Model peptide substrates and ligands in analysis of action of mammalian protein disulfide-isomerase (Q43909894)

28 November 2017

title

Model peptide substrates and ligands in analysis of action of mammalian protein disulfide-isomerase (English)

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28 November 2017

Robert B Freedman

1

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28 November 2017

Peter Klappa

series ordinal

2

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28 November 2017

Lloyd W Ruddock

series ordinal

3

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28 November 2017

language of work or name

English

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publication date

1 January 2002

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28 November 2017

published in

Methods in Enzymology

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28 November 2017

volume

348

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28 November 2017

page(s)

342-354

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Protein disulphide isomerase: building bridges in protein folding

28 November 2017

cites work

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The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules

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Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase

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The protein disulphide-isomerase family: unravelling a string of folds

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Mechanisms and catalysts of disulfide bond formation in proteins

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Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor

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Characterisation of the dominant oxidative folding intermediate of hen lysozyme

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The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.

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Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase

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Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase

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Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptide

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The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency

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7 January 2021

pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate

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Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase.

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In vivo cross-linking of protein disulfide isomerase to immunoglobulins

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7 January 2021

Protein Disulphide Isomerase and a Lumenal Cyclophilin-Type Peptidyl Prolyl Cis-Trans Isomerase are in Transient Contact with Secretory Proteins During Late Stages of Translocation

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7 January 2021

Pancreas specific protein disulfide isomerase, PDIp, is in transient contact with secretory proteins during late stages of translocation.

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7 January 2021

Interactions between protein disulphide isomerase and peptides

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7 January 2021

A pancreas-specific glycosylated protein disulphide-isomerase binds to misfolded proteins and peptides with an interaction inhibited by oestrogens

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7 January 2021

The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

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Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp

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The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligands

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7 January 2021

10.1016/S0076-6879(02)48653-3

Identifiers

DOI

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28 November 2017

1 reference