Evidence map›Paper›PMID 23224428›Full record

ReviewCellular and molecular life sciences : CMLS2013

Functional diversity and pharmacological profiles of the FKBPs and their complexes with small natural ligands.

Andrzej Galat

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. FKBP25 participates in DNA double-strand break repair.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2020
    Article
  5. Article
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  8. Review
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  12. Review
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  14. Transformation of quiescent adult oligodendrocyte precursor cells into malignant glioma through a multistep reactivation process.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Basic Tilted Helix Bundle - a new protein fold in human FKBP25/FKBP3 and HectD1.Biochemical and biophysical research communications · 2014
    Article
  16. Article
  17. Crystal structure and conformational flexibility of the unligated FK506-binding protein FKBP12.6.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  18. Article
  19. 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

1 author at 1 institution in 1 country.

Andrzej GalatCommissariat à l'Energie Atomique, Direction des Sciences du Vivant, Institut de Biologie et de Technologies de Saclay, Service d'Ingénierie Moléculaire des Protéines, Bat. 152, 91191, Gif-sur-Yvette Cedex, France. galat@dsvidf.cea.fr
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

From 5 to 12 FK506-binding proteins (FKBPs) are encoded in the genomes of disparate marine organisms, which appeared at the dawn of evolutionary events giving rise to primordial multicellular organisms with elaborated internal body plan. Fifteen FKBPs, several FKBP-like proteins and some splicing variants of them are expressed in humans. Human FKBP12 and some of its paralogues bind to different macrocyclic antibiotics such as FK506 or rapamycin and their derivatives. FKBP12/(macrocyclic antibiotic) complexes induce diverse pharmacological activities such as immunosuppression in humans, anticancerous actions and as sustainers of quiescence in certain organisms. Since the FKBPs bind to various assemblies of proteins and other intracellular components, their complexes with the immunosuppressive drugs may differentially perturb miscellaneous cellular functions. Sequence-structure relationships and pharmacological profiles of diverse FKBPs and their involvement in crucial intracellular signalization pathways and modulation of cryptic intercellular communication networks were discussed.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsAnti-Bacterial AgentsAntineoplastic AgentsCell CommunicationCell NucleusHumansImmunosuppression TherapyLigandsMolecular Sequence DataProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidSirolimusTacrolimus Binding ProteinsAnti-Bacterial AgentsAntineoplastic AgentsLigandsSirolimusTacrolimus Binding Proteins

Identifiers

PMID23224428
PMCPMC11113493
OpenAlexW2076339566

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.