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http://purl.uniprot.org/citations/37844714http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37844714http://www.w3.org/2000/01/rdf-schema#comment"Heat shock proteins (HSP) are a large family of peptide proteins that are widely found in cells. Studies have shown that the expression and function of HSPs in cells are very complex, and they can participate in cellular physiological and pathological processes through multiple pathways. Multiple heat shock proteins are associated with cancer cell growth, proliferation, metastasis, and resistance to anticancer drugs, and they play a key role in cancer development by ensuring the correct folding or degradation of proteins in cancer cells. As research hotspots, HSP90, HSP70 and HSP27 have been extensively studied in cancer so far. However, HSP20, also referred to as HSPB6, as a member of the small heat shock protein family, has been shown to play an important role in the cardiovascular system, but little research has been conducted on HSP20 in cancer. This review summarizes the current cellular functions of HSP20 in different cancer types, as well as its effects on cancer proliferation, progression, prognosis, and its other functions in cancer, to illustrate the close association between HSP20 and cancer. We show that, unlike most HSPs, HSP20 mainly plays an active anticancer role in cancer development, which is expected to provide new ideas and help for cancer diagnosis and treatment and research."xsd:string
http://purl.uniprot.org/citations/37844714http://purl.org/dc/terms/identifier"doi:10.1016/j.cellsig.2023.110928"xsd:string
http://purl.uniprot.org/citations/37844714http://purl.uniprot.org/core/author"Jin H."xsd:string
http://purl.uniprot.org/citations/37844714http://purl.uniprot.org/core/author"Tian Y."xsd:string
http://purl.uniprot.org/citations/37844714http://purl.uniprot.org/core/author"Wu Y."xsd:string
http://purl.uniprot.org/citations/37844714http://purl.uniprot.org/core/author"Zhao J."xsd:string
http://purl.uniprot.org/citations/37844714http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37844714http://purl.uniprot.org/core/name"Cell Signal"xsd:string
http://purl.uniprot.org/citations/37844714http://purl.uniprot.org/core/pages"110928"xsd:string
http://purl.uniprot.org/citations/37844714http://purl.uniprot.org/core/title"Cellular functions of heat shock protein 20 (HSPB6) in cancer: A review."xsd:string
http://purl.uniprot.org/citations/37844714http://purl.uniprot.org/core/volume"112"xsd:string
http://purl.uniprot.org/citations/37844714http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37844714
http://purl.uniprot.org/citations/37844714http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/37844714
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http://purl.uniprot.org/uniprot/#_B4DUL6-mappedCitation-37844714http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37844714
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http://purl.uniprot.org/uniprot/O14558http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/37844714
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