Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Margaret J. Sampson"'
Autor:
Dawna L. Armstrong, Margaret J. Sampson, William K. Decker, William J. Craigen, M. John Hicks, Wim Ruitenbeek, Arthur L. Beaudet
Publikováno v:
Journal of Biological Chemistry, 276, 39206-39212
Journal of Biological Chemistry, 276, pp. 39206-39212
Journal of Biological Chemistry, 276, pp. 39206-39212
Voltage-dependent anion channels (VDACs), also known as mitochondrial porins, are small channel proteins involved in the translocation of metabolites across the mitochondrial outer membrane. A single channel-forming protein is found in yeast, whereas
Publikováno v:
Journal of Membrane Biology. 170:89-102
The channel-forming protein called VDAC forms the major pathway in the mitochondrial outer membrane and controls metabolite flux across that membrane. The different VDAC isoforms of a species may play different roles in the regulation of mitochondria
Publikováno v:
Journal of Biological Chemistry. 273:30482-30486
Voltage-dependent anion channels (VDACs) are pore-forming proteins found in the outer mitochondrial membrane of all eucaryotes. VDACs are the major pathway for metabolites through the outer mitochondrial membrane and, in mammals, bind several cytosol
Publikováno v:
Journal of Biological Chemistry. 272:18966-18973
Voltage-dependent anion channels (VDACs) are pore-forming proteins found in the outer mitochondrial membrane of all eucaryotes. VDACs are the binding sites for several cytosolic enzymes, including the isoforms of hexokinase and glycerol kinase. VDACs
Autor:
A.H.M. Mahbubul Huq, William J. Craigen, Christine M. Disteche, William K. Decker, Mary Beth Dinulos, Rhonda S. Lovell, Margaret J. Sampson
Publikováno v:
Genomics. 36:530-534
Glycerol kinase (Gyk) participates in the metabolism of endogenously derived and dietary glycerol. Deficiency of the human enzyme activity is an X-linked recessive disorder with a clinical picture varying from childhood metabolic crisis to asymptomat
Publikováno v:
Genomics. 36:192-196
Voltage-dependent anion channels (VDACs) are small pore-forming channels found in the outer membrane of mitochondria. VDACs translocate adenine nucleotides and are the binding sites for several cytosolic kinases important in intermediary metabolism.
Autor:
Michael J. Levy, Edwin J. Weeber, J. David Sweatt, Margaret J. Sampson, Keltoum Anflous, William J. Craigen, Dawna L. Armstrong, Sarah E. Brown
Publikováno v:
The Journal of biological chemistry. 277(21)
Mitochondrial outer membrane permeability is conferred by a family of porin proteins. Mitochondrial porins conduct small molecules and constitute one component of the permeability transition pore that opens in response to apoptotic signals. Because m
Publikováno v:
Biochimica et biophysica acta. 1452(1)
Voltage-dependent anion channels (VDACs, also known as mitochondrial porins) are small pore-forming proteins of the mitochondrial outer membrane found in all eukaryotes. Mammals harbor three distinct VDAC isoforms, with each protein sharing 65–70%
Publikováno v:
Genomics. 33(2)
Voltage-dependent anion channels (VDACs) are small pore-forming channels found in the mitochondrial outer membrane of all eukaryotes. VDACs conduct adenine nucleotides and are the binding sites for several cytosolic enzymes, including the isoforms of
Autor:
Margaret J. Sampson, Erwin Fleissner
Publikováno v:
The Hastings Center Report. 30:4