百日咳毒素和霍乱毒素对膜成分的ADP核糖基化作用。 - Suppr

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超能文献

ADP-ribosylation of membrane components by pertussis and cholera toxin.

作者信息

Ribeiro-Neto F A, Mattera R, Hildebrandt J D, Codina J, Field J B, Birnbaumer L, Sekura R D

出版信息

Methods Enzymol. 1985;109:566-72. doi: 10.1016/0076-6879(85)09115-7.

DOI:10.1016/0076-6879(85)09115-7

PMID:2859516

Abstract

摘要

相似文献

ADP-ribosylation of membrane components by pertussis and cholera toxin.百日咳毒素和霍乱毒素对膜成分的ADP核糖基化作用。

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Rat heart cell membranes contain three substrates for cholera toxin-catalyzed ADP-ribosylation and a single substrate for pertussis toxin-catalyzed ADP-ribosylation.

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[Receptor-adenylate cyclase coupling--receptor-GTP binding protein(N) coupling and ADP-ribosylation of N by bacterial toxins].[受体 - 腺苷酸环化酶偶联——受体 - GTP 结合蛋白（N）偶联以及细菌毒素对 N 的 ADP 核糖基化作用]

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ADP-ribosylation of the inhibitory guanine nucleotide regulatory protein (Ni) as a possible mechanism underlying development of beta-adrenergic responses during primary culture of rat hepatocytes.抑制性鸟嘌呤核苷酸调节蛋白（Ni）的ADP核糖基化作用，可能是大鼠肝细胞原代培养过程中β-肾上腺素能反应发生的潜在机制。

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Loss of the inhibitory function of the guanine nucleotide regulatory component of adenylate cyclase due to its ADP ribosylation by islet-activating protein, pertussis toxin, in adipocyte membranes.在脂肪细胞膜中，由于胰岛激活蛋白百日咳毒素使其发生ADP核糖基化，导致腺苷酸环化酶的鸟嘌呤核苷酸调节成分的抑制功能丧失。

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Functional modification by cholera-toxin-catalyzed ADP-ribosylation of a guanine-nucleotide-binding regulatory protein serving as the substrate of pertussis toxin.霍乱毒素催化的鸟嘌呤核苷酸结合调节蛋白的ADP核糖基化对其功能的修饰，该蛋白作为百日咳毒素的底物。

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