Zobrazeno 1 - 5
of 5
pro vyhledávání: '"D H Needleman"'
Autor:
H S Kim, W K Wilson, D H Needleman, F D Pinkerton, D K Wilson, F A Quiocho, G J Schroepfer, Jr
Publikováno v:
Journal of Lipid Research, Vol 30, Iss 2, Pp 247-261 (1989)
3 beta-Hydroxy-5 alpha-cholest-8(14)-en-15-one (I) is a potent inhibitor of sterol synthesis with significant hypocholesterolemic activity. (25R)-3 beta,26-Dihydroxy-5 alpha-cholest-8(14)-en-15-one (II) has been shown to be a major metabolite of I af
Externí odkaz:
https://doaj.org/article/8f8985ab75134d23853f8a93bc6f2786
Publikováno v:
The American journal of physiology. 272(5 Pt 1)
The effect of D-erythro-C18-sphingosine (sphingosine) and related compounds on the Ca(2+)-release channel (ryanodine binding protein) was examined on rabbit skeletal muscle membranes, on the purified ryanodine binding protein, and on the channel reco
Autor:
C, Callaway, A, Seryshev, J P, Wang, K J, Slavik, D H, Needleman, C, Cantu, Y, Wu, T, Jayaraman, A R, Marks, S L, Hamilton
Publikováno v:
The Journal of biological chemistry. 269(22)
The Ca2+ release channel of skeletal muscle sarcoplasmic reticulum is modulated in a biphasic manner by the plant alkaloid ryanodine and there are two distinct binding sites on this channel for ryanodine. The Ca2+ release channel is a homotetramer wi
Publikováno v:
The Journal of biological chemistry. 268(28)
Both high and low affinity binding sites for [3H]ryanodine exist in sarcoplasmic reticulum membranes derived from rabbit skeletal muscle. Negatively cooperative binding of [3H]ryanodine at one of four initially identical sites cannot account for some
Autor:
G J, Schroepfer, A J, Chu, D H, Needleman, A, Izumi, P T, Nguyen, K S, Wang, J M, Little, B C, Sherrill, A, Kisic
Publikováno v:
The Journal of biological chemistry. 263(9)
The metabolism of 5 alpha-cholest-8(14)-en-3 beta-ol-15-one has been studied after intravenous administration to bile duct-cannulated rats. Very rapid and substantial conversion of the 15-ketosterol to polar biliary metabolites was observed in both m