Evidence map›Paper›PMID 29686082›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Reduction in adaptor amounts establishes degradation hierarchy among protease substrates.

Jinki Yeom, Xiaohui Gao, Eduardo A Groisman

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. 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
2.2field-weighted citation impact, top 12% 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, 21 citations in OpenAlex.

  1. Article
  2. Global analysis of protein degradation reveals instability of diverse regulators inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Review
  6. How Bacterial Pathogens Coordinate Appetite with Virulence.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  7. Review
  8. Article
  9. Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. How the PhoP/PhoQ System Controls Virulence and MgMicrobiology and molecular biology reviews : MMBR · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Small proteins regulateProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. The expanded specificity and physiological role of a widespread N-degron recognin.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Article
  18. N-degron and C-degron pathways of protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

3 authors at 1 institution in 1 country.

Jinki YeomDepartment of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT 06536.
Xiaohui GaoDepartment of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT 06536.
Eduardo A GroismanDepartment of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT 06536; eduardo.groisman@yale.edu.ORCID 0000-0001-6860-7691
Yale University · US

Funding

REGULATION OF SALMONELLA VIRULENCE BY THE PHOP PROTEINR01AI049561 · NIAID · YALE UNIVERSITY · PI Eduardo Groisman · 2001 to 2026
$9.7M
NIAID NIH HHS R01 AI049561
6 · The paper itself

Abstract

ATP-dependent proteases control critical cellular processes, including development, physiology, and virulence. A given protease may recognize a substrate directly via an unfoldase domain or subunit or indirectly via an adaptor that delivers the substrate to the unfoldase. We now report that cells achieve differential stability among substrates of a given protease by modulating adaptor amounts. We establish that the regulatory protein PhoP represses transcription of the gene specifying the ClpAP protease adaptor ClpS when the bacteria

Indexed as

ProteolysisBacterial ProteinsBase SequenceCarrier ProteinsEscherichia coliEscherichia coli ProteinsSalmonellaSequence HomologySubstrate SpecificityBacterial ProteinsCarrier ProteinsClpS protein, E coliEscherichia coli ProteinsPhoP protein, BacteriaPhoP protein, E coliClpAPClpScytoplasmic Mg2+PhoPproteolysis

Identifiers

PMID29686082
PMCPMC5948988
OpenAlexW2799627339

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.