Zobrazeno 1 - 10
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pro vyhledávání: '"C W, Slayman"'
Autor:
C W Slayman
Publikováno v:
IEEE Transactions on Nuclear Science.
Several broad spectrum, high energy neutron source facilities exist throughout the world for accelerated soft error testing. However, none accurately replicate the terrestrial neutron spectra across the range of 1 MeV to 1 GeV. The objective of this
Publikováno v:
The Journal of biological chemistry. 276(25)
In P(2)-type ATPases, a stalk region connects the cytoplasmic part of the molecule, which binds and hydrolyzes ATP, to the membrane-embedded part through which cations are pumped. The present study has used cysteine scanning mutagenesis to examine st
Publikováno v:
The Journal of biological chemistry. 275(27)
In the P(2)-type ATPases, there is growing evidence that four alpha-helical stalk segments connect the cytoplasmic part of the molecule, responsible for ATP binding and hydrolysis, to the membrane-embedded part that mediates cation transport. The pre
Autor:
B M, Alberts, F J, Ayala, D, Botstein, E, Frank, E W, Holmes, R D, Lee, E R, Macagno, P, Marrack, S, Oparil, S H, Orkin, A H, Rubenstein, C W, Slayman, P F, Sparling, L R, Squire, P H, von Hippel, K R, Yamamoto
Publikováno v:
Science (New York, N.Y.). 285(5428)
Publikováno v:
Acta physiologica Scandinavica. Supplementum. 643
Publikováno v:
The Journal of biological chemistry. 273(34)
Mutations at the phosphorylation site (Asp-378) of the yeast plasma-membrane H+-ATPase have been shown previously to cause misfolding of the ATPase, preventing normal movement along the secretory pathway; Asp-378 mutations also block the biogenesis o
Publikováno v:
The Journal of biological chemistry. 272(3)
We have taken advantage of cysteine mutants described previously (Petrov, V. V., and Slayman, C. W. (1995) J. Biol. Chem. 270, 28535-28540) to map the sites at which N-ethylmaleimide (NEM) reacts with the plasma-membrane H+ATPase (PMA)1 of Saccharomy
Autor:
C. W. Slayman, R. Rao
Publikováno v:
Biochemistry and Molecular Biology ISBN: 9783662103692
The E1E2- or P-ATPases are a large and physiologically important family of cation pumps, widely distributed in both prokaryotic and eukaryotic cells (Table 1). In eubacteria, they play a series of specialized roles: scavenging potassium ions from the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c189cece8883c9adf3a1ae6e419cb08c
https://doi.org/10.1007/978-3-662-10367-8_2
https://doi.org/10.1007/978-3-662-10367-8_2
Publikováno v:
Symposia of the Society for Experimental Biology. 48
The yeast plasma-membrane H(+)-ATPase is a member of the P-family of cation transporters, which share a characteristic membrane topology together with consensus sequences for ATP binding and formation of a beta-aspartyl phosphate reaction intermediat
Autor:
R, Rao, C W, Slayman
Publikováno v:
The Journal of biological chemistry. 268(9)
A diagnostic feature of P-ATPases is a phosphorylation motif (DKTGTLT), located in the hydrophilic center of the polypeptide chain, within which the beta-aspartyl-phosphate reaction intermediate is formed. The roles of four invariant residues (Lys379