Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4 (Q27673881)

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Likun Wang

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Xi'e Wang

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Fei Sun

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Chih-chen Wang

Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p

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language of work or name

English

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publication date

1 January 2012

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published in

Biochemical Journal

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volume

441

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issue

1

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page(s)

113-8

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cites work

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Structure, mechanism and regulation of peroxiredoxins

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Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling

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ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin

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Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function

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Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum

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Peroxiredoxin 4 knockout results in elevated spermatogenic cell death via oxidative stress

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Phasercrystallographic software

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Refinement of macromolecular structures by the maximum-likelihood method

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

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UCSF Chimera--a visualization system for exploratory research and analysis

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Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics

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Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation

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Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin

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Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase

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B- to plasma-cell terminal differentiation entails oxidative stress and profound reshaping of the antioxidant responses

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Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells.

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A molecular specificity code for the three mammalian KDEL receptors

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Typical 2-Cys peroxiredoxins--structures, mechanisms and functions.

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Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery

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Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation

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Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin

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Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

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Experimental assessment of differences between related protein crystal structures

21 January 2018

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https://api.crossref.org/works/10.1042%2FBJ20110380

Activity assay of mammalian 2-cys peroxiredoxins using yeast thioredoxin reductase system

21 January 2018

1 reference

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Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence

21 January 2018

1 reference

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Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110380

Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins

21 January 2018

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Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins.

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21 January 2018

Identifiers

DOI

10.1042/BJ20110380

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

21916849

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Consolidated OpenCitations Corpus – April 2017