Evidence map›Paper›PMID 34685574›Full record

ReviewCells2021

Targeting Chaperone/Co-Chaperone Interactions with Small Molecules: A Novel Approach to Tackle Neurodegenerative Diseases.

Lisha Wang, Liza Bergkvist, Rajnish Kumar, Bengt Winblad, Pavel F Pavlov

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2021. 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 29% 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, 15 citations in OpenAlex.

  1. Article
  2. Structural analysis ofbioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Chaperone Activators.Sub-cellular biochemistry · 2024
    Review
  9. Review
  10. 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

5 authors at 2 institutions in 2 countries.

Lisha WangDepartment of Neuroscience Care and Society, Division of Neurogeriatrics, Karolinska Institutet, 17164 Solna, Sweden.ORCID 0000-0002-6482-1073
Liza BergkvistDepartment of Neuroscience Care and Society, Division of Neurogeriatrics, Karolinska Institutet, 17164 Solna, Sweden.
Rajnish KumarDepartment of Neuroscience Care and Society, Division of Neurogeriatrics, Karolinska Institutet, 17164 Solna, Sweden.
Bengt WinbladDepartment of Neuroscience Care and Society, Division of Neurogeriatrics, Karolinska Institutet, 17164 Solna, Sweden.
Pavel F PavlovDepartment of Neuroscience Care and Society, Division of Neurogeriatrics, Karolinska Institutet, 17164 Solna, Sweden.ORCID 0000-0002-9823-5654
Karolinska Institutet · SEKarolinska University Hospital · SE

Funding

Alzheimer Foundation AF940014Brain Foundation Fo 2019-0140Foundation for Geriatric Diseases at Karolinska Institutet 2021-00681Gun and Bertil Stohnes Foundation 0Gunvor and Josef Anérs Foundation 0Magnus Bergvalls Foundation 0Mar-garetha af Ugglas Foundation 0Swedish Research Council 2018-02843the Foundation for Old Servants 2020-01028Tore Nilssons Foundation for medical research 0
6 · The paper itself

Abstract

The dysfunction of the proteostasis network is a molecular hallmark of neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, and amyotrophic lateral sclerosis. Molecular chaperones are a major component of the proteostasis network and maintain cellular homeostasis by folding client proteins, assisting with intracellular transport, and interfering with protein aggregation or degradation. Heat shock protein 70 kDa (Hsp70) and 90 kDa (Hsp90) are two of the most important chaperones whose functions are dependent on ATP hydrolysis and collaboration with their co-chaperones. Numerous studies implicate Hsp70, Hsp90, and their co-chaperones in neurodegenerative diseases. Targeting the specific protein-protein interactions between chaperones and their particular partner co-chaperones with small molecules provides an opportunity to specifically modulate Hsp70 or Hsp90 function for neurodegenerative diseases. Here, we review the roles of co-chaperones in Hsp70 or Hsp90 chaperone cycles, the impacts of co-chaperones in neurodegenerative diseases, and the development of small molecules modulating chaperone/co-chaperone interactions. We also provide a future perspective of drug development targeting chaperone/co-chaperone interactions for neurodegenerative diseases.

Indexed as

HumansMolecular ChaperonesNeurodegenerative DiseasesMolecular Chaperonesco-chaperonesHsp70Hsp90neurodegenerative diseasessmall molecules

Identifiers

PMID34685574
PMCPMC8534281
OpenAlexW3204674528

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.