Evidence map›Paper›PMID 23920495›Full record

ReviewJournal of molecular microbiology and biotechnology2013

Prokaryotic proteasomes: nanocompartments of degradation.

Matthew A Humbard, Julie A Maupin-Furlow

Abstract readReview
In one paragraph

Review in Journal of molecular microbiology and biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. Protein degradation by a component of the chaperonin-linked protease ClpP.Genes to cells : devoted to molecular & cellular mechanisms · 2024
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Cell Clearing Systems Bridging Neuro-Immunity and Synaptic Plasticity.International journal of molecular sciences · 2019
    Review
  8. Review
  9. Article
  10. Structural analysis of the dodecameric proteasome activator PafE in Mycobacterium tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. 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 2 institutions in 1 country.

Matthew A HumbardLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Md., USA.
Julie A Maupin-Furlow
National Institutes of Health · USUniversity of Florida · US

Funding

Ubiquitin-like Small Archaeal Protein Modification (SAMPylation)R01GM057498 · NIGMS · UNIVERSITY OF FLORIDA · PI MAUPIN-FURLOW, JULIE A · 2000 to 2024
$4.9M
Intramural NIH HHSNIGMS NIH HHS R01 GM057498NIGMS NIH HHS R01 GM57498
6 · The paper itself

Abstract

Proteasomes are self-compartmentalized energy-dependent proteolytic machines found in Archaea, Actinobacteria species of bacteria and eukaryotes. Proteasomes consist of two separate protein complexes, the core particle that hydrolyzes peptide bonds and an AAA+ ATPase domain responsible for the binding, unfolding and translocation of protein substrates into the core particle for degradation. Similarly to eukaryotes, proteasomes play a central role in protein degradation and can be essential in Archaea. Core particles associate with and utilize a variety of ATPase complexes to carry out protein degradation in Archaea. In actinobacterial species, such as Mycobacterium tuberculosis, proteasome-mediated degradation is associated with pathogenesis and does not appear to be essential. Interestingly, both actinobacterial species and Archaea use small proteins to covalently modify proteins, prokaryotic ubiquitin-like proteins (Pup) in Actinobacteria and ubiquitin-like small archaeal modifier proteins (SAMP) in Archaea. These modifications may play a role in proteasome targeting similar to the ubiquitin-proteasome system in eukaryotes.

Indexed as

ProteolysisActinobacteriaArchaeaArchaeal ProteinsBacterial ProteinsProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalArchaeal ProteinsBacterial ProteinsProteasome Endopeptidase Complex

Identifiers

PMID23920495
PMCPMC3936408
OpenAlexW2032690262

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.