Evidence map›Paper›PMID 34943954›Full record

ReviewCells2021

HSP70s in Breast Cancer: Promoters of Tumorigenesis and Potential Targets/Tools for Therapy.

Alexander E Kabakov, Vladimir L Gabai

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
2.9field-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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. The addition of heat shock protein 70 toOpen veterinary journal · 2025
    Article
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  11. Article
  12. Article
  13. Review
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  16. Article
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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

2 authors at 1 institution in 1 country.

Alexander E KabakovDepartment of Radiation Biochemistry, A. Tsyb Medical Radiological Research Center-Branch of the National Medical Research Radiological Center of the Ministry of Health of the Russian Federation, Koroleva 4, 249036 Obninsk, Russia.ORCID 0000-0003-1041-1543
Vladimir L GabaiCureLab Oncology Inc., Dedham, MA 02026, USA.
Ministry of Health of the Russian Federation · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The high frequency of breast cancer worldwide and the high mortality among women with this malignancy are a serious challenge for modern medicine. A deeper understanding of the mechanisms of carcinogenesis and emergence of metastatic, therapy-resistant breast cancers would help development of novel approaches to better treatment of this disease. The review is dedicated to the role of members of the heat shock protein 70 subfamily (HSP70s or HSPA), mainly inducible HSP70, glucose-regulated protein 78 (GRP78 or HSPA5) and GRP75 (HSPA9 or mortalin), in the development and pathogenesis of breast cancer. Various HSP70-mediated cellular mechanisms and pathways which contribute to the oncogenic transformation of mammary gland epithelium are reviewed, as well as their role in the development of human breast carcinomas with invasive, metastatic traits along with the resistance to host immunity and conventional therapeutics. Additionally, intracellular and cell surface HSP70s are considered as potential targets for therapy or sensitization of breast cancer. We also discuss a clinical implication of Hsp70s and approaches to targeting breast cancer with gene vectors or nanoparticles downregulating HSP70s, natural or synthetic (small molecule) inhibitors of HSP70s, HSP70-binding antibodies, HSP70-derived peptides, and HSP70-based vaccines.

Indexed as

Breast NeoplasmsCarcinogenesisEndoplasmic Reticulum Chaperone BiPFemaleHSP70 Heat-Shock ProteinsHumansMembrane ProteinsMitochondrial ProteinsEndoplasmic Reticulum Chaperone BiPglucose-regulated proteinsHSP70 Heat-Shock ProteinsHSPA5 protein, humanHSPA9 protein, humanMembrane ProteinsMitochondrial Proteinscancer stem cellschemotherapyepithelial-to-mesenchymal transitionglucose-regulated proteinheat shock proteinimmunotherapymammary glandmortalinradiotherapy

Identifiers

PMID34943954
PMCPMC8700403
OpenAlexW4200257923

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.