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http://purl.uniprot.org/citations/14699151http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14699151http://www.w3.org/2000/01/rdf-schema#comment"bcl-2 protects cells from apoptosis initiated by a variety of stimuli including loss of cell adhesion. Mice deficient in bcl-2 (bcl-2-/-) develop renal hypoplastic/cystic dysplasia, a condition that leads to significant morbidity and mortality in children. The precise mechanism of action of bcl-2 has not been elucidated. bcl-2 may merely facilitate survival of precursor cells and/or may play a more "active" role during morphogenesis by interacting with other proteins such as paxillin. Recent work in this laboratory demonstrated that bcl-2 directly associates with paxillin. The data presented here demonstrate that the bcl-2 homology 4 (BH4) domain, specifically amino acids 17-31, is necessary for the bcl-2 interaction with paxillin. Paxillin also associated with the BH4 domains of more closely related bcl-2 family members, bcl-xL and bcl-w, compared with that from the non-mammalian homologue ced9. Tyrosines 21 and 28 in the bcl-2 BH4 domain were essential for interaction with paxillin. In embryonic kidney organ culture, incubation with the bcl-2 BH4 domain resulted in inhibition of ureteric bud branching. Therefore, these data suggest that the interaction of bcl-2 with paxillin plays an important role during nephrogenesis."xsd:string
http://purl.uniprot.org/citations/14699151http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m310079200"xsd:string
http://purl.uniprot.org/citations/14699151http://purl.uniprot.org/core/author"Sorenson C.M."xsd:string
http://purl.uniprot.org/citations/14699151http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14699151http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/14699151http://purl.uniprot.org/core/pages"11368-11374"xsd:string
http://purl.uniprot.org/citations/14699151http://purl.uniprot.org/core/title"Interaction of bcl-2 with Paxillin through its BH4 domain is important during ureteric bud branching."xsd:string
http://purl.uniprot.org/citations/14699151http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/14699151http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14699151
http://purl.uniprot.org/citations/14699151http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14699151
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http://purl.uniprot.org/uniprot/#_A0A0J9YTZ8-mappedCitation-14699151http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14699151
http://purl.uniprot.org/uniprot/#_A0A140VJQ8-mappedCitation-14699151http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14699151
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http://purl.uniprot.org/uniprot/#_A0A0J9YV30-mappedCitation-14699151http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14699151
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http://purl.uniprot.org/uniprot/#_A0A1D5RMM8-mappedCitation-14699151http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14699151
http://purl.uniprot.org/uniprot/#_P10415-mappedCitation-14699151http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14699151
http://purl.uniprot.org/uniprot/#_P10417-mappedCitation-14699151http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14699151
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http://purl.uniprot.org/uniprot/#_A0A1B0GRW6-mappedCitation-14699151http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14699151