Výsledky vyhledávání

Phosphorylation state and biological function of a mutant human insulin receptor Val996

Autor: Yasuo Akanuma, M Odawara, F Takaku, Masato Kasuga, Kazuyuki Tobe, Ritsuko Yamamoto-Honda, O Koshio, Yoshikazu Shibasaki, K Momomura, Takashi Kadowaki

Publikováno v: Journal of Biological Chemistry. 265:14777-14783

Chinese hamster ovary (CHO) cell transfectants that expressed human insulin receptors whose glycine 996 was substituted by valine were studied. Receptor processing and insulin binding were unaffected by this mutation; however, this mutant insulin rec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0f46eb19298e7022d9c10ab708e7037
https://doi.org/10.1016/s0021-9258(18)77180-9

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Normal insulin receptor substrate-1 phosphorylation in autophosphorylation-defective truncated insulin receptor. Evidence that phosphorylation of substrates might be sufficient for certain biological effects evoked by insulin

Autor: Yoshikazu Shibasaki, Yasuo Akanuma, Yoshifumi Mori, K Momomura, Ritsuko Yamamoto-Honda, Takashi Kadowaki, Yasushi Kaburagi, Kazuyuki Tobe, Yoshikazu Tamori, O Koshio

Publikováno v: The Journal of biological chemistry. 268(22)

A mutant human insulin receptor that lacked the 82 amino acids of the COOH terminus of the beta-subunit (del82) was studied. Both the wild type insulin receptor (HIR) and the mutant receptor were expressed in Chinese hamster ovary (CHO) cells by stab

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1166d1e78502d148a61e4c625ab10061
https://pubmed.ncbi.nlm.nih.gov/8344965

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Enhanced insulin-induced mitogenesis and mitogen-activated protein kinase activities in mutant insulin receptors with substitution of two COOH-terminal tyrosine autophosphorylation sites by phenylalanine

Autor: Ritsuko Yamamoto-Honda, Kazuyuki Tobe, O Koshio, Hiroshi Sakura, Yasuo Akanuma, A Ando, Yasushi Kaburagi, Yoshio Yazaki, K Momomura, Yoshikazu Tamori

Publikováno v: The Journal of biological chemistry. 267(18)

We have studied the function of a mutant human insulin receptor in which two COOH-terminal autophosphorylation sites (Tyr-1316 and -1322) were replaced by phenylalanine (F/Y COOH-terminal 2 tyrosines (CT2)). In addition, we have also constructed a mu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b24f94bb91ed2680f66ef771a04b96aa
https://pubmed.ncbi.nlm.nih.gov/1618780

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Insulin and 12-O-tetradecanoylphorbol-13-acetate activation of two immunologically distinct myelin basic protein/microtubule-associated protein 2 (MBP/MAP2) kinases via de novo phosphorylation of threonine and tyrosine residues

Autor: Kenshiro Hara, Eisuke Nishida, Kazuyuki Tobe, K Ueki, O Koshio, Yukiko Gotoh, Takashi Kadowaki, K Momomura, Yasuo Akanuma, Hiroyuki Tamemoto

Publikováno v: The Journal of biological chemistry. 266(36)

Two site-specific antibodies have been prepared by immunizing rabbits with chemically synthesized peptides derived from the partial cDNA-predicted amino acid sequence of extracellular signal-regulated kinase 1 (ERK1), which has been proposed to encod

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35bfef9fe764999ea55e7615d17257aa
https://pubmed.ncbi.nlm.nih.gov/1662217

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Concanavalin A-induced receptor aggregation stimulates the tyrosine kinase activity of the insulin receptor in intact cells

Autor: T Shiba, K Tobe, O Koshio, R Yamamoto, Y Shibasaki, N Matsumoto, S Toyoshima, T Osawa, Y Akanuma, F Takaku, M Kasuga

Concanavalin A (ConA) stimulated the phosphorylation of the beta-subunit of the insulin receptor and an Mr-185,000 protein on serine and tyrosine residues in intact H-35 rat hepatoma cells. This Mr-185,000 protein whose phosphorylation was stimulated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::575fcfb53cb09aa42bd5c2be5a80744c
https://europepmc.org/articles/PMC1131367/

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Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells

Autor: Y Akanuma, Masato Kasuga, O Koshio

Publikováno v: Biochemical Journal. 250:95-101

H-35 rat hepatoma cells were labelled with [32P]orthophosphate and their insulin receptors isolated on wheat germ agglutinin (WGA)-agarose and anti-(insulin receptor) serum. The incubation of these cells with 10 mM-H2O2 for 10 min increased the phosp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed77d61527e954d3da4f26681872fecc
https://doi.org/10.1042/bj2500095

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Tyrosine Phosphorylation of pp185 by Insulin Receptor Kinase in a Cell-free System

Autor: Kazuyuki Tobe, O Koshio, Yasuo Akanuma, T Izumi, Masato Kasuga, Y Tashiro-Hashimoto, F Takaku

Publikováno v: Journal of Biological Chemistry. 264:6879-6885

Insulin treatment of rat H-35 hepatoma cells causes rapid tyrosine phosphorylation of a high molecular weight protein termed pp185 besides autophosphorylation of the beta-subunit of the insulin receptor (IR) in an intact cell system. To elucidate the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bb1d1d483b80e53acbd32212ee9ddd9f
https://doi.org/10.1016/s0021-9258(18)83513-x

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Tyrosine phosphorylation of pp185 by insulin receptor kinase in a cell-free system

Autor: Y, Tashiro-Hashimoto, K, Tobe, O, Koshio, T, Izumi, F, Takaku, Y, Akanuma, M, Kasuga

Publikováno v: The Journal of biological chemistry. 264(12)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f2a157ad6df6d4289c1378cf5e94efe0
https://pubmed.ncbi.nlm.nih.gov/2468662

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