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http://purl.uniprot.org/citations/36261086http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36261086http://www.w3.org/2000/01/rdf-schema#comment"E3 ligases are involved in various cellular biological processes, and their loss of function or improper targeting can induce multiple types of human diseases. F-box protein 7(FBXO7) is a unit in the SKP1-Cullin1-F-box (SCF) SCFFBXO7 E3 ligase composite, playing the role of recognizing some substrates. Additionally, FBXO7 is involved in the regulation of the proteasome complex, mitophagy, the cell cycle, cell proliferation, and germ cell differentiation. Although many articles have reviewed the pathogenesis of FBXO7, which is associated with Parkinson disease-15 (PARKIN15), a summary of the role of FBXO7 as an E3 ligase and its SCF-independent function is incomplete, as well as an overview of FBXO7 in cancer. Therefore, we summarized FBXO7-related substrates and the roles of FBXO7 in human cancers. In addition, based on previous studies, we supplemented the newly discovered FBXO7 mutations in PARKIN15 patients and some potential pathogenic mechanisms that may lead to PARKIN15. A profound exploration of the general pathophysiological mechanisms of this protein could provide potential evidence for the targeted treatment of PARKIN15 and malignant tumors."xsd:string
http://purl.uniprot.org/citations/36261086http://purl.org/dc/terms/identifier"doi:10.1016/j.gene.2022.146972"xsd:string
http://purl.uniprot.org/citations/36261086http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/36261086http://purl.uniprot.org/core/author"Zhong Y."xsd:string
http://purl.uniprot.org/citations/36261086http://purl.uniprot.org/core/author"Ye M."xsd:string
http://purl.uniprot.org/citations/36261086http://purl.uniprot.org/core/author"Jin X."xsd:string
http://purl.uniprot.org/citations/36261086http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/36261086http://purl.uniprot.org/core/name"Gene"xsd:string
http://purl.uniprot.org/citations/36261086http://purl.uniprot.org/core/pages"146972"xsd:string
http://purl.uniprot.org/citations/36261086http://purl.uniprot.org/core/title"The characteristics of FBXO7 and its role in human diseases."xsd:string
http://purl.uniprot.org/citations/36261086http://purl.uniprot.org/core/volume"851"xsd:string
http://purl.uniprot.org/citations/36261086http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/36261086
http://purl.uniprot.org/citations/36261086http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/36261086
http://purl.uniprot.org/uniprot/#_A8K7F7-mappedCitation-36261086http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36261086
http://purl.uniprot.org/uniprot/#_Q9Y3I1-mappedCitation-36261086http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36261086
http://purl.uniprot.org/uniprot/#_Q5HYB3-mappedCitation-36261086http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36261086
http://purl.uniprot.org/uniprot/Q9Y3I1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36261086
http://purl.uniprot.org/uniprot/A8K7F7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36261086
http://purl.uniprot.org/uniprot/Q5HYB3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36261086