Evidence map›Paper›PMID 14532117›Full record

ArticleThe EMBO journal2003

CHIP activates HSF1 and confers protection against apoptosis and cellular stress.

Qian Dai, Chunlian Zhang, Yaxu Wu, Holly McDonough, Ryan A Whaley, Virginia Godfrey, Hui-Hua Li, Nageswara Madamanchi, Wanping Xu, Len Neckers and 2 more

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 173 papers.

0numbers the graph read from it
0cells of the map it votes in
173citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

173 citing papers in PubMed, 318 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Chaperone Proteins: The Rising Players in Muscle Atrophy.Journal of cachexia, sarcopenia and muscle · 2025
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Thermal Stress and Nuclear Transport.Advances in experimental medicine and biology · 2024
    Review
  15. Article
  16. Article
  17. HSF1 and Its Role in Huntington's Disease Pathology.Advances in experimental medicine and biology · 2023
    Review
  18. Article
  19. Review
  20. Article

113 more citing papers are in PubMed but not listed here.

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

12 authors at 1 institution in 1 country.

Qian DaiCarolina Cardiovascular Biology Center, and Department of Medicine, University of North Carolina, Chapel Hill, NC, USA.
Chunlian Zhang
Yaxu Wu
Holly McDonough
Ryan A Whaley
Virginia Godfrey
Hui-Hua Li
Nageswara Madamanchi
Wanping Xu
Len Neckers
Douglas Cyr
Cam Patterson
University of North Carolina at Chapel Hill · US

Funding

Roles for Hsp70 and Hsp40 in Membrane Protein TriageR01GM056981 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CYR, DOUGLAS M · 1998 to 2019
$6.1M
Myocyte Signaling and the Response to StressR37HL065619 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PATTERSON, WINSTON C · 2010 to 2019
$3.7M
ROLE OF HSP90/GFP94 CHAPERONE PROTEINS IN CELLULAR SIGNAL TRANSDUCTIONZ01SC010074 · SC · DIVISION OF CLINICAL SCIENCES - NCI · PI NECKERS, LEONARD · 1996 to 2008
$3.7M
CHIP: A link between the chaperone &proteasome systemsR01GM061728 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SCHISLER, JONATHAN C. · 2001 to 2013
$3.4M
Myocyte signaling and the response to stressR01HL065619 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PATTERSON, WINSTON C · 2001 to 2009
$2.7M
NHLBI NIH HHS HL65619NHLBI NIH HHS R01 HL065619NHLBI NIH HHS R37 HL065619NIGMS NIH HHS GM56981NIGMS NIH HHS GM61728NIGMS NIH HHS R01 GM056981NIGMS NIH HHS R01 GM061728
6 · The paper itself

Abstract

Induction of molecular chaperones is the characteristic protective response to environmental stress, and is regulated by a transcriptional program that depends on heat shock factor 1 (HSF1), which is normally under negative regulatory control by molecular chaperones Hsp70 and Hsp90. In metazoan species, the chaperone system also provides protection against apoptosis. We demonstrate that the dual function co-chaperone/ubiquitin ligase CHIP (C-terminus of Hsp70-interacting protein) regulates activation of the stress-chaperone response through induced trimerization and transcriptional activation of HSF1, and is required for protection against stress-induced apoptosis in murine fibroblasts. The consequences of this function are demonstrated by the phenotype of mice lacking CHIP, which develop normally but are temperature-sensitive and develop apoptosis in multiple organs after environmental challenge. CHIP exerts a central and unique role in tuning the response to stress at multiple levels by regulation of protein quality control and transcriptional activation of stress response signaling.

Indexed as

Amino Acid SubstitutionAnimalsApoptosisCells, CulturedChlorocebus aethiopsCOS CellsDNA-Binding ProteinsFibroblastsGene Expression RegulationHeat Shock Transcription FactorsHot TemperatureHSP70 Heat-Shock ProteinsMiceMice, KnockoutMutagenesis, Site-DirectedPromoter Regions, GeneticDNA-Binding ProteinsHeat Shock Transcription FactorsHSF1 protein, humanHSP70 Heat-Shock ProteinsRecombinant ProteinsSTUB1 protein, humanTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID14532117
PMCPMC213783
OpenAlexW2098076627

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.