Evidence map›Paper›PMID 15497498›Full record

ReviewCell stress & chaperones2004

Tetratricopeptide repeat cochaperones in steroid receptor complexes.

David F Smith

Open access · greenAbstract readReview
In one paragraph

Review in Cell stress & chaperones, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed, 2 pooled it
4.7field-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

72 citing papers in PubMed, 2 syntheses or guidelines pooled it, 152 citations in OpenAlex.

  1. Pooled it
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  3. Review
  4. [A pan-cancer analysis of TTC9A expression level and its correlation with prognosis and immune microenvironment].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2024
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12 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

1 author at 1 institution in 1 country.

David F SmithS.C. Johnson Research Center, Mayo Clinic Scottsdale, Scottsdale, AZ 85259, USA. smith.david26@mayo.edu
Mayo Clinic in Arizona · US

Funding

CHAPERONE INTERACTIONS WITH REGULATORY PROTEINSR01DK044923 · NIDDK · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI SMITH, DAVID F. · 1992 to 2006
$1.7M
INTERACTION OF PROGESTERONE RECEPTOR WITH FKBPSR01DK048218 · NIDDK · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI SMITH, DAVID F. · 1994 to 2006
$1.5M
NIDDK NIH HHS R01 DK044923NIDDK NIH HHS R01 DK048218NIDDK NIH HHS R01 DK44923NIDDK NIH HHS R01 DK48218
6 · The paper itself

Abstract

The molecular chaperone machinery contains multiple protein components that have 1 or more structural domains composed of tetratricopeptide repeat (TPR) motifs. Many other proteins of separate or unknown function also have TPR domains, so this motif is not exclusive to molecular chaperones. A general function of TPR domains is to bind other polypeptides, but this otherwise prosaic function has been exploited in an assortment of ways that link chaperones and other protein systems into cooperative networks. Among the best-characterized TPR proteins are several cochaperones that participate in assembly and regulation of steroid receptor complexes. Steroid receptors, members of the nuclear receptor subfamily, are hormone-dependent transcription factors that regulate many vertebrate pathways of homeostasis, growth, differentiation, reproduction, and pathology and, as such, have been of great interest to biologists and clinicians. Moreover, the steroid receptors are among the first recognized native clients for chaperones and have been widely studied models for complex chaperone interactions. To provide a coherent, representative minireview of TPR protein function, the scope of this article has been narrowed down primarily to functions of steroid receptor-associated TPR cochaperones.

Indexed as

Repetitive Sequences, Nucleic AcidAnimalsHumansModels, BiologicalModels, MolecularMolecular ChaperonesPeptidesProtein Structure, SecondaryProtein Structure, TertiaryReceptors, SteroidTranscription FactorsMolecular ChaperonesPeptidesReceptors, SteroidTranscription Factors

Identifiers

PMID15497498
PMCPMC1065291
OpenAlexW2121034018

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.