Evidence map›Paper›PMID 26468185›Full record

ReviewThe Journal of neuroscience : the official journal of the Society for Neuroscience2015

Chaperones in Neurodegeneration.

Iris Lindberg, James Shorter, R Luke Wiseman, Fabrizio Chiti, Chad A Dickey, Pamela J McLean

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.3field-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

57 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Gastrointestinal dysmotility in rodent models of Parkinson's disease.American journal of physiology. Gastrointestinal and liver physiology · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Chaperoning activity of the cyclophilin family prevents tau aggregation.Protein science : a publication of the Protein Society · 2022
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Cereblon Regulates the Proteotoxicity of Tau by Tuning the Chaperone Activity of DNAJA1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  19. Article
  20. Combating deleterious phase transitions in neurodegenerative disease.Biochimica et biophysica acta. Molecular cell research · 2021
    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 6 institutions in 2 countries.

Iris LindbergUniversity of Maryland School of Medicine, Baltimore, Maryland 21201, ilindberg@som.umaryland.edu.
James ShorterUniversity of Pennsylvania, Philadelphia, Pennsylvania 19104.
R Luke WisemanThe Scripps Research Institute, La Jolla, California 92037.
Fabrizio ChitiUniversity of Florence, 50121 Florence, Italy.
Chad A DickeyUniversity of South Florida, Tampa, Florida 33620, and.
Pamela J McLeanMayo Clinic, Jacksonville, Florida 32224.ORCID http://orcid.org/0000-0003-4870-5715
Scripps Research Institute · USUniversity of Florence · ITUniversity of Maryland, Baltimore · USUniversity of Pennsylvania · USUniversity of South Florida · USWinnMed · 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
OPIOID PEPTIDE SYNTHESIZING ENZYMESR01DA005084 · NIDA · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDBERG, IRIS · 1988 to 2014
$4.4M
Defining the mechanistic basis of a prion disaggregaseR01GM099836 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SHORTER, JAMES · 2013 to 2024
$3.9M
Amyloid elimination by Hsp104 and substrate-optimized variantsDP2OD002177 · OD · UNIVERSITY OF PENNSYLVANIA · PI SHORTER, JAMES · 2007 to 2007
$2.4M
Direct Regulation of Extracellular Proteostasis by the Unfolded Protein ResponseR01NS092829 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI WISEMAN, ROCKLAND LUKE · 2015 to 2019
$2.1M
Modeling stress-related psychopathology through FKBP5 manipulationR01MH103848 · NIMH · UNIVERSITY OF SOUTH FLORIDA · PI BLAIR, LAURA J · 2014 to 2018
$1.9M
Extracellular alpha-synuclein in Parkinson's DiseaseR01NS073740 · NINDS · MAYO CLINIC JACKSONVILLE · PI MCLEAN, PAMELA J · 2011 to 2015
$1.7M
TARGETING ENDOGENOUS SIGNALING PATHWAYS TO AMELIORATE SYSTEMIC AMYLOIDOSESR01DK102635 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI MURPHY, GEORGE J, WISEMAN, ROCKLAND LUKE · 2014 to 2017
$823k
Exploring mechanisms of TDP-43 aggregation and disaggregationR21NS067354 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI SHORTER, JAMES · 2009 to 2010
$436k
The Secretory Chaperone 7B2 as an Endogenous Regulator of Amyloid PathologyR21AG045741 · NIA · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDBERG, IRIS · 2014 to 2015
$427k
Opioid Peptide Synthesizing EnzymesR56DA005084 · NIDA · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDBERG, IRIS · 2016 to 2016
$174k
NIA NIH HHS AG045741NIA NIH HHS R21 AG045741NIDA NIH HHS DA05084NIDA NIH HHS R01 DA005084NIDA NIH HHS R56 DA005084NIDDK NIH HHS DK102635NIDDK NIH HHS R01 DK102635NIGMS NIH HHS GM099836NIGMS NIH HHS R01 GM099836NIH HHS DP2 OD002177NIH HHS DP2OD002177NIMH NIH HHS MH103848NIMH NIH HHS R01 MH103848NINDS NIH HHS NS067354NINDS NIH HHS NS073740NINDS NIH HHS NS073899NINDS NIH HHS NS092829NINDS NIH HHS R01 NS073740NINDS NIH HHS R01 NS073899NINDS NIH HHS R01 NS092829NINDS NIH HHS R21 NS067354
6 · The paper itself

Abstract

Cellular protein homeostasis (proteostasis) maintains the integrity of the proteome and includes protein synthesis, folding, oligomerization, and turnover; chaperone proteins assist with all of these processes. Neurons appear to be especially susceptible to failures in proteostasis, and this is now increasingly recognized as a major origin of neurodegenerative disease. This review, based on a mini-symposium presented at the 2015 Society for Neuroscience meeting, describes new work in the area of neuronal proteostasis, with a specific focus on the roles and therapeutic uses of protein chaperones. We first present a brief review of protein misfolding and aggregation in neurodegenerative disease. We then discuss different aspects of chaperone control of neuronal proteostasis on topics ranging from chaperone engineering, to chaperone-mediated blockade of protein oligomerization and cytotoxicity, to the potential rescue of neurodegenerative processes using modified chaperone proteins. SIGNIFICANCE STATEMENT: Aberrant protein homeostasis within neurons results in protein misfolding and aggregation. In this review, we discuss specific roles for protein chaperones in the oligomerization, assembly, and disaggregation of proteins known to be abnormally folded in neurodegenerative disease. Collectively, our goal is to identify therapeutic mechanisms to reduce the cellular toxicity of abnormal aggregates.

Indexed as

AnimalsHumansMolecular ChaperonesNeurodegenerative DiseasesMolecular Chaperoneschaperoneheat shock proteinsneurodegenerationParkinson's diseaseprotein misfoldingproteostasis

Identifiers

PMID26468185
PMCPMC4604223
OpenAlexW2209051641

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.