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Adenosine Activates AMPK to Phosphorylate Bcl-X<sub>L</sub> Responsible for Mitochondrial Damage and DIABLO Release in HuH-7 Cells
Author(s) -
Donqin Yang,
Takahiro Yaguchi,
Takashi Nakano,
Tomoyuki Nishizaki
Publication year - 2011
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000325207
Subject(s) - ampk , microbiology and biotechnology , protein kinase a , phosphorylation , small interfering rna , adenosine , amp activated protein kinase , apoptosis , tfam , transfection , chemistry , activator (genetics) , mitochondrion , biology , biochemistry , mitochondrial biogenesis , gene
Accumulating evidence has pointed to AMP-activated protein kinase (AMPK) as an inducer of apoptosis in a variety of cancer cells. The present study aimed at understanding AMPK signals for adenosine-induced HuH-7 cell apoptosis.

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