Evidence map›Paper›PMID 29764935›Full record

ArticleThe Journal of biological chemistry2018

The disorderly conduct of Hsc70 and its interaction with the Alzheimer's-related Tau protein.

Isabelle R Taylor, Atta Ahmad, Taia Wu, Bryce A Nordhues, Anup Bhullar, Jason E Gestwicki, Erik R P Zuiderweg

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  3. Article
  4. Article
  5. DnaJs are enriched in tau regulators.International journal of biological macromolecules · 2023
    Article
  6. Article
  7. Review
  8. Effect of evolution of the C-terminal region on chaperone activity of Hsp70.Protein science : a publication of the Protein Society · 2023
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
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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

7 authors at 4 institutions in 1 country.

Isabelle R Taylorthe Institute for Neurodegenerative Disease, University of California at San Francisco, San Francisco, California 94158, and.
Atta AhmadFrom the Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109.
Taia Wuthe Institute for Neurodegenerative Disease, University of California at San Francisco, San Francisco, California 94158, and.
Bryce A Nordhuesthe Department of Molecular Medicine and Byrd Alzheimer's Institute, University of South Florida, Tampa, Florida 33613.
Anup BhullarFrom the Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109.
Jason E Gestwickithe Institute for Neurodegenerative Disease, University of California at San Francisco, San Francisco, California 94158, and Jason.Gestwicki@ucsf.edu.ORCID 0000-0002-6125-3154
Erik R P ZuiderwegFrom the Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109, zuiderwe@umich.edu.ORCID 0000-0001-6766-6446
University of Michigan · USUniversity of California, San Francisco · USInstitute for Neurodegenerative Disorders · USUniversity of South Florida · US

Funding

Molecular Chaperones and Small MoleculesR01NS059690 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jason E Gestwicki · 2008 to 2026
$7.9M
RESEARCH TRAINING IN CHEMISTRY AND CHEMICAL BIOLOGYT32GM064337 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2002 to 2021
$7.8M
NIGMS NIH HHS T32 GM064337NINDS NIH HHS R01 NS059690
6 · The paper itself

Abstract

Hsp70 chaperones bind to various protein substrates for folding, trafficking, and degradation. Considerable structural information is available about how prokaryotic Hsp70 (DnaK) binds substrates, but less is known about mammalian Hsp70s, of which there are 13 isoforms encoded in the human genome. Here, we report the interaction between the human Hsp70 isoform heat shock cognate 71-kDa protein (Hsc70 or HSPA8) and peptides derived from the microtubule-associated protein Tau, which is linked to Alzheimer's disease. For structural studies, we used an Hsc70 construct (called BETA) comprising the substrate-binding domain but lacking the lid. Importantly, we found that truncating the lid does not significantly impair Hsc70's chaperone activity or allostery

Indexed as

Protein FoldingProtein Interaction Domains and MotifsAdenosine TriphosphateAlzheimer DiseaseBinding SitesCrystallography, X-RayHSC70 Heat-Shock ProteinsHumansProtein BindingProtein Conformationtau ProteinsAdenosine TriphosphateHSC70 Heat-Shock Proteinstau Proteinschaperonemicrotubule-associated protein (MAP)nuclear magnetic resonance (NMR)protein complexprotein conformation

Identifiers

PMID29764935
PMCPMC6036187
OpenAlexW2804204431

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.