ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2013
Peptide aptamers: tools to negatively or positively modulate HSPB1(27) function.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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.
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
20 citing papers in PubMed, 49 citations in OpenAlex.
- DNAJC24 suppresses breast cancer malignancy and serves as a prognostic biomarker.Cancer cell international · 2025Article
- SAA3 deficiency exacerbates intestinal fibrosis in DSS-induced IBD mouse model.Cell death discovery · 2025Article
- Atractylenolide I inhibits EMT and enhances the antitumor effect of cabozantinib in prostate cancerFrontiers in oncology · 2022Article
- 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
- Comprehensive Pan-Cancer Analysis of Heat Shock Protein 110, 90, 70, and 60 Families.Frontiers in molecular biosciences · 2021Article
- Small Heat Shock Proteins in Cancers: Functions and Therapeutic Potential for Cancer Therapy.International journal of molecular sciences · 2020Review
- Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy.Cells · 2019Review
- Article
- RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain.Biochemical and biophysical research communications · 2017Article
- Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach.International journal of molecular sciences · 2017Review
- Ligand-targeted theranostic nanomedicines against cancer.Journal of controlled release : official journal of the Controlled Release Society · 2016Review
- Overcoming HSP27-mediated resistance by altered dimerization of HSP27 using small molecules.Oncotarget · 2016Article
- Advances in HSP27 and HSP90-targeting strategies for glioblastoma.Journal of neuro-oncology · 2016Review
- Synthetic biology for pharmaceutical drug discovery.Drug design, development and therapy · 2015Review
- HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.Cancers · 2014Article
- Chaperones: needed for both the good times and the bad times.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Self-assembly of protein aggregates in ageing disorders: the lens and cataract model.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Pathology-dependent effects linked to small heat shock proteins expression: an update.Scientifica · 2012Review
- Neuropathy- and myopathy-associated mutations in human small heat shock proteins: Characteristics and evolutionary history of the mutation sites.Mutation research. Reviews in mutation researchReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human HSP27 (HSPB1) is a molecular chaperone sensor which, through dynamic changes in its phosphorylation and oligomerization, allows cells to adapt to changes in their physiology and/or mount a protective response to injuries. In pathological conditions, the high level of HSPB1 expression can either be beneficial, such as in diseases characterized by cellular degenerations, or be malignant in cancer cells where it promotes tumourigenesis, metastasis and anti-cancer drug resistance. Structural changes allow HSPB1 to interact with specific client protein partners in order to modulate their folding/activity and/or half-life. Therefore, the search is open for therapeutic compounds aimed at either down- or upregulating HSPB1 activity. In this respect, we have previously described two peptide aptamers (PA11 and PA50) that specifically interact with HSPB1 small oligomers and decrease its anti-apoptotic and tumourigenic activities. A novel analysis of the different HSPB1-interacting aptamers that were isolated earlier revealed that one aptamer (PA23) has the intriguing ability to stimulate the protective activity of HSPB1. We show here that this aptamer abolishes the dominant negative effect induced by the R120G mutant of αB-crystallin (HSPB5) by disrupting its interaction with HSPB1. Hence, developing structure-based interfering strategies could lead to the discovery of HSPB1-based therapeutic drugs.
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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.