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Barry T. Nall - Publications

Affiliations: 
The University of Texas Health Science Center at San Antonio, San Antonio, TX, United States 
Area:
Biochemistry
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42 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
2005 Wang L, Rivera EV, Benavides-Garcia MG, Nall BT. Loop entropy and cytochrome c stability. Journal of Molecular Biology. 353: 719-29. PMID 16182309 DOI: 10.1016/J.Jmb.2005.08.038  0.419
2002 Benavides-Garcia MG, Rivera EV, Ramos W, Hinck AP, Nall BT. Backbone sequential resonance assignments of yeast iso-2 cytochrome c, reduced and oxidized forms. Journal of Biomolecular Nmr. 22: 93-4. PMID 11885986 DOI: 10.1023/A:1013801402362  0.322
2000 Pierce MM, Nall BT. Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization Journal of Molecular Biology. 298: 955-969. PMID 10801361 DOI: 10.1006/Jmbi.2000.3700  0.505
2000 Panda M, Benavides-Garcia MG, Pierce MM, Nall BT. Cytochrome c folds through a smooth funnel Protein Science. 9: 536-543. PMID 10752615 DOI: 10.1110/Ps.9.3.536  0.457
2000 Raman CS, Jemmerson R, Nall BT. Antibody-detected folding: kinetics of surface epitope formation are distinct from other folding phases. Protein Science : a Publication of the Protein Society. 9: 129-37. PMID 10739255 DOI: 10.1110/Ps.9.1.129  0.447
1999 Liggins JR, Lo TP, Brayer GD, Nall BT. Thermal stability of hydrophobic heme pocket variants of oxidized cytochrome c. Protein Science : a Publication of the Protein Society. 8: 2645-54. PMID 10631980 DOI: 10.1110/Ps.8.12.2645  0.414
1999 Pierce MM, Raman CS, Nall BT. Isothermal titration calorimetry of protein-protein interactions. Methods (San Diego, Calif.). 19: 213-21. PMID 10527727 DOI: 10.1006/Meth.1999.0852  0.342
1998 McGee WA, Nall BT. Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force Protein Science. 7: 1071-1082. PMID 9605312 DOI: 10.1002/Pro.5560070501  0.465
1997 Veeraraghavan S, Nall BT, Fink AL. Effect of prolyl isomerase on the folding reactions of staphylococcal nuclease Biochemistry. 36: 15134-15139. PMID 9398241 DOI: 10.1021/Bi971357R  0.416
1997 Pierce MM, Nall BT. Fast folding of cytochrome c Protein Science. 6: 618-627. PMID 9070444 DOI: 10.1002/Pro.5560060311  0.486
1997 Pierce MM, McGee WA, Nall BT. Kinetic barriers in cytochrome folding Faseb Journal. 11.  0.349
1996 Veeraraghavan S, Holzman TF, Nall BT. Autocatalyzed protein folding Biochemistry. 35: 10601-10607. PMID 8718848 DOI: 10.1021/Bi960329Q  0.442
1996 McGee WA, Rosell FI, Liggins JR, Rodriguez-Ghidarpour S, Luo Y, Chen J, Brayer GD, Mauk AG, Nall BT. Thermodynamic cycles as probes of structure in unfolded proteins. Biochemistry. 35: 1995-2007. PMID 8639684 DOI: 10.1021/Bi951228F  0.45
1995 Raman CS, Allen MJ, Nall BT. Enthalpy of antibody--cytochrome c binding. Biochemistry. 34: 5831-8. PMID 7727444 DOI: 10.1021/Bi00017A015  0.379
1995 Veeraraghavan S, Rodriguez-Ghidarpour S, MacKinnon C, McGee WA, Pierce MM, Nall BT. Prolyl isomerase as a probe of stability of slow-folding intermediates Biochemistry. 34: 12892-12902. PMID 7548046 DOI: 10.1021/Bi00039A052  0.438
1994 Veeraraghavan S, Nall BT. Characterization of folding intermediates using prolyl isomerase Biochemistry. 33: 687-692. PMID 8292595 DOI: 10.1021/Bi00169A009  0.493
1994 Liggins JR, Sherman F, Mathews AJ, Nall BT. Differential scanning calorimetric study of the thermal unfolding transitions of yeast iso-1 and iso-2 cytochromes c and three composite isozymes. Biochemistry. 33: 9209-19. PMID 8049222 DOI: 10.1021/Bi00197A024  0.426
1994 Allen MJ, Jemmerson R, Nall BT. Rapid refolding of native epitopes on the surface of cytochrome c. Biochemistry. 33: 3967-73. PMID 7511412 DOI: 10.1021/Bi00179A024  0.478
1992 Raman CS, Jemmerson R, Nall BT, Allen MJ. Diffusion-limited rates for monoclonal antibody binding to cytochrome c. Biochemistry. 31: 10370-9. PMID 1329947 DOI: 10.1021/Bi00157A027  0.456
1992 Murphy MEP, Nall BT, Brayer GD. Structure determination and analysis of yeast iso-2-cytochrome c and a composite mutant protein Journal of Molecular Biology. 227: 160-176. PMID 1326054 DOI: 10.1016/0022-2836(92)90689-H  0.369
1991 Muthukrishnan K, Nall BT. Effective concentrations of amino acid side chains in an unfolded protein Biochemistry. 30: 4706-4710. PMID 1851434 DOI: 10.1021/Bi00233A010  0.43
1990 Nall BT, Zuniga EH. Rates and energetics of tyrosine ring flips in yeast iso-2-cytochrome c. Biochemistry. 29: 7576-84. PMID 2176821 DOI: 10.1021/Bi00485A006  0.367
1989 Nall BT, Zuniga EH, White TB, Wood LC, Ramdas L. Replacement of a conserved proline and the alkaline conformational change in iso-2-cytochrome c. Biochemistry. 28: 9834-9. PMID 2558730 DOI: 10.1021/Bi00451A043  0.526
1989 Leung CJ, Nall BT, Brayer GD. Crystallization of yeast iso-2-cytochrome c using a novel hair seeding technique Journal of Molecular Biology. 206: 783-785. PMID 2544732 DOI: 10.1016/0022-2836(89)90585-8  0.312
1988 Wood LC, White TB, Ramdas L, Nall BT. Replacement of a conserved proline eliminates the absorbance-detected slow folding phase of iso-2-cytochrome c. Biochemistry. 27: 8562-8. PMID 2851328 DOI: 10.1021/Bi00423A009  0.545
1988 Wood LC, Muthukrishnan K, White TB, Ramdas L, Nall BT. Construction and characterization of mutant iso-2-cytochromes c with replacement of conserved prolines. Biochemistry. 27: 8554-61. PMID 2851327 DOI: 10.1021/Bi00423A008  0.487
1988 Nall BT, Osterhout JJ, Ramdas L. pH dependence of folding of iso-2-cytochrome c Biochemistry. 27: 7310-7314. PMID 2849990 DOI: 10.1021/Bi00419A020  0.456
1988 Wood LC, White TB, Ramdas L, Nall BT. Replacement of a conserved proline eliminates the absorbance-detected slow folding phase of iso-2-cytochrome c Biochemistry. 27: 8562-8568.  0.473
1988 Wood LC, Muthukrishnan K, White TB, Ramdas L, Nall BT. Construction and characterization of mutant iso-2-cytochromes c with replacement of conserved prolines Biochemistry. 27: 8554-8561.  0.409
1987 White TB, Berget PB, Nall BT. Changes in conformation and slow refolding kinetics in mutant iso-2-cytochrome c with replacement of a conserved proline residue. Biochemistry. 26: 4358-66. PMID 2822088 DOI: 10.1021/Bi00388A026  0.52
1986 Ramdas L, Nall BT. Folding/unfolding kinetics of mutant forms of iso-1-cytochrome c with replacement of proline-71. Biochemistry. 25: 6959-6964. PMID 3026440 DOI: 10.1021/Bi00370A033  0.549
1986 Ramdas L, Sherman F, Nall BT. Guanidine hydrochloride induced equilibrium unfolding of mutant forms of iso-1-cytochrome c with replacement of proline-71. Biochemistry. 25: 6952-6958. PMID 3026439 DOI: 10.1021/Bi00370A032  0.359
1986 Nall BT. Native or nativelike species are transient intermediates in folding of alkaline iso-2 cytochrome c Biochemistry. 25: 2974-2978. PMID 3013289 DOI: 10.1021/Bi00358A036  0.498
1985 Lin SH, Konishi Y, Nall BT, Scheraga HA. Influence of an extrinsic cross-link on the folding pathway of ribonuclease A. Kinetics of folding-unfolding. Biochemistry. 24: 2680-6. PMID 4027220 DOI: 10.1021/Bi00332A013  0.448
1985 Osterhout JJ, Nall BT. Slow refolding kinetics in yeast iso-2 cytochrome c Biochemistry. 24: 7999-8005. PMID 3004570 DOI: 10.1021/Bi00348A024  0.485
1985 Osterhout JJ, Muthukrishnan K, Nall BT. pH-induced conformation changes and equilibrium unfolding in yeast iso-2 cytochrome c Biochemistry. 24: 6680-6684. PMID 3002448 DOI: 10.1021/Bi00344A057  0.468
1983 Zuniga EH, Nall BT. Folding of yeast iso-1-AM cytochrome c. Biochemistry. 22: 1430-7. PMID 6301549 DOI: 10.1021/Bi00275A017  0.489
1983 Nall BT. Structural intermediates in folding of yeast iso-2 cytochrome c Biochemistry. 22: 1423-1429. PMID 6301548 DOI: 10.1021/Bi00275A016  0.463
1981 Nall BT, Landers TA. Guanidine hydrochloride induced unfolding of yeast iso-2 cytochrome c Biochemistry. 20: 5403-5411. PMID 6271187 DOI: 10.1021/Bi00522A008  0.502
1978 Nall BT, Garel JR, Baldwin RL. Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease A Journal of Molecular Biology. 118: 317-330. PMID 633363 DOI: 10.1016/0022-2836(78)90231-0  0.438
1977 Nall BT, Baldwin RL. Thermal unfolding transition of ribonuclease A measured by 2′-CMP binding Biochemistry. 16: 3572-3576. PMID 19055 DOI: 10.1021/Bi00635A011  0.415
1976 Garel JR, Nall BT, Baldwin RL. Guanidine unfolded state of ribonuclease A contains both fast and slow refolding species Proceedings of the National Academy of Sciences of the United States of America. 73: 1853-1857. PMID 1064858 DOI: 10.1073/Pnas.73.6.1853  0.43
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