| http://purl.uniprot.org/citations/8183370 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8183370 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8183370 | http://www.w3.org/2000/01/rdf-schema#comment | "Bcl-2 was isolated from the t(14;18) chromosomal breakpoint in follicular B-cell lymphoma. Bcl-2 has the unique oncogenic role of extending cell survival by inhibiting a variety of apoptotic deaths. An emerging family of Bcl-2-related proteins share two highly conserved regions referred to here as Bcl-2 homology 1 and 2 (BH1 and BH2) domains (Fig. 1). This includes Bax which heterodimerizes with Bcl-2 and when overexpressed counteracts Bcl-2. We report here that site-specific mutagenesis of Bcl-2 establishes the two domains as novel dimerization motifs. Substitution of Gly 145 in BH1 domain or Trp 188 in BH2 domain completely abrogated Bcl-2's death-repressor activity in interleukin-3 deprivation, gamma-irradiation and glucocorticoid-induced apoptosis. Mutations that affected Bcl-2's function also disrupted its heterodimerization with Bax, yet still permitted Bcl-2 homodimerization. These results establish a functional role for the BH1 and BH2 domains and suggest Bcl-2 exerts its action through heterodimerization with Bax."xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.org/dc/terms/identifier | "doi:10.1038/369321a0"xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.org/dc/terms/identifier | "doi:10.1038/369321a0"xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/author | "Korsmeyer S.J."xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/author | "Korsmeyer S.J."xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/author | "Oltvai Z.N."xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/author | "Oltvai Z.N."xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/author | "Yin X.-M."xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/author | "Yin X.-M."xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/pages | "321-323"xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/pages | "321-323"xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/title | "BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax."xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/title | "BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax."xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/volume | "369"xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://purl.uniprot.org/core/volume | "369"xsd:string |
| http://purl.uniprot.org/citations/8183370 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8183370 |
| http://purl.uniprot.org/citations/8183370 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8183370 |
| http://purl.uniprot.org/citations/8183370 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8183370 |
| http://purl.uniprot.org/citations/8183370 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8183370 |