Oxidative protein folding in eukaryotes: mechanisms and consequences (Q24676827)

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English	Oxidative protein folding in eukaryotes: mechanisms and consequences	scientific article

Statements

instance of

scholarly article

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review article

2 references

stated in

PubMed

retrieved

12 October 2019

stated in

PubMed

retrieved

15 December 2019

title

Oxidative protein folding in eukaryotes: mechanisms and consequences (English)

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main subject

cell biology

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protein folding

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cell

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PubMed

retrieved

12 October 2019

membrane protein

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stated in

PubMed

retrieved

15 December 2019

author

Jonathan Weissman

series ordinal

2

object named as

Jonathan S Weissman

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author name string

Benjamin P Tu

series ordinal

1

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language of work or name

English

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publication date

2 February 2004

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stated in

PubMed Central

retrieved

12 October 2019

stated in

PubMed Central

retrieved

15 December 2019

published in

Journal of Cell Biology

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stated in

PubMed Central

retrieved

12 October 2019

stated in

PubMed Central

retrieved

15 December 2019

volume

164

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issue

3

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page(s)

341-6

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cites work

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

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PubMed Central

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Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1

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7 April 2017

ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family

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PubMed Central

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7 April 2017

Manipulation of oxidative protein folding and PDI redox state in mammalian cells

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PubMed Central

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7 April 2017

Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum

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PubMed Central

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7 April 2017

Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response

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PubMed Central

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7 April 2017

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

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PubMed Central

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7 April 2017

A pathway for disulfide bond formation in vivo

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PubMed Central

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7 April 2017

A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p

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PubMed Central

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7 April 2017

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

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PubMed Central

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7 April 2017

An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins

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PubMed Central

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7 April 2017

Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family

1 reference

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PubMed Central

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7 April 2017

Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase

1 reference

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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7 April 2017

Ero1p: A Novel and Ubiquitous Protein with an Essential Role in Oxidative Protein Folding in the Endoplasmic Reticulum

1 reference

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PubMed Central

reference URL

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7 April 2017

The ERO1 Gene of Yeast Is Required for Oxidation of Protein Dithiols in the Endoplasmic Reticulum

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stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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7 April 2017

Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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7 April 2017

Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes

1 reference

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PubMed Central

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7 April 2017

Pathways for protein disulphide bond formation

1 reference

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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7 April 2017

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

1 reference

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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7 April 2017

The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1‐Lα

1 reference

stated in

PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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7 April 2017

An integrated stress response regulates amino acid metabolism and resistance to oxidative stress

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

retrieved

7 April 2017

Oxidized redox state of glutathione in the endoplasmic reticulum

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stated in

PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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7 April 2017

Quantitating protein synthesis, degradation, and endogenous antigen processing

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

retrieved

28 September 2017

The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function

1 reference

stated in

PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 September 2017

Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.

1 reference

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 September 2017

Biochemical basis of oxidative protein folding in the endoplasmic reticulum

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 September 2017

A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 September 2017

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 September 2017

Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo

1 reference

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 September 2017

The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 September 2017

Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 September 2017

Molecular and cellular aspects of thiol-disulfide exchange.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

retrieved

28 September 2017

Active Site Mutations in Yeast Protein Disulfide Isomerase Cause Dithiothreitol Sensitivity and a Reduced Rate of Protein Folding in the Endoplasmic Reticulum

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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30 May 2018

ERV1 is involved in the cell-division cycle and the maintenance of mitochondrial genomes in Saccharomyces cerevisiae

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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30 May 2018

Identification of a protein required for disulfide bond formation in vivo

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

retrieved

30 May 2018

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 November 2018

Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2172237

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28 November 2018

Chromatographic determination of flavin derivatives in baker's yeast

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/14757749

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Oxidative protein folding is driven by the electron transport system

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/14757749

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/14757749

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Competition between glutathione and protein thiols for disulphide-bond formation

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/14757749

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/14757749

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Disulfide bonds are generated by quinone reduction

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/14757749

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/14757749

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1083/JCB.200311055

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1412767

OpenCitations bibliographic resource ID

1412767

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1412767

PMC publication ID

2172237

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1412767

PubMed publication ID

14757749

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1412767

ResearchGate publication ID

8890247

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