Evidence map›Paper›PMID 26071189›Full record

ReviewGene2015

Regulation and function of the human HSP90AA1 gene.

Abbey D Zuehlke, Kristin Beebe, Len Neckers, Thomas Prince

Abstract readReview
In one paragraph

Review in Gene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 199 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
199citing papers in PubMed, 3 pooled it
5.0field-weighted citation impact, top 4% 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

199 citing papers in PubMed, 3 syntheses or guidelines pooled it, 339 citations in OpenAlex.

  1. Pooled it
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  8. HSP90α lactylation orchestrates PGC1α and LRPGC1 nuclear translocation driving mitochondrial biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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139 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

4 authors at 2 institutions in 1 country.

Abbey D ZuehlkeUrologic Oncologic Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA. Electronic address: abbey.zuehlke@nih.gov.
Kristin BeebeUrologic Oncologic Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA.
Len NeckersUrologic Oncologic Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA.
Thomas PrinceUrologic Oncologic Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA.
Center for Cancer Research · USNational Cancer Institute · US

Funding

Role of HSP90 Family Chaperone Proteins in Cellular Signal TransductionZIASC010074 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI NECKERS, LEONARD · 2009 to 2025
$13.3M
Post-translational modifications of Hsp90 that impact drug efficacyZIABC011032 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NECKERS, LEONARD · 2009 to 2025
$11.5M
BioGPS: Extensible Web 2.0 gene portal for structured and unstructured annotationR01GM083924 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SU, ANDREW I, WU, CHUNLEI · 2008 to 2021
$5.6M
The Gene Wiki: Community intelligence applied to gene annotationR01GM089820 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SU, ANDREW I · 2010 to 2021
$5.2M
ROLE OF HSP90/GFP94 CHAPERONE PROTEINS IN CELLULAR SIGNAL TRANSDUCTIONZ01SC010074 · SC · DIVISION OF CLINICAL SCIENCES - NCI · PI NECKERS, LEONARD · 1996 to 2008
$3.7M
Post-translational modifications of Hsp90 that impact drug efficacyZ01BC011032 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NECKERS, LEONARD · 2008 to 2008
$664k
Intramural NIH HHS Z01 BC011032Intramural NIH HHS Z01 SC010074Intramural NIH HHS ZIA BC011032Intramural NIH HHS ZIA SC010074NIGMS NIH HHS GM089820NIGMS NIH HHS R01 GM083924
6 · The paper itself

Abstract

Heat shock protein 90α (Hsp90α), encoded by the HSP90AA1 gene, is the stress inducible isoform of the molecular chaperone Hsp90. Hsp90α is regulated differently and has different functions when compared to the constitutively expressed Hsp90β isoform, despite high amino acid sequence identity between the two proteins. These differences are likely due to variations in nucleotide sequence within non-coding regions, which allows for specific regulation through interaction with particular transcription factors, and to subtle changes in amino acid sequence that allow for unique post-translational modifications. This article will specifically focus on the expression, function and regulation of Hsp90α.

Indexed as

AnimalsGene ExpressionGene Expression RegulationHSP90 Heat-Shock ProteinsHumansNeoplasmsPromoter Regions, GeneticProtein Interaction MapsProtein Processing, Post-TranslationalHSP90AA1 protein, humanHSP90 Heat-Shock ProteinsCancerDrug targetGene ontologyGene promoterHeat shock elementHeat shock proteinInteractomeMolecular chaperonePost-translational modificationStress response

Identifiers

PMID26071189
PMCPMC4519370
OpenAlexW630675343

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.