Evidence map›Paper›PMID 21113270›Full record

ArticleNucleus (Austin, Tex.)

Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore.

Mario D Galigniana, Pablo C Echeverría, Alejandra G Erlejman, Graciela Piwien-Pilipuk

Open access · hybridAbstract read
In one paragraph

Article in Nucleus (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 110 citations in OpenAlex.

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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 3 institutions in 2 countries.

Mario D GalignianaDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina. mgali@dna.uba.ar
Pablo C Echeverría
Alejandra G Erlejman
Graciela Piwien-Pilipuk
Fundación Ciencias Exactas y Naturales · ARUniversity of Buenos Aires · ARUniversity of Geneva · CH

Funding

Chaperones, immunophilins and nuclear receptor shuttlingR03TW007162 · FIC · UNIVERSITY OF MISSISSIPPI MED CTR · PI GOMEZ-SANCHEZ, CELSO ENRIQUE · 2007 to 2009
$107k
C/EBPb and heterochromatin: their role in adipogenesisR03TW008143 · FIC · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWARTZ, JESSICA · 2009 to 2011
$103k
FIC NIH HHS R03 TW007162FIC NIH HHS R03 TW008143
6 · The paper itself

Abstract

In the absence of hormone, corticosteroid receptors such as GR (glucocorticoid receptor) and (mineralocorticoid receptor) are primarily located in the cytoplasm. Upon steroid-binding, they rapidly accumulate in the nucleus. Regardless of their primary location, these receptors and many other nuclear factors undergo a constant and dynamic nucleocytoplasmic shuttling. All members of the steroid receptor family are known to form large oligomeric structures with the heat-shock proteins of 90-kDa (hsp90) and 70-kDa (hsp70), the small acidic protein p23, and a tetratricopeptide repeat (TPR) -domain protein such as FK506-binding proteins (FKBPs), cyclophilins (CyPs) or the serine/threonine protein phosphatase 5 (PP5). It has always been stated that the dissociation of the chaperone heterocomplex (a process normally referred to as receptor "transformation") is the first step that permits the nuclear import of steroid receptors. However the experimental evidence is consistent with a model where the chaperone machinery is required for the retrotransport of the receptor through the cytoplasm and also facilitates the passage through the nuclear pore. Recent evidence indicates that the hsp90-based chaperone system also interacts with structures of the nuclear pore such as importin β and the integral nuclear pore glycoprotein Nup62 facilitating the passage of the untransformed receptor through the nuclear pore.

Indexed as

Active Transport, Cell Nucleusbeta KaryopherinsCell NucleusCyclophilinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsImmunophilinsModels, MolecularMolecular ChaperonesNuclear PoreNuclear ProteinsPhosphoprotein PhosphatasesReceptors, SteroidTacrolimus Binding Proteinsbeta KaryopherinsCyclophilinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsImmunophilinsMolecular ChaperonesNuclear ProteinsPhosphoprotein Phosphatasesprotein phosphatase 5Receptors, SteroidTacrolimus Binding Proteinsdyneinheat-shock proteinsimmunophilinsimportinsnucleoporinsshuttling

Identifiers

PMID21113270
PMCPMC2990191
OpenAlexW1995288330

What OpenQuestion holds

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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.