A Minami, M Iseki, K Kishi, M Wang, M Ogura, … - Diabetes, 2003 - Am Diabetes Assoc A tyrosine kinase adaptor protein containing pleckstrin homology and SH2 domains
(APS) is rapidly and strongly tyrosine phosphorylated by insulin receptor kinase
upon insulin stimulation. The function of APS in insulin signaling has ... Cited by 58 - Related articles - BL Direct - All 4 versions
MY Ahn, KD Katsanakis, F Bheda, TS Pillay - Journal of Biological Chemistry, 2004 - ASBMB APS (adapter protein with Pleckstrin homology and Src homology 2 domains) is
recruited by the autophosphorylated insulin receptor and is essential for Glut4
translocation. Although both APS and CAP (c-Cbl-associated protein) ... Cited by 42 - Related articles - BL Direct - All 4 versions
M Li, D Ren, M Iseki, S Takaki, L Rui - Endocrinology, 2006 - Endocrine Soc SH2-B and APS, two members of a pleckstrin homology and SH2 domain-containing
adaptor family, promote both insulin and leptin signaling in a similar fashion
in cultured cells. In addition, APS mediates insulin-stimulated activation ... Cited by 18 - Related articles - BL Direct - All 4 versions
- ►nih.gov S Ohtsuka, S Takaki, M Iseki, K Miyoshi, N … - Molecular and Cellular Biology, 2002 - Am Soc Microbiol Many growth factors and hormones modulate the reproductive status in mammals.
Among these, insulin and insulin-like growth factor I (IGF-I) regulate the
development of gonadal tissues. SH2-B has been shown to interact with ... Cited by 45 - Related articles - BL Direct - All 5 versions
Z Ahmed, BJ Smith, TS Pillay - Febs Letters, 2000 - Elsevier The APS adapter protein is rapidly tyrosine-phosphorylated following insulin
stimulation. In insulin-stimulated 3T3-L1 adipocytes, APS co-precipitated with
phosphorylated c-Cbl. In CHO.T-APS cells overexpressing the insulin ... Cited by 78 - Related articles - All 5 versions
- ►nih.gov C Duan, H Yang, MF White, L Rui - Molecular and Cellular Biology, 2004 - Am Soc Microbiol Insulin regulates glucose homeostasis by binding and activating the insulin
receptor, and defects in insulin responses (insulin resistance) induce type 2
diabetes. SH2-B, an Src homology 2 (SH2) and pleckstrin homology domain- ... Cited by 38 - Related articles - BL Direct - All 7 versions
SA Moodie, J Alleman-Sposeto, TA Gustafson - Journal of Biological Chemistry, 1999 - ASBMB In order to identify novel substrates involved in insulin receptor signaling, a
yeast two-hybrid 3T3-L1 adipocyte cDNA library was screened with the cytoplasmic
domain of the human insulin receptor as bait. Here we describe the ... Cited by 84 - Related articles - BL Direct - All 4 versions
- ►nih.gov M Iseki, C Kubo, SM Kwon, A Yamaguchi, Y … - Molecular and Cellular Biology, 2004 - Am Soc Microbiol APS (adaptor molecule containing PH and SH2 domains) is an intracellular adaptor
protein that forms an adaptor family along with Lnk and SH2-B. While experiments
using cultured cell lines have demonstrated that APS is phosphorylated in ... Cited by 16 - Related articles - BL Direct - All 5 versions
- ►nih.gov J Liu, A Kimura, CA Baumann, AR Saltiel - Molecular and Cellular Biology, 2002 - Am Soc Microbiol APS is a Cbl-binding protein that is tyrosine phosphorylated by the insulin
receptor kinase. Insulin-stimulated phosphorylation of tyrosine 618 in APS is
necessary for its association with c-Cbl and the subsequent tyrosine ... Cited by 115 - Related articles - BL Direct - All 6 versions
- ►nih.gov [PDF] Z Ahmed, TS Pillay - Biochemical Journal, 2003 - pubmedcentral.nih.gov Page 1. Biochem. J. (2003) 371, 405–412 (Printed in Great Britain) 405 Adapter
protein with a pleckstrin homology (PH) and an Src homology 2 ... Cited by 31 - Related articles - BL Direct - All 7 versions