Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells. (Q40041803)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18052930%20AND%20SRC:MED&resulttype=core&format=json

28 December 2019

title

Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells (English)

1 reference

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28 December 2019

main subject

endoplasmic reticulum

0 references

author

Neil J. Bulleid

series ordinal

3

1 reference

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28 December 2019

author name string

Timothy J Tavender

series ordinal

1

1 reference

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28 December 2019

Alyson M Sheppard

series ordinal

2

1 reference

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28 December 2019

language of work or name

English

0 references

publication date

1 April 2008

1 reference

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28 December 2019

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28 December 2019

volume

411

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28 December 2019

issue

1

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28 December 2019

page(s)

191-199

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Human peroxiredoxin 1 and 2 are not duplicate proteins: the unique presence of CYS83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2

28 December 2019

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22 September 2017

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22 September 2017

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

22 September 2017

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22 September 2017

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22 September 2017

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22 September 2017

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Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein

22 September 2017

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A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress

22 September 2017

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22 September 2017

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Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site

22 September 2017

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XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

22 September 2017

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A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation

22 September 2017

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Characterization of the Mycobacterium tuberculosis H37Rv alkyl hydroperoxidase AhpC points to the importance of ionic interactions in oligomerization and activity

22 September 2017

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The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins

22 September 2017

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Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution

22 September 2017

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Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

22 September 2017

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Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product

22 September 2017

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Activation of active-site cysteine residues in the peroxiredoxin-type tryparedoxin peroxidase of Crithidia fasciculata

22 September 2017

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Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member

22 September 2017

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22 September 2017

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22 September 2017

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22 September 2017

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22 September 2017

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22 September 2017

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25 September 2017

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25 September 2017

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15 June 2018

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20 August 2018

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The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum

20 August 2018

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

20 August 2018

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Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium.

20 August 2018

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The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells

20 August 2018

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Identification by anti-idiotype antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal

20 August 2018

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Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter pylori

1 October 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/18052930

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12 December 2020

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Identifiers

DOI

10.1042/BJ20071428

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18052930%20AND%20SRC:MED&resulttype=core&format=json

release_ehmskw5icra4dbuaudimecrrmm

28 December 2019

Fatcat ID

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Fatcat

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mapped directly with Wikidata item

24 November 2022

based on heuristic

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28 December 2019

PubMed publication ID

18052930

1 reference