JT Brozinick, BR Roberts, GL Dohm - Diabetes, 2003 - Am Diabetes Assoc Recent evidence has shown that activation of phosphatidyinositol-3-kinase (PI3K)
and Akt, necessary for insulin stimulation of glucose transport, is impaired in
insulin resistance. It is unknown, however, which Akt isoform shows ... Cited by 67 - Related articles - BL Direct - All 4 versions
A Krook, M Bjornholm, D Galuska, XJ Jiang, … - DIABETES-NEW YORK-, 2000 - Am Diabetes Assoc We characterized metabolic and mitogenic signaling pathways in isolated skeletal
muscle from well-matched type 2 diabetic and control subjects. Time course
studies of the insulin receptor, insulin receptor substrate ( IRS )-1/2, ... Cited by 207 - Related articles - BL Direct - All 4 versions
M Beeson, MP Sajan, M Dizon, D Grebenev, J … - Diabetes, 2003 - Am Diabetes Assoc Insulin resistance in type 2 diabetes is partly due to impaired glucose
transport in skeletal muscle. Atypical protein kinase C (aPKC) and protein
kinase B (PKB), operating downstream of phosphatidylinositol (PI) 3-kinase ... Cited by 90 - Related articles - BL Direct - All 4 versions
C Pender, ID Goldfine, JL Kulp, CJ Tanner, … - Metabolism, 2005 - Elsevier Obesity is associated with impaired insulin-stimulated glucose disposal in the
skeletal muscle, but whether this is an intrinsic or acquired factor is unknown.
In many patients with type 2 diabetes mellitus (T2D) and their nondiabetic ... Cited by 13 - Related articles - All 8 versions
- ►diabetesjournals.org [PDF] A Krook, RA Roth, XJ Jiang, JR Zierath, H … - Diabetes, 1998 - Am Diabetes Assoc The serine/threonine kinase Akt (PKB/Rac) has been implicated as playing a role
in the insulin-signaling pathway to glucose transport. Little is known regarding
the regulation of Akt kinase activity in insulin-sensitive tissues, such as ... Cited by 216 - Related articles - BL Direct - All 4 versions
M Meyer, K Levin, T Grimmsmann, H Beck- … - Diabetologia, 2002 - Springer Aims/hypothesis. Alterations in insulin signalling could contribute to insulin
resistance in Type II (non-insulin- dependent) diabetes mellitus. Some of these
alterations could be secondary to the diabetic state, ie. the hyper- ... Cited by 34 - Related articles - BL Direct - All 3 versions
H Tsuchida, M Björnholm, M Fernström, D … - Pflügers Archiv European Journal of Physiology, 2002 - Springer Page 1. Pflugers Arch - Eur J Physiol (2002) 445:25–31 DOI 10.1007/s00424-
002-0907-9 ORI GI NAL AR TI CLE Hiroki Tsuchida · Marie ... Cited by 10 - Related articles - BL Direct - All 3 versions
- ►jbc.org SS Bae, H Cho, J Mu, MJ Birnbaum - Journal of Biological Chemistry, 2003 - ASBMB Recent data have implicated the serine/threonine protein kinase Akt/protein
kinase B (PKB) in a diverse array of physiological pathways, raising the
question of how biological specificity is maintained. Partial clarification ... Cited by 145 - Related articles - BL Direct - All 4 versions
- ►physiology.org AR Gosmanov, GE Umpierrez, AH Karabell, … - American Journal of Physiology- Endocrinology And …, 2004 - Am Physiological Soc Although a pharmacological dose of insulin produces a dramatic increase in
phosphorylation and activity of Akt isoforms 1 and 2 in mammalian skeletal
muscle, few studies have examined the effect of physiological ... Cited by 24 - Related articles - All 4 versions
- ►shouxi.net HKR Karlsson, JR Zierath, S Kane, A Krook, … - Diabetes, 2005 - Am Diabetes Assoc AS160 is a newly described substrate for the protein kinase Akt that links
insulin signaling and GLUT4 trafficking. In this study, we determined the
expression of and in vivo insulin action on AS160 in human skeletal muscle. ... Cited by 77 - Related articles - All 5 versions
