Evidence map›Paper›PMID 29180682›Full record

ArticleScientific reports2017

Features of reactive cysteines discovered through computation: from kinase inhibition to enrichment around protein degrons.

Nicholas J Fowler, Christopher F Blanford, Sam P de Visser, Jim Warwicker

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Proteasomal surveillance of exposed cysteines.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Reactive oxygen species: role in obesity and mitochondrial energy efficiency.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
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  7. Article
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  14. Computational Structural Biology ofFrontiers in oncology · 2018
    Review
  15. Article
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

4 authors at 1 institution in 1 country.

Nicholas J FowlerThe Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom.ORCID 0000-0002-6005-935X
Christopher F BlanfordThe Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom.ORCID 0000-0002-0112-7818
Sam P de VisserThe Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom.
Jim WarwickerThe Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom. jim.warwicker@manchester.ac.uk.ORCID 0000-0002-1302-0815
University of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J014478/1
6 · The paper itself

Abstract

Large-scale characterisation of cysteine modification is enabling study of the physicochemical determinants of reactivity. We find that location of cysteine at the amino terminus of an α-helix, associated with activity in thioredoxins, is under-represented in human protein structures, perhaps indicative of selection against background reactivity. An amino-terminal helix location underpins the covalent linkage for one class of kinase inhibitors. Cysteine targets for S-palmitoylation, S-glutathionylation, and S-nitrosylation show little correlation with pKa values predicted from structures, although flanking sequences of S-palmitoylated sites are enriched in positively-charged amino acids, which could facilitate palmitoyl group transfer to substrate cysteine. A surprisingly large fraction of modified sites, across the three modifications, would be buried in native protein structure. Furthermore, modified cysteines are (on average) closer to lysine ubiquitinations than are unmodified cysteines, indicating that cysteine redox biology could be associated with protein degradation and degron recognition.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsComputational BiologyCysteineDrug DiscoveryHumansMiceModels, BiologicalPhosphotransferasesProtein ConformationProtein DomainsProtein FoldingProtein Kinase InhibitorsProtein Processing, Post-TranslationalStructure-Activity RelationshipCysteinePhosphotransferasesProtein Kinase Inhibitors

Identifiers

PMID29180682
PMCPMC5703995
OpenAlexW2769480569

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.