Purification of a protein having pore forming activity from the rat liver mitochondrial outer membrane.
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Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrierThe biogenesis and function of eukaryotic porinsChannels in mitochondrial membranes: knowns, unknowns, and prospects for the future.Toward the molecular structure of the mitochondrial channel, VDAC.Structural analysis of mitochondrial pores.Circular dichroism studies of the mitochondrial channel, VDAC, from Neurospora crassaConformational change in the mitochondrial channel, VDAC, detected by electron cryo-microscopyVoltage-dependent anion-selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum.Ultrasteep voltage dependence in a membrane channelBiophysical properties of porin pores from mitochondrial outer membrane of eukaryotic cells.Purification and properties of the voltage-dependent anion channel of the outer mitochondrial membrane.Outer-membrane permeability of bacteria.The specific binding of the microtubule-associated protein 2 (MAP2) to the outer membrane of rat brain mitochondria.Incorporation into phospholipid vesicles of pore-like properties from Golgi membranes of lactating-rat mammary gland.Pore properties of the Golgi membrane from lactating-rat mammary gland. Effects of pH and temperature and reconstitution into phospholipid vesicles.Altered metabolic states do not change the intracellular distribution of hexokinase in Zajdela hepatoma ascites cells.Interaction of non-classical detergents with the mitochondrial porin. A new purification procedure and characterization of the pore-forming unit.Characterization of SH groups in porin of bovine heart mitochondria. Porin cysteines are localized in the channel walls.Identification of a new pore in the mitochondrial outer membrane of a porin-deficient yeast mutant.Studies on human porin: XIII. The type-1 VDAC 'porin 31HL' biotinylated at the plasmalemma of trypan blue excluding human B lymphocytes.Elimination and restoration of voltage dependence in the mitochondrial channel, VDAC, by graded modification with succinic anhydride.Evidence for titratable gating charges controlling the voltage dependence of the outer mitochondrial membrane channel, VDAC.The gate of mitochondrial porin channel is controlled by a number of negative and positive charges.Voltage gating in VDAC is markedly inhibited by micromolar quantities of aluminum.The role of sterols in the functional reconstitution of water-soluble mitochondrial porins from plantsThe Role of the N and C Termini of RecombinantNeurosporaMitochondrial Porin in Channel Formation and Voltage-dependent GatingApproaches for Preparation and Biophysical Characterization of Transmembrane β-Barrels
P2860
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P2860
Purification of a protein having pore forming activity from the rat liver mitochondrial outer membrane.
description
1982 nî lūn-bûn
@nan
1982年の論文
@ja
1982年学术文章
@wuu
1982年学术文章
@zh-cn
1982年学术文章
@zh-hans
1982年学术文章
@zh-my
1982年学术文章
@zh-sg
1982年學術文章
@yue
1982年學術文章
@zh
1982年學術文章
@zh-hant
name
Purification of a protein havi ...... mitochondrial outer membrane.
@en
Purification of a protein havi ...... mitochondrial outer membrane.
@nl
type
label
Purification of a protein havi ...... mitochondrial outer membrane.
@en
Purification of a protein havi ...... mitochondrial outer membrane.
@nl
prefLabel
Purification of a protein havi ...... mitochondrial outer membrane.
@en
Purification of a protein havi ...... mitochondrial outer membrane.
@nl
P2093
P2860
P356
P1433
P1476
Purification of a protein havi ...... mitochondrial outer membrane.
@en
P2093
P2860
P356
10.1042/BJ2080077
P407
P577
1982-10-01T00:00:00Z