Evidence map›Paper›PMID 42109524›Full record

ReviewFrontiers in molecular biosciences2026

Recent insights into HSP70: proteostasis and beyond.

Kristina Pustovaya, Artem Venediktov, Vladislav Soldatov, Egor Kuzmin, Ksenia Pokidova, Viktoria Gartzeva, Olga Payushina, Vassiliy Tsytsarev, Igor Meglinski, Gennadii Piavchenko

Abstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

10 authors.

Kristina Pustovaya *Human Anatomy and Histology Department, I. M. Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia.
Artem Venediktov *Human Anatomy and Histology Department, I. M. Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia.
Vladislav SoldatovMagnetic Resonance Imaging Laboratory, CIC biomaGUNE, Parque Cientifico y Tecnologico de Gipuzkoa Paseo Miramon, Donostia/San Sebastian, Gipuzkoa, Spain.
Egor KuzminHuman Anatomy and Histology Department, I. M. Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia.
Ksenia PokidovaHuman Anatomy and Histology Department, I. M. Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia.
Viktoria GartzevaHuman Anatomy and Histology Department, I. M. Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia.
Olga PayushinaHuman Anatomy and Histology Department, I. M. Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia.
Vassiliy TsytsarevWhiting School of Engineering, Johns Hopkins University, Baltimore, MD, United States.
Igor MeglinskiHuman Anatomy and Histology Department, I. M. Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia.
Gennadii PiavchenkoHuman Anatomy and Histology Department, I. M. Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since the 1980s, 70 kDa heat shock proteins (HSP70s) have been recognized as central regulators of proteostasis, with diverse roles in cellular physiology and pathology. Recent research has significantly expanded our understanding of these molecular chaperones, revealing functions that extend beyond their classical roles in proteostasis. In this review, we integrate these emerging insights with foundational knowledge by outlining the biology of HSP70s, with particular emphasis on recent discoveries, such as new data on the substrate specificity and molecular dynamics of HSP70-client interactions. In addition, increasing evidence highlights their noncanonical anti-inflammatory properties, as well as other nonimmune functions, including the promotion of adipose tissue browning and the enhancement of angiogenesis through extracellular HSP70 activity. Finally, although HSP70s have long been known to regulate mRNA degradation in a transcript-specific manner, new findings demonstrate their ability to bind double-stranded RNA, further broadening their functional repertoire.

Indexed as

GRP78HSC70HSPA1Amolecular chaperonesmortalinprotein quality control

Identifiers

PMID42109524
PMCPMC13149161

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.