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1 ietic and lymphoid lines contained the least BAD protein.
2 ent with the presence of hyperphosphorylated BAD protein.
3 death regardless of the level of coexpressed Bad protein.
4 paB-independent inactivation of proapoptotic BAD protein.
5 nd inactivation of the proapoptotic BH3-only BAD protein.
6 es phosphorylation of serine 112 (Ser112) in Bad protein, a member of the Bcl-2 family that plays a c
7 ylation and inactivation of the proapoptotic BAD protein, a target of Pim1.
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
12                                The mammalian BAD protein belongs to the BH3-only subgroup of the BCL-
13 o-apoptotic Bcl-2 associated death promoter (BAD) protein by post-transcriptional downregulation.
14 nriched for the expression of phosphorylated BAD protein compared to non-TNBC tumours.
15                                          The BAD protein derived from 11 of 41 tumor lines that expre
16                                    Bcl-2 and BAD protein diminished with DHF but were restored by CRT
17       Overexpression of the 15-kDa truncated BAD protein enhanced TGF-beta 1-induced apoptosis, where
18                                Inhibition of BAD protein expression with specific antisense oligonucl
19 the Fas-FasL pathway, but Bcl-XL and phospho-Bad protein expressions were diminished, suggesting invo
20 uorescein-labeled peptide [the BH3 domain of BAD protein (F-Bad 6)] to Bcl-xL.
21 xpression and intracellular locations of the BAD protein in vivo and provide insights into the regula
22 locks apoptosis induced by d120 mutant or by BAD protein independently of U(S)3, (iii) U(S)3 protein
23                       Phosphorylation of the Bad protein is a key regulatory event in the prevention
24                                          The BAD protein is a pro-apoptotic member of the Bcl-2 famil
25 ay function through stable expression of the BAD protein is capable of sensitizing human epithelial o
26                Bak was barely detectable and Bad protein level decreased in cells undergoing apoptosi
27 ion of BAD, suggesting dynamic regulation of BAD protein levels in vivo.
28 nces did not arise from differences in total Bad protein levels.
29 and CDK4/6 but increased p21, caspase-9, and BAD protein levels.
30          Our results indicate that the human BAD protein, like its mouse homologue, is able to induce
31         The Bcl-2-associated death promoter (BAD) protein, like many other BH3-only proteins, is know
32 nous agents (e.g., sorbitol, Fas ligand, and BAD protein) or replication-incompetent mutants (e.g., t
33                                      Bax and Bad proteins remained relatively constant throughout dif
34 inhibition of kinases known to phosphorylate BAD protein resulted in increased sensitivity to platinu
35 Incubation of active MAP kinase members with Bad protein showed serine 112 phosphorylation of Bad by
36  identified the minimal domain in the murine Bad protein that can dimerize with Bcl-xL.
37                       The relative levels of BAD protein varied widely among established human tumor
38                                              BAD protein was detectable by immunoblotting in many nor
39 PyMT-Bad(+/+) suggesting that phosphorylated BAD protein was inert.
40 culating B-CLL cells, whereas the Bcl-XL and BAD proteins were not present.