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Title:
The mitochondrial benzodiazepine receptor: Evidence for association with the voltage-dependent anion channel (VDAC) | Journal of Bioenergetics and Biomembranes
Description:
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. The proposed subunit composition of the purified mBzR complex isolated from rat kidney mitochondria includes VDAC, which functions as a recognition site for benzodiazepines (e.g., flunitrazepam), the adenine nucleotide carrier (ADC), and an 18 kDa outer membrane protein identified by covalent labelling with the mBzR antagonists isoquinoline carboxamides (e.g., PK 14105).
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google, scholar, chem, biol, snyder, pharmacol, article, mcenery, sci, biochem, krueger, access, pedersen, usa, science, privacy, cookies, content, journal, mitochondrial, receptor, anion, channel, vdac, receptors, febs, natl, acad, biochim, biophys, acta, verma, information, publish, search, benzodiazepine, voltagedependent, skolnick, brdiczka, lett, proc, eur, fur, mol, newman, snowman, data, log, research, association,
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voltage-dependent anion channel 6-dihydro-5-methyl-6-oxo-4h-imidazo[1 month download article/chapter mitochondrial membrane proteins imaging benzodiazepine receptors high-affinity receptors mitochondrial benzodiazepine receptor isoquinoline-3-carboxamide privacy choices/manage cookies related subjects 3-isoquinoline-carboxylic acid full article pdf n-methyl-n cell calcium 9 european economic area mitochondrial receptor proposed subunit composition adenine nucleotide carrier conditions privacy policy check access instant access accepting optional cookies journal finder publish main content log article mcenery article journal 4]benzodiazepine-3-carboxylate biomembranes article article log 3-dihydro-1-methyl-5 receptor res privacy policy anholt personal data article cite books a optional cookies manage preferences maryland maureen journal publish protein chem /drug res data protection essential cookies cookies skip subscription content similar content institution subscribe nature usage analysis
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mainEntity:
headline:The mitochondrial benzodiazepine receptor: Evidence for association with the voltage-dependent anion channel (VDAC)
description: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. The proposed subunit composition of the purified mBzR complex isolated from rat kidney mitochondria includes VDAC, which functions as a recognition site for benzodiazepines (e.g., flunitrazepam), the adenine nucleotide carrier (ADC), and an 18 kDa outer membrane protein identified by covalent labelling with the mBzR antagonists isoquinoline carboxamides (e.g., PK 14105).
datePublished:
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pageEnd:69
sameAs:https://doi.org/10.1007/BF00769532
keywords:
Mitochondria
receptor
benzodiazepine
isoquinoline carboxamide
anion channel
Bioorganic Chemistry
Biochemistry
general
Animal Anatomy / Morphology / Histology
Animal Biochemistry
Organic Chemistry
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headline:The mitochondrial benzodiazepine receptor: Evidence for association with the voltage-dependent anion channel (VDAC)
description: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. The proposed subunit composition of the purified mBzR complex isolated from rat kidney mitochondria includes VDAC, which functions as a recognition site for benzodiazepines (e.g., flunitrazepam), the adenine nucleotide carrier (ADC), and an 18 kDa outer membrane protein identified by covalent labelling with the mBzR antagonists isoquinoline carboxamides (e.g., PK 14105).
datePublished:
dateModified:
pageStart:63
pageEnd:69
sameAs:https://doi.org/10.1007/BF00769532
keywords:
Mitochondria
receptor
benzodiazepine
isoquinoline carboxamide
anion channel
Bioorganic Chemistry
Biochemistry
general
Animal Anatomy / Morphology / Histology
Animal Biochemistry
Organic Chemistry
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