Evidence map›Paper›PMID 25257025›Full record

ReviewCells2014

Bacterial effectors and their functions in the ubiquitin-proteasome system: insight from the modes of substrate recognition.

Minsoo Kim, Ryota Otsubo, Hanako Morikawa, Akira Nishide, Kenji Takagi, Chihiro Sasakawa, Tsunehiro Mizushima

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The emerging role of Deubiquitinases (DUBs) in parasites: A foresight review.Frontiers in cellular and infection microbiology · 2022
    Review
  9. Review
  10. Role of RONS and eIFs in Cancer Progression.Oxidative medicine and cellular longevity · 2021
    Review
  11. Ubiquitination ofmBio · 2019
    Article
  12. A Pathogen and a Non-pathogen Spotted Fever GroupFrontiers in cellular and infection microbiology · 2019
    Article
  13. Article
  14. Article
  15. Host FIH-Mediated Asparaginyl Hydroxylation of TranslocatedFrontiers in cellular and infection microbiology · 2017
    Article
  16. Crystal structure of the substrate-recognition domain of the Shigella E3 ligase IpaH9.8.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
  17. Article
  18. ROS and ROS-Mediated Cellular Signaling.Oxidative medicine and cellular longevity · 2016
    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

7 authors at 2 institutions in 1 country.

Minsoo KimDivision of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Shirokanedai 4-6-1, Minato-ku 4-6-1, Tokyo 108-8639, Japan. minsoo@ims.u-tokyo.ac.jp.
Ryota OtsuboDivision of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Shirokanedai 4-6-1, Minato-ku 4-6-1, Tokyo 108-8639, Japan. r-otsubo@ims.u-tokyo.ac.jp.
Hanako MorikawaDivision of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Shirokanedai 4-6-1, Minato-ku 4-6-1, Tokyo 108-8639, Japan. h-mrkw@ims.u-tokyo.ac.jp.
Akira NishidePicobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1, Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan. rj12k019@stkt.u-hyogo.ac.jp.
Kenji TakagiPicobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1, Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan. ktakagi@sci.u-hyogo.ac.jp.
Chihiro SasakawaDivision of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Shirokanedai 4-6-1, Minato-ku 4-6-1, Tokyo 108-8639, Japan. sasakawa@ims.u-tokyo.ac.jp.
Tsunehiro MizushimaPicobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1, Kouto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan. mizushi@sci.u-hyogo.ac.jp.
The University of Tokyo · JPUniversity of Hyogo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein ubiquitination plays indispensable roles in the regulation of cell homeostasis and pathogenesis of neoplastic, infectious, and neurodegenerative diseases. Given the importance of this modification, it is to be expected that several pathogenic bacteria have developed the ability to utilize the host ubiquitin system for their own benefit. Modulation of the host ubiquitin system by bacterial effector proteins inhibits innate immune responses and hijacks central signaling pathways. Bacterial effectors mimic enzymes of the host ubiquitin system, but may or may not be structurally similar to the mammalian enzymes. Other effectors bind and modify components of the host ubiquitin system, and some are themselves subject to ubiquitination. This review will describe recent findings, based on structural analyses, regarding how pathogens use post-translational modifications of proteins to establish an infection.

Identifiers

PMID25257025
PMCPMC4197628
OpenAlexW2040391028

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.