. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR Journal of the American Chemical Society. 114: 6291-6293. DOI: 10.1021/JA00042A003 |
0.395 |
|
1992 |
Ikura M, Bax A. Isotope-filtered 2D NMR of a protein-peptide complex: study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin Journal of the American Chemical Society. 114: 2433-2440. DOI: 10.1021/JA00033A019 |
0.346 |
|
1992 |
Kay LE, Nicholson LK, Delaglio F, Bax A, Torchia DA. Pulse sequences for removal of the effects of cross correlation between dipolar and chemical-shift anisotropy relaxation mechanisms on the measurement of heteronuclear T1 and T2 values in proteins Journal of Magnetic Resonance (1969). 97: 359-375. DOI: 10.1016/0022-2364(92)90320-7 |
0.42 |
|
1992 |
Grzesiek S, Ikura M, Marius Clore G, Gronenborn AM, Bax A. A 3D triple-resonance NMR technique for qualitative measurement of carbonyl-Hβ J couplings in isotopically enriched proteins Journal of Magnetic Resonance (1969). 96: 215-221. DOI: 10.1016/0022-2364(92)90307-S |
0.382 |
|
1992 |
Bax A, Pochapsky SS. Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients Journal of Magnetic Resonance (1969). 99: 638-643. DOI: 10.1016/0022-2364(92)90221-R |
0.319 |
|
1992 |
Grzesiek S, Bax A. An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins Journal of Magnetic Resonance (1969). 99: 201-207. DOI: 10.1016/0022-2364(92)90169-8 |
0.408 |
|
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 |
0.597 |
|
1992 |
Grzesiek S, Bax A. Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein Journal of Magnetic Resonance (1969). 96: 432-440. DOI: 10.1016/0022-2364(92)90099-S |
0.38 |
|
1992 |
Kay LE, Bull TE, Nicholson LK, Griesinger C, Schwalbe H, Bax A, Torchia DA. The measurement of heteronuclear transverse relaxation times in ax3 spin systems via polarization-transfer techniques Journal of Magnetic Resonance (1969). 100: 538-558. DOI: 10.1016/0022-2364(92)90058-F |
0.518 |
|
1991 |
Sklenár V, Kypr J, Bax A, Zon G, Vorlícková M. N.m.r. and c.d. studies of the DNA fragments d(TATATATA) and d(TATATA) in solution. International Journal of Biological Macromolecules. 11: 273-7. PMID 2489092 DOI: 10.1016/0141-8130(89)90019-6 |
0.315 |
|
1991 |
Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM. Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy. Biochemistry. 29: 8172-84. PMID 2261471 DOI: 10.1021/Bi00487A027 |
0.436 |
|
1991 |
Ikura M, Kay LE, Krinks M, Bax A. Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix. Biochemistry. 30: 5498-504. PMID 2036419 DOI: 10.1021/Bi00236A024 |
0.534 |
|
1991 |
Clore GM, Kay LE, Bax A, Gronenborn AM. Four-dimensional 13C/13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1 beta. Biochemistry. 30: 12-8. PMID 1988012 DOI: 10.1021/Bi00215A002 |
0.564 |
|
1991 |
Ikura M, Spera S, Barbato G, Kay LE, Krinks M, Bax A. Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. Biochemistry. 30: 9216-28. PMID 1909892 DOI: 10.1021/Bi00102A013 |
0.593 |
|
1991 |
Delaglio F, Torchia DA, Bax A. Measurement of 15N-13C J couplings in staphylococcal nuclease. Journal of Biomolecular Nmr. 1: 439-46. PMID 1841710 DOI: 10.1007/Bf02192865 |
0.327 |
|
1991 |
Ikura M, Kay LE, Bax A. Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution. Journal of Biomolecular Nmr. 1: 299-304. PMID 1841700 DOI: 10.1007/Bf01875522 |
0.561 |
|
1991 |
Bax A, Ikura M, Kay LE, Barbato G, Spera S. Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination. Ciba Foundation Symposium. 161: 108-19; discussion 1. PMID 1814691 |
0.527 |
|
1991 |
Powers R, Clore GM, Bax A, Garrett DS, Stahl SJ, Wingfield PT, Gronenborn AM. Secondary structure of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy. Journal of Molecular Biology. 221: 1081-90. PMID 1719214 DOI: 10.1016/0022-2836(91)90920-2 |
0.434 |
|
1991 |
Glaudemans CP, Lerner L, Daves GD, Kovác P, Venable R, Bax A. Significant conformational changes in an antigenic carbohydrate epitope upon binding to a monoclonal antibody. Biochemistry. 29: 10906-11. PMID 1703008 DOI: 10.1021/BI00501A007 |
0.367 |
|
1991 |
Spera S, Bax A. Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts Journal of the American Chemical Society. 113: 5490-5492. DOI: 10.1021/JA00014A071 |
0.358 |
|
1991 |
Bax A. Experimental NMR techniques for studies of biopolymers Current Opinion in Structural Biology. 1: 1030-1035. DOI: 10.1016/0959-440x(91)90102-y |
0.401 |
|
1991 |
Bax A, Ikura M, Kay LE, Zhu G. Removal of F1 baseline distortion and optimization of folding in multidimensional NMR spectra Journal of Magnetic Resonance (1969). 91: 174-178. DOI: 10.1016/0022-2364(91)90422-P |
0.494 |
|
1991 |
Kay LE, Ikura M, Bax A. The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins Journal of Magnetic Resonance (1969). 91: 84-92. DOI: 10.1016/0022-2364(91)90410-U |
0.598 |
|
1991 |
Powers R, Gronenborn AM, Marius Clore G, Bax A. Three-dimensional triple-resonance NMR of 13C/15N-enriched proteins using constant-time evolution Journal of Magnetic Resonance (1969). 94: 209-213. DOI: 10.1016/0022-2364(91)90312-H |
0.34 |
|
1991 |
Kay LE, Ikura M, Zhu G, Bax A. Four-dimensional heteronuclear triple-resonance NMR of isotopically enriched proteins for sequential assignment of backbone atoms Journal of Magnetic Resonance (1969). 91: 422-428. DOI: 10.1016/0022-2364(91)90208-B |
0.528 |
|
1991 |
Archer SJ, Ikura M, Torchia DA, Bax A. An alternative 3D NMR technique for correlating backbone 15N with side chain Hβ resonances in larger proteins Journal of Magnetic Resonance (1969). 95: 636-641. DOI: 10.1016/0022-2364(91)90182-S |
0.402 |
|
1991 |
Bax A. One and Two Dimensional NMR Spectroscopy. VonAtta-ur-Rahman. Elsevier, Amsterdam 1989. XIX, 578 S., geb. HFl. 355.00.-ISBN 0-444-87316-3 Angewandte Chemie. 103: 221-222. DOI: 10.1002/ange.19911030235 |
0.325 |
|
1990 |
Clore GM, Bax A, Wingfield PT, Gronenborn AM. Identification and localization of bound internal water in the solution structure of interleukin 1 beta by heteronuclear three-dimensional 1H rotating-frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy. Biochemistry. 29: 5671-6. PMID 2383553 DOI: 10.1021/Bi00476A004 |
0.391 |
|
1990 |
Kay LE, Clore GM, Bax A, Gronenborn AM. Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution. Science (New York, N.Y.). 249: 411-4. PMID 2377896 DOI: 10.1126/Science.2377896 |
0.582 |
|
1990 |
Ikura M, Kay LE, Bax A. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry. 29: 4659-67. PMID 2372549 DOI: 10.1021/Bi00471A022 |
0.602 |
|
1990 |
Ikura M, Marion D, Kay LE, Shih H, Krinks M, Klee CB, Bax A. Heteronuclear 3D NMR and isotopic labeling of calmodulin. Towards the complete assignment of the 1H NMR spectrum. Biochemical Pharmacology. 40: 153-60. PMID 2372304 DOI: 10.1016/0006-2952(90)90190-V |
0.548 |
|
1990 |
Ikura M, Krinks M, Torchia DA, Bax A. An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling. Febs Letters. 266: 155-8. PMID 2114317 DOI: 10.1016/0014-5793(90)81528-V |
0.382 |
|
1990 |
Williamson D, McLennan IJ, Bax A, Gamcsik MP, Glickson JD. Two-dimensional NMR study of bleomycin and its zinc(II) complex: Reassignment of13C resonances Journal of Biomolecular Structure and Dynamics. 8: 375-398. PMID 1702638 DOI: 10.1080/07391102.1990.10507811 |
0.356 |
|
1990 |
Ikura M, Bax A, Clore GM, Gronenborn AM. Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional NMR spectroscopy Journal of the American Chemical Society. 112: 9020-9022. DOI: 10.1021/Ja00180A080 |
0.366 |
|
1990 |
Clore GM, Szabo A, Bax A, Kay LE, Driscoll PC, Gronenborn AM. Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins Journal of the American Chemical Society. 112: 4989-4991. DOI: 10.1021/Ja00168A070 |
0.473 |
|
1990 |
Kay LE, Ikura M, Bax A. Proton-proton correlation via carbon-carbon couplings: a three-dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13 Journal of the American Chemical Society. 112: 888-889. DOI: 10.1021/Ja00158A070 |
0.51 |
|
1990 |
Bax A, Clore G, Driscoll PC, Gronenborn AM, Ikura M, Kay LE. Practical aspects of proton-carbon-carbon-proton three-dimensional correlation spectroscopy of 13C-labeled proteins Journal of Magnetic Resonance (1969). 87: 620-627. DOI: 10.1016/0022-2364(90)90320-9 |
0.574 |
|
1990 |
Bax A, Ikura M, Kay LE, Torchia DA, Tschudin R. Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins Journal of Magnetic Resonance (1969). 86: 304-318. DOI: 10.1016/0022-2364(90)90262-8 |
0.554 |
|
1990 |
Ikura M, Kay LE, Tschudin R, Bax A. Three-dimensional NOESY-HMQC spectroscopy of a 13C-labeled protein Journal of Magnetic Resonance (1969). 86: 204-209. DOI: 10.1016/0022-2364(90)90227-Z |
0.573 |
|
1990 |
Kay LE, Bax A. New methods for the measurement of NHCαH coupling constants in 15N-labeled proteins Journal of Magnetic Resonance (1969). 86: 110-126. DOI: 10.1016/0022-2364(90)90215-U |
0.546 |
|
1990 |
Bax A, Clore G, Gronenborn AM. 1H1H correlation via isotropic mixing of 13C magnetization, a new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins Journal of Magnetic Resonance (1969). 88: 425-431. DOI: 10.1016/0022-2364(90)90202-K |
0.366 |
|
1990 |
Zhu G, Bax A. Improved linear prediction for truncated signals of known phase Journal of Magnetic Resonance (1969). 90: 405-410. DOI: 10.1016/0022-2364(90)90150-8 |
0.341 |
|
1990 |
Bax A. Book Review: One and Two Dimensional NMR Spectroscopy. By Atta-ur-Rahman Angewandte Chemie International Edition in English. 29: 935-936. DOI: 10.1002/anie.199009351 |
0.322 |
|
1989 |
Bax A. Homonuclear Hartmann-Hahn experiments. Methods in Enzymology. 176: 151-68. PMID 2811684 DOI: 10.1016/0076-6879(89)76010-9 |
0.378 |
|
1989 |
Bax A, Sparks SW, Torchia DA. Detection of insensitive nuclei. Methods in Enzymology. 176: 134-50. PMID 2811683 DOI: 10.1016/0076-6879(89)76009-2 |
0.4 |
|
1989 |
Kay LE, Torchia DA, Bax A. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry. 28: 8972-9. PMID 2690953 DOI: 10.1021/Bi00449A003 |
0.551 |
|
1989 |
Marion D, Driscoll PC, Kay LE, Wingfield PT, Bax A, Gronenborn AM, Clore GM. Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta. Biochemistry. 28: 6150-6. PMID 2675964 DOI: 10.1021/Bi00441A004 |
0.586 |
|
1989 |
Torchia DA, Sparks SW, Bax A. Staphylococcal nuclease: sequential assignments and solution structure. Biochemistry. 28: 5509-24. PMID 2673349 DOI: 10.1021/Bi00439A028 |
0.429 |
|
1989 |
Bax A. Two-dimensional NMR and protein structure. Annual Review of Biochemistry. 58: 223-56. PMID 2673010 DOI: 10.1146/ANNUREV.BI.58.070189.001255 |
0.365 |
|
1989 |
Gronenborn AM, Bax A, Wingfield PT, Clore GM. A powerful method of sequential proton resonance assignment in proteins using relayed 15N-1H multiple quantum coherence spectroscopy. Febs Letters. 243: 93-8. PMID 2537752 DOI: 10.1016/0014-5793(89)81224-4 |
0.412 |
|
1989 |
Torchia DA, Sparks SW, Young PE, Bax A. Proline assignments and identification of the cis K116/P117 peptide bond in liganded staphylococcal nuclease using isotope edited 2D NMR spectroscopy Journal of the American Chemical Society. 111: 8315-8317. DOI: 10.1021/Ja00203A063 |
0.315 |
|
1989 |
Kay LE, Brooks B, Sparks SW, Torchia DA, Bax A. Measurement of NH-C.alpha.H coupling constants in staphylococcal nuclease by two-dimensional NMR and comparison with x-ray crystallographic results Journal of the American Chemical Society. 111: 5488-5490. DOI: 10.1021/Ja00196A078 |
0.531 |
|
1989 |
Marion D, Kay LE, Sparks SW, Torchia DA, Bax A. Three-dimensional heteronuclear NMR of nitrogen-15 labeled proteins Journal of the American Chemical Society. 111: 1515-1517. DOI: 10.1021/Ja00186A066 |
0.527 |
|
1989 |
Bax A, Kay LE, Sparks SW, Torchia DA. Line narrowing of amide proton resonances in 2D NMR spectra of proteins Journal of the American Chemical Society. 111: 408-409. DOI: 10.1021/Ja00183A082 |
0.53 |
|
1989 |
Marion D, Ikura M, Bax A. Improved solvent suppression in one- and two-dimensional NMR spectra by convolution of time-domain data Journal of Magnetic Resonance (1969). 84: 425-430. DOI: 10.1016/0022-2364(89)90391-0 |
0.332 |
|
1989 |
Marion D, Bax A. Baseline correction of 2D FT NMR spectra using a simple linear prediction extrapolation of the time-domain data Journal of Magnetic Resonance (1969). 83: 205-211. DOI: 10.1016/0022-2364(89)90307-7 |
0.318 |
|
1989 |
Inagaki F, Shimada I, Kohda D, Suzuki A, Bax A. Relayed HOHAHA, a useful method for extracting subspectra of individual components of sugar chains Journal of Magnetic Resonance (1969). 81: 186-190. DOI: 10.1016/0022-2364(89)90278-3 |
0.39 |
|
1989 |
Marion D, Ikura M, Tschudin R, Bax A. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins Journal of Magnetic Resonance (1969). 85: 393-399. DOI: 10.1016/0022-2364(89)90152-2 |
0.354 |
|
1989 |
Kay LE, Bax A. Separation of NH and NH2 resonances in 1H-detected heteronuclear multiple-quantum correlation spectra Journal of Magnetic Resonance (1969). 84: 598-603. DOI: 10.1016/0022-2364(89)90125-X |
0.511 |
|
1989 |
Kay LE, Marion D, Bax A. Practical aspects of 3D heteronuclear NMR of proteins Journal of Magnetic Resonance (1969). 84: 72-84. DOI: 10.1016/0022-2364(89)90006-1 |
0.488 |
|
1988 |
Marion D, Zasloff M, Bax A. A two-dimensional NMR study of the antimicrobial peptide magainin 2 Febs Letters. 227: 21-26. PMID 3338566 DOI: 10.1016/0014-5793(88)81405-4 |
0.349 |
|
1988 |
Bax A, Summers MF, Egan W, Guirgis N, Schneerson R, Robbins JB, Orskov F, Orskov I, Vann WF. Structural studies of the Escherichia coli K93 and K53 capsular polysaccharides. Carbohydrate Research. 173: 53-64. PMID 3128402 DOI: 10.1016/S0008-6215(00)90802-4 |
0.624 |
|
1988 |
Clore GM, Bax A, Wingfield P, Gronenborn AM. Long-range 15N-1H correlation as an aid to sequential proton resonance assignment of proteins. Application to the DNA-binding protein ner from phage Mu. Febs Letters. 238: 17-21. PMID 3049156 DOI: 10.1016/0014-5793(88)80216-3 |
0.415 |
|
1988 |
Torchia DA, Sparks SW, Bax A. NMR signal assignments of amide protons in the alpha-helical domains of staphylococcal nuclease. Biochemistry. 27: 5135-41. PMID 2844251 DOI: 10.1021/Bi00414A028 |
0.398 |
|
1988 |
Ziffer H, Bax A, Highet RJ, Green B. Investigation by two-dimensional NMR of the structure and stereochemistry of a methyl p-nitrocinnamate photodimer The Journal of Organic Chemistry. 53: 895-896. DOI: 10.1021/JO00239A046 |
0.304 |
|
1988 |
Torchia DA, Sparks SW, Bax A. Delineation of .alpha.-helical domains in deuteriated Staphylococcal nuclease by 2D NOE NMR spectroscopy Journal of the American Chemical Society. 110: 2320-2321. DOI: 10.1021/Ja00215A063 |
0.325 |
|
1988 |
Williamson D, Bax A. Resolution-enhanced correlation of 1H and 31P chemical shifts Journal of Magnetic Resonance (1969). 76: 174-177. DOI: 10.1016/0022-2364(88)90213-2 |
0.319 |
|
1988 |
Bax A, Marion D. Improved resolution and sensitivity in 1H-detected heteronuclear multiple-bond correlation spectroscopy Journal of Magnetic Resonance (1969). 78: 186-191. DOI: 10.1016/0022-2364(88)90172-2 |
0.31 |
|
1988 |
Bax A, Lerner L. Measurement of 1H-1H coupling constants in DNA fragments by 2D NMR Journal of Magnetic Resonance (1969). 79: 429-438. DOI: 10.1016/0022-2364(88)90080-7 |
0.365 |
|
1988 |
Bax A. Correction of cross-peak intensities in 2D spin-locked NOE spectroscopy for offset and Hartmann-Hahn effects Journal of Magnetic Resonance (1969). 77: 134-147. DOI: 10.1016/0022-2364(88)90038-8 |
0.338 |
|
1987 |
Lerner L, Bax A. Application of new, high-sensitivity, 1H13C-N.M.R.-spectral techniques to the study of oligosaccharides Carbohydrate Research. 166: 35-46. PMID 3652076 DOI: 10.1016/0008-6215(87)80042-3 |
0.357 |
|
1987 |
Byrd RA, Egan W, Summers MF, Bax A. New n.m.r.-spectroscopic approaches for structural studies of polysaccharides: application to the Haemophilus influenzae type a capsular polysaccharide. Carbohydrate Research. 166: 47-58. PMID 3498535 DOI: 10.1016/0008-6215(87)80043-5 |
0.685 |
|
1987 |
Sklenár V, Brooks BR, Zon G, Bax A. Absorption mode two-dimensional NOE spectroscopy of exchangeable protons in oligonucleotides. Febs Letters. 216: 249-52. PMID 3034676 DOI: 10.1016/0014-5793(87)80699-3 |
0.347 |
|
1987 |
Sklenar V, Bax A. Measurement of proton-phosphorus-31 NMR coupling constants in double-stranded DNA fragments Journal of the American Chemical Society. 109: 7525-7526. DOI: 10.1021/JA00258A044 |
0.326 |
|
1987 |
Bax A, Sklenar V, Clore GM, Gronenborn AM. Water suppression in two-dimensional spin-locked NMR experiments using a novel phase-cycling procedure Journal of the American Chemical Society. 109: 6511-6513. DOI: 10.1021/JA00255A047 |
0.301 |
|
1987 |
Sklenar V, Bax A, Zon G. Assignment of Z DNA NMR spectra of poly d(Gm5C) by two-dimensional multinuclear spectroscopy Journal of the American Chemical Society. 109: 2221-2222. DOI: 10.1021/JA00241A071 |
0.334 |
|
1987 |
Bax A, Marzilli LG, Summers MF. New insights into the solution behavior of cobalamins. Studies of the base-off form of coenzyme B12 using modern two-dimensional NMR methods Journal of the American Chemical Society. 109: 566-574. DOI: 10.1021/Ja00236A040 |
0.728 |
|
1987 |
Sklenář V, Bax A. Spin-echo water suppression for the generation of pure-phase two-dimensional NMR spectra Journal of Magnetic Resonance (1969). 74: 469-479. DOI: 10.1016/0022-2364(87)90269-1 |
0.33 |
|
1987 |
Bax A, Weiss MA. Simplification of two-dimensional NOE spectra of proteins by 13C labeling Journal of Magnetic Resonance (1969). 71: 571-575. DOI: 10.1016/0022-2364(87)90259-9 |
0.35 |
|
1987 |
Sklenáǩ V, Bax A. Two-dimensional heteronuclear chemical-shift correlation in proteins at natural abundance 15N and 13C levels Journal of Magnetic Resonance (1969). 71: 379-383. DOI: 10.1016/0022-2364(87)90073-4 |
0.425 |
|
1987 |
Subramanian S, Bax A. Generation of pure phase NMR subspectra for measurement of homonuclear coupling constants Journal of Magnetic Resonance (1969). 71: 325-330. DOI: 10.1016/0022-2364(87)90063-1 |
0.364 |
|
1987 |
Sklenář V, Tschudin R, Bax A. Water suppression using a combination of hard and soft pulses Journal of Magnetic Resonance (1969). 75: 352-357. DOI: 10.1016/0022-2364(87)90041-2 |
0.333 |
|
1987 |
BAX A, MARZILLI LG, SUMMERS MF. ChemInform Abstract: New Insights into the Solution Behavior of Cobalamins. Studies of the Base-Off Form of Coenzyme B12 Using Modern Two-Dimensional NMR Methods. Cheminform. 18. DOI: 10.1002/chin.198722039 |
0.402 |
|
1986 |
Sklenár V, Miyashiro H, Zon G, Miles HT, Bax A. Assignment of the 31P and 1H resonances in oligonucleotides by two-dimensional NMR spectroscopy. Febs Letters. 208: 94-8. PMID 3770213 DOI: 10.1016/0014-5793(86)81539-3 |
0.39 |
|
1986 |
Bax A, Lerner L. Two-dimensional nuclear magnetic resonance spectroscopy Science. 232: 960-967. PMID 3518060 DOI: 10.1126/SCIENCE.3518060 |
0.401 |
|
1986 |
Bax A, Aszalos A, Dinya Z, Sudo K. Structure elucidation of the antibiotic desertomycin through the use of new two-dimensional NMR techniques Journal of the American Chemical Society. 108: 8056-8063. DOI: 10.1021/JA00285A029 |
0.307 |
|
1986 |
Sarkar SK, Glickson JD, Bax A. Assignment of secondary amide 15N resonances of bleomycin A2 by two-dimensional multiple-quantum 1H-15N shift-correlation NMR spectroscopy Journal of the American Chemical Society. 108: 6814-6816. DOI: 10.1021/Ja00281A065 |
0.359 |
|
1986 |
Summers MF, Marzilli LG, Bax A. Complete proton and carbon-13 assignments of coenzyme B12 through the use of new two-dimensional NMR experiments Journal of the American Chemical Society. 108: 4285-4294. DOI: 10.1021/Ja00275A008 |
0.72 |
|
1986 |
Bax A, Summers MF. Proton and carbon-13 assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR Journal of the American Chemical Society. 108: 2093-2094. DOI: 10.1021/Ja00268A061 |
0.676 |
|
1986 |
Edwards MW, Bax A. Complete proton and carbon-13 NMR assignment of the alkaloid gephyrotoxin through the use of homonuclear Hartmann-Hahn and two-dimensional spectroscopy Journal of the American Chemical Society. 108: 918-923. DOI: 10.1021/JA00265A013 |
0.383 |
|
1986 |
Bax A, Subramanian S. Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy Journal of Magnetic Resonance (1969). 67: 565-569. DOI: 10.1016/0022-2364(86)90395-1 |
0.366 |
|
1986 |
Lerner L, Bax A. Sensitivity-enhanced two-dimensional heteronuclear relayed coherence transfer NMR spectroscopy Journal of Magnetic Resonance (1969). 69: 375-380. DOI: 10.1016/0022-2364(86)90091-0 |
0.336 |
|
1986 |
Bax A, Sklenář V, Summers MF. Direct identification of relayed nuclear overhauser effects Journal of Magnetic Resonance (1969). 70: 327-331. DOI: 10.1016/0022-2364(86)90018-1 |
0.637 |
|
1986 |
Summers MF, Marzilli LG, Bax A. Complete 1H and 13C assignments of coenzyme B12 through the use of new two-dimensional NMR experiments Journal of the American Chemical Society. 108: 4285-4294. DOI: 10.1002/Chin.198648053 |
0.735 |
|
1986 |
BAX A, FERRETTI JA, NASHED N, JERINA DM. ChemInform Abstract: Complete1H and13C NMR Assignment of Complex Polycyclic Aromatic Hydrocarbons. Chemischer Informationsdienst. 17. DOI: 10.1002/Chin.198606042 |
0.319 |
|
1986 |
Bax A, Summers MF. 1H and 13C assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR Journal of the American Chemical Society. 108: 2093-2094. |
0.664 |
|
1985 |
Borah B, Cohen JS, Bax A. Conformation of double-stranded polydeoxynucleotides in solution by proton two-dimensional nuclear Overhauser enhancement spectroscopy. Biopolymers. 24: 747-65. PMID 4016214 DOI: 10.1002/Bip.360240503 |
0.31 |
|
1985 |
Davis DG, Bax A. Simplification of proton NMR spectra by selective excitation of experimental subspectra Journal of the American Chemical Society. 107: 7197-7198. DOI: 10.1021/JA00310A085 |
0.325 |
|
1985 |
Davis DG, Bax A. Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy Journal of the American Chemical Society. 107: 2820-2821. DOI: 10.1021/JA00295A052 |
0.358 |
|
1985 |
Sarkar SK, Bax A. A simple and sensitive one-dimensional NMR technique for correlation of proton and carbon chemical shifts Journal of Magnetic Resonance (1969). 62: 109-112. DOI: 10.1016/0022-2364(85)90300-2 |
0.338 |
|
1985 |
Szeverenyi NM, Bax A, Maciel GE. Magic-angle hopping as an alternative to magic-angle spinning for solid state NMR Journal of Magnetic Resonance (1969). 61: 440-447. DOI: 10.1016/0022-2364(85)90184-2 |
0.712 |
|
1985 |
Bax A, Davis DG, Sarkar SK. An improved method for two-dimensional heteronuclear relayed-coherence-transfer NMR spectroscopy Journal of Magnetic Resonance (1969). 63: 230-234. DOI: 10.1016/0022-2364(85)90176-3 |
0.377 |
|
1985 |
Bax A, Davis DG. Practical aspects of two-dimensional transverse NOE spectroscopy Journal of Magnetic Resonance (1969). 63: 207-213. DOI: 10.1016/0022-2364(85)90171-4 |
0.336 |
|
1985 |
Davis DG, Bax A. Separation of chemical exchange and cross-relaxation effects in two-dimensional NMR spectroscopy Journal of Magnetic Resonance (1969). 64: 533-535. DOI: 10.1016/0022-2364(85)90119-2 |
0.361 |
|
1985 |
Bax A, Drobny G. Optimization of two-dimensional homonuclear relayed coherence transfer NMR spectroscopy Journal of Magnetic Resonance (1969). 61: 306-320. DOI: 10.1016/0022-2364(85)90085-X |
0.302 |
|
1984 |
Bax A, Egan W, Ková P. New NHR Techniques for Structure Determination and Resonance Assignments of Complex Carbohydrates Journal of Carbohydrate Chemistry. 3: 593-611. DOI: 10.1080/07328308408057920 |
0.38 |
|
1984 |
Bax A, Byrd RA, Aszalos A. Spin multiplet enhancement in two-dimensional correlated NMR spectroscopy Journal of the American Chemical Society. 106: 7632-7633. DOI: 10.1021/Ja00336A059 |
0.302 |
|
1984 |
Early TA, Haw JF, Bax A, Maciel GE, Puar MS. Carbon-13 nuclear magnetic resonance studies of a solid inclusion complex The Journal of Physical Chemistry. 88: 324-327. DOI: 10.1021/J150646A032 |
0.496 |
|
1984 |
Bax A. Structure determination and spectral assignment by pulsed polarization transfer via long-range 1H13C couplings Journal of Magnetic Resonance (1969). 57: 314-318. DOI: 10.1016/0022-2364(84)90133-1 |
0.342 |
|
1984 |
Bax A, Hawkins BL, Maciel GE. Off resonance cross-polarization: A technique to reduce rf power requirements for magnetization transfer experiments in solids Journal of Magnetic Resonance (1969). 59: 530-535. DOI: 10.1016/0022-2364(84)90090-8 |
0.524 |
|
1984 |
Bax A, Sarkar SK. Elimination of refocusing pulses in NMR experiments Journal of Magnetic Resonance (1969). 60: 170-176. DOI: 10.1016/0022-2364(84)90045-3 |
0.316 |
|
1984 |
Bax A, Hawkins BL, Maciel GE, Szeverenyi NM. Two‐Dimensional Nmr Spectroscopy Cheminform. 16: 137-145. DOI: 10.1007/978-94-009-6378-8_4 |
0.702 |
|
1984 |
EARLY TA, HAW JF, BAX A, MACIEL GE, PUAR MS. ChemInform Abstract: CARBON-13 NUCLEAR MAGNETIC RESONANCE STUDIES OF A SOLID INCLUSION COMPLEX Chemischer Informationsdienst. 15. DOI: 10.1002/CHIN.198417074 |
0.435 |
|
1984 |
Early TA, Haw JF, Bax A, Maciel GE, Puar MS. Carbon-13 nuclear magnetic resonance studies of a solid inclusion complex Journal of Physical Chemistry. 88: 324-327. |
0.431 |
|
1983 |
Griffey RH, Poulter CD, Bax A, Hawkins BL, Yamaizumi Z, Nishimura S. Multiple quantum two-dimensional 1H--15N nuclear magnetic resonance spectroscopy: chemical shift correlation maps for exchangeable imino protons of Escherichia coli tRNAMetf in water. Proceedings of the National Academy of Sciences of the United States of America. 80: 5895-7. PMID 6351069 DOI: 10.1073/Pnas.80.19.5895 |
0.38 |
|
1983 |
Bax A, Griffey RH, Hawkins BL. Sensitivity-enhanced correlation of nitrogen-15 and proton chemical shifts in natural-abundance samples via multiple quantum coherence Journal of the American Chemical Society. 105: 7188-7190. DOI: 10.1021/ja00362a038 |
0.309 |
|
1983 |
Szeverenyi NM, Bax A, Maciel GE. Proton-exchange rates in solid tropolone as measured via carbon-13 CP/MAS NMR Journal of the American Chemical Society. 105: 2579-2582. DOI: 10.1021/Ja00347A012 |
0.701 |
|
1983 |
Bax A, Szeverenyi NM, Maciel GE. Chemical shift anisotropy in powdered solids studied by 2D FT CP/MAS NMR Journal of Magnetic Resonance (1969). 51: 400-408. DOI: 10.1016/0022-2364(83)90292-5 |
0.698 |
|
1983 |
Bax A, Szeverenyi NM, Maciel GE. Correlation of isotropic shifts and chemical shift anisotropies by two-dimensional fourier-transform magic-angle hopping nmr spectroscopy Journal of Magnetic Resonance (1969). 52: 147-152. DOI: 10.1016/0022-2364(83)90267-6 |
0.721 |
|
1983 |
Bax A, Early TA, Maciel GE. Proton chemical shifts in polycrystalline solids determined by off-resonance decoupling 13C CPMAS NMR Journal of Magnetic Resonance (1969). 52: 35-41. DOI: 10.1016/0022-2364(83)90254-8 |
0.586 |
|
1983 |
Bax A, Griffey RH, Hawkins BL. Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR Journal of Magnetic Resonance (1969). 55: 301-315. DOI: 10.1016/0022-2364(83)90241-X |
0.357 |
|
1983 |
Bax A. Broadband homonuclear decoupling in heteronuclear shift correlation NMR spectroscopy Journal of Magnetic Resonance (1969). 53: 517-520. DOI: 10.1016/0022-2364(83)90225-1 |
0.384 |
|
1983 |
Bax A, Szeverenyi NM, Maciel GE. Chemical shift anisotropy in powdered solids studied by 2D FT NMR with flipping of the spinning axis Journal of Magnetic Resonance (1969). 55: 494-497. DOI: 10.1016/0022-2364(83)90134-8 |
0.715 |
|
1983 |
Bax A. Two-dimensional heteronuclear relayed coherence transfer spectroscopy Journal of Magnetic Resonance (1969). 53: 149-153. DOI: 10.1016/0022-2364(83)90086-0 |
0.337 |
|
1983 |
Bax A, Mareci TH. Practical aspects of carbon-13 double quantum NMR Journal of Magnetic Resonance (1969). 53: 360-363. DOI: 10.1016/0022-2364(83)90040-9 |
0.337 |
|
1983 |
Szeverenyi NM, Bax A, Maciel GE. Proton-exchange rates in solid tropolone as measured via 13C CP/MAS NMR Journal of the American Chemical Society. 105: 2579-2582. |
0.503 |
|
1982 |
Bax A, Freeman R. Long-range proton-carbon-13 NMR spin coupling constants Journal of the American Chemical Society. 104: 1099-1100. DOI: 10.1021/Ja00368A033 |
0.526 |
|
1982 |
Bax A, Szeverenyi NM, Maciel GE. Pulsed polarization transfer for 13C NMR in solids Journal of Magnetic Resonance (1969). 50: 227-232. DOI: 10.1016/0022-2364(82)90052-X |
0.7 |
|
1981 |
Bax A, Freeman R, Frenkiel TA. An NMR technique for tracing out the carbon skeleton of an organic molecule Journal of the American Chemical Society. 103: 2102-2104. DOI: 10.1021/Ja00398A044 |
0.479 |
|
1981 |
Bax A, Freeman R. Investigation of complex networks of spin-spin coupling by two-dimensional NMR Journal of Magnetic Resonance (1969). 44: 542-561. DOI: 10.1016/0022-2364(81)90287-0 |
0.543 |
|
1981 |
Bax A, Morris GA. An improved method for heteronuclear chemical shift correlation by two-dimensional NMR Journal of Magnetic Resonance (1969). 42: 501-505. DOI: 10.1016/0022-2364(81)90272-9 |
0.347 |
|
1981 |
Bax A, Freeman R. Relative signs of NMR spin coupling constants by two-dimensional Fourier transform spectroscopy Journal of Magnetic Resonance (1969). 45: 177-181. DOI: 10.1016/0022-2364(81)90113-X |
0.464 |
|
1981 |
Bax A, Freeman R, Frenkiel T, Levitt M. Assignment of carbon-13 NMR spectra via double-quantum coherence Journal of Magnetic Resonance (1969). 43: 478-483. DOI: 10.1016/0022-2364(81)90060-3 |
0.515 |
|
1981 |
Bax A, Freeman R, Morris GA. A simple method for suppressing dispersion-mode contributions in NMR spectra: The “pseudo echo” Journal of Magnetic Resonance (1969). 43: 333-338. DOI: 10.1016/0022-2364(81)90045-7 |
0.5 |
|
1981 |
Bax A, Freeman R, Morris G. Correlation of proton chemical shifts by two-dimensional Fourier transform NMR Journal of Magnetic Resonance (1969). 42: 164-168. DOI: 10.1016/0022-2364(81)90022-6 |
0.463 |
|
1980 |
Bax A, Freeman R, Kempsell SP. Natural abundance carbon-13-carbon-13 coupling observed via double-quantum coherence Journal of the American Chemical Society. 102: 4849-4851. DOI: 10.1021/Ja00534A056 |
0.472 |
|
1980 |
Bax A, Freeman R. Investigation of 13C13C couplings in natural abundance samples: The strong coupling case Journal of Magnetic Resonance (1969). 41: 507-511. DOI: 10.1016/0022-2364(80)90309-1 |
0.47 |
|
1980 |
Bax A, Mehlkopf T, Smidt J, Freeman R. A simple method for detection of zero-quantum transitions in NMR Journal of Magnetic Resonance (1969). 41: 502-506. DOI: 10.1016/0022-2364(80)90308-X |
0.711 |
|
1980 |
Bax A, Freeman R. Enhanced NMR resolution by restricting the effective sample volume Journal of Magnetic Resonance (1969). 37: 177-181. DOI: 10.1016/0022-2364(80)90104-3 |
0.427 |
|
1980 |
Bax A, Freeman R, Kempsell SP. Investigation of 13C13C long-range couplings in natural-abundance samples Journal of Magnetic Resonance (1969). 41: 349-353. DOI: 10.1016/0022-2364(80)90083-9 |
0.466 |
|
1980 |
Bax A, De Jong PG, Mehlkopf AF, Smidt J. Separation of the different orders of NMR multiple-quantum transitions by the use of pulsed field gradients Chemical Physics Letters. 69: 567-570. DOI: 10.1016/0009-2614(80)85130-X |
0.766 |
|
1979 |
Emid S, Bax A, Konijnendijk J, Smidt J, Pines A. Multiple quantum coherence in dipolar relaxation measurements Physica B+C. 96: 333-336. DOI: 10.1016/0378-4363(79)90018-4 |
0.67 |
|
1979 |
Bax A, Mehlkopf AF, Smidt J. Homonuclear broadband-decoupled absorption spectra, with linewidths which are independent of the transverse relaxation rate Journal of Magnetic Resonance (1969). 35: 167-169. DOI: 10.1016/0022-2364(79)90088-X |
0.765 |
|
1979 |
Bax A, Mehlkopf AF, Smidt J. Absorption spectra from phase-modulated spin echoes Journal of Magnetic Resonance (1969). 35: 373-377. DOI: 10.1016/0022-2364(79)90060-X |
0.766 |
|
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