Evidence map›Paper›PMID 28515311›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway.

Jang-Hyun Oh, Ju-Yeon Hyun, Alexander Varshavsky

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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
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.

Jang-Hyun OhDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Ju-Yeon HyunDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Alexander VarshavskyDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125 avarsh@caltech.edu.

Funding

The Functions, Mechanisms, and Regulation of N-Terminal ArginylationR01GM031530 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALEXANDER J VARSHAVSKY · 1985 to 2026
$14.5M
Ubiquitin Ligases, Mechanisms and Functions of the N-End Rule PathwayR01DK039520 · NIDDK · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI VARSHAVSKY, ALEXANDER J · 1988 to 2025
$10.0M
MECHANICS AND FUNCTIONS OF THE N-END RULE PATHWAYR37DK039520 · NIDDK · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI VARSHAVSKY, ALEXANDER J · 1998 to 2007
$4.4M
Ubiquitin Ligases, Mechanisms and Functions of the N-End Rule PathwayR56DK039520 · NIDDK · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI VARSHAVSKY, ALEXANDER J · 2008 to 2008
$161k
NIDDK NIH HHS R01 DK039520NIDDK NIH HHS R37 DK039520NIDDK NIH HHS R56 DK039520NIGMS NIH HHS R01 GM031530
6 · The paper itself

Abstract

We found that the heat shock protein 90 (Hsp90) chaperone system of the yeast

Indexed as

AcetylationCheckpoint Kinase 1Enzyme StabilityGenes, FungalHomeodomain ProteinsHSP90 Heat-Shock ProteinsMetabolic Networks and PathwaysMutationN-Terminal Acetyltransferase APromoter Regions, GeneticProteolysisRegulonSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityTranscription FactorsCheckpoint Kinase 1CUP9 protein, S cerevisiaeHomeodomain ProteinsHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsN-Terminal Acetyltransferase ASaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitin-Protein LigasesUBR1 protein, S cerevisiaeUfd4 protein, S cerevisiaeChk1Naa10protein degradationUbr1Ufd4

Identifiers

PMID28515311
PMCPMC5465900

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.