| Year |
Citation |
Score |
| 2019 |
Orlovsky NI, Al-Hashimi HM, Oas TG. Exposing hidden high-affinity RNA conformational states. Journal of the American Chemical Society. PMID 31815464 DOI: 10.1021/Jacs.9B10535 |
0.39 |
|
| 2018 |
Qi Y, Martin JW, Barb AW, Thélot F, Yan A, Donald BR, Oas TG. Continuous Interdomain Orientation Distributions Reveal Components of Binding Thermodynamics. Journal of Molecular Biology. PMID 29924964 DOI: 10.1016/J.Jmb.2018.06.022 |
0.322 |
|
| 2016 |
Shah R, Ohashi T, Erickson HP, Oas TG. Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: Thermodynamic Stability Correlates with Rates of Unfolding Rather than Folding. The Journal of Biological Chemistry. PMID 27909052 DOI: 10.1074/Jbc.M116.760371 |
0.423 |
|
| 2015 |
Mosley PL, Daniels KG, Oas TG. Electrostatic Energetics of Bacillus subtilis Ribonuclease P Protein Determined by Nuclear Magnetic Resonance-Based Histidine pKa Measurements. Biochemistry. 54: 5379-88. PMID 26267651 DOI: 10.1021/Acs.Biochem.5B00138 |
0.395 |
|
| 2015 |
Daniels KG, Suo Y, Oas TG. Conformational kinetics reveals affinities of protein conformational states. Proceedings of the National Academy of Sciences of the United States of America. 112: 9352-7. PMID 26162682 DOI: 10.1073/Pnas.1502084112 |
0.453 |
|
| 2015 |
Deis LN, Wu Q, Wang Y, Qi Y, Daniels KG, Zhou P, Oas TG. Suppression of conformational heterogeneity at a protein-protein interface. Proceedings of the National Academy of Sciences of the United States of America. 112: 9028-33. PMID 26157136 DOI: 10.1073/Pnas.1424724112 |
0.459 |
|
| 2015 |
Deis LN, Wu Q, Wang Y, Qi Y, Daniels KG, Zhou P, Oas TG. Suppression of conformational heterogeneity at a protein-protein interface Proceedings of the National Academy of Sciences of the United States of America. 112: 9028-9033. DOI: 10.1073/pnas.1424724112 |
0.332 |
|
| 2015 |
Qi Y, Martin JW, Yan A, Thelot F, Donald BR, Oas TG. Visualizing the Inter-Domain Motions of a Pathogenic Protein using Sparse RDC Data Biophysical Journal. 108: 58a. DOI: 10.1016/J.Bpj.2014.11.353 |
0.388 |
|
| 2014 |
Deis LN, Pemble CW, Qi Y, Hagarman A, Richardson DC, Richardson JS, Oas TG. Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity. Structure (London, England : 1993). 22: 1467-77. PMID 25295398 DOI: 10.1016/J.Str.2014.08.014 |
0.409 |
|
| 2014 |
Capp JA, Hagarman A, Richardson DC, Oas TG. The statistical conformation of a highly flexible protein: small-angle X-ray scattering of S. aureus protein A. Structure (London, England : 1993). 22: 1184-95. PMID 25087509 DOI: 10.1016/J.Str.2014.06.011 |
0.437 |
|
| 2014 |
Daniels KG, Tonthat NK, McClure DR, Chang YC, Liu X, Schumacher MA, Fierke CA, Schmidler SC, Oas TG. Ligand concentration regulates the pathways of coupled protein folding and binding. Journal of the American Chemical Society. 136: 822-5. PMID 24364358 DOI: 10.1021/Ja4086726 |
0.64 |
|
| 2014 |
Shah RS, Oas TG, Erickson HP. Determining the Rate of Unfolding and Refolding of FNIII Domains by Labeling Buried Cysteine Biophysical Journal. 106: 258a. DOI: 10.1016/J.Bpj.2013.11.1516 |
0.325 |
|
| 2011 |
Kahsai AW, Xiao K, Rajagopal S, Ahn S, Shukla AK, Sun J, Oas TG, Lefkowitz RJ. Multiple ligand-specific conformations of the β2-adrenergic receptor. Nature Chemical Biology. 7: 692-700. PMID 21857662 DOI: 10.1038/Nchembio.634 |
0.348 |
|
| 2011 |
Isom DG, Marguet PR, Oas TG, Hellinga HW. A miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity. Proteins. 79: 1034-47. PMID 21387407 DOI: 10.1002/Prot.22932 |
0.471 |
|
| 2011 |
Hagarman A, Franch WR, Oas TG. Biophysical Characterization of the Igg Binding Domains of Protein a In Staphylococcus Aureus Biophysical Journal. 100: 227a. DOI: 10.1016/J.Bpj.2010.12.1452 |
0.439 |
|
| 2010 |
Chang YC, Franch WR, Oas TG. Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance. Biochemistry. 49: 9428-37. PMID 20843005 DOI: 10.1021/Bi100287Y |
0.719 |
|
| 2010 |
Chang YC, Oas TG. Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand. Biochemistry. 49: 5086-96. PMID 20476778 DOI: 10.1021/Bi100222H |
0.697 |
|
| 2010 |
Isom DG, Vardy E, Oas TG, Hellinga HW. Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. Proceedings of the National Academy of Sciences of the United States of America. 107: 4908-13. PMID 20194783 DOI: 10.1073/Pnas.0910421107 |
0.45 |
|
| 2009 |
Hammes GG, Chang YC, Oas TG. Conformational selection or induced fit: a flux description of reaction mechanism. Proceedings of the National Academy of Sciences of the United States of America. 106: 13737-41. PMID 19666553 DOI: 10.1073/Pnas.0907195106 |
0.597 |
|
| 2007 |
Henkels CH, Chang YC, Chamberlin SI, Oas TG. Dynamics of backbone conformational heterogeneity in Bacillus subtilis ribonuclease P protein. Biochemistry. 46: 15062-75. PMID 18052200 DOI: 10.1021/Bi701425N |
0.781 |
|
| 2007 |
Schmidler SC, Lucas JE, Oas TG. Statistical estimation of statistical mechanical models: helix-coil theory and peptide helicity prediction. Journal of Computational Biology : a Journal of Computational Molecular Cell Biology. 14: 1287-310. PMID 18047425 DOI: 10.1089/Cmb.2007.0008 |
0.303 |
|
| 2007 |
Nobles KN, Guan Z, Xiao K, Oas TG, Lefkowitz RJ. The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2. The Journal of Biological Chemistry. 282: 21370-81. PMID 17513300 DOI: 10.1074/Jbc.M611483200 |
0.31 |
|
| 2007 |
Valiaev A, Lim DW, Oas TG, Chilkoti A, Zauscher S. Force-induced prolyl cis-trans isomerization in elastin-like polypeptides. Journal of the American Chemical Society. 129: 6491-7. PMID 17469821 DOI: 10.1021/Ja070147R |
0.327 |
|
| 2007 |
Chugha P, Oas TG. Backbone dynamics of the monomeric lambda repressor denatured state ensemble under nondenaturing conditions. Biochemistry. 46: 1141-51. PMID 17260944 DOI: 10.1021/Bi061371G |
0.783 |
|
| 2006 |
Arora P, Hammes GG, Oas TG. Folding mechanism of a multiple independently-folding domain protein: double B domain of protein A. Biochemistry. 45: 12312-24. PMID 17014084 DOI: 10.1021/Bi060923S |
0.598 |
|
| 2006 |
Henkels CH, Oas TG. Ligation-state hydrogen exchange: coupled binding and folding equilibria in ribonuclease P protein. Journal of the American Chemical Society. 128: 7772-81. PMID 16771491 DOI: 10.1021/Ja057279+ |
0.796 |
|
| 2006 |
Hilser VJ, García-Moreno E B, Oas TG, Kapp G, Whitten ST. A statistical thermodynamic model of the protein ensemble. Chemical Reviews. 106: 1545-58. PMID 16683744 DOI: 10.1021/Cr040423+ |
0.746 |
|
| 2006 |
Chugha P, Sage HJ, Oas TG. Methionine oxidation of monomeric lambda repressor: the denatured state ensemble under nondenaturing conditions. Protein Science : a Publication of the Protein Society. 15: 533-42. PMID 16452618 DOI: 10.1110/Ps.051856406 |
0.782 |
|
| 2005 |
Henkels CH, Oas TG. Thermodynamic characterization of the osmolyte- and ligand-folded states of Bacillus subtilis ribonuclease P protein. Biochemistry. 44: 13014-26. PMID 16185070 DOI: 10.1021/Bi0504613 |
0.79 |
|
| 2004 |
Kapp GT, Richardson JS, Oas TG. Kinetic role of helix caps in protein folding is context-dependent. Biochemistry. 43: 3814-23. PMID 15049688 DOI: 10.1021/Bi035683K |
0.78 |
|
| 2004 |
Arora P, Oas TG, Myers JK. Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsec. Protein Science : a Publication of the Protein Society. 13: 847-53. PMID 15044721 DOI: 10.1110/Ps.03541304 |
0.578 |
|
| 2004 |
Vu DM, Myers JK, Oas TG, Dyer RB. Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein. Biochemistry. 43: 3582-9. PMID 15035628 DOI: 10.1021/Bi036203S |
0.459 |
|
| 2004 |
Dimitriadis G, Drysdale A, Myers JK, Arora P, Radford SE, Oas TG, Smith DA. Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump. Proceedings of the National Academy of Sciences of the United States of America. 101: 3809-14. PMID 15007169 DOI: 10.1073/pnas.0306433101 |
0.556 |
|
| 2003 |
Hanson WM, Beeser SA, Oas TG, Goldenberg DP. Identification of a residue critical for maintaining the functional conformation of BPTI. Journal of Molecular Biology. 333: 425-41. PMID 14529627 DOI: 10.1016/J.Jmb.2003.08.023 |
0.463 |
|
| 2002 |
Powell KD, Ghaemmaghami S, Wang MZ, Ma L, Oas TG, Fitzgerald MC. A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution. Journal of the American Chemical Society. 124: 10256-7. PMID 12197709 DOI: 10.1021/Ja026574G |
0.598 |
|
| 2002 |
Myers JK, Oas TG. Mechanism of fast protein folding. Annual Review of Biochemistry. 71: 783-815. PMID 12045111 DOI: 10.1146/Annurev.Biochem.71.110601.135346 |
0.452 |
|
| 2001 |
Ghaemmaghami S, Oas TG. Quantitative protein stability measurement in vivo. Nature Structural Biology. 8: 879-82. PMID 11573094 DOI: 10.1038/Nsb1001-879 |
0.653 |
|
| 2001 |
Myers JK, Morris DP, Greenleaf AL, Oas TG. Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1. Biochemistry. 40: 8479-86. PMID 11456485 DOI: 10.1021/Bi0027884 |
0.31 |
|
| 2001 |
Myers JK, Oas TG. Preorganized secondary structure as an important determinant of fast protein folding. Nature Structural Biology. 8: 552-8. PMID 11373626 DOI: 10.1038/88626 |
0.472 |
|
| 2001 |
Henkels CH, Kurz JC, Fierke CA, Oas TG. Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. Biochemistry. 40: 2777-89. PMID 11258888 DOI: 10.1021/Bi002078Y |
0.794 |
|
| 2000 |
Ghaemmaghami S, Fitzgerald MC, Oas TG. A quantitative, high-throughput screen for protein stability. Proceedings of the National Academy of Sciences of the United States of America. 97: 8296-301. PMID 10890887 DOI: 10.1073/Pnas.140111397 |
0.654 |
|
| 2000 |
Burton RE, Hunt JA, Fierke CA, Oas TG. Novel disulfide engineering in human carbonic anhydrase II using the PAIRWISE side-chain geometry database. Protein Science : a Publication of the Protein Society. 9: 776-85. PMID 10794421 DOI: 10.1110/Ps.9.4.776 |
0.421 |
|
| 1999 |
Myers JK, Oas TG. Reinterpretation of GCN4-p1 folding kinetics: partial helix formation precedes dimerization in coiled coil folding. Journal of Molecular Biology. 289: 205-9. PMID 10366499 DOI: 10.1006/Jmbi.1999.2747 |
0.432 |
|
| 1999 |
Myers JK, Oas TG. Contribution of a buried hydrogen bond to lambda repressor folding kinetics. Biochemistry. 38: 6761-8. PMID 10346896 DOI: 10.1021/Bi990088X |
0.399 |
|
| 1998 |
Beeser SA, Oas TG, Goldenberg DP. Determinants of backbone dynamics in native BPTI: cooperative influence of the 14-38 disulfide and the Tyr35 side-chain. Journal of Molecular Biology. 284: 1581-96. PMID 9878372 DOI: 10.1006/Jmbi.1998.2240 |
0.454 |
|
| 1998 |
Hilser VJ, Dowdy D, Oas TG, Freire E. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. Proceedings of the National Academy of Sciences of the United States of America. 95: 9903-8. PMID 9707573 DOI: 10.1073/Pnas.95.17.9903 |
0.42 |
|
| 1998 |
Ghaemmaghami S, Word JM, Burton RE, Richardson JS, Oas TG. Folding kinetics of a fluorescent variant of monomeric lambda repressor. Biochemistry. 37: 9179-85. PMID 9636065 DOI: 10.1021/bi980356b |
0.615 |
|
| 1998 |
Burton RE, Myers JK, Oas TG. Protein folding dynamics: quantitative comparison between theory and experiment. Biochemistry. 37: 5337-43. PMID 9548914 DOI: 10.1021/Bi980245C |
0.422 |
|
| 1997 |
Beeser SA, Goldenberg DP, Oas TG. Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI. Journal of Molecular Biology. 269: 154-64. PMID 9193007 DOI: 10.1006/Jmbi.1997.1031 |
0.476 |
|
| 1997 |
Burton RE, Huang GS, Daugherty MA, Calderone TL, Oas TG. The energy landscape of a fast-folding protein mapped by Ala-->Gly substitutions. Nature Structural Biology. 4: 305-10. PMID 9095199 DOI: 10.1038/Nsb0497-305 |
0.463 |
|
| 1996 |
Burton RE, Huang GS, Daugherty MA, Fullbright PW, Oas TG. Microsecond protein folding through a compact transition state. Journal of Molecular Biology. 263: 311-22. PMID 8913309 DOI: 10.1006/Jmbi.1996.0577 |
0.43 |
|
| 1996 |
Calderone TL, Stevens RD, Oas TG. High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli. Journal of Molecular Biology. 262: 407-12. PMID 8893852 DOI: 10.1006/Jmbi.1996.0524 |
0.327 |
|
| 1996 |
Huang GS, Oas TG. Heat and cold denatured states of monomeric lambda repressor are thermodynamically and conformationally equivalent. Biochemistry. 35: 6173-80. PMID 8639557 DOI: 10.1021/Bi960250L |
0.408 |
|
| 1995 |
Huang GS, Oas TG. Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding. Biochemistry. 34: 3884-92. PMID 7696251 DOI: 10.1021/Bi00012A003 |
0.493 |
|
| 1995 |
Huang GS, Oas TG. Submillisecond folding of monomeric lambda repressor. Proceedings of the National Academy of Sciences of the United States of America. 92: 6878-82. PMID 7624336 DOI: 10.1073/Pnas.92.15.6878 |
0.471 |
|
| 1994 |
Wild C, Dubay JW, Greenwell T, Baird T, Oas TG, McDanal C, Hunter E, Matthews T. Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proceedings of the National Academy of Sciences of the United States of America. 91: 12676-80. PMID 7809100 DOI: 10.1073/Pnas.91.26.12676 |
0.313 |
|
| 1992 |
Wild C, Oas T, Mcdanal C, Bolognesi D, Matthews T. A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition Proceedings of the National Academy of Sciences of the United States of America. 89: 10537-10541. PMID 1438243 DOI: 10.1073/Pnas.89.21.10537 |
0.308 |
|
| 1990 |
Oas TG, McIntosh LP, O'Shea EK, Dahlquist FW, Kim PS. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry. 29: 2891-4. PMID 2337572 DOI: 10.1021/Bi00464A001 |
0.737 |
|
| 1990 |
Copié V, Kolbert AC, Drewry DH, Bartlett PA, Oas TG, Griffin RG. Inhibition of thermolysin by phosphonamidate transition-state analogues: measurement of 31P-15N bond lengths and chemical shifts in two enzyme-inhibitor complexes by solid-state nuclear magnetic resonance. Biochemistry. 29: 9176-84. PMID 2271586 DOI: 10.1021/Bi00491A011 |
0.72 |
|
| 1989 |
Oas TG, Hartzell CJ, Drobny GP, Dahlquist FW. Selective NMR detection of 13C15N dipole pairs in solid samples Journal of Magnetic Resonance (1969). 81: 395-399. DOI: 10.1016/0022-2364(89)90072-3 |
0.512 |
|
| 1988 |
Oas TG, Kim PS. A peptide model of a protein folding intermediate. Nature. 336: 42-8. PMID 3185721 DOI: 10.1038/336042A0 |
0.565 |
|
| 1988 |
Oas TG, Griffin RG, Levitt MH. Rotary resonance recoupling of dipolar interactions in solid‐state nuclear magnetic resonance spectroscopy The Journal of Chemical Physics. 89: 692-695. DOI: 10.1063/1.455191 |
0.593 |
|
| 1988 |
Raleigh DP, Kolbert AC, Oas TG, Levitt MH, Griffin RG. Enhancement of the effect of small anisotropies in magic-angle spinning nuclear magnetic resonance Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases. 84: 3691-3711. DOI: 10.1039/F19888403691 |
0.663 |
|
| 1988 |
Levitt MH, Oas TG, Griffin RG. Rotary Resonance Recoupling in Heteronuclear Spin Pair Systems Israel Journal of Chemistry. 28: 271-282. DOI: 10.1002/Ijch.198800039 |
0.593 |
|
| 1987 |
Oas TG, Hartzell CJ, Dahlquist FW, Drobny GP. The amide 15N chemical shift tensors of four peptides determined from 13C dipole-coupled chemical shift powder patterns Journal of the American Chemical Society. 109: 5962-5966. DOI: 10.1021/Ja00254A011 |
0.559 |
|
| 1987 |
Oas TG, Hartzell CJ, McMahon TJ, Drobny GP, Dahlquist FW. The carbonyl 13C chemical shift tensors of five peptides determined from 15N dipole-coupled chemical shift powder patterns Journal of the American Chemical Society. 109: 5956-5962. DOI: 10.1021/Ja00254A010 |
0.557 |
|
| 1987 |
GRIFFEY RH, REDFIELD AG, MCINTOSH LP, OAS TG, DAHLQUIST FW. ChemInform Abstract: Assignment of Proton Amide Resonances of T4 Lysozyme by 13C and 15N Multiple Isotopic Labeling. Cheminform. 18. DOI: 10.1002/chin.198711040 |
0.497 |
|
| 1986 |
Griffey RH, Redfield AG, McIntosh LP, Oas TG, Dahlquist FW. Assignment of proton amide resonances of T4 lysozyme by carbon-13 and nitrogen-15 multiple isotopic labeling Journal of the American Chemical Society. 108: 6816-6817. DOI: 10.1021/Ja00281A066 |
0.513 |
|
| 1986 |
Griffey RH, Redfield AG, McIntosh LP, Oas TG, Dahlquist FW. Assignment of proton amide resonances of T4 lysozyme by 13C and 15N multiple isotopic labeling Journal of the American Chemical Society. 108: 6816-6817. |
0.497 |
|
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