Evidence map›Paper›PMID 25628064›Full record

ReviewJournal of neurochemistry2015

The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease.

Laura J Blair, Jeremy D Baker, Jonathan J Sabbagh, Chad A Dickey

Abstract readReview
In one paragraph

Review in Journal of neurochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

62 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Cerebrospinal fluid proteomics for predictive assessment of Alzheimer's Disease risk.medRxiv : the preprint server for health sciences · 2025
    Article
  8. Article
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  11. Article
  12. Review
  13. Review
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  17. MACSPI enables tissue-selective proteomic and interactomic analyses in multicellular organisms.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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.

Laura J BlairDepartment of Molecular Medicine, Byrd Alzheimer's Institute, University of South Florida, Tampa, Florida, USA.
Jeremy D Baker
Jonathan J Sabbagh
Chad A Dickey

Funding

The Hsp90 cochaperone FKBP51 regulates tau structure and functionR01NS073899 · NINDS · UNIVERSITY OF SOUTH FLORIDA · PI Laura J Blair · 2011 to 2026
$6.9M
Modeling stress-related psychopathology through FKBP5 manipulationR01MH103848 · NIMH · UNIVERSITY OF SOUTH FLORIDA · PI BLAIR, LAURA J · 2014 to 2018
$1.9M
NIMH NIH HHS R01 MH103848NINDS NIH HHS NIH/NINDS R01 NS073899NINDS NIH HHS R01 NS073899
6 · The paper itself

Abstract

Peptidyl-prolyl cis/trans isomerases (PPIases), a unique family of molecular chaperones, regulate protein folding at proline residues. These residues are abundant within intrinsically disordered proteins, like the microtubule-associated protein tau. Tau has been shown to become hyperphosphorylated and accumulate as one of the two main pathological hallmarks in Alzheimer's disease, the other being amyloid beta (Ab). PPIases, including Pin1, FK506-binding protein (FKBP) 52, FKBP51, and FKBP12, have been shown to interact with and regulate tau biology. This interaction is particularly important given the numerous proline-directed phosphorylation sites found on tau and the role phosphorylation has been found to play in pathogenesis. This regulation then affects downstream aggregation and oligomerization of tau. However, many PPIases have yet to be explored for their effects on tau biology, despite the high likelihood of interaction based on proline content. Moreover, Pin1, FKBP12, FKBP52, cyclophilin (Cyp) A, CypB, and CypD have been shown to also regulate Ab production or the toxicity associated with Ab pathology. Therefore, PPIases directly and indirectly regulate pathogenic protein multimerization in Alzheimer's disease and represent a family rich in targets for modulating the accumulation and toxicity.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsHumansMolecular ChaperonesPeptidylprolyl Isomerasetau ProteinsAmyloid beta-PeptidesMolecular ChaperonesPeptidylprolyl Isomerasetau ProteinsAlzheimer's diseaseamyloid βchaperoneimmunophilinPPIasetau

Identifiers

PMID25628064
PMCPMC4361273

What OpenQuestion holds

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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 OpenQuestion graph.