Evidence map›Paper›PMID 32443761›Full record

ReviewCells2020

Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets.

Maxim Shevtsov, Zsolt Balogi, William Khachatryan, Huile Gao, László Vígh, Gabriele Multhoff

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed, 2 pooled it
4.3field-weighted citation impact, top 4% 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

56 citing papers in PubMed, 2 syntheses or guidelines pooled it, 80 citations in OpenAlex.

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  18. Exploring Molecular Pathways in Exercise-Induced Recovery from Traumatic Brain Injury.Medical science monitor : international medical journal of experimental and clinical research · 2025
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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

6 authors at 6 institutions in 4 countries.

Maxim ShevtsovCenter for Translational Cancer Research Technische Universität München (TranslaTUM), Radiation Immuno-Oncology Group, Klinikum rechts der Isar, Einstein Str. 25; 81675 Munich, Germany.
Zsolt BalogiInstitute of Biochemistry and Medical Chemistry, Medical School, University of Pecs, Szigeti str. 12, 7624 Pecs, Hungary.
William KhachatryanAlmazov National Medical Research Centre, Polenov Russian Scientific Research Institute of Neurosurgery, Mayakovskogo str. 12, 191104 St. Petersburg, Russia.
Huile GaoKey Laboratory of Drug-Targeting and Drug Delivery System of the Education Ministry, Sichuan Engineering Laboratory for Plant-Sourced Drug and Sichuan Research Center for Drug Precision Industrial Technology, West China School of Pharmacy, Sichuan University, Chengdu 610064, China.ORCID 0000-0002-5355-7238
László VíghInstitute of Biochemistry, Biological Research Centre, Temesvári krt. 62, 6726 Szeged, Hungary.
Gabriele MulthoffCenter for Translational Cancer Research Technische Universität München (TranslaTUM), Radiation Immuno-Oncology Group, Klinikum rechts der Isar, Einstein Str. 25; 81675 Munich, Germany.
Far Eastern Federal University · RUFederal Almazov North-West Medical Research Centre · RUHUN-REN Szegedi Biológiai Kutatóközpont · HUInstitute of Biochemistry · HUSichuan University · CNTUM Klinikum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock proteins (HSPs) constitute a large family of conserved proteins acting as molecular chaperones that play a key role in intracellular protein homeostasis, regulation of apoptosis, and protection from various stress factors (including hypoxia, thermal stress, oxidative stress). Apart from their intracellular localization, members of different HSP families such as small HSPs, HSP40, HSP60, HSP70 and HSP90 have been found to be localized on the plasma membrane of malignantly transformed cells. In the current article, the role of membrane-associated molecular chaperones in normal and tumor cells is comprehensively reviewed with implications of these proteins as plausible targets for cancer therapy and diagnostics.

Indexed as

Clinical Trials as TopicEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHumansMembrane ProteinsModels, BiologicalNeoplasmsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSPA5 protein, humanMembrane ProteinscalreticulinGRP78GRP96heat shock proteinsHSP27HSP40HSP60HSP70HSP90targeted diagnostics and therapy

Identifiers

PMID32443761
PMCPMC7290778
OpenAlexW3026416704

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.