Evidence map›Paper›PMID 38965067›Full record

ReviewGenes to cells : devoted to molecular & cellular mechanisms2024

Protein degradation by a component of the chaperonin-linked protease ClpP.

Fumihiro Ishikawa, Michio Homma, Genzoh Tanabe, Takayuki Uchihashi

Abstract readReview
In one paragraph

Review in Genes to cells : devoted to molecular & cellular mechanisms, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Protein degradation by a component of the chaperonin-linked protease ClpP.Genes to cells : devoted to molecular & cellular mechanisms · 2024
    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.

Fumihiro IshikawaFaculty of Pharmacy, Kindai University, Osaka, Japan.
Michio HommaDepartment of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.ORCID https://orcid.org/0000-0002-5371-001X
Genzoh TanabeFaculty of Pharmacy, Kindai University, Osaka, Japan.
Takayuki UchihashiDivision of Material Science, Graduate School of Science, Nagoya University, Nagoya, Japan.

Funding

Japan Society for the Promotion of Science 20H03220
6 · The paper itself

Abstract

In cells, proteins are synthesized, function, and degraded (dead). Protein synthesis (spring) is important for the life of proteins. However, how proteins die is equally important for organisms. Proteases are secreted from cells and used as nutrients to break down external proteins. Proteases degrade unwanted and harmful cellular proteins. In eukaryotes, a large enzyme complex called the proteasome is primarily responsible for cellular protein degradation. Prokaryotes, such as bacteria, have similar protein degradation systems. In this review, we describe the structure and function of the ClpXP complex in the degradation system, which is an ATP-dependent protease in bacterial cells, with a particular focus on ClpP.

Indexed as

Endopeptidase ClpProteolysisBacterial ProteinsChaperoninsProteasome Endopeptidase ComplexBacterial ProteinsChaperoninsEndopeptidase ClpProteasome Endopeptidase ComplexATPaseClpXE. coliLonproteasome

Identifiers

PMID38965067
PMCPMC11448347

What OpenQuestion holds

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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.