Zobrazeno 1 - 10
of 60
pro vyhledávání: '"V W, RODWELL"'
Autor:
I P Williamson, V W Rodwell
Publikováno v:
Journal of Lipid Research, Vol 22, Iss 1, Pp 184-187 (1981)
For precise determination of the catalytic activity of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase (EC 1.1.1.34), the HMG-CoA employed as substrate must be free of HMG, CoA, and other inhibitors of HMG-CoA reductase activity. The standa
Externí odkaz:
https://doaj.org/article/191a236712f54465a12b62b2857a4e84
Autor:
H J Harwood, Jr, V W Rodwell
Publikováno v:
Journal of Lipid Research, Vol 23, Iss 5, Pp 754-761 (1982)
Assay of HMG-CoA reductase kinase activity requires HMG-CoA reductase (reductase, E.C. 1.1.1.34) free of associated reductase kinase. Microsomal reductase insensitive to inactivation by Mg-nucleotides alone may be prepared by heating microsomes at 50
Externí odkaz:
https://doaj.org/article/1b9977719c154b8b87aafc15a9263797
Autor:
N L Young, V W Rodwell
Publikováno v:
Journal of Lipid Research, Vol 18, Iss 5, Pp 572-581 (1977)
Methods were developed for the assay of hydroxymethylglutaryl-CoA reductase (NADPH) activity in microsomes from rat leukocytes. The activity in freshly isolated leukocytes is low compared to rat liver but can be assayed reliably. The patterns of resp
Externí odkaz:
https://doaj.org/article/8b9353c993644929ac90aa298e926610
Regulation of vertebrate liver HMG-CoA reductase via reversible modulation of its catalytic activity
Autor:
C F Hunter, V W Rodwell
Publikováno v:
Journal of Lipid Research, Vol 21, Iss 4, Pp 399-405 (1980)
We have investigated the comparative biochemistry of in vitro regulation of HMG-CoA reductase (EC 1.1.1.34) in microsomal preparations from the livers of nine vertebrates. In all instances, reductase activity was rapidly and profoundly decreased by a
Externí odkaz:
https://doaj.org/article/f8d76426543347e581560f098c43c8da
Autor:
P J Kennelly, V W Rodwell
Publikováno v:
Journal of Lipid Research, Vol 26, Iss 8, Pp 903-914 (1985)
Externí odkaz:
https://doaj.org/article/1c3c2b3e2e5743529e31296f3f75a77b
Autor:
V W, Rodwell, M J, Beach, K M, Bischoff, D A, Bochar, B G, Darnay, J A, Friesen, J F, Gill, M, Hedl, T, Jordan-Starck, P J, Kennelly, D Y, Kim, Y, Wang
Publikováno v:
Methods in enzymology. 324
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::19559ba4ddab6de6a4e92422c3495968
https://pubmed.ncbi.nlm.nih.gov/10989436
https://pubmed.ncbi.nlm.nih.gov/10989436
Autor:
K M, Bischoff, V W, Rodwell
Publikováno v:
Protein science : a publication of the Protein Society. 6(1)
Mutant 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases of the halophilic archaeon Haloferax volcanii were constructed to test the proposed mechanism that phosphorylation downregulates the activity of higher eukarya HMG-CoA reductases via c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::74e6d20175d010d4a7f26f573b2a081e
https://pubmed.ncbi.nlm.nih.gov/9007988
https://pubmed.ncbi.nlm.nih.gov/9007988
Autor:
R V, Omkumar, V W, Rodwell
Publikováno v:
The Journal of biological chemistry. 269(24)
The attenuation of catalytic activity that accompanies phosphorylation of Ser871 of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (EC 1.1.1.34) reflects primarily the introduction of negative charge (Omkumar, R. V., Darnay,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bd04a1f7d87adb7f593bdfa883a0205a
https://pubmed.ncbi.nlm.nih.gov/8207009
https://pubmed.ncbi.nlm.nih.gov/8207009
Autor:
K, Frimpong, V W, Rodwell
Publikováno v:
The Journal of biological chemistry. 269(15)
We employed the overexpressed catalytic domains of wild-type Syrian hamster 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase, EC 1.1.1.34) and of mutant enzymes E558Q, H865Q, and D766N to investigate the roles of Glu558, His865, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::32b5d5dd94632a1e7f2bdbdec9e94625
https://pubmed.ncbi.nlm.nih.gov/7908908
https://pubmed.ncbi.nlm.nih.gov/7908908
Publikováno v:
The Journal of biological chemistry. 269(9)
Attenuation of Syrian hamster 3-hydroxy-3-methyl-glutaryl coenzyme A reductase (HMG-CoA reductase, EC 1.1.1.34) activity by in vitro phosphorylation was studied using AMP-activated protein kinase and wild-type and mutant forms of HMG-CoA reductase. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::aea3d1c74bfb8889f6fcf700939fdd3b
https://pubmed.ncbi.nlm.nih.gov/8120043
https://pubmed.ncbi.nlm.nih.gov/8120043