HIRAM GILBERT to Catalysis
This is a "connection" page, showing publications HIRAM GILBERT has written about Catalysis.
Connection Strength
0.557
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Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae. J Biol Chem. 2004 Aug 13; 279(33):34095-100.
Score: 0.055
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Protein disulfide isomerase. Biochim Biophys Acta. 2004 Jun 01; 1699(1-2):35-44.
Score: 0.055
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Zinc-dependent dimerization of the folding catalyst, protein disulfide isomerase. Protein Sci. 2004 Jul; 13(7):1902-7.
Score: 0.055
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Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase. J Biol Chem. 2003 Feb 28; 278(9):7154-9.
Score: 0.050
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Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum. J Biol Chem. 2001 Jan 05; 276(1):281-6.
Score: 0.044
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A 21-kDa C-terminal fragment of protein-disulfide isomerase has isomerase, chaperone, and anti-chaperone activities. J Biol Chem. 1997 Dec 26; 272(52):32988-94.
Score: 0.035
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Protein disulfide isomerase and assisted protein folding. J Biol Chem. 1997 Nov 21; 272(47):29399-402.
Score: 0.035
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Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry. 1996 Feb 13; 35(6):1972-80.
Score: 0.031
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Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains. J Biol Chem. 1994 Dec 09; 269(49):30946-52.
Score: 0.029
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Catalysis of protein folding by agarose-immobilized protein disulfide isomerase. Protein Expr Purif. 1994 Apr; 5(2):144-8.
Score: 0.027
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Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J Biol Chem. 1994 Mar 11; 269(10):7764-71.
Score: 0.027
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Determination of the amino acid sequence requirements for catalysis by the highly proficient orotidine monophosphate decarboxylase. Protein Sci. 2011 Nov; 20(11):1891-906.
Score: 0.023
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Catalysis of thiol/disulfide exchange: single-turnover reduction of protein disulfide-isomerase by glutathione and catalysis of peptide disulfide reduction. Biochemistry. 1989 Sep 05; 28(18):7298-305.
Score: 0.020
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Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC. J Biol Chem. 2009 Sep 04; 284(36):23972-9.
Score: 0.020
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Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. J Biol Chem. 2006 Feb 24; 281(8):4911-9.
Score: 0.015
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Catalysis of thiol/disulfide exchange. Glutaredoxin 1 and protein-disulfide isomerase use different mechanisms to enhance oxidase and reductase activities. J Biol Chem. 2005 Jun 03; 280(22):21099-106.
Score: 0.015
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Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways. Proc Natl Acad Sci U S A. 2004 Jul 06; 101(27):10018-23.
Score: 0.014
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Conserved residues flanking the thiol/disulfide centers of protein disulfide isomerase are not essential for catalysis of thiol/disulfide exchange. Biochemistry. 1992 May 05; 31(17):4205-10.
Score: 0.006