Evidence map›Paper›PMID 8590809›Full record

ArticleMolecular biology of the cell1995

A role for Hsp90 in retinoid receptor signal transduction.

S J Holley, K R Yamamoto

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. Role of PARP-1 in prostate cancer.American journal of clinical and experimental urology · 2015
    Review
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  15. Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  16. Article
  17. Hsp90 is required for pheromone signaling in yeast.Molecular biology of the cell · 1998
    Article
  18. Article
  19. Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  20. Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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 1 institution in 1 country.

S J HolleyDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco 94143-0450, USA.
K R Yamamoto
University of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitous heat shock protein Hsp90 appears to participate directly in the function of a broad range of cellular signal transduction components, including steroid hormone receptors; however, an evolutionarily related subclass of intracellular receptors, exemplified by the retinoid receptors RAR and RXR, had been inferred from biochemical studies to function independently of Hsp90. To examine this issue genetically, we measured mammalian and avian retinoid receptor activity in a Saccharomyces cerevisiae strain in which the expression of the yeast Hsp90 homologue could be conditionally repressed approximately 20-fold relative to wild type. We tested transcriptional activation by RAR or RXR-RAR, from two types of retinoic acid response elements, triggered by three different agonist ligands. In every condition, we found that activation was severely compromised under conditions of low Hsp90 expression. We showed that the defect was in signal transduction rather than transcription activation per se, and that high affinity hormone binding was abolished in extracts of cells producing low levels of Hsp90. We suggest that Hsp90 may function in at least one step of signal transduction by all members of the intracellular receptor superfamily.

Indexed as

Signal TransductionTranscriptional ActivationAnimalsBase Sequencebeta-GalactosidaseChickensCloning, MolecularDesoxycorticosteroneGenotypeHSP90 Heat-Shock ProteinsHumansMammalsMolecular Sequence DataMutagenesis, InsertionalOligodeoxyribonucleotidesPlasmidsbeta-GalactosidaseDesoxycorticosteroneHSP90 Heat-Shock ProteinsOligodeoxyribonucleotidesReceptors, Retinoic AcidRecombinant ProteinsRetinoid X ReceptorsTranscription FactorsTretinoin

Identifiers

PMID8590809
PMCPMC301336
OpenAlexW1988836082

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.