Evidence map›Paper›PMID 28699750›Full record

ReviewChemical reviews2018

Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.

Deborah Fass, Colin Thorpe

Abstract readReview
In one paragraph

Review in Chemical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
8.6field-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

91 citing papers in PubMed, 289 citations in OpenAlex.

  1. The Lord of the Rings: Cysteine bonds crosslink the tail of siphovirus.Protein science : a publication of the Protein Society · 2026
    Article
  2. Giant viruses encode vitamin K-based redox modules for lipid modification.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  17. CaNature cell biology · 2025
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31 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 2 institutions in 2 countries.

Deborah FassDepartment of Structural Biology, Weizmann Institute of Science , Rehovot 7610001, Israel.ORCID 0000-0001-9418-6069
Colin ThorpeDepartment of Chemistry and Biochemistry, University of Delaware , Newark, Delaware 19716, United States.
University of Delaware · USWeizmann Institute of Science · IL

Funding

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

Abstract

Cysteine thiols are among the most reactive functional groups in proteins, and their pairing in disulfide linkages is a common post-translational modification in proteins entering the secretory pathway. This modest amino acid alteration, the mere removal of a pair of hydrogen atoms from juxtaposed cysteine residues, contrasts with the substantial changes that characterize most other post-translational reactions. However, the wide variety of proteins that contain disulfides, the profound impact of cross-linking on the behavior of the protein polymer, the numerous and diverse players in intracellular pathways for disulfide formation, and the distinct biological settings in which disulfide bond formation can take place belie the simplicity of the process. Here we lay the groundwork for appreciating the mechanisms and consequences of disulfide bond formation in vivo by reviewing chemical principles underlying cysteine pairing and oxidation. We then show how enzymes tune redox-active cofactors and recruit oxidants to improve the specificity and efficiency of disulfide formation. Finally, we discuss disulfide bond formation in a cellular context and identify important principles that contribute to productive thiol oxidation in complex, crowded, dynamic environments.

Indexed as

BacteriaDisulfidesGlutathione PeroxidasePeriplasmPeroxiredoxinsProtein Disulfide-IsomerasesProtein FoldingProtein Processing, Post-TranslationalProteinsSulfhydryl CompoundsDisulfidesGlutathione PeroxidasePeroxiredoxinsProtein Disulfide-IsomerasesProteinsSulfhydryl Compounds

Identifiers

PMID28699750
PMCPMC5808910
OpenAlexW2734790238

What OpenQuestion holds

Textmetadata
LicenceTDM
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.