Evidence map›Paper›PMID 21523562›Full record

ReviewMolecular neurobiology2011

Bending tau into shape: the emerging role of peptidyl-prolyl isomerases in tauopathies.

John Koren, Umesh K Jinwal, Zachary Davey, Janine Kiray, Karthik Arulselvam, Chad A Dickey

Open access · greenAbstract readReview
In one paragraph

Review in Molecular neurobiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Differential regulation of MAP2 by phosphorylation events in proline-rich versus C-terminal domains.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Stressing Out Hsp90 in Neurotoxic Proteinopathies.Current topics in medicinal chemistry · 2016
    Review
  14. Article
  15. In Silico Insight into Potent of Anthocyanin Regulation of FKBP52 to Prevent Alzheimer's Disease.Evidence-based complementary and alternative medicine : eCAM · 2014
    Article
  16. Review
  17. Article
  18. 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

6 authors at 1 institution in 1 country.

John KorenDepartment of Molecular Medicine, USF Health Byrd Alzheimer's Institute, Tampa, FL 33613, USA.
Umesh K Jinwal
Zachary Davey
Janine Kiray
Karthik Arulselvam
Chad A Dickey
USF Health Byrd Alzheimer's Institute · US

Funding

The Hsp90 cochaperone FKBP51 regulates tau structure and functionR01NS073899 · NINDS · UNIVERSITY OF SOUTH FLORIDA · PI Laura J Blair · 2011 to 2026
$6.9M
Chaperone-mediated signaling in Alzheimer's diseaseR00AG031291 · NIA · UNIVERSITY OF SOUTH FLORIDA · PI DICKEY, CHAD A. · 2008 to 2010
$889k
NIA NIH HHS R00AG031291NINDS NIH HHS R01 NS073899NINDS NIH HHS R01NS073899
6 · The paper itself

Abstract

The Hsp90-associated cis-trans peptidyl-prolyl isomerase--FK506 binding protein 51 (FKBP51)--was recently found to co-localize with the microtubule (MT)-associated protein tau in neurons and physically interact with tau in brain tissues from humans who died from Alzheimer's disease (AD). Tau pathologically aggregates in neurons, a process that is closely linked with cognitive deficits in AD. Tau typically functions to stabilize and bundle MTs. Cellular events like calcium influx destabilize MTs, disengaging tau. This excess tau should be degraded, but sometimes it is stabilized and forms higher-order aggregates, a pathogenic hallmark of tauopathies. FKBP51 was also found to increase in forebrain neurons with age, further supporting a novel role for FKBP51 in tau processing. This, combined with compelling evidence that the prolyl isomerase Pin1 regulates tau stability and phosphorylation dynamics, suggests an emerging role for isomerization in tau pathogenesis.

Indexed as

AnimalsHumansIsomerismModels, BiologicalMolecular ChaperonesPeptidylprolyl IsomeraseTauopathiestau ProteinsMolecular ChaperonesPeptidylprolyl Isomerasetau Proteins

Identifiers

PMID21523562
PMCPMC3260650
OpenAlexW1971622495

What OpenQuestion holds

Textmetadata
LicenceTDM
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.