| Year |
Citation |
Score |
| 2015 |
Clark SA, Jespersen N, Woodward C, Barbar E. Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds. Febs Letters. 589: 2543-51. PMID 26226419 DOI: 10.1016/J.Febslet.2015.07.032 |
0.324 |
|
| 2008 |
Getun IV, Brown CK, Tulla-Puche J, Ohlendorf D, Woodward C, Barany G. Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin. Journal of Molecular Biology. 375: 812-23. PMID 18054043 DOI: 10.1016/J.Jmb.2007.10.084 |
0.634 |
|
| 2006 |
Tulla-Puche J, Getun IV, Angell YM, Alsina J, Albericio F, Woodward C, Barany G. Synthetic approaches to disulfide-free circular bovine pancreatic trypsin inhibitor (c-BPTI) analogues International Journal of Peptide Research and Therapeutics. 12: 93-104. DOI: 10.1007/S10989-006-9023-6 |
0.581 |
|
| 2005 |
Gross CM, Lelièvre D, Woodward CK, Barany G. Preparation of protected peptidyl thioester intermediates for native chemical ligation by Nalpha-9-fluorenylmethoxycarbonyl (Fmoc) chemistry: considerations of side-chain and backbone anchoring strategies, and compatible protection for N-terminal cysteine. The Journal of Peptide Research : Official Journal of the American Peptide Society. 65: 395-410. PMID 15787970 DOI: 10.1111/J.1399-3011.2005.00241.X |
0.58 |
|
| 2004 |
Woodward C, Carulla N, Barany G. Native state hydrogen-exchange analysis of protein folding and protein motional domains. Methods in Enzymology. 380: 379-400. PMID 15051346 DOI: 10.1016/S0076-6879(04)80017-X |
0.603 |
|
| 2004 |
Tulla-Puche J, Getun IV, Woodward C, Barany G. Native-like conformations are sampled by partially folded and disordered variants of bovine pancreatic trypsin inhibitor. Biochemistry. 43: 1591-8. PMID 14769035 DOI: 10.1021/Bi035301A |
0.623 |
|
| 2002 |
Carulla N, Barany G, Woodward C. Hydrogen exchange, core modules, and new designed proteins. Biophysical Chemistry. 101: 67-79. PMID 12487990 DOI: 10.1016/S0301-4622(02)00149-7 |
0.65 |
|
| 2002 |
Carulla N, Woodward C, Barany G. BetaCore, a designed water soluble four-stranded antiparallel beta-sheet protein. Protein Science : a Publication of the Protein Society. 11: 1539-51. PMID 12021452 DOI: 10.1110/Ps.4440102 |
0.617 |
|
| 2002 |
Li R, Battiste JL, Woodward C. Native-like interactions favored in the unfolded bovine pancreatic trypsin inhibitor have different roles in folding. Biochemistry. 41: 2246-53. PMID 11841216 DOI: 10.1021/Bi0116947 |
0.635 |
|
| 2002 |
Battiste JL, Li R, Woodward C. A highly destabilizing mutation, G37A, of the bovine pancreatic trypsin inhibitor retains the average native conformation but greatly increases local flexibility. Biochemistry. 41: 2237-45. PMID 11841215 DOI: 10.1021/Bi011693E |
0.604 |
|
| 2001 |
Barbar E, Hare M, Makokha M, Barany G, Woodward C. NMR-detected order in core residues of denatured bovine pancreatic trypsin inhibitor. Biochemistry. 40: 9734-42. PMID 11583174 DOI: 10.1021/Bi010483Z |
0.662 |
|
| 2001 |
Carulla N, Woodward C, Barany G. Toward new designed proteins derived from bovine pancreatic trypsin inhibitor (BPTI): covalent cross-linking of two 'core modules' by oxime-forming ligation. Bioconjugate Chemistry. 12: 726-41. PMID 11562191 DOI: 10.1021/Bc015518M |
0.657 |
|
| 2001 |
Woodward C, Barbar E, Carulla N, Battiste J, Barany G. Experimental approaches to protein folding based on the concept of a slow hydrogen exchange core. Journal of Molecular Graphics & Modelling. 19: 94-101. PMID 11381535 DOI: 10.1016/S1093-3263(00)00131-5 |
0.675 |
|
| 2000 |
Carulla N, Woodward C, Barany G. Synthesis and characterization of a beta-hairpin peptide that represents a 'core module' of bovine pancreatic trypsin inhibitor (BPTI). Biochemistry. 39: 7927-37. PMID 10891073 DOI: 10.1021/Bi992927L |
0.648 |
|
| 2000 |
Sareth S, Li H, Yamada H, Woodward CK, Akasaka K. Rapid internal dynamics of BPTI is insensitive to pressure. (15)N spin relaxation at 2 kbar. Febs Letters. 470: 11-4. PMID 10722836 DOI: 10.1016/S0014-5793(00)01283-7 |
0.327 |
|
| 2000 |
Woodward C, Barbar E, Carrula N, Battiste J, Barany G. Hydrogen exchange and protein folding Journal of Molecular Graphics and Modelling. 18: 557-558. DOI: 10.1016/S1093-3263(00)80140-0 |
0.619 |
|
| 1999 |
Akasaka K, Li H, Yamada H, Li R, Thoresen T, Woodward CK. Pressure response of protein backbone structure. Pressure-induced amide 15N chemical shifts in BPTI. Protein Science : a Publication of the Protein Society. 8: 1946-53. PMID 10548039 DOI: 10.1110/Ps.8.10.1946 |
0.582 |
|
| 1999 |
Li R, Woodward C. The hydrogen exchange core and protein folding. Protein Science. 8: 1571-1590. PMID 10452602 DOI: 10.1110/Ps.8.8.1571 |
0.658 |
|
| 1999 |
Woodward C. Advances in protein hydrogen exchange by mass spectrometry Journal of the American Society For Mass Spectrometry. 10: 672-674. DOI: 10.1016/S1044-0305(99)00060-4 |
0.347 |
|
| 1998 |
Woodward C, Li R. The slow-exchange core and protein folding Trends in Biochemical Sciences. 23: 379. PMID 9810224 DOI: 10.1016/S0968-0004(98)01282-1 |
0.603 |
|
| 1998 |
Liang J, Edelsbrunner H, Woodward C. Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein Science : a Publication of the Protein Society. 7: 1884-97. PMID 9761470 DOI: 10.1002/Pro.5560070905 |
0.605 |
|
| 1998 |
Barbar E, Hare M, Daragan V, Barany G, Woodward C. Dynamics of the conformational ensemble of partially folded bovine pancreatic trypsin inhibitor. Biochemistry. 37: 7822-33. PMID 9601043 DOI: 10.1021/Bi973102J |
0.663 |
|
| 1998 |
Vohník S, Hanson C, Tuma R, Fuchs JA, Woodward C, Thomas GJ. Conformation, stability, and active‐site cysteine titrations of Escherichia coli D26A thioredoxin probed by Raman spectroscopy Protein Science. 7: 193-200. PMID 9514274 DOI: 10.1002/Pro.5560070120 |
0.401 |
|
| 1997 |
Barbar E, Gross CM, Woodward C, Barany G. Chemical synthesis and nuclear magnetic resonance characterization of partially folded proteins. Methods in Enzymology. 289: 587-611. PMID 9353740 DOI: 10.1016/S0076-6879(97)89066-0 |
0.648 |
|
| 1997 |
Pan H, Barany G, Woodward C. Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor. Protein Science : a Publication of the Protein Society. 6: 1985-92. PMID 9300498 DOI: 10.1002/Pro.5560060919 |
0.622 |
|
| 1997 |
Barbar E, LiCata VJ, Barany G, Woodward C. Local fluctuations and global unfolding of partially folded BPTI detected by NMR. Biophysical Chemistry. 64: 45-57. PMID 9127937 DOI: 10.1016/S0301-4622(96)02210-7 |
0.668 |
|
| 1997 |
Ilyina E, Roongta V, Pan H, Woodward C, Mayo KH. A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association Biochemistry. 36: 3383-3388. PMID 9116018 DOI: 10.1021/Bi9622229 |
0.345 |
|
| 1996 |
Barbar E, Barany G, Woodward C. Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink. Folding & Design. 1: 65-76. PMID 9079365 DOI: 10.1016/S1359-0278(96)00013-2 |
0.673 |
|
| 1996 |
Barany G, Gross CM, Ferrer M, Barbar E, Pan H, Woodward C. Optimized methods for chemical synthesis of bovine pancreatic trypsin inhibitor (BPTI) analogues Techniques in Protein Chemistry. 7: 503-514. DOI: 10.1016/S1080-8914(96)80055-X |
0.638 |
|
| 1995 |
Wilson NA, Barbar E, Fuchs JA, Woodward C. Aspartic acid 26 in reduced Escherichia coli thioredoxin has a pKa > 9. Biochemistry. 34: 8931-9. PMID 7619792 DOI: 10.1021/Bi00028A001 |
0.405 |
|
| 1995 |
Pan H, Barbar E, Barany G, Woodward C. Extensive nonrandom structure in reduced and unfolded bovine pancreatic trypsin inhibitor. Biochemistry. 34: 13974-81. PMID 7577994 DOI: 10.1021/Bi00043A002 |
0.673 |
|
| 1995 |
Barbar E, Barany G, Woodward C. Dynamic structure of a highly ordered beta-sheet molten globule: multiple conformations with a stable core. Biochemistry. 34: 11423-434. PMID 7547870 DOI: 10.1021/Bi00036A015 |
0.678 |
|
| 1995 |
Ferrer M, Barany G, Woodward C. Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor. Nature Structural Biology. 2: 211-7. PMID 7539710 DOI: 10.1038/Nsb0395-211 |
0.637 |
|
| 1994 |
Woodward CK. Hydrogen exchange rates and protein folding Current Opinion in Structural Biology. 4: 112-116. DOI: 10.1016/S0959-440X(94)90068-X |
0.468 |
|
| 1993 |
Danishefsky AT, Housset D, Kim KS, Tao F, Fuchs J, Woodward C, Wlodawer A. Crevice-forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: crystal structures of F22A, Y23A, N43G, and F45A. Protein Science. 2: 577-587. PMID 8518731 DOI: 10.1002/Pro.5560020409 |
0.412 |
|
| 1993 |
Woodward C. Is the slow-exchange core the protein folding core? Trends in Biochemical Sciences. 18: 359-360. PMID 8256281 DOI: 10.1016/0968-0004(93)90086-3 |
0.422 |
|
| 1993 |
Li H, Hanson C, Fuchs JA, Woodward C, Thomas GJ. Determination of the pKa values of active-center cysteines, cysteines-32 and -35, in Escherichia coli thioredoxin by Raman spectroscopy. Biochemistry. 32: 5800-8. PMID 8099293 DOI: 10.1021/Bi00073A012 |
0.406 |
|
| 1993 |
Kim KS, Fuchs JA, Woodward CK. Hydrogen exchange identifies native-state motional domains important in protein folding. Biochemistry. 32: 9600-8. PMID 7690587 DOI: 10.1021/Bi00088A012 |
0.498 |
|
| 1993 |
Kim K, Tao F, Fuchs J, Woodward C, Danishefsky AT, Housset D, Wlodawer A. Crevice-forming mutants of bovine pancreatic trypsin inhibitor: Stability changes and new hydrophobic surface Protein Science. 2: 588-596. PMID 7686069 DOI: 10.1002/Pro.5560020410 |
0.396 |
|
| 1993 |
Makhatadze GI, Kim KS, Woodward C, Privalov PL. Thermodynamics of BPTI folding Protein Science. 2: 2028-2036. PMID 7507751 DOI: 10.1002/Pro.5560021204 |
0.336 |
|
| 1993 |
Tao F, Fuchs J, Woodward C. ΔΔG°(WT-mut) for BPTI Hydrophobic Core Mutants Measured by Hydrogen Isotope Exchange Techniques in Protein Chemistry. 549-556. DOI: 10.1016/B978-0-12-058757-5.50065-2 |
0.402 |
|
| 1992 |
Ellis LBM, Saurugger P, Woodward C. Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon. Biochemistry. 31: 4882-4891. PMID 1591248 DOI: 10.1021/Bi00135A020 |
0.389 |
|
| 1992 |
Gallagher W, Tao F, Woodward C. Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solution. Biochemistry. 31: 4673-80. PMID 1374641 DOI: 10.1021/Bi00134A020 |
0.385 |
|
| 1992 |
Ferrer M, Woodward C, Barany G. Solid-phase synthesis of bovine pancreatic trypsin inhibitor (BPTI) and two analogues. A chemical approach for evaluating the role of disulfide bridges in protein folding and stability. International Journal of Peptide and Protein Research. 40: 194-207. PMID 1282503 DOI: 10.1111/J.1399-3011.1992.Tb00292.X |
0.633 |
|
| 1991 |
Woodward C. Escherichia coli glutaredoxin: cloning and overexpression, thermodynamic stability of the oxidized and reduced forms, and report of an N-terminal extended species Biochemistry. 30: 5475-5484. PMID 2036416 DOI: 10.1021/Bi00236A021 |
0.374 |
|
| 1991 |
Woodward C. The conserved, buried aspartic acid in oxidized escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability Biochemistry®. 30: 7603-7609. PMID 1854757 DOI: 10.1021/Bi00244A032 |
0.407 |
|
| 1991 |
Housset D, Kim KS, Fuchs J, Woodward C, Wlodawer A. Crystal structure of a Y35G mutant of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology. 220: 757-70. PMID 1714504 DOI: 10.1016/0022-2836(91)90115-M |
0.365 |
|
| 1989 |
Langsetmo K, Fuchs J, Woodward C. Escherichia coli thioredoxin folds into two compact forms of different stability to urea denaturation. Biochemistry. 28: 3211-3220. PMID 2663067 DOI: 10.1021/Bi00434A015 |
0.373 |
|
| 1989 |
Gallagher WH, Woodward CK. The concentration dependence of the diffusion coefficient for bovine pancreatic trypsin inhibitor: a dynamic light scattering study of a small protein. Biopolymers. 28: 2001-24. PMID 2480823 DOI: 10.1002/Bip.360281115 |
0.329 |
|
| 1987 |
Tuchsen E, Woodward C. Hydrogen exchange of primary amide protons in basic pancreatic trypsin inhibitor: evidence for NH2 group rotation in buried asparagine side chains. Biochemistry. 26: 8073-8078. PMID 2450559 DOI: 10.1021/Bi00399A008 |
0.444 |
|
| 1987 |
Wlodawer A, Nachman J, Gilliland GL, Gallagher W, Woodward C. Structure of form III crystals of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology. 198: 469-480. PMID 2448484 DOI: 10.1016/0022-2836(87)90294-4 |
0.348 |
|
| 1987 |
Tüchsen E, Hayes JM, Ramaprasad S, Copie V, Woodward C. Solvent exchange of buried water and hydrogen exchange of peptide NH groups hydrogen bonded to buried waters in bovine pancreatic trypsin inhibitor. Biochemistry. 26: 5163-72. PMID 2444253 DOI: 10.1021/Bi00390A040 |
0.374 |
|
| 1987 |
Tüchsen E, Woodward C. Hydrogen exchange kinetics of surface peptide amides in bovine pancreatic trypsin inhibitor Journal of Molecular Biology. 193: 793-802. PMID 2441070 DOI: 10.1016/0022-2836(87)90359-7 |
0.43 |
|
| 1987 |
Brandt P, Woodward C. Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor beta-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor. Biochemistry. 26: 3156-3162. PMID 2440473 DOI: 10.1021/Bi00385A032 |
0.369 |
|
| 1987 |
Tuchsen E, Woodward C. Assignment of asparagine-44 side-chain primary amide 1H NMR resonances and the peptide amide N1H resonance of glycine-37 in basic pancreatic trypsin inhibitor Biochemistry. 26: 1918-1925. PMID 2439116 DOI: 10.1021/Bi00381A020 |
0.37 |
|
| 1985 |
Akasaka K, Inoue T, Hatano H, Woodward CK. Hydrogen exchange kinetics of core peptide protons in Streptomyces subtilisin inhibitor. Biochemistry. 24: 2973-9. PMID 3893534 DOI: 10.1021/Bi00333A025 |
0.476 |
|
| 1985 |
Tüchsen E, Woodward C. Mechanism of surface peptide proton exchange in bovine pancreatic trypsin inhibitor. Salt effects and O-protonation. Journal of Molecular Biology. 185: 421-430. PMID 2414452 DOI: 10.1016/0022-2836(85)90413-9 |
0.383 |
|
| 1985 |
Tüchsen E, Woodward C. Hydrogen kinetics of peptide amide protons at the bovine pancreatic trypsin inhibitor protein-solvent interface. Journal of Molecular Biology. 185: 405-419. PMID 2414451 DOI: 10.1016/0022-2836(85)90412-7 |
0.443 |
|
| 1984 |
Simon I, Tuchsen E, Woodward C. Effect of trypsin binding on the hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor .beta.-sheet NH's Biochemistry. 23: 2064-2068. DOI: 10.1021/Bi00304A028 |
0.441 |
|
| 1982 |
Woodward C, Simon I, Tüchsen E. Hydrogen exchange and the dynamic structure of proteins Molecular and Cellular Biochemistry. 48: 135-160. PMID 6757714 DOI: 10.1007/Bf00421225 |
0.482 |
|
| 1981 |
Hilton BD, Trudeau K, Woodward CK. Hydrogen exchange rates in pancreatic trypsin inhibitor are not correlated to thermal stability in urea. Biochemistry. 20: 4697-703. PMID 7295640 DOI: 10.1021/Bi00519A027 |
0.366 |
|
| 1980 |
Woodward CK, Hilton BD. Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor. Biophysical Journal. 32: 561-75. PMID 7248461 DOI: 10.1016/S0006-3495(80)84990-3 |
0.322 |
|
| 1979 |
Hilton BD, Woodward CK. On the mechanism of isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor. Biochemistry. 18: 5834-41. PMID 42434 DOI: 10.1021/Bi00593A013 |
0.357 |
|
| 1978 |
Hilton BD, Woodward CK. Nuclear magnetic resonance measurement of hydrogen exchange kinetics of single protons in basic pancreatic trypsin inhibitor. Biochemistry. 17: 3325-32. PMID 28747 DOI: 10.1021/Bi00609A024 |
0.359 |
|
| 1977 |
Woodward CK. Dynamic solvent accessibility in the soybean trypsin inhibitor--trypsin complex. Journal of Molecular Biology. 111: 509-15. PMID 17011 DOI: 10.1016/S0022-2836(77)80066-1 |
0.423 |
|
| 1975 |
Patel DJ, Canuel LL, Bovey FA, Woodward C. Assignment of the imidazole ring nitrogen protons of histidine 48 in the proton NMR spectrum of ribonuclease A in water solution. Biochimica Et Biophysica Acta. 400: 275-82. PMID 240416 DOI: 10.1016/0005-2795(75)90182-8 |
0.415 |
|
| 1975 |
Patel DJ, Woodward C, Canuel LL, Bovey FA. Correlation of exchangeable (NH) and nonexchangeable (C2H) histidine resonances in the proton NMR spectrum of ribonuclease A in aqueous solution. Biopolymers. 14: 975-86. PMID 239769 DOI: 10.1002/Bip.1975.360140507 |
0.417 |
|
| 1975 |
Patel DJ, Canuel LL, Woodward C, Bovey FA. Assignment of the histidine 12-threonine 45 hydrogen-bonded proton in the NMR spectrum of ribonuclease A in H2O. Biopolymers. 14: 959-74. PMID 239768 DOI: 10.1002/Bip.1975.360140506 |
0.427 |
|
| 1975 |
Woodward CK, Ellis LM. Hydrogen exchange kinetics changes upon formation of the soybean trypsin inhibitor-trypsin complex. Biochemistry. 14: 3419-23. PMID 238590 DOI: 10.1021/Bi00686A020 |
0.397 |
|
| 1975 |
Ellis LM, Bloomfield VA, Woodward CK. Hydrogen-tritium exchange kinetics of soybean trypsin inhibitor (Kunitz). Solvent accessibility in the folded conformation. Biochemistry. 14: 3413-9. PMID 238589 |
0.354 |
|
| 1975 |
Woodward CK, Ellis LM, Rosenberg A. The solvent dependence of hydrogen exchange kinetics of folded proteins. The Journal of Biological Chemistry. 250: 440-4. PMID 234429 |
0.32 |
|
| 1975 |
Woodward CK, Ellis LM, Rosenberg A. Solvent accessibility in folded proteins. Studies of hydrogen exchange in trypsin. The Journal of Biological Chemistry. 250: 432-9. PMID 234428 |
0.392 |
|
| 1972 |
Patel DJ, Woodward CK, Bovey FA. Proton nuclear magnetic resonance studies of ribonuclease A in H 2 O. Proceedings of the National Academy of Sciences of the United States of America. 69: 599-602. PMID 4501576 DOI: 10.1073/Pnas.69.3.599 |
0.34 |
|
| 1971 |
Woodward CK, Rosenberg A. Studies of hydrogen exchange in proteins. VI. Urea effects on ribonuclease exchange kinetics leading to a general model for hydrogen exchange from folded proteins. The Journal of Biological Chemistry. 246: 4114-21. PMID 5104484 |
0.333 |
|
| 1970 |
Woodward CK, Rosenberg A. Oxidized RNase as a protein model having no contribution to the hydrogen exchange rate from conformational restrictions. Proceedings of the National Academy of Sciences of the United States of America. 66: 1067-74. PMID 5273444 |
0.325 |
|
| 1969 |
Woodward CK, Read CP. Studies on membrane transport. VII. Transport of histidine through two distinct systems in the tapeworm Hymenolepis diminuta. Comparative Biochemistry and Physiology. 30: 1161-77. PMID 5349638 DOI: 10.1016/0010-406X(69)91051-2 |
0.519 |
|
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