Zobrazeno 1 - 10
of 74
pro vyhledávání: '"MICHAEL J. RUNSWICK"'
Autor:
Michael J. Runswick, John V. Bason, Martin G. Montgomery, Graham C. Robinson, Ian M. Fearnley, John E. Walker
Publikováno v:
Open Biology, Vol 3, Iss 2 (2013)
The mitochondrial F1-ATPase inhibitor protein, IF1, inhibits the hydrolytic, but not the synthetic activity of the F-ATP synthase, and requires the hydrolysis of ATP to form the inhibited complex. In this complex, the α-helical inhibitory region of
Externí odkaz:
https://doaj.org/article/cd035229ce724da68e175bd514bdacc5
Publikováno v:
Journal of Molecular Biology
In the structure of bovine F1-ATPase inhibited with residues 1–60 of the bovine inhibitor protein IF1, the α-helical inhibitor interacts with five of the nine subunits of F1-ATPase. In order to understand the contributions of individual amino acid
Publikováno v:
Proceedings of the National Academy of Sciences. 107:16823-16827
The catalytic domain of the F-ATPase in mitochondria protrudes into the matrix of the organelle, and is attached to the membrane domain by central and peripheral stalks. Energy for the synthesis of ATP from ADP and phosphate is provided by the transm
Autor:
Veronica Kane Dickson, John E. Walker, Andrew G. W. Leslie, Michael J. Runswick, Jocelyn A. Silvester
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:530-533
A subcomplex of the peripheral stalk or stator domain of the ATP synthase from bovine mitochondria has been expressed to high levels in a soluble form in Escherichia coli. The subcomplex consists of residues 79-184 of subunit b, residues 1-124 of sub
Publikováno v:
Journal of Molecular Biology. 342:593-603
The ATP synthase enzyme structure includes two stalk assemblies, the central stalk and the peripheral stalk. Catalysis involves rotation of the central stalk assembly together with the membrane-embedded ring of c-subunits driven by the trans-membrane
Autor:
Jorgina Satrústegui, Luigi Palmieri, Sebastián Cerdán, Ana Villa, Michael J. Runswick, Ferdinando Palmieri, Angelo Vozza, Emanuela Blanco, A. del Arco, John E. Walker, Santiago Cavero
Publikováno v:
Molecular Microbiology. 50:1257-1269
Summary The malate-aspartate NADH shuttle in mammalian cells requires the activity of the mitochondrial aspar- tate-glutamate carrier (AGC). Recently, we identified in man two AGC isoforms, aralar1 and citrin, which are regulated by calcium on the ex
Autor:
Judy Hirst, John E. Walker, Joe Carroll, Michael J. Runswick, Ian M. Fearnley, Richard J. Shannon
Publikováno v:
Journal of Biological Chemistry. 276:38345-38348
The sequences of 42 subunits of NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria have been described previously. Seven are encoded by mitochondrial DNA, whereas the remaining 35 are nuclear gene products imported into the org
Autor:
Ji-Chun Yang, David Neuhaus, Duncan J. Gordon-Smith, Hortense Videler, John E. Walker, Rodrigo J. Carbajo, Michael J. Runswick
Publikováno v:
Journal of Molecular Biology. 308:325-339
Bovine IF1 is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F1F0 ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dim
Autor:
Ferdinando Palmieri, Michael J. Runswick, Luigi Palmieri, John E. Walker, Giuseppe Fiermonte, Vincenza Dolce, Mario Ventura
Publikováno v:
Journal of Biological Chemistry. 276:8225-8230
In Saccharomyces cerevisiae, the genes ODC1 and ODC2 encode isoforms of the oxodicarboxylate carrier. They both transport C5-C7 oxodicarboxylates across the inner membranes of mitochondria and are members of the family of mitochondrial carrier protei
Autor:
Gennaro Agrimi, Ferdinando Palmieri, Luigi Palmieri, Michael J. Runswick, Ian M. Fearnley, John E. Walker
Publikováno v:
Journal of Biological Chemistry. 276:1916-1922
The nuclear genome of Saccharomyces cerevisiae encodes 35 members of a family of membrane proteins. Known members transport substrates and products across the inner membranes of mitochondria. We have localized two hitherto unidentified family members