Evidence map›Paper›PMID 30085058›Full record

ReviewFEMS microbiology letters2018

Bacterial secretion chaperones: the mycobacterial type VII case.

Trang H Phan, Edith N G Houben

Open access · hybridAbstract readReview
In one paragraph

Review in FEMS microbiology letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

6 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Differential expression of theApplied and environmental microbiology · 2024
    Article
  3. Modeling Tubercular ESX-1 Secretion Using Mycobacterium marinum.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  4. Review
  5. Review
  6. 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

2 authors at 1 institution in 1 country.

Trang H PhanSection Molecular Microbiology, Amsterdam Institute for Molecules, Medicines and Systems, Vrije Universiteit, Amsterdam, The Netherlands.
Edith N G HoubenSection Molecular Microbiology, Amsterdam Institute for Molecules, Medicines and Systems, Vrije Universiteit, Amsterdam, The Netherlands.
Vrije Universiteit Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chaperones are central players in maintaining the proteostasis in all living cells. Besides highly conserved generic chaperones that assist protein folding and assembly in the cytosol, additional more specific chaperones have evolved to ensure the successful trafficking of proteins with extra-cytoplasmic locations. Associated with the distinctive secretion systems present in bacteria, different dedicated chaperones have been described that not only keep secretory proteins in a translocation competent state, but often are also involved in substrate targeting to the specific translocation channel. Recently, a new class of such chaperones has been identified that are involved in the specific recognition of substrates transported via the type VII secretion pathway in mycobacteria. In this minireview, we provide an overview of the different bacterial chaperones with a focus on their roles in protein secretion and will discuss in detail the roles of mycobacterial type VII secretion chaperones in substrate recognition and targeting.

Indexed as

Bacterial Secretion SystemsBacterial ProteinsMolecular ChaperonesMycobacteriumProtein FoldingProtein TransportBacterial ProteinsBacterial Secretion SystemsMolecular Chaperones

Identifiers

PMID30085058
PMCPMC6109436
OpenAlexW2887297977

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.