Evidence map›Paper›PMID 30635401›Full record

ReviewThe Journal of biological chemistry2019

Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation.

Joyce Chiu, Philip J Hogg

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
13.7field-weighted citation impact, top 1% 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

76 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
  2. Oxidative protein folding and CaCellular and molecular life sciences : CMLS · 2026
    Review
  3. Article
  4. Review
  5. Biochemistry · 2026
    Article
  6. Article
  7. Dynamic regulation of receptor-modulated endothelial NADPH oxidases.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. Quantification of the Redox State of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  12. Classification of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  13. Using AlphaFold3 for the Interrogation of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  14. Estimate of Numbers of Disulfide-Bonded Protein States.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

16 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.

Joyce ChiuFrom the Centenary Institute, National Health and Medical Research Council Clinical Trials Centre, Sydney Medical School, University of Sydney, Camperdown, New South Wales 2006, Australia.
Philip J HoggFrom the Centenary Institute, National Health and Medical Research Council Clinical Trials Centre, Sydney Medical School, University of Sydney, Camperdown, New South Wales 2006, Australia phil.hogg@sydney.edu.au.ORCID 0000-0001-6486-2863
The University of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein disulfide bonds link pairs of cysteine residues in polypeptide chains. Many of these bonds serve a purely structural or energetic role, but a growing subset of cleavable disulfide bonds has been shown to control the function of the mature protein in which they reside. These allosteric disulfides and the factors that cleave these bonds are being identified across biological systems and life forms and have been shown to control hemostasis, the immune response, and viral infection in mammals. The discovery of these functional disulfides and a rationale for their facile nature has been aided by the emergence of a conformational signature for allosteric bonds. This post-translational modification mostly occurs extracellularly, making these chemical events prime drug targets. Indeed, a membrane-impermeable inhibitor of one of the cleaving factors is currently being trialed as an antithrombotic agent in cancer patients. Allosteric disulfides are firmly established as a sophisticated means by which a protein's shape and function can be altered; however, the full scope of this biological regulation will not be realized without new tools and techniques to study this regulation and innovative ways of targeting it.

Indexed as

HemostasisImmunityAnimalsHumansNeoplasm ProteinsNeoplasmsProtein Processing, Post-TranslationalVirus DiseasesNeoplasm Proteinsallostericcysteinecystinedisulfidedisulfide bonddrug discoveryoxidation-reduction (redox)oxidoreductasepost-translational modificationprotein chemical modificationprotein chemistryprotein conformationprotein disulfide isomeraseprotein dynamicthiol

Identifiers

PMID30635401
PMCPMC6393624
OpenAlexW2908893558

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.