Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis

scientific article published on 25 March 2003

Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M213098200
P698PubMed publication ID12657644

P2093author name stringDoo Yeon Kim
Cheol O Joe
Gary G Meadows
Jungyeon Won
Muhnho La
Doyeun Kim
P2860cites workAkt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factorQ22009126
Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blockedQ24318845
Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155Q24532078
Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteinsQ24673877
Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand bindingQ27619633
Ca2+-induced apoptosis through calcineurin dephosphorylation of BADQ28140882
BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survivalQ28145685
The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9Q28272159
Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteinsQ28293607
Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)Q28297419
The structural basis for 14-3-3:phosphopeptide binding specificityQ29547190
Mitochondria and apoptosisQ29547905
The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosisQ29616513
An improved method for the construction of high efficiency cDNA library in plasmid or lambda vectorQ33839035
Akt/Protein kinase B inhibits cell death by preventing the release of cytochrome c from mitochondriaQ33959022
BH3-Only proteins-essential initiators of apoptotic cell deathQ34117362
14-3-3 proteins: regulation of subcellular localization by molecular interferenceQ34127838
14-3-3: modulators of signaling proteins?Q34324416
14-3-3 proteins: key regulators of cell division, signalling and apoptosis.Q34400246
14-3-3 proteins block apoptosis and differentially regulate MAPK cascadesQ34661998
Mitochondria, the killer organelles and their weaponsQ34736668
14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteinsQ35624026
A yeast mating-selection scheme for detection of protein-protein interactionsQ40399743
Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathwayQ40986827
Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signalsQ41050794
The role of the Caspase family of cysteine proteases in apoptosisQ41433521
Caspases and caspase inhibitorsQ41633125
Akt inhibits the orphan nuclear receptor Nur77 and T-cell apoptosisQ43662770
Protease Involvement in Fodrin Cleavage and Phosphatidylserine Exposure in ApoptosisQ61466723
Remodeling for DemolitionQ63408385
Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexesQ73487291
Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase AQ77406620
P433issue21
P407language of work or nameEnglishQ1860
P304page(s)19347-19351
P577publication date2003-03-25
P1433published inJournal of Biological ChemistryQ867727
P1476titleCleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis
P478volume278

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