Evidence map›Paper›PMID 32487747›Full record

ReviewThe Journal of biological chemistry2020

How the assembly and protection of the bacterial cell envelope depend on cysteine residues.

Jean-François Collet, Seung-Hyun Cho, Bogdan I Iorga, Camille V Goemans

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 43 citations in OpenAlex.

  1. Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. The emerging roles of disulfidptosis in cancer.Apoptosis : an international journal on programmed cell death · 2026
    Review
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  10. Disulfidptosis: A new type of cell death.Apoptosis : an international journal on programmed cell death · 2024
    Review
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  17. A conserved zinc-binding site inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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 3 institutions in 3 countries.

Jean-François Colletde Duve Institute, UCLouvain, Brussels, Belgium; WELBIO, Brussels, Belgium. Electronic address: jfcollet@uclouvain.be.
Seung-Hyun Chode Duve Institute, UCLouvain, Brussels, Belgium; WELBIO, Brussels, Belgium.
Bogdan I Iorgade Duve Institute, UCLouvain, Brussels, Belgium; Université Paris-Saclay, CNRS UPR 2301, Institut de Chimie des Substances Naturelles, Gif-sur-Yvette, France.
Camille V GoemansEuropean Molecular Biology Laboratory, Heidelberg, Germany.
de Duve Institute · BECentre National de la Recherche Scientifique · FREuropean Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cell envelope of Gram-negative bacteria is a multilayered structure essential for bacterial viability; the peptidoglycan cell wall provides shape and osmotic protection to the cell, and the outer membrane serves as a permeability barrier against noxious compounds in the external environment. Assembling the envelope properly and maintaining its integrity are matters of life and death for bacteria. Our understanding of the mechanisms of envelope assembly and maintenance has increased tremendously over the past two decades. Here, we review the major achievements made during this time, giving central stage to the amino acid cysteine, one of the least abundant amino acid residues in proteins, whose unique chemical and physical properties often critically support biological processes. First, we review how cysteines contribute to envelope homeostasis by forming stabilizing disulfides in crucial bacterial assembly factors (LptD, BamA, and FtsN) and stress sensors (RcsF and NlpE). Second, we highlight the emerging role of enzymes that use cysteine residues to catalyze reactions that are necessary for proper envelope assembly, and we also explain how these enzymes are protected from oxidative inactivation. Finally, we suggest future areas of investigation, including a discussion of how cysteine residues could contribute to envelope homeostasis by functioning as redox switches. By highlighting the redox pathways that are active in the envelope of

Indexed as

Cell WallCysteineEscherichia coliEscherichia coli ProteinsCysteineEscherichia coli Proteinsbacterial signal transductionBamACpxdisulfideDsbADsbCDsbDFtsNGram-negative bacteriaLdtAl,d-transpeptidaselipopolysaccharideLptDNlpEouter membraneoxidative stresspeptidoglycanRcsFRcs systemsulfenic acidthioredoxinYbiS

Identifiers

PMID32487747
PMCPMC7443483
OpenAlexW3031810862

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.