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Terrence G. Oas - Publications

Affiliations: 
Biochemistry and Chemistry Duke University, Durham, NC 
Area:
protein folding, protein translocation, bacterial infection, ribonucleoprotein assembly and cellular signaling
Website:
http://www.biochem.duke.edu/modules/biochem_oas_lab/index.php?id=1

72 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
2012 Zhang J, Parlak Z, Bowers CM, Oas T, Zauscher S. Mapping mechanical properties of organic thin films by force-modulation microscopy in aqueous media. Beilstein Journal of Nanotechnology. 3: 464-74. PMID 23019540 DOI: 10.3762/bjnano.3.53  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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+  0.96
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+  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
2002 Ghaemmaghami S, Fitzgerald MC, Oas TG. Quantitative protein stability measurement in living bacteria Proceedings 50th Asms Conference On Mass Spectrometry and Allied Topics. 109-110.  0.96
2002 Fitzgerald MC, Powell KD, Wang MZ, Ma L, Ghaemmaghami S, Oas TG. A general mass spectrometry-based method for the quantitation of protein-ligand binding interactions in solution Proceedings 50th Asms Conference On Mass Spectrometry and Allied Topics. 395-396.  0.96
2001 Ghaemmaghami S, Oas TG. Quantitative protein stability measurement in vivo. Nature Structural Biology. 8: 879-82. PMID 11573094 DOI: 10.1038/nsb1001-879  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
1998 Burton RE, Busby RS, Oas TG. ALASKA: A Mathematica package for two-state kinetic analysis of protein folding reactions Journal of Biomolecular Nmr. 11: 355-359.  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
1996 Huang GS, Oas TG. Heat and cold denatured states of monomeric λ represser are thermodynamically and conformationally equivalen Biochemistry. 35: X-6180.  0.96
1995 Huang GS, Oas TG. Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding. Biochemistry. 34: 3884-92. PMID 7696251  0.96
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  0.96
1995 Breiner KM, Daugherty MA, Oas TG, Thorp HH. An anionic diplatinum DNA photocleavage agent: Chemical mechanism and footprinting of λ repressor Journal of the American Chemical Society. 117: 11673-11679. DOI: 10.1021/ja00152a007  0.96
1994 Oas TG, Endow SA. Springs and hinges: dynamic coiled coils and discontinuities. Trends in Biochemical Sciences. 19: 51-4. PMID 8160263 DOI: 10.1016/0968-0004(94)90030-2  0.96
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  0.96
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  0.96
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  0.96
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  0.96
1990 Myers RA, Mcintosh JM, Imperial J, Williams RW, Oas T, Haack JA, Hernandez JF, Rivier J, Cruz LJ, Olivera BM. Peptides from conus venoms which affect ca+plus; entry into neurons Toxin Reviews. 9: 179-202. DOI: 10.3109/15569549009033113  0.96
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  0.96
1988 Oas TG, Kim PS. A peptide model of a protein folding intermediate. Nature. 336: 42-8. PMID 3185721 DOI: 10.1038/336042a0  0.96
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  0.96
1988 Oas TG, Drobny GP, Dahlquistt FW. A new iterative least-squares method for the extraction of NMR parameters from nonideal powder patterns Journal of Magnetic Resonance (1969). 78: 408-424. DOI: 10.1016/0022-2364(88)90129-1  0.96
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.  0.96
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  0.6
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.  0.96
1987 Hartzell CJ, Whitfield M, Oas TG, Drobny GP. Determination of the 15N and 13C chemical shift tensors of L-[13C]alanyl-L-[15N]alanine from the dipole-coupled powder patterns Journal of the American Chemical Society. 109: 5966-5969.  0.96
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.  0.96
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  0.6
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.  0.96
1978 Meyers PA, Oas TG. COMPARISON OF ASSOCIATIONS OF DIFFERENT HYDROCARBONS WITH CLAY PARTICLES IN SIMULATED SEAWATER Environmental Science and Technology. 12: 934-937.  0.96
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