- ►shouxi.net Z Yi, P Langlais, EA De Filippis, M Luo, CR … - Diabetes, 2007 - Am Diabetes Assoc OBJECTIVE—Research has focused on insulin receptor substrate (IRS)-1 as a
locus for insulin resistance. Tyrosine phosphorylation of IRS-1 initiates
insulin signaling, whereas serine/threonine phosphorylation alters the ... Cited by 7 - Related articles - BL Direct - All 5 versions
- ►endojournals.org M Luo, P Langlais, Z Yi, N Lefort, EA De … - Endocrinology, 2007 - Endocrine Soc The function of insulin receptor substrate-1 (IRS-1) is regulated by both
tyrosine and serine/threonine phosphorylation. Phosphorylation of some
serine/threonine residues in IRS-1 dampens insulin signaling, whereas ... Cited by 8 - Related articles - BL Direct - All 3 versions
- ►endojournals.org J Giraud, M Haas, EP Feener, KD Copps, X … - Molecular Endocrinology, 2007 - Endocrine Soc Multisite phosphorylation of Irs1 on serine and threonine residues regulates
insulin signaling that can contribute to insulin resistance. We identified by
mass spectrometry the phosphorylation of Ser522 in rat Irs1 (S522 Irs1 ). ... Cited by 6 - Related articles - BL Direct - All 3 versions
- ►endojournals.org S Lee, EG Lynn, J Kim, MJ Quon - Endocrinology, 2008 - Endocrine Soc Protein kinase C- , a downstream effector of phosphatidylinositol 3-kinase
(PI3K), phosphorylates insulin receptor substrate (IRS)-1 on serine residues
impairing activation of PI3K in response to insulin. Because IRS-1 is ... Cited by 2 - Related articles - BL Direct - All 4 versions
C Weigert, M Kron, H Kalbacher, AK Pohl, H … - Molecular Endocrinology, 2008 - Endocrine Soc Transduction of the insulin signal is mediated by multisite Tyr and Ser/Thr
phosphorylation of the insulin receptor substrates (IRSs). Previous studies on
the function of single-site phosphorylation, particularly phosphorylation ... Cited by 2 - Related articles - All 3 versions
- ►endojournals.org M Luo, S Reyna, L Wang, ZP Yi, C Carroll, LQ … - Endocrinology, 2005 - Endocrine Soc Insulin receptor substrate 1 (IRS-1), an intracellular substrate of the insulin
receptor tyrosine kinase, also is heavily phosphorylated on serine and threonine
residues, and several serine phosphorylation sites alter the function of ... Cited by 16 - Related articles - BL Direct - All 5 versions
- ►missouri.edu [PDF] Z Yi, M Luo, LJ Mandarino, SM Reyna, CA … - Journal of the American Society for Mass Spectrometry, 2006 - Elsevier Serine/threonine phosphorylation of insulin receptor substrate-1 (IRS-1)
regulates the function and subsequent insulin signaling of this protein. Human
IRS-1 has 1242 amino acid residues, including 182 serines and 60 ... Cited by 9 - Related articles - All 7 versions
- ►endojournals.org Y Cho, M Ariga, Y Uchijima, K Kimura, JY … - Endocrinology, 2006 - Endocrine Soc Chronic excess of GH is known to cause hyperinsulinemia and insulin resistance.
We developed human GH transgenic (TG) rats, which were characterized by high
plasma levels of human GH and IGF-I. These TG rats showed higher levels of ... Cited by 4 - Related articles - BL Direct - All 4 versions
S Boura-Halfon, Y Zick - American Journal of Physiology- Endocrinology And …, 2009 - Am Physiological Soc Insulin signaling at target tissues is essential for growth and development and
for normal homeostasis of glucose, fat, and protein metabolism. Control over
this process is therefore tightly regulated. It can be achieved by a ... Cited by 6 - Related articles - All 3 versions
- ►endojournals.org R Nawaratne, A Gray, CH Jorgensen, CP … - Molecular Endocrinology, 2006 - Endocrine Soc Phosphorylation of insulin receptor substrate (IRS) proteins on serine residues
is an important posttranslational modification that is linked to insulin
resistance. Several phosphoserine sites on IRS1 have been identified; the ... Cited by 13 - Related articles - BL Direct - All 5 versions
