Insulin-stimulated serine and threonine phosphorylation of the human insulin receptor. An assessment of the role of serines 1305/1306 and threonine 1348 by their replacement with neutral or negatively charged amino acids.

J.M. Tavaré; B. Zhang; L. Ellis; R.A. Roth

doi:10.1016/s0021-9258(18)54708-6

Insulin-stimulated serine and threonine phosphorylation of the human insulin receptor. An assessment of the role of serines 1305/1306 and threonine 1348 by their replacement with neutral or negatively charged amino acids.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)54708-6 ◽

1991 ◽

Vol 266 (32) ◽

pp. 21804-21809

Author(s):

J.M. Tavaré ◽

B. Zhang ◽

L. Ellis ◽

R.A. Roth

Keyword(s):

Amino Acids ◽

Insulin Receptor ◽

Human Insulin ◽

Charged Amino Acids ◽

Human Insulin Receptor

Download Full-text

Role of signal transduction pathways in hepatic transformation induced by overexpression of the human insulin receptor substrate-1 (IRS-1)

Hepatology ◽

10.1016/0270-9139(95)94521-0 ◽

1995 ◽

Vol 22 (4) ◽

pp. A199

Author(s):

T ITO

Keyword(s):

Signal Transduction ◽

Insulin Receptor ◽

Human Insulin ◽

Signal Transduction Pathways ◽

Insulin Receptor Substrate ◽

Insulin Receptor Substrate 1 ◽

Human Insulin Receptor

Download Full-text

The regulatory role of known tyrosine autophosphorylation sites of the insulin receptor kinase domain. An assessment by replacement with neutral and negatively charged amino acids.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)35272-9 ◽

1991 ◽

Vol 266 (2) ◽

pp. 990-996 ◽

Cited By ~ 1

Author(s):

B Zhang ◽

J M Tavaré ◽

L Ellis ◽

R A Roth

Keyword(s):

Amino Acids ◽

Insulin Receptor ◽

Kinase Domain ◽

Regulatory Role ◽

Receptor Kinase ◽

Charged Amino Acids ◽

Insulin Receptor Kinase ◽

Tyrosine Autophosphorylation

Download Full-text

O-8: Localization of the class I disulfide bonds of the human insulin receptor and the role of class I disulfide bonds in insulin receptor signal transduction

Experimental and Clinical Endocrinology & Diabetes ◽

10.1055/s-0029-1211499 ◽

2009 ◽

Vol 104 (S 02) ◽

pp. 14-14

Author(s):

Kuanghui Lu ◽

Guido Guidotti

Keyword(s):

Signal Transduction ◽

Insulin Receptor ◽

Human Insulin ◽

Disulfide Bonds ◽

Class I ◽

Receptor Signal ◽

Human Insulin Receptor

Download Full-text

Deletion of C-terminal 113 amino acids impairs processing and internalization of human insulin receptor: Comparison of receptors expressed in CHO and NIH-3T3 cells

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research ◽

10.1016/0167-4889(93)90090-c ◽

1993 ◽

Vol 1220 (1) ◽

pp. 1-14 ◽

Cited By ~ 10

Author(s):

Rachel Levy-Toledano ◽

Domenico Accili ◽

Simeon I. Taylor

Keyword(s):

Amino Acids ◽

Insulin Receptor ◽

Human Insulin ◽

3T3 Cells ◽

Human Insulin Receptor ◽

Nih 3T3 ◽

Nih 3T3 Cells

Download Full-text

The role of COOH-terminal and acidic domains in the activity and stability of human insulin receptor protein tyrosine kinase studied by purified deletion mutants of the beta subunit domain.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)41549-9 ◽

1993 ◽

Vol 268 (30) ◽

pp. 22444-22449

Author(s):

P.F. Yan ◽

S.L. Li ◽

S.J. Liang ◽

S Giannini ◽

Y Fujita-Yamaguchi

Keyword(s):

Tyrosine Kinase ◽

Insulin Receptor ◽

Human Insulin ◽

Protein Tyrosine Kinase ◽

Beta Subunit ◽

Receptor Protein ◽

Deletion Mutants ◽

Human Insulin Receptor ◽

Receptor Protein Tyrosine Kinase

Download Full-text

The role of polybasic compounds in determining the tyrosyl phosphorylation of calmodulin by the human insulin receptor

Cellular Signalling ◽

10.1016/0898-6568(93)90032-h ◽

1993 ◽

Vol 5 (6) ◽

pp. 709-725 ◽

Cited By ~ 1

Author(s):

Mark K. Saville ◽

Miles D. Houslay

Keyword(s):

Insulin Receptor ◽

Human Insulin ◽

Human Insulin Receptor ◽

Tyrosyl Phosphorylation

Download Full-text

Human insulin-receptor gene. Partial sequence and amplification of exons by polymerase chain reaction

Diabetes ◽

10.2337/diabetes.39.1.123 ◽

1990 ◽

Vol 39 (1) ◽

pp. 123-128 ◽

Cited By ~ 16

Author(s):

S. Seino ◽

M. Seino ◽

G. I. Bell

Keyword(s):

Polymerase Chain Reaction ◽

Insulin Receptor ◽

Human Insulin ◽

Receptor Gene ◽

Partial Sequence ◽

Chain Reaction ◽

Insulin Receptor Gene ◽

Human Insulin Receptor ◽

Polymerase Chain

Download Full-text

Substitution of lysine for asparagine at position 15 in the alpha-subunit of the human insulin receptor. A mutation that impairs transport of receptors to the cell surface and decreases the affinity of insulin binding.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)30636-1 ◽

1990 ◽

Vol 265 (31) ◽

pp. 19143-19150

Author(s):

T Kadowaki ◽

H Kadowaki ◽

D Accili ◽

S.I. Taylor

Keyword(s):

Cell Surface ◽

Insulin Receptor ◽

Human Insulin ◽

Insulin Binding ◽

Alpha Subunit ◽

Human Insulin Receptor

Download Full-text

Deletion analysis of the human insulin receptor ectodomain reveals independently folded soluble subdomains and insulin binding by a monomeric alpha-subunit.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)38291-2 ◽

1990 ◽

Vol 265 (22) ◽

pp. 13248-13253 ◽

Cited By ~ 1

Author(s):

E M Schaefer ◽

K Siddle ◽

L Ellis

Keyword(s):

Insulin Receptor ◽

Human Insulin ◽

Insulin Binding ◽

Deletion Analysis ◽

Alpha Subunit ◽

Human Insulin Receptor

Download Full-text

Intracellular signaling by a mutant human insulin receptor lacking the carboxyl-terminal tyrosine autophosphorylation sites.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)50389-1 ◽

1992 ◽

Vol 267 (13) ◽

pp. 9065-9070

Author(s):

Y Takata ◽

N.J. Webster ◽

J.M. Olefsky

Keyword(s):

Insulin Receptor ◽

Human Insulin ◽

Intracellular Signaling ◽

Human Insulin Receptor ◽

Carboxyl Terminal ◽

Tyrosine Autophosphorylation

Download Full-text