Evidence map›Paper›PMID 23521714›Full record

ReviewBiochemistry2013

Structure and biophysics of type III secretion in bacteria.

Srirupa Chatterjee, Sukanya Chaudhury, Andrew C McShan, Kawaljit Kaur, Roberto N De Guzman

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
11.8field-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

64 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Computational prediction of secreted proteins in gram-negative bacteria.Computational and structural biotechnology journal · 2021
    Review
  14. Review
  15. Article
  16. Microorganisms · 2020
    Review
  17. Article
  18. Article
  19. NovelFrontiers in microbiology · 2020
    Article
  20. High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article

4 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

5 authors at 1 institution in 1 country.

Srirupa ChatterjeeDepartment of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, USA.
Sukanya Chaudhury
Andrew C McShan
Kawaljit Kaur
Roberto N De Guzman
University of Kansas · US

Funding

PHARMACEUTICAL ASPECTS OF BIOTECHNOLOGY TRAININGT32GM008359 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI SIAHAAN, TERUNA J., VOLKIN, DAVID · 1989 to 2018
$5.0M
NMR studies of bacterial needle and tip proteinsR01AI074856 · NIAID · UNIVERSITY OF KANSAS LAWRENCE · PI DE GUZMAN, ROBERTO N · 2008 to 2018
$3.6M
NIAID NIH HHS R01 AI074856NIAID NIH HHS R01AI074856NIGMS NIH HHS T32 GM008359NIGMS NIH HHS T32-GM008359
6 · The paper itself

Abstract

Many plant and animal bacterial pathogens assemble a needle-like nanomachine, the type III secretion system (T3SS), to inject virulence proteins directly into eukaryotic cells to initiate infection. The ability of bacteria to inject effectors into host cells is essential for infection, survival, and pathogenesis for many Gram-negative bacteria, including Salmonella, Escherichia, Shigella, Yersinia, Pseudomonas, and Chlamydia spp. These pathogens are responsible for a wide variety of diseases, such as typhoid fever, large-scale food-borne illnesses, dysentery, bubonic plague, secondary hospital infections, and sexually transmitted diseases. The T3SS consists of structural and nonstructural proteins. The structural proteins assemble the needle apparatus, which consists of a membrane-embedded basal structure, an external needle that protrudes from the bacterial surface, and a tip complex that caps the needle. Upon host cell contact, a translocon is assembled between the needle tip complex and the host cell, serving as a gateway for translocation of effector proteins by creating a pore in the host cell membrane. Following delivery into the host cytoplasm, effectors initiate and maintain infection by manipulating host cell biology, such as cell signaling, secretory trafficking, cytoskeletal dynamics, and the inflammatory response. Finally, chaperones serve as regulators of secretion by sequestering effectors and some structural proteins within the bacterial cytoplasm. This review will focus on the latest developments and future challenges concerning the structure and biophysics of the needle apparatus.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsBacterial Secretion SystemsBiophysicsGram-Negative BacteriaHost-Pathogen InteractionsProtein ConformationSalmonellaShigellaYersinia pestisBacterial Outer Membrane ProteinsBacterial ProteinsBacterial Secretion Systems

Identifiers

PMID23521714
PMCPMC3711828
OpenAlexW1999248739

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.