Evidence map›Paper›PMID 32318709›Full record

ReviewBiochemical Society transactions2020

Post-translational modifications and stress adaptation: the paradigm of FKBP51.

Theo Rein

Open access · bronzeAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Knocking out Fkbp51 decreases CClCell & bioscience · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Post-translational Modifications in Brain Diseases: A Future for Biomarkers.Advances in experimental medicine and biology · 2022
    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.

Theo ReinMax Planck Institute of Psychiatry, Department of Translational Research in Psychiatry, Munich, Germany.
Max Planck Institute of Psychiatry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adaptation to stress is a fundamental requirement to cope with changing environmental conditions that pose a threat to the homeostasis of cells and organisms. Post-translational modifications (PTMs) of proteins represent a possibility to quickly produce proteins with new features demanding relatively little cellular resources. FK506 binding protein (FKBP) 51 is a pivotal stress protein that is involved in the regulation of several executers of PTMs. This mini-review discusses the role of FKBP51 in the function of proteins responsible for setting the phosphorylation, ubiquitination and lipidation of other proteins. Examples include the kinases Akt1, CDK5 and GSK3β, the phosphatases calcineurin, PP2A and PHLPP, and the ubiquitin E3-ligase SKP2. The impact of FKBP51 on PTMs of signal transduction proteins significantly extends the functional versatility of this protein. As a stress-induced protein, FKBP51 uses re-setting of PTMs to relay the effect of stress on various signaling pathways.

Indexed as

Protein Processing, Post-TranslationalStress, PhysiologicalCyclin-Dependent Kinase 5Glycogen Synthase Kinase 3 betaHumansLipidsNuclear ProteinsPhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein Phosphatase 2Proto-Oncogene Proteins c-aktSignal TransductionS-Phase Kinase-Associated ProteinsTacrolimus Binding Protein 5Tacrolimus Binding ProteinsAKT1 protein, humanCDK5 protein, humanCyclin-Dependent Kinase 5Glycogen Synthase Kinase 3 betaLipidsNuclear ProteinsPHLPP1 protein, humanPhosphoprotein PhosphatasesProtein Phosphatase 2Proto-Oncogene Proteins c-aktSKP2 protein, humanS-Phase Kinase-Associated ProteinsTacrolimus Binding Protein 5Tacrolimus Binding ProteinsUbiquitinFKBP51post-translational modificationsignal transductionstress response

Identifiers

PMID32318709
PMCPMC7200631
OpenAlexW3016375261

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.