http://purl.uniprot.org/citations/29106904 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/29106904 | http://www.w3.org/2000/01/rdf-schema#comment | "Prothymosin α (ProTα) is an acidic protein with a nuclear role related to the chromatin activity through its interaction with histones in mammalian cells. ProTα acts as an anti-apoptotic factor involved in the control of the apoptosome activity in the cytoplasm, however the mechanisms underlying this function are still known. ProTα shares similar biological functions with acidic nuclear-cytoplasmic shuttling proteins included in SET and ANP32 family members. Using affinity chromatography, co-immunoprecipitation and chemical cross-linking, we demonstrate that ProTα interacts with SET, ANP32A and ANP32B proteins. The study by mass spectrometry of the complexes stabilized by chemical cross-linking showed that associations of ProTα consist of six highly acidic ProTα-complexes, which corresponds to differentiated interactions of ProTα either with SET or ANP32 proteins. The presence in the ProTα-complexes of cytoplasmic proteins involved in membrane remodeling and proteins implicated in the mitochondrial permeability, seems to indicate that they could be related to a cytoplasmic-mitochondrial activity. According to the cellular function of the characterized targets of ProTα, and the evolution in the composition of the diverse ProTα-complexes when proliferation activity was reduced or apoptosis induced, leads to hypothesized that ProTα interactions might be related to the proliferation activity and control of the cell survival."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.abb.2017.10.014"xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/author | "Moreira D."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/author | "Freire M."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/author | "Covelo G."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/author | "Diaz-Jullien C."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/author | "Sarandeses C.S."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/author | "Barbeito P."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/author | "Freire-Cobo C."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/author | "Muras J."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/name | "Arch Biochem Biophys"xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/pages | "74-86"xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/title | "Prothymosin alpha interacts with SET, ANP32A and ANP32B and other cytoplasmic and mitochondrial proteins in proliferating cells."xsd:string |
http://purl.uniprot.org/citations/29106904 | http://purl.uniprot.org/core/volume | "635"xsd:string |
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