Evidence map›Paper›PMID 41369326›Full record

ReviewCells2025

Heat Shock Protein Chaperome Is a Multi-Faceted Vector for Tumor Cell Migratory Activity, Invasion, and Metastasis.

Viacheslav Fedorov, Andrey Kurkin, Georgii Fofanov, Vitaliya Kaneva, Anna Kondratenko, Stephanie E Combs, Maxim Shevtsov

Abstract readReview
In one paragraph

Review in Cells, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
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.

Viacheslav FedorovDepartment of Inorganic Chemistry and Biophysics, Saint-Petersburg State University of Veterinary Medicine, 196084 Saint-Petersburg, Russia.ORCID 0000-0002-0239-7473
Andrey KurkinLaboratory of Biomedical Nanotechnologies, Institute of Cytology of the Russian Academy of Sciences (RAS), 194064 Saint-Petersburg, Russia.ORCID 0009-0007-5685-926X
Georgii FofanovPersonalized Medicine Centre, Almazov National Medical Research Centre, 197341 Saint-Petersburg, Russia.
Vitaliya KanevaMolecular Biotechnology Department, Saint-Petersburg State Technological Institute (Technical University), 190013 Saint-Petersburg, Russia.
Anna KondratenkoMolecular Biotechnology Department, Saint-Petersburg State Technological Institute (Technical University), 190013 Saint-Petersburg, Russia.
Stephanie E CombsDepartment of Radiation Oncology, Technische Universität München (TUM), Klinikum Rechts der Isar, 81675 Munich, Germany.
Maxim ShevtsovLaboratory of Biomedical Nanotechnologies, Institute of Cytology of the Russian Academy of Sciences (RAS), 194064 Saint-Petersburg, Russia.ORCID 0000-0002-8539-2239

Funding

Validating establishment of functional safety in skin interface with deeply porous transcutaneous pylon for direct skeletal attachment of limb prosthesesR44AR079960 · NIAMS · POLY-ORTH INTERNATIONAL · PI PITKIN, MARK · 2021 to 2022
$1.7M
Deutsche Forschungsgemeinschaft DFG funding programme Open Access PublishingNIAMS NIH HHS R44 AR079960
6 · The paper itself

Abstract

Heat shock proteins (HSPs), in particular, representatives of the HSP70 and HSP90 families, are the folding centers of cell proteins and have been proven to be overexpressed in various types of solid and hematological malignancies. With their involvement in a number of cellular functions (e.g., protection from various stresses including radiochemotherapy, transport regulation, apoptotic signal inhibition, etc.), these chaperones are a valuable target for cancer progression research. However, recent focus has shifted to the HSP interaction network, which includes many molecules involved in cell migration and invasion pathways. Investigating the interplay between different co-chaperones and their effect on cell motility may help with establishing a palette of available diagnostic and therapeutic targets for highly invasive cancer types. In this review, we describe current models of the HSP functional cycle and recent studies proving links between these cycle regulators and contributions to cell migration. Based on detailed studies of various co-chaperones' involvement in cancer progression, the network approach gives much necessary molecular context to previously established HSP functions.

Indexed as

Cell MovementHeat-Shock ProteinsNeoplasmsAnimalsHumansNeoplasm InvasivenessNeoplasm MetastasisHeat-Shock Proteinscancer cell migrationcancer progressionchaperomeheat shock proteinsHSP70HSP90invasionmolecular network

Identifiers

PMID41369326
PMCPMC12691156

What Socratic 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 Socratic graph.