Evidence map›Paper›PMID 30717249›Full record

ReviewBiomolecules2019

Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52

Nadia R Zgajnar, Sonia A De Leo, Cecilia M Lotufo, Alejandra G Erlejman, Graciela Piwien-Pilipuk, Mario D Galigniana

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.5field-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

52 citing papers in PubMed, 91 citations in OpenAlex.

  1. FKBP51: A new target for Parkinson's disease.Neural regeneration research · 2026
    Article
  2. Article
  3. Review
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  8. Genome-wide identification and expression analyses ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. DnaJs are enriched in tau regulators.International journal of biological macromolecules · 2023
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review
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

6 authors at 1 institution in 1 country.

Nadia R ZgajnarInstituto de Biología y Medicina Experimental/CONICET, Buenos Aires 1428, Argentina. nadiazgajnar@gmail.com.
Sonia A De LeoDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires-CONICET, Buenos Aires 1428, Argentina. sonydeleo@hotmail.com.
Cecilia M LotufoInstituto de Biología y Medicina Experimental/CONICET, Buenos Aires 1428, Argentina. cecilialotufo@yahoo.com.ar.
Alejandra G ErlejmanDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires-CONICET, Buenos Aires 1428, Argentina. erlejman@qb.fcen.uba.ar.
Graciela Piwien-PilipukInstituto de Biología y Medicina Experimental/CONICET, Buenos Aires 1428, Argentina. gpiwien@conicet.gov.ar.
Mario D GalignianaInstituto de Biología y Medicina Experimental/CONICET, Buenos Aires 1428, Argentina. mgaligniana@conicet.gov.ar.
Consejo Nacional de Investigaciones Científicas y Técnicas · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this chaperone, immunophilins contribute to the regulation of the biological functions of several client-proteins. Among these Hsp90-binding immunophilins, there are two highly homologous members named FKBP51 and FKBP52 (FK506-binding protein of 51-kDa and 52-kDa, respectively) that were first characterized as components of the Hsp90-based heterocomplex associated to steroid receptors. Afterwards, they emerged as likely contributors to a variety of other hormone-dependent diseases, stress-related pathologies, psychiatric disorders, cancer, and other syndromes characterized by misfolded proteins. The differential biological actions of these immunophilins have been assigned to the structurally similar, but functionally divergent enzymatic domain. Nonetheless, they also require the complementary input of the TPR domain, most likely due to their dependence with the association to Hsp90 as a functional unit. FKBP51 and FKBP52 regulate a variety of biological processes such as steroid receptor action, transcriptional activity, protein conformation, protein trafficking, cell differentiation, apoptosis, cancer progression, telomerase activity, cytoskeleton architecture, etc. In this article we discuss the biology of these events and some mechanistic aspects.

Indexed as

AnimalsHSP90 Heat-Shock ProteinsHumansImmunophilinsModels, MolecularMolecular StructureProtein BindingHSP90 Heat-Shock ProteinsImmunophilinscell differentiationdyneinFKBP51FKBP52Hsp90neurodifferentiationNF-Btelomerase

Identifiers

PMID30717249
PMCPMC6406450
OpenAlexW2912308905

What Socratic holds

Textmetadata
LicenceCC BY
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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 Socratic graph.