Results 141 to 150 of about 8,482 (180)
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Journal of Bioenergetics and Biomembranes, 2008
Normal cells of aerobic organisms synthesize the energy they require in the form of ATP via the process of oxidative phosphorylation. This complex system resides in the mitochondria of cells and utilizes oxygen to produce a majority of cellular ATP.
Andrew M, Campbell, Samuel H P, Chan
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Normal cells of aerobic organisms synthesize the energy they require in the form of ATP via the process of oxidative phosphorylation. This complex system resides in the mitochondria of cells and utilizes oxygen to produce a majority of cellular ATP.
Andrew M, Campbell, Samuel H P, Chan
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Journal of Bioenergetics and Biomembranes, 2008
Recently, it was demonstrated that some anti-cancer agents used mitochondrial voltage-dependent anion channels (VDAC1-3 isoforms) as their pharmacological target. VDACs are expressed more highly in cancer cells than normal cells; thus the VDAC-dependent cytotoxic agents can have cancer-selectivity. Furanonaphthoquinones (FNQs) induced caspase-dependent
Eriko, Simamura +3 more
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Recently, it was demonstrated that some anti-cancer agents used mitochondrial voltage-dependent anion channels (VDAC1-3 isoforms) as their pharmacological target. VDACs are expressed more highly in cancer cells than normal cells; thus the VDAC-dependent cytotoxic agents can have cancer-selectivity. Furanonaphthoquinones (FNQs) induced caspase-dependent
Eriko, Simamura +3 more
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[Voltage-dependent anion channels (VDAC) on human sperm membrane].
Zhonghua nan ke xue = National journal of andrology, 2007To further study gene expression and characterization of voltage-dependent anion channels (VDACs) on human spermatozoa.VDACs were cloned by PCR from the testis cDNA library. Recombinant human sperm VDACs were produced in E. coli system by molecular cloning technology.
Zeng-jun, Wang +3 more
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Purification of VDAC (Voltage-dependent anion-selective channel) from rat liver mitochondria
The Journal of Membrane Biology, 1983The outer membrane of rat liver mitochondria contains a channel-forming protein known as VDAC (voltage-dependent anion-selective channel). This protein has been functionally purified by a combination of ion exchange chromatography, gel filtration and affinity chromatography on a Concanavalin A-containing column.
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Plant Molecular Biology, 1995
The mitochondrial outer membrane of eukaryotic cells contains voltage-dependent anion channels (VDAC) also termed porins. Three cDNAs from wheat (Triticum aestivum) were isolated and sequenced (Tavdac 1-3). They share 65% similarity of their amino acid sequences, and therefore they probably represent isoforms.
Elkeles, A. +4 more
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The mitochondrial outer membrane of eukaryotic cells contains voltage-dependent anion channels (VDAC) also termed porins. Three cDNAs from wheat (Triticum aestivum) were isolated and sequenced (Tavdac 1-3). They share 65% similarity of their amino acid sequences, and therefore they probably represent isoforms.
Elkeles, A. +4 more
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Current Pharmaceutical Design, 2006
Research over the last decade has extended the prevailing view of mitochondria to include functions well beyond the critical bioenergetics role in supplying ATP. It is now recognized that mitochondria play a crucial role in cell signaling events, inter-organelle communication, aging, many diseases, cell proliferation and cell death.
V, Shoshan-Barmatz +3 more
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Research over the last decade has extended the prevailing view of mitochondria to include functions well beyond the critical bioenergetics role in supplying ATP. It is now recognized that mitochondria play a crucial role in cell signaling events, inter-organelle communication, aging, many diseases, cell proliferation and cell death.
V, Shoshan-Barmatz +3 more
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Journal of Bioenergetics and Biomembranes, 1992
Specific, high-affinity receptors for numerous drugs have recently been localized to mitochondrial membrane proteins. This review discusses the association of the mitochondrial receptor for benzodiazepines (mBzR) with the voltage-dependent anion channel (VDAC), indicating a possible auxiliary role for VDAC as a putative drug binding protein.
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Specific, high-affinity receptors for numerous drugs have recently been localized to mitochondrial membrane proteins. This review discusses the association of the mitochondrial receptor for benzodiazepines (mBzR) with the voltage-dependent anion channel (VDAC), indicating a possible auxiliary role for VDAC as a putative drug binding protein.
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Current Medicinal Chemistry, 2003
Voltage-dependent anion channels (VDAC) are major constituents of the outer mitochondrial membrane. Over the past few years, several hypotheses and mechanisms have been forwarded for and against a role for VDAC in outer mitochondrial membrane permeability and the subsequent release of apoptosis promoting factors.
David J, Granville, Roberta A, Gottlieb
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Voltage-dependent anion channels (VDAC) are major constituents of the outer mitochondrial membrane. Over the past few years, several hypotheses and mechanisms have been forwarded for and against a role for VDAC in outer mitochondrial membrane permeability and the subsequent release of apoptosis promoting factors.
David J, Granville, Roberta A, Gottlieb
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Annals of the New York Academy of Sciences, 1980
VDAC is a channel-forming protein, located in the outer mitochondrial membrane, whose properties are consistent with the known permeability behavior of that membrane. When extracted with Triton X-100, VDAC exists as a 110,000 molecular weight glycoprotein complex which is a prepackaged channel. When inserted into liposomes, the permeability increase to
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VDAC is a channel-forming protein, located in the outer mitochondrial membrane, whose properties are consistent with the known permeability behavior of that membrane. When extracted with Triton X-100, VDAC exists as a 110,000 molecular weight glycoprotein complex which is a prepackaged channel. When inserted into liposomes, the permeability increase to
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Advances in TRP channel drug discovery: from target validation to clinical studies
Nature Reviews Drug Discovery, 2021Ari-Pekka Koivisto +2 more
exaly