Evidence map›Paper›PMID 32184949›Full record

ArticleACS medicinal chemistry letters2020

Hsp70 and the Unfolded Protein Response as a Challenging Drug Target and an Inspiration for Probe Molecule Development.

Leila Terrab, Peter Wipf

Abstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–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

17 citing papers in PubMed.

  1. Review
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  12. Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
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  16. Article
  17. The Role of Heat Shock Protein 70 kDa in Asthma.Journal of asthma and allergy · 2020
    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

2 authors.

Leila TerrabDepartment of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.
Peter WipfDepartment of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unfolded protein response (UPR) is a cellular stress response mechanism that is critical for cell survival. Pharmacological modulation of the ATPase activity of the chaperone Hsp70 can trigger UPR-mediated cell death, thus removing pathogenic cells in human malignancies, or, alternatively, stimulate survival, thereby preventing apoptosis in neuronal cells and slowing the progress of inflammation, neurodegeneration, and aging. This Viewpoint highlights the complexity of the protein homeostasis network and discusses different approaches for modulating Hsp70 activity, including the use of a chemical reaction development-inspired library of Hsp70 agonists and antagonists.

Identifiers

PMID32184949
PMCPMC7073878

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.