Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding (Q44038518)

29 November 2017

Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding (English)

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29 November 2017

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Chiara Cabrele

1

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29 November 2017

Stella Fiori

series ordinal

2

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29 November 2017

Stefano Pegoraro

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3

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29 November 2017

Luis Moroder

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4

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29 November 2017

1 June 2002

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29 November 2017

Chemistry and Biology

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29 November 2017

9

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29 November 2017

6

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29 November 2017

731-740

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Protein disulfide isomerase is both an enzyme and a chaperone

29 November 2017

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Enzymatic catalysis of disulfide formation

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Protein disulphide isomerase: building bridges in protein folding

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Protein folding in the bacterial periplasm

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7 January 2021

https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

1 reference

7 January 2021

Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin.

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase.

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

A single dipeptide sequence modulates the redox properties of a whole enzyme family

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Why is DsbA such an oxidizing disulfide catalyst?

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

New synthesis of somatostatin according to the S-tert-butylthiocysteine procedure

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

REDUCTION-POTENTIAL OF GLUTATHIONE

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

A small-molecule catalyst of protein folding in vitro and in vivo

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategies

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

The CXXC motif: imperatives for the formation of native disulfide bonds in the cell.

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl) phenylazobenzoic acid as backbone constituent.

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases

1 reference

https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family.

1 reference

https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of protein disulfide reduction.

1 reference

https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Ionization-reactivity relationships for cysteine thiols in polypeptides.

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7 January 2021

Native disulfide bond formation in proteins

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7 January 2021

Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl-mixed disulfides in ribonuclease A.

1 reference

https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Refolding by disulfide isomerization: the mixed disulfide between ribonuclease T1 and glutathione as a model refolding substrate

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Chaperone activity of DsbC

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7 January 2021

Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Photomodulation of conformational states. Synthesis of cyclic peptides with backbone-azobenzene moieties

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Thioredoxin-catalyzed refolding of disulfide-containing proteins

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridine

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Direct measurement of the equilibrium between glutathione and dithiothreitol by high performance liquid chromatography

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Spectrophotometric assay of bovine pancreatic ribonuclease by the use of cytidine 2':3'-phosphate

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

Pathways of folding of reduced bovine pancreatic ribonuclease

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https://api.crossref.org/works/10.1016%2FS1074-5521%2802%2900152-7

7 January 2021

10.1016/S1074-5521(02)00152-7

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DOI

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29 November 2017

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