منابع مشابه
Bid, but not Bax, regulates VDAC channels.
During apoptosis, cytochrome c is released from mitochondria into the cytosol, where it participates in caspase activation. Various and often conflicting mechanisms have been proposed to account for the increased permeability of the mitochondrial outer membrane that is responsible for this process. The voltage-dependent anion channel (VDAC) is the major permeability pathway for metabolites in t...
متن کاملDynamics of nucleotides in VDAC channels: structure-specific noise generation.
Nucleotide penetration into the voltage-dependent mitochondrial ion channel (VDAC) reduces single-channel conductance and generates excess current noise through a fully open channel. VDAC channels were reconstituted into planar phospholipid membranes bathed in 1.0 M NaCl. At a given nucleotide concentration, the average decrease in small-ion channel conductance induced by mononucleotides ATP, A...
متن کاملVDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function.
The mitochondrial channel, VDAC, forms large (3 nm in diameter) aqueous pores through membranes. We measured ATP flow (using the luciferin/luciferase method) through these channels after reconstitution into planar phospholipid membranes. In the open state of VDAC, as many as 2 x 10(6) ATP molecules can flow through one channel per second. The half-maximum rate occurs at approximately 75 mM ATP....
متن کاملSize-dependent forced PEG partitioning into channels: VDAC, OmpC, and α-hemolysin.
Nonideal polymer mixtures of PEGs of different molecular weights partition differently into nanosize protein channels. Here, we assess the validity of the recently proposed theoretical approach of forced partitioning for three structurally different β-barrel channels: voltage-dependent anion channel from outer mitochondrial membrane VDAC, bacterial porin OmpC (outer membrane protein C), and bac...
متن کاملApoptosis: it's BAK to VDAC.
The voltage-dependent anion channel (VDAC) of the mitochondrial outer membrane (MOM; Mannella & Kinnally, 2008)—also known as mitochondrial porin—has long been implicated in regulating the mitochondrial response to certain cell death stimuli (Galluzzi & Kroemer, 2007). This includes a potential role in MOM permeabilization (MOMP) during apoptosis, which is a necessary step in the release of cyt...
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ژورنال
عنوان ژورنال: IUBMB Life (International Union of Biochemistry and Molecular Biology: Life)
سال: 2001
ISSN: 1521-6543,1521-6551
DOI: 10.1080/15216540152845902