Výsledky vyhledávání - "N B. Ruderman"

AMPK as a metabolic switch in rat muscle, liver and adipose tissue after exercise

Autor: N B, Ruderman, H, Park, V K, Kaushik, D, Dean, S, Constant, M, Prentki, A K, Saha

Publikováno v: Acta physiologica Scandinavica. 178(4)

An increasing body of evidence has revealed that activation of adenosine monophosphate (AMP)-activated protein kinase (AMPK)-activated protein kinase increases fatty acid oxidation by lowering the concentration of malonyl coenzyme A (CoA), an inhibit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b4da0bdb5d30d74da6c2e62a7e30f88b
https://pubmed.ncbi.nlm.nih.gov/12864749

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Malonyl CoA as a metabolic switch and a regulator of insulin sensitivity

Autor: N B, Ruderman, A K, Saha, D, Vavvas, T, Kurowski, D R, Laybutt, C, Schmitz-Peiffer, T, Biden, E W, Kraegen

Publikováno v: Advances in experimental medicine and biology. 441

Malonyl CoA is a regulator of carnitine palmitoyl transferase 1 (CPT1), the enzyme that controls the transfer of long chain fatty acyl CoA into mitochondria where it is oxidized. Recent studies indicate that in skeletal muscle the concentration of ma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4db3ccf25db316a03f9839ee8a80a067
https://pubmed.ncbi.nlm.nih.gov/9781332

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The phosphatidylinositol 3-kinase serine kinase phosphorylates IRS-1. Stimulation by insulin and inhibition by Wortmannin

Autor: K, Lam, C L, Carpenter, N B, Ruderman, J C, Friel, K L, Kelly

Publikováno v: The Journal of biological chemistry. 269(32)

Phosphatidylinositol 3-kinase (PI 3-kinase) is a heterodimer composed of an 85-kDa subunit that binds tyrosyl-phosphorylated proteins via its SH2 domains and a 110-kDa catalytic subunit. Expression and mutagenesis experiments have shown that the 110-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::153862b4e4867357152240306d554b89
https://pubmed.ncbi.nlm.nih.gov/8051164

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Insulin-stimulated phosphatidylinositol 3-kinase. Association with a 185-kDa tyrosine-phosphorylated protein (IRS-1) and localization in a low density membrane vesicle

Autor: K L, Kelly, N B, Ruderman

Publikováno v: The Journal of biological chemistry. 268(6)

Insulin stimulates the appearance of anti-tyrosine(P)-immunoprecipitable phosphatidylinositol 3-kinase (PI 3-kinase) activity in adipocytes, predominantly in an intracellular membrane fraction (Kelly, K. L., Ruderman, N. B., and Chen, K. S. (1992) J.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1df66bb0b8f70de96039cd8c672c3380
https://pubmed.ncbi.nlm.nih.gov/8382701

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Glucose and diabetic vascular disease

Autor: N B, Ruderman, J R, Williamson, M, Brownlee

Publikováno v: FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 6(11)

The central therapeutic problem in diabetes mellitus is prevention and treatment of the chronic vascular disease associated with this disorder. Prolonged exposure to hyperglycemia is the primary factor associated with the development of diabetes-spec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7dccff39d2be3a6b32450b630fcf4ce2
https://pubmed.ncbi.nlm.nih.gov/1644256

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Phosphatidylinositol-3-kinase in isolated rat adipocytes. Activation by insulin and subcellular distribution

Autor: K L, Kelly, N B, Ruderman, K S, Chen

Publikováno v: The Journal of biological chemistry. 267(5)

Insulin increases phosphatidylinositol-3-kinase (PI-3-kinase) activity in Chinese hamster ovary cells transfected with human insulin receptor (Ruderman, N. B., Kapeller, R., White, M. F., and Cantley, L. C. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 14

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::015507d24ca34b7883b422c3a58ac02b
https://pubmed.ncbi.nlm.nih.gov/1310686

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