ArticleOncogene2011
Inhibition of heat shock protein 27 (HspB1) tumorigenic functions by peptide aptamers.
Article in Oncogene, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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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.
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.
Who cites it
42 citing papers in PubMed, 83 citations in OpenAlex.
- Review
- Review
- The Interplay between Heat Shock Proteins and Cancer Pathogenesis: A Novel Strategy for Cancer Therapeutics.Cancers · 2024Review
- Blood plasma derived extracellular vesicles (BEVs): particle purification liquid chromatography (PPLC) and proteomic analysis reveals BEVs as a potential minimally invasive tool for predicting response to breast cancer treatment.Breast cancer research and treatment · 2022Article
- The Role of Heat Shock Protein 27 in Carcinogenesis and Treatment of Colorectal Cancer.Current pharmaceutical design · 2022Review
- Heat Shock Proteins 27, 70, and 110: Expression and Prognostic Significance in Colorectal Cancer.Cancers · 2021Article
- Small Hsps as Therapeutic Targets of Cystic Fibrosis Transmembrane Conductance Regulator Protein.International journal of molecular sciences · 2021Review
- Chemical validation of a druggable site on Hsp27/HSPB1 using in silico solvent mapping and biophysical methods.Bioorganic & medicinal chemistry · 2021Article
- DNAJC12 as a Mediator Between ESR1 and ERBB4 in Breast Carcinoma Cells.Frontiers in oncology · 2021Article
- Small Heat Shock Proteins in Cancers: Functions and Therapeutic Potential for Cancer Therapy.International journal of molecular sciences · 2020Review
- Targeting SOX2 Protein with Peptide Aptamers for Therapeutic Gains against Esophageal Squamous Cell Carcinoma.Molecular therapy : the journal of the American Society of Gene Therapy · 2020Article
- Heat-shock proteins: chaperoning DNA repair.Oncogene · 2020Review
- Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy.Cells · 2019Review
- Epigenetic Alterations of Heat Shock Proteins (HSPs) in Cancer.International journal of molecular sciences · 2019Review
- Heat Shock Proteins in Cancer Immunotherapy.Journal of oncology · 2019Review
- Heat shock proteins and cancer: intracellular chaperones or extracellular signalling ligands?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach.International journal of molecular sciences · 2017Review
- PTRF suppresses the progression of colorectal cancers.Oncotarget · 2017Article
- Heat-shock protein 27 (HSP27, HSPB1) is synthetic lethal to cells with oncogenic activation of MET, EGFR and BRAF.Molecular oncology · 2017Article
- Overcoming HSP27-mediated resistance by altered dimerization of HSP27 using small molecules.Oncotarget · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human heat shock protein 27 (Hsp27, HspB1) is an anti-apoptotic protein characterized for its tumorigenic and metastatic properties, and now referenced as a major therapeutic target in many types of cancer. Hsp27 biochemical properties rely on a structural oligomeric and dynamic organization. Downregulation by small interfering RNA or inhibition with dominant-negative mutant have proven their efficiency to counteract the anti-apoptotic and protective properties of Hsp27. In this study, we report the isolation and characterization of Hsp27-targeted molecules interfering with its structural organization. Using the peptide aptamer (PA) strategy, we isolated PAs that specifically interact with Hsp27 and not with the other members of the small heat shock protein family. In mammalian cell cultures, PAs expression perturbed the dimerization and oligomerization of Hsp27, and acted as negative regulators of the anti-apoptotic and cytoprotective activities of this protein. Further studies analyzing SQ20B cell xenografts in immunocompromised mice showed that PAs strongly reduced tumor development through cell cycle arrest. Our data suggest that PAs could provide a potential tool to develop strategies for the discovery of Hsp27 chemical inhibitors.
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Registered trials
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.