Evidence map›Paper›PMID 22920901›Full record

ReviewCurrent pharmaceutical design2013

Hsp70 protein complexes as drug targets.

Victoria A Assimon, Anne T Gillies, Jennifer N Rauch, Jason E Gestwicki

Open access · greenAbstract readReview
In one paragraph

Review in Current pharmaceutical design, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

71 citing papers in PubMed, 113 citations in OpenAlex.

  1. Development of domain-specific probes ofAntimicrobial agents and chemotherapy · 2026
    Article
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  7. Review
  8. Review
  9. Article
  10. ACS chemical biology · 2023
    Article
  11. Article
  12. Article
  13. A novel and unique ATP hydrolysis to AMP by a human Hsp70 Binding immunoglobin protein (BiP).Protein science : a publication of the Protein Society · 2022
    Article
  14. Article
  15. Review
  16. Article
  17. General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021
    Article
  18. Review
  19. Review
  20. Review

11 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 at 1 institution in 1 country.

Victoria A AssimonDepartment of Pathology, Life Sciences Institute, University of Michigan, 210 Washtenaw Ave., Ann Arbor, MI 48109-2216, USA.
Anne T Gillies
Jennifer N Rauch
Jason E Gestwicki
Washtenaw Community College · US

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
Molecular Chaperones and Small MoleculesR01NS059690 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jason E Gestwicki · 2008 to 2026
$7.9M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
NIGMS NIH HHS GM008353NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32 GM145304NINDS NIH HHS NS059690NINDS NIH HHS R01 NS059690
6 · The paper itself

Abstract

Heat shock protein 70 (Hsp70) plays critical roles in proteostasis and is an emerging target for multiple diseases. However, competitive inhibition of the enzymatic activity of Hsp70 has proven challenging and, in some cases, may not be the most productive way to redirect Hsp70 function. Another approach is to inhibit Hsp70's interactions with important co-chaperones, such as J proteins, nucleotide exchange factors (NEFs) and tetratricopeptide repeat (TPR) domain-containing proteins. These co-chaperones normally bind Hsp70 and guide its many diverse cellular activities. Complexes between Hsp70 and co-chaperones have been shown to have specific functions, including roles in pro-folding, pro-degradation and pro-trafficking pathways. Thus, a promising strategy may be to block protein- protein interactions between Hsp70 and its co-chaperones or to target allosteric sites that disrupt these contacts. Such an approach might shift the balance of Hsp70 complexes and re-shape the proteome and it has the potential to restore healthy proteostasis. In this review, we discuss specific challenges and opportunities related to these goals. By pursuing Hsp70 complexes as drug targets, we might not only develop new leads for therapeutic development, but also discover new chemical probes for use in understanding Hsp70 biology.

Indexed as

AnimalsDrug Delivery SystemsHSP70 Heat-Shock ProteinsHumansProtein BindingProtein Structure, SecondaryHSP70 Heat-Shock Proteins

Identifiers

PMID22920901
PMCPMC3593251
OpenAlexW2112374700

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.