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1 paB-independent inactivation of proapoptotic BAD protein.
2 ietic and lymphoid lines contained the least BAD protein.
3 ent with the presence of hyperphosphorylated BAD protein.
4 nd inactivation of the proapoptotic BH3-only BAD protein.
5 death regardless of the level of coexpressed Bad protein.
6 es phosphorylation of serine 112 (Ser112) in Bad protein, a member of the Bcl-2 family that plays a c
8 o a 25-residue peptide from the proapoptotic Bad protein and a 16-residue peptide from the proapoptot
9 n cell survival by inactivating proapoptotic Bad protein and suppressing caspase activation, its stim
10 antibodies were generated against the human BAD protein and used to evaluate its expression by immun
11 rylation of Bcl-2-associated death promoter (Bad) protein, and weaker caspase-3 activation in cytokin
13 o-apoptotic Bcl-2 associated death promoter (BAD) protein by post-transcriptional downregulation.
18 the Fas-FasL pathway, but Bcl-XL and phospho-Bad protein expressions were diminished, suggesting invo
20 xpression and intracellular locations of the BAD protein in vivo and provide insights into the regula
21 locks apoptosis induced by d120 mutant or by BAD protein independently of U(S)3, (iii) U(S)3 protein
24 ay function through stable expression of the BAD protein is capable of sensitizing human epithelial o
30 nous agents (e.g., sorbitol, Fas ligand, and BAD protein) or replication-incompetent mutants (e.g., t
32 Incubation of active MAP kinase members with Bad protein showed serine 112 phosphorylation of Bad by
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