RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/31960115http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31960115http://www.w3.org/2000/01/rdf-schema#comment"Phosphatidylethanolamine-binding protein 1 (PEBP1), a small 21 kDa protein, is implicated in several key processes of the living cell. The deregulation of PEBP1, especially its downregulation, leads to major diseases such as cancer and Alzheimer's disease. PEBP1 was found to interact with numerous proteins, especially kinases and GTPases, generally inhibiting their activity. To understand the basic functionality of this amazing small protein, we have considered several known processes that it modulates and we have discussed the role of each molecular target in these processes. Here, we propose that cortical actin organization, associated with membrane changes, is involved in the majority of the processes modulated by PEBP1. Furthermore, based on recent data, we summarize some key PEBP1-interacting proteins, and we report their respective functions and focus on their relationships with actin organization. We suggest that, depending on the cell status and environment, PEBP1 is an organizer of the actin-membrane composite material."xsd:string
http://purl.uniprot.org/citations/31960115http://purl.org/dc/terms/identifier"doi:10.1007/s00018-020-03455-5"xsd:string
http://purl.uniprot.org/citations/31960115http://purl.uniprot.org/core/author"Schoentgen F."xsd:string
http://purl.uniprot.org/citations/31960115http://purl.uniprot.org/core/author"Jonic S."xsd:string
http://purl.uniprot.org/citations/31960115http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/31960115http://purl.uniprot.org/core/name"Cell Mol Life Sci"xsd:string
http://purl.uniprot.org/citations/31960115http://purl.uniprot.org/core/pages"859-874"xsd:string
http://purl.uniprot.org/citations/31960115http://purl.uniprot.org/core/title"PEBP1/RKIP behavior: a mirror of actin-membrane organization."xsd:string
http://purl.uniprot.org/citations/31960115http://purl.uniprot.org/core/volume"77"xsd:string
http://purl.uniprot.org/citations/31960115http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31960115
http://purl.uniprot.org/citations/31960115http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31960115
http://purl.uniprot.org/uniprot/#_A0A0K0K1J6-mappedCitation-31960115http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31960115
http://purl.uniprot.org/uniprot/#_B4DRT4-mappedCitation-31960115http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31960115
http://purl.uniprot.org/uniprot/#_D9IAI1-mappedCitation-31960115http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31960115
http://purl.uniprot.org/uniprot/#_P30086-mappedCitation-31960115http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31960115
http://purl.uniprot.org/uniprot/#_V9HW05-mappedCitation-31960115http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31960115
http://purl.uniprot.org/uniprot/P30086http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31960115
http://purl.uniprot.org/uniprot/D9IAI1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31960115
http://purl.uniprot.org/uniprot/V9HW05http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31960115
http://purl.uniprot.org/uniprot/A0A0K0K1J6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31960115
http://purl.uniprot.org/uniprot/B4DRT4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31960115