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177 related items for PubMed ID: 8019144
1. Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin. Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ. J Biomol NMR; 1994 May; 4(3):411-32. PubMed ID: 8019144 [Abstract] [Full Text] [Related]
2. Replacement of Trp28 in Escherichia coli thioredoxin by site-directed mutagenesis affects thermodynamic stability but not function. Slaby I, Cerna V, Jeng MF, Dyson HJ, Holmgren A. J Biol Chem; 1996 Feb 09; 271(6):3091-6. PubMed ID: 8621706 [Abstract] [Full Text] [Related]
6. Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure, and global fold. Dyson HJ, Holmgren A, Wright PE. Biochemistry; 1989 Aug 22; 28(17):7074-87. PubMed ID: 2684270 [Abstract] [Full Text] [Related]
11. The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol. Höög JO, Jörnvall H, Holmgren A, Carlquist M, Persson M. Eur J Biochem; 1983 Oct 17; 136(1):223-32. PubMed ID: 6352262 [Abstract] [Full Text] [Related]
12. Differences between the electronic environments of reduced and oxidized Escherichia coli DsbA inferred from heteronuclear magnetic resonance spectroscopy. Couprie J, Remerowski ML, Bailleul A, Courçon M, Gilles N, Quéméneur E, Jamin N. Protein Sci; 1998 Oct 17; 7(10):2065-80. PubMed ID: 9792093 [Abstract] [Full Text] [Related]