{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hou C"],"funding":["863 program","National Key Research and Development Program","National Natural Science Foundation of China"],"pagination":["5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5828088"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16"],"pubmed_abstract":["<h4>Background</h4>Protein kinase C ζ (PKCζ), an isoform of the atypical protein kinase C, is a pivotal regulator in cancer. However, the molecular and cellular mechanisms whereby PKCζ regulates tumorigenesis and metastasis are still not fully understood. In this study, proteomics and bioinformatics analyses were performed to establish a protein-protein interaction (PPI) network associated with PKCζ, laying a stepping stone to further understand the diverse biological roles of PKCζ.<h4>Methods</h4>Protein complexes associated with PKCζ were purified by co-immunoprecipitation from breast cancer cell MDA-MB-231 and identified by LC-MS/MS. Two biological replicates and two technical replicates were analyzed. The observed proteins were filtered using the CRAPome database to eliminate the poten"],"journal":["Proteome science"],"pubmed_title":["Profiling the interactome of protein kinase C ζ by proteomics and bioinformatics."],"pmcid":["PMC5828088"],"funding_grant_id":["31671421","2015AA020403","81472683","61376082","21575103","2016YFC0900100"],"pubmed_authors":["Liu H","Dang M","Li Y","Zhang N","Hou C","Qin G","Chen R"],"additional_accession":[]},"is_claimable":false,"name":"Profiling the interactome of protein kinase C ζ by proteomics and bioinformatics.","description":"<h4>Background</h4>Protein kinase C ζ (PKCζ), an isoform of the atypical protein kinase C, is a pivotal regulator in cancer. However, the molecular and cellular mechanisms whereby PKCζ regulates tumorigenesis and metastasis are still not fully understood. In this study, proteomics and bioinformatics analyses were performed to establish a protein-protein interaction (PPI) network associated with PKCζ, laying a stepping stone to further understand the diverse biological roles of PKCζ.<h4>Methods</h4>Protein complexes associated with PKCζ were purified by co-immunoprecipitation from breast cancer cell MDA-MB-231 and identified by LC-MS/MS. Two biological replicates and two technical replicates were analyzed. The observed proteins were filtered using the CRAPome database to eliminate the poten","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018","modification":"2025-04-21T20:14:29.868Z","creation":"2019-03-26T23:04:58Z"},"accession":"S-EPMC5828088","cross_references":{"pubmed":["29491746"],"doi":["10.1186/s12953-018-0134-8"]}}