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Scholar Results 1 - 10 of about 101 related to Bruss: Increased phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle.... (0.10 sec) 

Increased phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle in …

- shouxi.net
MD Bruss, EB Arias, GE Lienhard, GD Cartee - Diabetes, 2005 - Am Diabetes Assoc
In 3T3-L1 adipocytes, insulin-stimulated GLUT4 translocation requires
phosphorylation of the protein designated Akt substrate of 160 kDa (AS160). Both
insulin and contractions activate Akt in skeletal muscle. Therefore, we ...
Cited by 102 - Related articles - All 8 versions

AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic …

- shouxi.net
JT Treebak, S Glund, A Deshmukh, DK Klein, … - Diabetes, 2006 - Am Diabetes Assoc
AMP-activated protein kinase (AMPK) is a heterotrimeric protein that regulates
glucose transport mediated by cellular stress or pharmacological agonists such
as 5-aminoimidazole-4-carboxamide 1 β-d-ribonucleoside (AICAR). AS160, a ...
Cited by 82 - Related articles - BL Direct - All 7 versions

Distinct signals regulate AS160 phosphorylation in response to insulin, AICAR, and …

- shouxi.net
HF Kramer, CA Witczak, N Fujii, N Jessen, … - Diabetes, 2006 - Am Diabetes Assoc
Insulin and contraction increase GLUT4 translocation in skeletal muscle via
distinct signaling mechanisms. Akt substrate of 160 kDa (AS160) mediates
insulin-stimulated GLUT4 translocation in L6 myotubes, presumably through ...
Cited by 85 - Related articles - BL Direct - All 6 versions

AS160 regulates insulin-and contraction-stimulated glucose uptake in mouse skeletal …

- shouxi.net
HF Kramer, CA Witczak, EB Taylor, N Fujii, … - Journal of Biological Chemistry, 2006 - ASBMB
Insulin and contraction are potent stimulators of GLUT4 translocation and
increase skeletal muscle glucose uptake. We recently identified the Rab
GTPase-activating protein (GAP) AS160 as a putative point of convergence ...
Cited by 63 - Related articles - All 6 versions

Insulin-stimulated Phosphorylation of a Rab GTPase-activating Protein Regulates GLUT 4 …


H Sano, S Kane, E Sano, CP Miinea, JM … - Journal of Biological Chemistry, 2003 - ASBMB
Insulin stimulates the rapid translocation of intracellular glucose transporters
of the GLUT4 isotype to the plasma membrane in fat and muscle cells. The
connections between known insulin signaling pathways and the protein ...
Cited by 251 - Related articles - BL Direct - All 4 versions

Exercise-induced phosphorylation of the novel Akt substrates AS160 and filamin A in human …

- shouxi.net
A Deshmukh, VG Coffey, Z Zhong, AV Chibalin … - Diabetes, 2006 - Am Diabetes Assoc
Skeletal muscle contraction stimulates multiple signaling cascades that govern a
variety of metabolic and transcriptional events. Akt/protein kinase B regulates
metabolism and growth/muscle hypertrophy, but contraction effects on this ...
Cited by 44 - Related articles - BL Direct - All 5 versions

Insulin stimulation of GLUT4 exocytosis, but not its inhibition of endocytosis, is …

- molbiolcell.org
A Zeigerer, MK McBrayer, TE McGraw - Molecular biology of the cell, 2004 - Am Soc Cell Biol
Insulin maintains whole body blood glucose homeostasis, in part, by regulating
the amount of the GLUT4 glucose transporter on the cell surface of fat and
muscle cells. Insulin induces the redistribution of GLUT4 from ...
Cited by 127 - Related articles - BL Direct - All 8 versions

A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte …

- jbc.org
S Kane, H Sano, SCH Liu, JM Asara, WS Lane … - Journal of Biological Chemistry, 2002 - ASBMB
This study describes a method for the identification of the substrates of
specific serine kinases. An antibody specific for the phosphomotif generated by
the kinase is used to isolate phosphorylated substrates by ...
Cited by 207 - Related articles - BL Direct - All 5 versions

AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase- …


CP Mîinea, H Sano, S Kane, E Sano, M … - Biochemical Journal, 2005 - pubmedcentral.nih.gov
Recently, we described a 160 kDa protein (designated AS160, for Akt substrate of
160 kDa) with a predicted Rab GAP (GTPase-activating protein) domain that is
phosphorylated on multiple sites by the protein kinase Akt. Phosphorylation ...
Cited by 88 - Related articles - BL Direct - All 7 versions

Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle …

- 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 78 - Related articles - All 5 versions


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