Evidence map›Paper›PMID 32020694›Full record

ReviewProtein science : a publication of the Protein Society2020

Bacterial secretins: Mechanisms of assembly and membrane targeting.

Yuri Rafael de Oliveira Silva, Carlos Contreras-Martel, Pauline Macheboeuf, Andréa Dessen

Open access · hybridAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Electron Cryo-Tomography Reveals thebioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Type IV pili ofEcoSal Plus · 2024
    Review
  7. Article
  8. Article
  9. Landmark Discoveries and Recent Advances in Type IV Pilus Research.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. The T3SS ofMicroorganisms · 2020
    Review
  18. Article
  19. Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020
    Review
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 2 institutions in 2 countries.

Yuri Rafael de Oliveira SilvaBrazilian Biosciences National Laboratory (LNBio), CNPEM, Campinas, São Paulo, Brazil.
Carlos Contreras-MartelUniversité Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), Grenoble, France.
Pauline MacheboeufUniversité Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), Grenoble, France.
Andréa DessenBrazilian Biosciences National Laboratory (LNBio), CNPEM, Campinas, São Paulo, Brazil.ORCID 0000-0001-6487-4020
Centre National de la Recherche Scientifique · FRUniversidade Estadual de Campinas (UNICAMP) · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secretion systems are employed by bacteria to transport macromolecules across membranes without compromising their integrities. Processes including virulence, colonization, and motility are highly dependent on the secretion of effector molecules toward the immediate cellular environment, and in some cases, into the host cytoplasm. In Type II and Type III secretion systems, as well as in Type IV pili, homomultimeric complexes known as secretins form large pores in the outer bacterial membrane, and the localization and assembly of such 1 MDa molecules often relies on pilotins or accessory proteins. Significant progress has been made toward understanding details of interactions between secretins and their partner proteins using approaches ranging from bacterial genetics to cryo electron microscopy. This review provides an overview of the mode of action of pilotins and accessory proteins for T2SS, T3SS, and T4PS secretins, highlighting recent near-atomic resolution cryo-EM secretin complex structures and underlining the importance of these interactions for secretin functionality.

Indexed as

BacteriaBacterial Outer Membrane ProteinsCryoelectron MicroscopyModels, MolecularSecretinBacterial Outer Membrane ProteinsSecretinbacterial virulenceprotein-protein interactionssecretintoxin secretionType IV pilus systemTypes II and III secretion systems

Identifiers

PMID32020694
PMCPMC7096711
OpenAlexW3005373240

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.