Evidence map›Paper›PMID 20136510›Full record

ReviewAntioxidants & redox signaling2010

Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins.

Vamsi K Kodali, Colin Thorpe

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
6.8field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

71 citing papers in PubMed, 130 citations in OpenAlex.

  1. Oxidative protein folding and CaCellular and molecular life sciences : CMLS · 2026
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11 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Vamsi K KodaliDepartment of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19711, USA.
Colin Thorpe
University of Delaware · US

Funding

Flavoproteins in Oxidative Protein FoldingR01GM026643 · NIGMS · UNIVERSITY OF DELAWARE · PI THORPE, COLIN · 1985 to 2019
$6.6M
NIGMS NIH HHS GM26643NIGMS NIH HHS R01 GM026643
6 · The paper itself

Abstract

Flavin-linked sulfhydryl oxidases participate in the net generation of disulfide bonds during oxidative protein folding in the endoplasmic reticulum. Members of the Quiescin-sulfhydryl oxidase (QSOX) family catalyze the facile direct introduction of disulfide bonds into unfolded reduced proteins with the reduction of molecular oxygen to generate hydrogen peroxide. Current progress in dissecting the mechanism of QSOX enzymes is reviewed, with emphasis on the CxxC motifs in the thioredoxin and Erv/ALR domains and the involvement of the flavin prosthetic group. The tissue distribution and intra- and extracellular location of QSOX enzymes are discussed, and suggestions for the physiological role of these enzymes are presented. The review compares the substrate specificity and catalytic efficiency of the QSOX enzymes with members of the Ero1 family of flavin-dependent sulfhydryl oxidases: enzymes believed to play key roles in disulfide generation in yeast and higher eukaryotes. Finally, limitations of our current understanding of disulfide generation in metazoans are identified and questions posed for the future.

Indexed as

Protein FoldingAnimalsDisulfidesEndoplasmic ReticulumFlavoproteinsHumansOxidation-ReductionOxidoreductases Acting on Sulfur Group DonorsDisulfidesFlavoproteinsOxidoreductases Acting on Sulfur Group Donors

Identifiers

PMID20136510
PMCPMC2959182
OpenAlexW2088913673

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.