Evidence map›Paper›PMID 30158430›Full record

ReviewInternational journal of molecular sciences2018

The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease.

Abdullah Hoter, Marwan E El-Sabban, Hassan Y Naim

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 362 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
362citing papers in PubMed, 2 pooled it
15.9field-weighted citation impact, top 1% 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

362 citing papers in PubMed, 2 syntheses or guidelines pooled it, 650 citations in OpenAlex.

  1. Plant-Based HSP90 Inhibitors in Breast Cancer Models: A Systematic Review.International journal of molecular sciences · 2024
    Pooled it
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  9. Review
  10. Nitration in cancer signaling.Redox biology · 2026
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302 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

3 authors at 3 institutions in 3 countries.

Abdullah HoterDepartment of Biochemistry and Chemistry of Nutrition, Faculty of Veterinary Medicine, Cairo University, Giza 12211, Egypt. abdullah.hoter@vet.cu.edu.eg.
Marwan E El-SabbanDepartment of Anatomy, Cell Biology and Physiological Sciences, Faculty of Medicine, American University of Beirut, Beirut, Lebanon. me00@aub.edu.lb.
Hassan Y NaimDepartment of Physiological Chemistry, University of Veterinary Medicine Hannover, Hannover 30559, Germany. hassan.naim@tiho-hannover.de.ORCID 0000-0003-4884-8425
American University of Beirut · LBCairo University · EGUniversity of Veterinary Medicine Hannover, Foundation · DE

Funding

American University of Beirut Intramural funding to M.E.S.Deutscher Akademischer Austauschdienst Scholarship to A.H.Stiftung Tierärztliche Hochschule Hannover Intramural funding to H.Y.N.
6 · The paper itself

Abstract

The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are involved in myriad cellular processes. Their distribution in various cellular compartments underlines their essential roles in cellular homeostasis. HSP90 and its co-chaperones orchestrate crucial physiological processes such as cell survival, cell cycle control, hormone signaling, and apoptosis. Conversely, HSP90, and its secreted forms, contribute to the development and progress of serious pathologies, including cancer and neurodegenerative diseases. Therefore, targeting HSP90 is an attractive strategy for the treatment of neoplasms and other diseases. This manuscript will review the general structure, regulation and function of HSP90 family and their potential role in pathophysiology.

Indexed as

AnimalsApoptosisCell CycleCell SurvivalHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMembrane ProteinsMolecular Chaperonesglucose-regulated proteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMembrane ProteinsMolecular ChaperonesGRP94HSP90molecular chaperonespathophysiologystructure and functionTRAP1

Identifiers

PMID30158430
PMCPMC6164434
OpenAlexW2889502232

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.