| http://purl.uniprot.org/citations/21454712 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21454712 | http://www.w3.org/2000/01/rdf-schema#comment | "Previous studies have suggested that the BH3 domain of the proapoptotic Bcl-2 family member Noxa only interacts with the anti-apoptotic proteins Mcl-1 and A1 but not Bcl-2. In view of the similarity of the BH3 binding domains of these anti-apoptotic proteins as well as recent evidence that studies of isolated BH3 domains can potentially underestimate the binding between full-length Bcl-2 family members, we examined the interaction of full-length human Noxa with anti-apoptotic human Bcl-2 family members. Surface plasmon resonance using bacterially expressed proteins demonstrated that Noxa binds with mean dissociation constants (K(D)) of 3.4 nm for Mcl-1, 70 nm for Bcl-x(L), and 250 nm for wild type human Bcl-2, demonstrating selectivity but not absolute specificity of Noxa for Mcl-1. Further analysis showed that the Noxa/Bcl-2 interaction reflected binding between the Noxa BH3 domain and the Bcl-2 BH3 binding groove. Analysis of proteins expressed in vivo demonstrated that Noxa and Bcl-2 can be pulled down together from a variety of cells. Moreover, when compared with wild type Bcl-2, certain lymphoma-derived Bcl-2 mutants bound Noxa up to 20-fold more tightly in vitro, pulled down more Noxa from cells, and protected cells against killing by transfected Noxa to a greater extent. When killing by bortezomib (an agent whose cytotoxicity in Jurkat T-cell leukemia cells is dependent on Noxa) was examined, apoptosis was enhanced by the Bcl-2/Bcl-x(L) antagonist ABT-737 or by Bcl-2 down-regulation and diminished by Bcl-2 overexpression. Collectively, these observations not only establish the ability of Noxa and Bcl-2 to interact but also identify Bcl-2 overexpression as a potential mechanism of bortezomib resistance."xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.189092"xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/author | "Lee S.H."xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/author | "Schmitz I."xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/author | "Takahashi R."xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/author | "Kaufmann S.H."xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/author | "Smith A.J."xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/author | "Dai H."xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/author | "Correia C."xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/pages | "17682-17692"xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/title | "Noxa/Bcl-2 protein interactions contribute to bortezomib resistance in human lymphoid cells."xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://purl.uniprot.org/core/volume | "286"xsd:string |
| http://purl.uniprot.org/citations/21454712 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21454712 |
| http://purl.uniprot.org/citations/21454712 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21454712 |
| http://purl.uniprot.org/uniprot/Q13794#attribution-2B0D03397C9D0E94310028332AC3A3D6 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21454712 |
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