| http://purl.uniprot.org/citations/9463381 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9463381 | http://www.w3.org/2000/01/rdf-schema#comment | "Bcl-2 and close homologues such as Bcl-xL promote cell survival, while other relatives such as Bax antagonize this function. Since only the pro-survival family members possess a conserved N-terminal region denoted BH4, we have explored the role of this amphipathic helix for their survival function and for interactions with several agonists of apoptosis, including Bax and CED-4, an essential regulator in the nematode Caenorhabditis elegans. BH4 of Bcl-2 could be replaced by that of Bcl-x without perturbing function but not by a somewhat similar region near the N-terminus of Bax. Bcl-2 cell survival activity was reduced by substitutions in two of ten conserved BH4 residues. Deletion of BH4 rendered Bcl-2 (and Bcl-xL) inactive but did not impair either Bcl-2 homodimerization or ability to bind to Bax or five other pro-apoptotic relatives (Bak, Bad, Bik, Bid or Bim). Hence, association with these death agonists is not sufficient to promote cell survival. Significantly, however, Bcl-xL lacking BH4 lost the ability both to bind CED-4 and antagonize its pro-apoptotic activity. These results favour the hypothesis that the BH4 domain of pro-survival Bcl-2 family members allows them to sequester CED-4 relatives and thereby prevent apoptosis."xsd:string |
| http://purl.uniprot.org/citations/9463381 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/17.4.1029"xsd:string |
| http://purl.uniprot.org/citations/9463381 | http://purl.uniprot.org/core/author | "Adams J.M."xsd:string |
| http://purl.uniprot.org/citations/9463381 | http://purl.uniprot.org/core/author | "Huang D.C."xsd:string |
| http://purl.uniprot.org/citations/9463381 | http://purl.uniprot.org/core/author | "Cory S."xsd:string |
| http://purl.uniprot.org/citations/9463381 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9463381 | http://purl.uniprot.org/core/name | "EMBO J"xsd:string |
| http://purl.uniprot.org/citations/9463381 | http://purl.uniprot.org/core/pages | "1029-1039"xsd:string |
| http://purl.uniprot.org/citations/9463381 | http://purl.uniprot.org/core/title | "The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4."xsd:string |
| http://purl.uniprot.org/citations/9463381 | http://purl.uniprot.org/core/volume | "17"xsd:string |
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