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Journal Abstract Search
181 related items for PubMed ID: 6358211
1. Proton stoichiometry in the reduction of the FAD and disulfide of Escherichia coli thioredoxin reductase. Evidence for a base at the active site. O'Donnell ME, Williams CH. J Biol Chem; 1983 Nov 25; 258(22):13795-805. PubMed ID: 6358211 [Abstract] [Full Text] [Related]
4. Graphical analysis of interactions between oxidation-reduction sites in two site oxidation-reduction proteins. O'Donnell ME, Williams CH. Anal Biochem; 1984 Jan 25; 136(1):235-46. PubMed ID: 6370035 [Abstract] [Full Text] [Related]
6. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. Waksman G, Krishna TS, Williams CH, Kuriyan J. J Mol Biol; 1994 Feb 25; 236(3):800-16. PubMed ID: 8114095 [Abstract] [Full Text] [Related]
7. Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin. Veine DM, Mulrooney SB, Wang PF, Williams CH. Protein Sci; 1998 Jun 25; 7(6):1441-50. PubMed ID: 9655349 [Abstract] [Full Text] [Related]
8. Characterization of two active site mutations of thioredoxin reductase from Escherichia coli. Prongay AJ, Engelke DR, Williams CH. J Biol Chem; 1989 Feb 15; 264(5):2656-64. PubMed ID: 2644268 [Abstract] [Full Text] [Related]
11. Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Lennon BW, Williams CH, Ludwig ML. Science; 2000 Aug 18; 289(5482):1190-4. PubMed ID: 10947986 [Abstract] [Full Text] [Related]
12. Lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides. Hopkins N, Williams CH. Biochemistry; 1995 Sep 19; 34(37):11766-76. PubMed ID: 7547909 [Abstract] [Full Text] [Related]
13. Mechanism and structure of thioredoxin reductase from Escherichia coli. Williams CH. FASEB J; 1995 Oct 19; 9(13):1267-76. PubMed ID: 7557016 [Abstract] [Full Text] [Related]
14. Reaction of both active site thiols of reduced thioredoxin reductase with N-ethylmaleimide. O'Donnell ME, Williams CH. Biochemistry; 1985 Dec 17; 24(26):7617-21. PubMed ID: 3912005 [Abstract] [Full Text] [Related]
15. Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57. Dyson HJ, Jeng MF, Tennant LL, Slaby I, Lindell M, Cui DS, Kuprin S, Holmgren A. Biochemistry; 1997 Mar 04; 36(9):2622-36. PubMed ID: 9054569 [Abstract] [Full Text] [Related]
16. Properties of lipoamide dehydrogenase and thioredoxin reductase from Escherichia coli altered by site-directed mutagenesis. Williams CH, Allison N, Russell GC, Prongay AJ, Arscott LD, Datta S, Sahlman L, Guest JR. Ann N Y Acad Sci; 1989 Mar 04; 573():55-65. PubMed ID: 2699405 [No Abstract] [Full Text] [Related]
17. Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Hopkins N, Williams CH. Biochemistry; 1995 Sep 19; 34(37):11757-65. PubMed ID: 7547908 [Abstract] [Full Text] [Related]
18. Enzyme-monitored turnover of Escherichia coli thioredoxin reductase: insights for catalysis. Lennon BW, Williams CH. Biochemistry; 1996 Apr 16; 35(15):4704-12. PubMed ID: 8664260 [Abstract] [Full Text] [Related]
19. Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor. Lennon BW, Williams CH, Ludwig ML. Protein Sci; 1999 Nov 16; 8(11):2366-79. PubMed ID: 10595539 [Abstract] [Full Text] [Related]
20. Oxidation-reduction potentials of flavin and Mo-pterin centers in assimilatory nitrate reductase: variation with pH. Kay CJ, Solomonson LP, Barber MJ. Biochemistry; 1990 Dec 04; 29(48):10823-8. PubMed ID: 2176886 [Abstract] [Full Text] [Related] Page: [Next] [New Search]