Replacement of insulin receptor tyrosine residues 1162 and 1163 does not alter the mitogenic effect of the hormone.
about
The insulin receptor with phenylalanine replacing tyrosine-1146 provides evidence for separate signals regulating cellular metabolism and growthAbnormal regulation of ribosomal protein S6 kinase by insulin in skeletal muscle of insulin-resistant humans.Activation of skeletal muscle casein kinase II by insulin is not diminished in subjects with insulin resistanceActivation of glucose transport by a natural mutation in the human insulin receptorTransmembrane signaling by an insulin receptor lacking a cytoplasmic beta-subunit domain.Enhancement of transforming potential of human insulinlike growth factor 1 receptor by N-terminal truncation and fusion to avian sarcoma virus UR2 gag sequence.Effect of microinjection of a low-Mr human placenta protein tyrosine phosphatase on induction of meiotic cell division in Xenopus oocytesActivation of phosphatidylinositol 3-kinase by insulin.Insulin action 1991.Insulin activates nuclear factor kappa B in mammalian cells through a Raf-1-mediated pathway.Mutation of a conserved amino acid residue (tryptophan 1173) in the tyrosine kinase domain of the IGF-I receptor abolishes autophosphorylation but does not eliminate biologic function.Insulin and insulin-like growth factor-I induced phosphorylation in neurally derived cells.Mutations of the platelet-derived growth factor receptor that cause a loss of ligand-induced conformational change, subtle changes in kinase activity, and impaired ability to stimulate DNA synthesis.Insulin and insulin-like growth factor I exert different effects on plasminogen activator production or cell growth in the ovine thyroid cell line OVNIS.Changes in insulin-receptor tyrosine, serine and threonine phosphorylation as a result of substitution of tyrosine-1162 with phenylalanine.Mitogenically uncoupled insulin and IGF-I receptors of differentiated human neuroblastoma cells are functional and mediate ligand-induced signals.Two sequences flanking the major autophosphorylation site of the insulin receptor are essential for tyrosine kinase activation.Characterization of insulin-stimulated protein serine/threonine kinases in CHO cells expressing human insulin receptors with point and deletion mutations.Inhibitory effect of fluoride on insulin receptor autophosphorylation and tyrosine kinase activitySustained signalling from the insulin receptor after stimulation with insulin analogues exhibiting increased mitogenic potencyInsulin receptor function is inhibited by guanosine 5'-[gamma-thio]triphosphate (GTP[S])Inhibitors of chymotrypsin-like activities selectively block the mitotic pathway in rat hepatoma cells.Annexin II is a novel player in insulin signal transduction. Possible association between annexin II phosphorylation and insulin receptor internalization.
P2860
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P2860
Replacement of insulin receptor tyrosine residues 1162 and 1163 does not alter the mitogenic effect of the hormone.
description
1988 nî lūn-bûn
@nan
1988 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Replacement of insulin recepto ...... togenic effect of the hormone.
@ast
Replacement of insulin recepto ...... togenic effect of the hormone.
@en
type
label
Replacement of insulin recepto ...... togenic effect of the hormone.
@ast
Replacement of insulin recepto ...... togenic effect of the hormone.
@en
prefLabel
Replacement of insulin recepto ...... togenic effect of the hormone.
@ast
Replacement of insulin recepto ...... togenic effect of the hormone.
@en
P2093
P2860
P356
P1476
Replacement of insulin recepto ...... togenic effect of the hormone.
@en
P2093
Contreres JO
P2860
P304
P356
10.1073/PNAS.85.21.8032
P407
P577
1988-11-01T00:00:00Z