| Year |
Citation |
Score |
| 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 |
0.373 |
|
| 2017 |
Alderson TR, Charlier C, Torchia DA, Anfinrud P, Bax A. Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy. Journal of the American Chemical Society. 139: 11036-11039. PMID 28766333 DOI: 10.1021/Jacs.7B06676 |
0.348 |
|
| 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 |
0.382 |
|
| 2015 |
Torchia DA. NMR studies of dynamic biomolecular conformational ensembles. Progress in Nuclear Magnetic Resonance Spectroscopy. 84: 14-32. PMID 25669739 DOI: 10.1016/J.Pnmrs.2014.11.001 |
0.394 |
|
| 2012 |
Fawzi NL, Ying J, Torchia DA, Clore GM. Probing exchange kinetics and atomic resolution dynamics in high-molecular-weight complexes using dark-state exchange saturation transfer NMR spectroscopy. Nature Protocols. 7: 1523-33. PMID 22814391 DOI: 10.1038/Nprot.2012.077 |
0.376 |
|
| 2011 |
Fawzi NL, Ying J, Ghirlando R, Torchia DA, Clore GM. Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR. Nature. 480: 268-72. PMID 22037310 DOI: 10.1038/Nature10577 |
0.401 |
|
| 2011 |
Torchia DA. Dynamics of biomolecules from picoseconds to seconds at atomic resolution. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 212: 1-10. PMID 21840740 DOI: 10.1016/J.Jmr.2011.07.010 |
0.338 |
|
| 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 |
0.411 |
|
| 2010 |
Fawzi NL, Ying J, Torchia DA, Clore GM. Kinetics of amyloid beta monomer-to-oligomer exchange by NMR relaxation. Journal of the American Chemical Society. 132: 9948-51. PMID 20604554 DOI: 10.1021/Ja1048253 |
0.376 |
|
| 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 |
0.324 |
|
| 2007 |
Louis JM, Ishima R, Torchia DA, Weber IT. HIV-1 protease: structure, dynamics, and inhibition. Advances in Pharmacology (San Diego, Calif.). 55: 261-98. PMID 17586318 DOI: 10.1016/S1054-3589(07)55008-8 |
0.369 |
|
| 2007 |
Ishima R, Torchia DA, Louis JM. Mutational and structural studies aimed at characterizing the monomer of HIV-1 protease and its precursor. The Journal of Biological Chemistry. 282: 17190-9. PMID 17412697 DOI: 10.1074/Jbc.M701304200 |
0.418 |
|
| 2007 |
Bax A, Torchia DA. Structural biology: molecular machinery in action. Nature. 445: 609. PMID 17237759 DOI: 10.1038/Nature05566 |
0.342 |
|
| 2005 |
Ishima R, Torchia DA. Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters. Journal of Biomolecular Nmr. 32: 41-54. PMID 16041482 DOI: 10.1007/S10858-005-3593-Z |
0.305 |
|
| 2004 |
Ishima R, Baber J, Louis JM, Torchia DA. Carbonyl carbon transverse relaxation dispersion measurements and ms-micros timescale motion in a protein hydrogen bond network. Journal of Biomolecular Nmr. 29: 187-98. PMID 15014232 DOI: 10.1023/B:Jnmr.0000019249.50306.5D |
0.422 |
|
| 2004 |
Jacob J, Louis JM, Richter BW, Duckett CS, Torchia DA. The C-terminal domain of viral IAP associated factor (cVIAF) is a structural homologue of phosducin: resonance assignments and secondary structure of the C-terminal domain of VIAF. Journal of Biomolecular Nmr. 28: 197-8. PMID 14755167 DOI: 10.1023/B:Jnmr.0000013820.43366.99 |
0.659 |
|
| 2003 |
Ishima R, Torchia DA, Lynch SM, Gronenborn AM, Louis JM. Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor. The Journal of Biological Chemistry. 278: 43311-9. PMID 12933791 DOI: 10.1074/Jbc.M307549200 |
0.388 |
|
| 2003 |
Katoh E, Louis JM, Yamazaki T, Gronenborn AM, Torchia DA, Ishima R. A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex. Protein Science : a Publication of the Protein Society. 12: 1376-85. PMID 12824484 DOI: 10.1110/Ps.0300703 |
0.391 |
|
| 2003 |
Ishima R, Torchia DA. Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach. Journal of Biomolecular Nmr. 25: 243-8. PMID 12652136 DOI: 10.1023/A:1022851228405 |
0.394 |
|
| 2003 |
Louis JM, Ishima R, Nesheiwat I, Pannell LK, Lynch SM, Torchia DA, Gronenborn AM. Revisiting monomeric HIV-1 protease. Characterization and redesign for improved properties. The Journal of Biological Chemistry. 278: 6085-92. PMID 12468541 DOI: 10.1074/Jbc.M209726200 |
0.398 |
|
| 2003 |
Torchia DA, Ishima R. Molecular structure and dynamics of proteins in solution: Insights derived from high-resolution NMR approaches Pure and Applied Chemistry. 75: 1371-1381. DOI: 10.1351/Pac200375101371 |
0.4 |
|
| 2002 |
Jacob J, Louis JM, Nesheiwat I, Torchia DA. Biosynthetically directed fractional 13C labeling facilitates identification of Phe and Tyr aromatic signals in proteins. Journal of Biomolecular Nmr. 24: 231-5. PMID 12522310 DOI: 10.1023/A:1021662423490 |
0.702 |
|
| 2002 |
Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE. An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates. Journal of the American Chemical Society. 124: 10743-53. PMID 12207529 DOI: 10.1021/Ja0204776 |
0.352 |
|
| 2002 |
Freedberg DI, Ishima R, Jacob J, Wang YX, Kustanovich I, Louis JM, Torchia DA. Rapid structural fluctuations of the free HIV protease flaps in solution: relationship to crystal structures and comparison with predictions of dynamics calculations. Protein Science : a Publication of the Protein Society. 11: 221-32. PMID 11790832 DOI: 10.1110/Ps.33202 |
0.705 |
|
| 2001 |
Sayers EW, Torchia DA. Use of the carbonyl chemical shift to relieve degeneracies in triple-resonance assignment experiments. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 153: 246-53. PMID 11740901 DOI: 10.1006/Jmre.2001.2440 |
0.406 |
|
| 2001 |
Ishima R, Louis JM, Torchia DA. Optimized labeling of 13CHD2 methyl isotopomers in perdeuterated proteins: potential advantages for 13C relaxation studies of methyl dynamics of larger proteins. Journal of Biomolecular Nmr. 21: 167-71. PMID 11727980 DOI: 10.1023/A:1012482426306 |
0.357 |
|
| 2001 |
Ishima R, Ghirlando R, Tözsér J, Gronenborn AM, Torchia DA, Louis JM. Folded monomer of HIV-1 protease. The Journal of Biological Chemistry. 276: 49110-6. PMID 11598128 DOI: 10.1074/Jbc.M108136200 |
0.402 |
|
| 2001 |
Markus MA, Triantafillidou D, Choli-Papadopoulou T, Torchia DA. 1H, 15N, and 13C assignments and secondary structure identification for full-length ribosomal protein L11 from Thermus thermophilus. Journal of Biomolecular Nmr. 20: 293-4. PMID 11519754 DOI: 10.1023/A:1011275602138 |
0.4 |
|
| 2001 |
Ishima R, Petkova AP, Louis JM, Torchia DA. Comparison of methyl rotation axis order parameters derived from model-free analyses of (2)H and (13)C longitudinal and transverse relaxation rates measured in the same protein sample. Journal of the American Chemical Society. 123: 6164-71. PMID 11414851 DOI: 10.1021/Ja0104711 |
0.406 |
|
| 2001 |
Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. Biochemical and Biophysical Research Communications. 280: 460-5. PMID 11162539 DOI: 10.1006/Bbrc.2000.4146 |
0.351 |
|
| 2001 |
Ishima R, Louis JM, Torchia DA. Characterization of two hydrophobic methyl clusters in HIV-1 protease by NMR spin relaxation in solution. Journal of Molecular Biology. 305: 515-21. PMID 11152609 DOI: 10.1006/Jmbi.2000.4321 |
0.317 |
|
| 2000 |
Sayers EW, Gerstner RB, Draper DE, Torchia DA. Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy. Biochemistry. 39: 13602-13. PMID 11063598 DOI: 10.1021/Bi0013391 |
0.439 |
|
| 2000 |
Ishima R, Torchia DA. Protein dynamics from NMR. Nature Structural Biology. 7: 740-3. PMID 10966641 DOI: 10.1038/78963 |
0.377 |
|
| 2000 |
Wang YX, Jacob J, Wingfield PT, Palmer I, Stahl SJ, Kaufman JD, Huang PL, Huang PL, Lee-Huang S, Torchia DA. Anti-HIV and anti-tumor protein MAP30, a 30 kDa single-strand type-I RIP, shares similar secondary structure and beta-sheet topology with the A chain of ricin, a type-II RIP. Protein Science : a Publication of the Protein Society. 9: 138-44. PMID 10739256 DOI: 10.1110/Ps.9.1.138 |
0.707 |
|
| 2000 |
Markus M, Gerstner R, Draper D, Torchia D. 1H, 13C, and 15N Chemical Shift Assignments for Ribosomal Protein S4 delta 41 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4577 |
0.404 |
|
| 2000 |
Ishima R, Louis JM, Torchia DA. Transverse13C Relaxation of CHD2Methyl Isotopmers To Detect Slow Conformational Changes of Protein Side Chains [J. Am. Chem. Soc.1999,121, 11589−11590]. Journal of the American Chemical Society. 122: 548-548. DOI: 10.1021/Ja995542Z |
0.318 |
|
| 1999 |
Wang YX, Neamati N, Jacob J, Palmer I, Stahl SJ, Kaufman JD, Huang PL, Huang PL, Winslow HE, Pommier Y, Wingfield PT, Lee-Huang S, Bax A, Torchia DA. Solution structure of anti-HIV-1 and anti-tumor protein MAP30: structural insights into its multiple functions. Cell. 99: 433-42. PMID 10571185 DOI: 10.1016/S0092-8674(00)81529-9 |
0.664 |
|
| 1999 |
Ishima R, Torchia DA. Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. Journal of Biomolecular Nmr. 14: 369-72. PMID 10526408 DOI: 10.1023/A:1008324025406 |
0.34 |
|
| 1999 |
Ishima R, Freedberg DI, Wang YX, Louis JM, Torchia DA. Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function. Structure (London, England : 1993). 7: 1047-55. PMID 10508781 DOI: 10.1016/S0969-2126(99)80172-5 |
0.44 |
|
| 1999 |
Markus MA, Gerstner RB, Draper DE, Torchia DA. Refining the overall structure and subdomain orientation of ribosomal protein S4 delta41 with dipolar couplings measured by NMR in uniaxial liquid crystalline phases. Journal of Molecular Biology. 292: 375-87. PMID 10493882 DOI: 10.1006/Jmbi.1999.3061 |
0.392 |
|
| 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 |
0.709 |
|
| 1999 |
Ishima R, Louis JM, Torchia DA. Transverse 1H cross relaxation in 1H-15N correlated 1H CPMG experiments. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 137: 289-92. PMID 10053163 DOI: 10.1006/Jmre.1998.1672 |
0.349 |
|
| 1999 |
Ishima R, Louis JM, Torchia DA. Transverse 13C relaxation of CHD2 methyl isotopmers to detect slow conformational changes of protein side chains [12] Journal of the American Chemical Society. 121: 11589-11590. DOI: 10.1021/Ja992836B |
0.351 |
|
| 1999 |
Katoh E, Yamazaki T, Kiso Y, Wingfield PT, Stahl SJ, Kaufman JD, Torchia DA. Determination of the rate of monomer interchange in a ligand-bound homodimeric protein from NOESY cross peaks: Application to the HIV protease/KNI-529 complex [6] Journal of the American Chemical Society. 121: 2607-2608. DOI: 10.1021/Ja984041V |
0.311 |
|
| 1998 |
Markus MA, Gerstner RB, Draper DE, Torchia DA. The solution structure of ribosomal protein S4 delta41 reveals two subdomains and a positively charged surface that may interact with RNA. The Embo Journal. 17: 4559-71. PMID 9707416 DOI: 10.1093/Emboj/17.16.4559 |
0.333 |
|
| 1998 |
Copié V, Tomita Y, Akiyama SK, Aota S, Yamada KM, Venable RM, Pastor RW, Krueger S, Torchia DA. Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structure. Journal of Molecular Biology. 277: 663-82. PMID 9533887 DOI: 10.1006/Jmbi.1998.1616 |
0.394 |
|
| 1998 |
Ishima R, Wingfield PT, Stahl SJ, Kaufman JD, Torchia DA. Using amide 1H and 15N transverse relaxation to detect millisecond time-scale motions in perdeuterated proteins: Application to HIV-1 protease Journal of the American Chemical Society. 120: 10534-10542. DOI: 10.1021/Ja981546C |
0.393 |
|
| 1998 |
Freedberg DI, Wang YX, Stahl SJ, Kaufman JD, Wingfield PT, Kiso Y, Torchia DA. Flexibility and function in HIV protease: Dynamics of the HIV-1 protease bound to the asymmetric inhibitor kynostatin 272 (KNI-272) Journal of the American Chemical Society. 120: 7916-7923. DOI: 10.1021/Ja981206R |
0.383 |
|
| 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 |
Hinck AP, Markus MA, Huang S, Grzesiek S, Kustonovich I, Draper DE, Torchia DA. The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA. Journal of Molecular Biology. 274: 101-13. PMID 9398519 DOI: 10.1006/Jmbi.1997.1379 |
0.638 |
|
| 1997 |
Stubbs JT, Mintz KP, Eanes ED, Torchia DA, Fisher LW. Characterization of native and recombinant bone sialoprotein: delineation of the mineral-binding and cell adhesion domains and structural analysis of the RGD domain. Journal of Bone and Mineral Research : the Official Journal of the American Society For Bone and Mineral Research. 12: 1210-22. PMID 9258751 DOI: 10.1359/Jbmr.1997.12.8.1210 |
0.324 |
|
| 1997 |
Markus MA, Hinck AP, Huang S, Draper DE, Torchia DA. High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. Nature Structural Biology. 4: 70-7. PMID 8989327 DOI: 10.1038/Nsb0197-70 |
0.647 |
|
| 1996 |
Pelton JG, Torchia DA, Remington SJ, Murphy KP, Meadow ND, Roseman S. Structures of active site histidine mutants of IIIGlc, a major signal-transducing protein in Escherichia coli. Effects on the mechanisms of regulation and phosphoryl transfer. The Journal of Biological Chemistry. 271: 33446-56. PMID 8969208 DOI: 10.1074/Jbc.271.52.33446 |
0.368 |
|
| 1996 |
Yamazaki T, Hinck AP, Wang YX, Nicholson LK, Torchia DA, Wingfield P, Stahl SJ, Kaufman JD, Chang CH, Domaille PJ, Lam PY. Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy. Protein Science : a Publication of the Protein Society. 5: 495-506. PMID 8868486 DOI: 10.1002/Pro.5560050311 |
0.739 |
|
| 1996 |
Wang YX, Freedberg DI, Grzesiek S, Torchia DA, Wingfield PT, Kaufman JD, Stahl SJ, Chang CH, Hodge CN. Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy. Biochemistry. 35: 12694-704. PMID 8841113 DOI: 10.1021/Bi9610764 |
0.34 |
|
| 1996 |
Copié V, Battles JA, Schwab JM, Torchia DA. Secondary structure of beta-hydroxydecanoyl thiol ester dehydrase, a 39-kDa protein, derived from H alpha, C alpha, C beta and CO signal assignments and the Chemical Shift Index: comparison with the crystal structure. Journal of Biomolecular Nmr. 7: 335-40. PMID 8765740 DOI: 10.1007/Bf00200435 |
0.415 |
|
| 1996 |
Wang YX, Freedberg DI, Yamazaki T, Wingfield PT, Stahl SJ, Kaufman JD, Kiso Y, Torchia DA. Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272. Biochemistry. 35: 9945-50. PMID 8756455 DOI: 10.1021/Bi961268Z |
0.374 |
|
| 1996 |
Hinck AP, Archer SJ, Qian SW, Roberts AB, Sporn MB, Weatherbee JA, Tsang ML, Lucas R, Zhang BL, Wenker J, Torchia DA. Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2. Biochemistry. 35: 8517-34. PMID 8679613 DOI: 10.1021/Bi9604946 |
0.605 |
|
| 1996 |
Wang YX, Freedberg DI, Wingfield PT, Stahl SJ, Kaufman JD, Kiso Y, Bhat TN, Erickson JW, Torchia DA. Bound water molecules at the interface between the HIV-1 protease and a potent inhibitor, KNI-272, determined by NMR Journal of the American Chemical Society. 118: 12287-12290. DOI: 10.1021/Ja962612I |
0.313 |
|
| 1995 |
Farrow NA, Zhang O, Szabo A, Torchia DA, Kay LE. Spectral density function mapping using 15N relaxation data exclusively. Journal of Biomolecular Nmr. 6: 153-62. PMID 8589604 DOI: 10.1007/Bf00211779 |
0.37 |
|
| 1995 |
Nicholson LK, Yamazaki T, Torchia DA, Grzesiek S, Bax A, Stahl SJ, Kaufman JD, Wingfield PT, Lam PY, Jadhav PK. Flexibility and function in HIV-1 protease. Nature Structural Biology. 2: 274-80. PMID 7796263 DOI: 10.1038/Nsb0495-274 |
0.64 |
|
| 1994 |
Yamazaki T, Nicholson LK, Torchia DA, Stahl SJ, Kaufman JD, Wingfield PT, Domaille PJ, Campbell-Burk S. Secondary structure and signal assignments of human-immunodeficiency-virus-1 protease complexed to a novel, structure-based inhibitor. European Journal of Biochemistry / Febs. 219: 707-12. PMID 8307036 DOI: 10.1111/J.1432-1033.1994.Tb19987.X |
0.663 |
|
| 1994 |
Archer SJ, Vinson VK, Pollard TD, Torchia DA. Elucidation of the poly-L-proline binding site in Acanthamoeba profilin I by NMR spectroscopy. Febs Letters. 337: 145-51. PMID 8287969 DOI: 10.1016/0014-5793(94)80262-9 |
0.342 |
|
| 1994 |
Yamazaki T, Nicholson LK, Torchia DA, Wingfield P, Stahl SJ, Kaufman JD, Eyermann CJ, Hodge CN, Lam PYS, Ru Y, Jadhav PK, Chang CH, Weber PC. NMR and X-ray evidence that the HIV protease catalytic aspartyl groups are protonated in the complex formed by the protease and a non-peptide cyclic urea-based inhibitor Journal of the American Chemical Society. 116: 10791-10792. DOI: 10.1021/Ja00102A057 |
0.616 |
|
| 1994 |
Grzesiek S, Bax A, Nicholson LK, Yamazaki T, Wingfield P, Stahl SJ, Eyermann CJ, Torchia DA, Nicholas Hodge C, Lam PYS, Jadhav PK, Chang CH. NMR evidence for the displacement of a conserved interior water molecule in HIV protease by a non-peptide cyclic urea-based inhibitor Journal of the American Chemical Society. 116: 1581-1582. DOI: 10.1021/Ja00083A058 |
0.612 |
|
| 1993 |
Pelton JG, Torchia DA, Meadow ND, Roseman S. Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Science : a Publication of the Protein Society. 2: 543-58. PMID 8518729 DOI: 10.1002/Pro.5560020406 |
0.428 |
|
| 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 |
0.409 |
|
| 1993 |
Archer SJ, Vinson VK, Pollard TD, Torchia DA. Secondary structure and topology of Acanthamoeba profilin I as determined by heteronuclear nuclear magnetic resonance spectroscopy. Biochemistry. 32: 6680-7. PMID 8329394 DOI: 10.1021/Bi00077A022 |
0.431 |
|
| 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 |
0.658 |
|
| 1992 |
Pelton JG, Torchia DA, Meadow ND, Roseman S. Structural comparison of phosphorylated and unphosphorylated forms of IIIGlc, a signal-transducing protein from Escherichia coli, using three-dimensional NMR techniques. Biochemistry. 31: 5215-24. PMID 1606145 DOI: 10.1021/Bi00137A017 |
0.437 |
|
| 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 |
0.605 |
|
| 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 |
0.61 |
|
| 1991 |
Baldisseri DM, Torchia DA, Poole LB, Gerlt JA. Deletion of the omega-loop in the active site of staphylococcal nuclease. 2. Effects on protein structure and dynamics. Biochemistry. 30: 3628-33. PMID 2015220 DOI: 10.1021/Bi00229A006 |
0.343 |
|
| 1991 |
Pelton JG, Torchia DA, Meadow ND, Wong CY, Roseman S. Secondary structure of the phosphocarrier protein IIIGlc, a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 88: 3479-83. PMID 2014267 DOI: 10.1073/Pnas.88.8.3479 |
0.43 |
|
| 1991 |
Pelton JG, Torchia DA, Meadow ND, Wong CY, Roseman S. 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques. Biochemistry. 30: 10043-57. PMID 1911770 DOI: 10.1021/Bi00105A032 |
0.356 |
|
| 1991 |
Baldisseri DM, Pelton JG, Sparks SW, Torchia DA. Complete 1H and 13C assignment of Lys and Leu sidechains of staphylococcal nuclease using HCCH-COSY and HCCH-TOCSY 3D NMR spectroscopy. Febs Letters. 281: 33-8. PMID 1901804 DOI: 10.1016/0014-5793(91)80352-4 |
0.433 |
|
| 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 |
0.344 |
|
| 1991 |
Mack JW, Torchia DA. A deuteron NMR study of the molecular dynamics of solid cyclopentane The Journal of Physical Chemistry. 95: 4207-4213. DOI: 10.1021/J100164A009 |
0.326 |
|
| 1991 |
Cole HBR, Torchia DA. An NMR study of the backbone dynamics of staphylococcal nuclease in the crystalline state Chemical Physics. 158: 271-281. DOI: 10.1016/0301-0104(91)87071-3 |
0.394 |
|
| 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 |
0.389 |
|
| 1991 |
Kay LE, Torchia DA. The effects of dipolar cross correlation on 13C methyl-carbon T1, T2, and NOE measurements in macromolecules Journal of Magnetic Resonance (1969). 95: 536-547. DOI: 10.1016/0022-2364(91)90167-R |
0.355 |
|
| 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 |
0.413 |
|
| 1990 |
Hiyama Y, Torchia DA. Heterogeneity of intact collagen by solid state multinuclear magnetic resonance. Basic Life Sciences. 56: 273-85. PMID 2078174 DOI: 10.1007/978-1-4684-5868-8_15 |
0.304 |
|
| 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 |
0.375 |
|
| 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 |
0.359 |
|
| 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 |
0.431 |
|
| 1989 |
Torchia DA, Sparks SW, Bax A. Staphylococcal nuclease: sequential assignments and solution structure. Biochemistry. 28: 5509-24. PMID 2673349 DOI: 10.1021/Bi00439A028 |
0.444 |
|
| 1989 |
Hiyama Y, Roy S, Cohen JS, Torchia DA. Solid-state deuterium NMR study of thymidine. Base rigidity and ribose ring flexibility in deoxynucleosides Journal of the American Chemical Society. 111: 8609-8613. DOI: 10.1021/Ja00205A008 |
0.304 |
|
| 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 |
0.302 |
|
| 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 |
0.349 |
|
| 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 |
0.347 |
|
| 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 |
0.351 |
|
| 1988 |
Cole HB, Sparks SW, Torchia DA. Comparison of the solution and crystal structures of staphylococcal nuclease with 13C and 15N chemical shifts used as structural fingerprints. Proceedings of the National Academy of Sciences of the United States of America. 85: 6362-5. PMID 3413101 DOI: 10.1073/Pnas.85.17.6362 |
0.422 |
|
| 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 |
0.393 |
|
| 1988 |
Mack JW, Torchia DA, Steinert PM. Solid-state NMR studies of the dynamics and structure of mouse keratin intermediate filaments. Biochemistry. 27: 5418-26. PMID 2460129 DOI: 10.1021/Bi00415A006 |
0.413 |
|
| 1988 |
Hiyama Y, Niu CH, Silverton JV, Bavoso A, Torchia DA. Determination of 15N chemical shift tensor via 15N-2H dipolar coupling in Boc-glycylglycyl[15N]glycine benzyl ester Journal of the American Chemical Society. 110: 2378-2383. DOI: 10.1021/Ja00216A006 |
0.326 |
|
| 1987 |
Sarkar SK, Hiyama Y, Niu CH, Young PE, Gerig JT, Torchia DA. Molecular dynamics of collagen side chains in hard and soft tissues. A multinuclear magnetic resonance study. Biochemistry. 26: 6793-800. PMID 3427044 DOI: 10.1021/Bi00395A032 |
0.385 |
|
| 1987 |
Shindo H, Hiyama Y, Roy S, Cohen JS, Torchia DA. Deuterium Nuclear Magnetic Resonance of Oriented DNA Fibers Bulletin of the Chemical Society of Japan. 60: 1631-1640. DOI: 10.1246/Bcsj.60.1631 |
0.319 |
|
| 1987 |
Hiyama Y, Roy S, Guo K, Butler LG, Torchia DA. Unusual asymmetry of methyl deuterium EFG in thymine: a solid state deuterium NMR and ab initio MO study Journal of the American Chemical Society. 109: 2525-2526. DOI: 10.1021/Ja00242A054 |
0.356 |
|
| 1987 |
Hiyama Y, Woyciesjes PM, Brown TL, Torchia DA. Magnesium-25 nuclear quadrupole resonance Journal of Magnetic Resonance (1969). 72: 1-12. DOI: 10.1016/0022-2364(87)90172-7 |
0.344 |
|
| 1986 |
Hiyama Y, Silverton JV, Torchia DA, Gerig JT, Hammond SJ. Molecular structure and dynamics of crystalline p-fluoro-D,L-phenylalanine. A combined X-ray/NMR investigation Journal of the American Chemical Society®. 108: 2715-2723. DOI: 10.1021/Ja00270A034 |
0.313 |
|
| 1986 |
Roy S, Hiyama Y, Torchia DA, Cohen JS. New enzymic synthesis of 2'-deoxynucleoside-2',2'-d2 and the determination of sugar ring flexibility by solid-state deuterium NMR Journal of the American Chemical Society. 108: 1675-1678. DOI: 10.1021/Ja00267A043 |
0.302 |
|
| 1985 |
Sarkar SK, Sullivan CE, Torchia DA. Nanosecond fluctuations of the molecular backbone of collagen in hard and soft tissues: a carbon-13 nuclear magnetic resonance relaxation study. Biochemistry. 24: 2348-54. PMID 3995016 DOI: 10.1021/Bi00330A033 |
0.406 |
|
| 1985 |
Torchia DA, Szabo A. The information content of powder lineshapes in the fast motion limit Journal of Magnetic Resonance (1969). 64: 135-141. DOI: 10.1016/0022-2364(85)90041-1 |
0.329 |
|
| 1985 |
Torchia DA, Hiyama Y, Sarkar SK. Multinuclear magnetic resonance studies of collagen molecular structure and dynamics Biopolymers. 24: 65-75. DOI: 10.1002/Bip.360240107 |
0.331 |
|
| 1984 |
Sarkar SK, Young PE, Sullivan CE, Torchia DA. Detection of cis and trans X-Pro peptide bonds in proteins by 13C NMR: application to collagen. Proceedings of the National Academy of Sciences of the United States of America. 81: 4800-3. PMID 6589627 DOI: 10.1073/Pnas.81.15.4800 |
0.367 |
|
| 1984 |
Sarkar SK, Torchia DA, Kopple KD, VanderHart DL. Study of proline peptide bond conformation and ring dynamics in crystalline cyclic peptides using carbon-13 MAS NMR Journal of the American Chemical Society. 106: 3328-3331. DOI: 10.1021/Ja00323A044 |
0.322 |
|
| 1984 |
Harbison GS, Jelinski LW, Stark RE, Torchia DA, Herzfeld J, Griffin RG. 15N chemical shift and 15N-13C dipolar tensors for the peptide bond in [1-13C]glycyl[15N]glycine hydrochloride monohydrate Journal of Magnetic Resonance (1969). 60: 79-82. DOI: 10.1016/0022-2364(84)90027-1 |
0.629 |
|
| 1984 |
Sarkar SK, Torchia DA, Kopple KD, Vanderhart DL. Study Of Proline Peptide Bond Conformation And Ring Dynamics In Crystalline Cyclic Peptides Using Carbon-13 Mas Nmr Cheminform. 15. DOI: 10.1002/Chin.198436058 |
0.313 |
|
| 1983 |
Torchia DA, Batchelder LS, Fleming WW, Jelinski LW, Sarkar SK, Sullivan CE. Mobility and function in elastin and collagen. Ciba Foundation Symposium. 93: 98-115. PMID 6551234 DOI: 10.1002/9780470720752.ch6 |
0.606 |
|
| 1983 |
Batchelder LS, Niu CH, Torchia DA. Methyl reorientation in polycrystalline amino acids and peptides: a deuteron NMR spin-lattice relaxation study Journal of the American Chemical Society. 105: 2228-2231. DOI: 10.1021/Ja00346A021 |
0.31 |
|
| 1983 |
Stark RE, Jelinski LW, Ruben DJ, Torchia DA, Griffin RG. 13C chemical shift and 13C-15N dipolar tensors for the peptide bond: [1-13C]glycyl[15N]glycine·HCl·H2O Journal of Magnetic Resonance (1969). 55: 266-273. DOI: 10.1016/0022-2364(83)90238-X |
0.648 |
|
| 1982 |
Ackerman SK, Noguchi CT, Schechter AN, Torchia DA. Proton-enhanced 13C NMR of normal human erythrocytes: characterization of motionally restricted molecules. Biochemical and Biophysical Research Communications. 106: 1161-8. PMID 7115395 DOI: 10.1016/0006-291X(82)91234-7 |
0.353 |
|
| 1982 |
Batchelder LS, Sullivan CE, Jelinski LW, Torchia DA. Characterization of leucine side-chain reorientation in collagen-fibrils by solid-state 2H NMR. Proceedings of the National Academy of Sciences of the United States of America. 79: 386-9. PMID 6952191 DOI: 10.1073/Pnas.79.2.386 |
0.67 |
|
| 1982 |
Torchia DA, Szabo A. Spin-lattice relaxation in solids Journal of Magnetic Resonance (1969). 49: 107-121. DOI: 10.1016/0022-2364(82)90301-8 |
0.301 |
|
| 1981 |
Torchia DA, Hasson MA, Hascall VC. 13C nuclear magnetic resonance suggests a flexible proteoglycan core protein. The Journal of Biological Chemistry. 256: 7129-38. PMID 6788760 |
0.328 |
|
| 1980 |
Jelinski LW, Torchia DA. Investigation of labeled amino acid side-chain motion in collagen using 13C nuclear magnetic resonance. Journal of Molecular Biology. 138: 255-72. PMID 7411609 DOI: 10.1016/0022-2836(80)90286-7 |
0.667 |
|
| 1980 |
Jelinski LW, Sullivan CE, Torchia DA. 2H NMR study of molecular motion in collagen fibrils. Nature. 284: 531-4. PMID 7366722 DOI: 10.1038/284531A0 |
0.635 |
|
| 1980 |
Jelinski LW, Sullivan CE, Batchelder LS, Torchia DA. Deuterium nuclear magnetic resonance of specifically labeled native collagen. Investigation of protein molecular dynamics using the quadrupolar echo technique. Biophysical Journal. 32: 515-29. PMID 7248459 DOI: 10.1016/S0006-3495(80)84987-3 |
0.671 |
|
| 1980 |
Jelinski LW, Sullivan C, Torchia D. Effect of proton spin diffusion on the 13C-{1H} NOE in hydrated macromolecules Journal of Magnetic Resonance (1969). 41: 133-139. DOI: 10.1016/0022-2364(80)90209-7 |
0.636 |
|
| 1979 |
Jelinski LW, Torchia DA. 13C/1H high power double magnetic resonance investigation of collagen backbone motion in fibrils and in solution. Journal of Molecular Biology. 133: 45-65. PMID 529282 DOI: 10.1016/0022-2836(79)90250-X |
0.655 |
|
| 1979 |
Noguchi CT, Torchia DA, Schechter AN. 13C NMR quantitation of polymer in deoxyhemoglobin S gels. Proceedings of the National Academy of Sciences of the United States of America. 76: 4936-40. PMID 291911 DOI: 10.1073/Pnas.76.10.4936 |
0.337 |
|
| 1976 |
Torchia DA, VanderHart DL. 13C Magnetic resonance evidence for anisotropic molecular motion in collagen fibrils. Journal of Molecular Biology. 104: 315-21. PMID 957438 DOI: 10.1016/0022-2836(76)90018-8 |
0.399 |
|
| 1975 |
Piez KA, Torchia DA. Possible contribution of ionic clustering to molecular packing of collagen. Nature. 258: 87. PMID 1186888 DOI: 10.1038/258087A0 |
0.335 |
|
| 1972 |
Torchia DA, Wong SC, Deber CM, Blout ER. Cyclic peptides. 3. Solution conformations of cyclo(serylprolylglycylserylprolylglycyl) from nuclear magnetic resonance. Journal of the American Chemical Society. 94: 616-20. PMID 5060992 DOI: 10.1021/Ja00757A049 |
0.319 |
|
| 1972 |
Torchia DA, Di Corato A, Wong SC, Deber CM, Blout ER. Cyclic peptides. II. Solution conformations of cyclo(ProlyLserylglycylprolylserylglycyl) from nuclear magnetic resonance. Journal of the American Chemical Society. 94: 609-15. PMID 5060991 DOI: 10.1021/Ja00757A048 |
0.315 |
|
| 1972 |
Deber CM, Torchia DA, Wong SC, Blout ER. Conformational interconversions of the cyclic hexapeptide cyclo(Pro-Gly) 3 . Proceedings of the National Academy of Sciences of the United States of America. 69: 1825-9. PMID 4505660 DOI: 10.1073/Pnas.69.7.1825 |
0.371 |
|
| 1971 |
Deber CM, Torchia DA, Blout ER. Cyclic peptides. I. Cyclo(tri-l-prolyl) and derivatives. Synthesis and molecular conformation from nuclear magnetic resonance. Journal of the American Chemical Society. 93: 4893-7. PMID 5118215 DOI: 10.1021/Ja00748A038 |
0.316 |
|
| 1967 |
Breit G, Polak JA, Torchia DA. N14(N14, N13)N15 reaction at low energies and the elastic scattering of N14 by N14 Physical Review. 161: 993-1005. DOI: 10.1103/Physrev.161.993 |
0.441 |
|
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