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免疫抑制剂去氧精胍菌素与热休克蛋白Hsp70家族成员的相互作用。

Interaction of the immunosuppressant deoxyspergualin with a member of the Hsp70 family of heat shock proteins.

作者信息

Nadler S G, Tepper M A, Schacter B, Mazzucco C E

机构信息

Bristol-Myers Squibb Pharmaceutical Research Institute, Wallingford, CT 06492.

出版信息

Science. 1992 Oct 16;258(5081):484-6. doi: 10.1126/science.1411548.

Abstract

Deoxyspergualin (DSG) is a potent immunosuppressant whose mechanism of action remains unknown. To elucidate its mechanism of action, an intracellular DSG binding protein was identified. DSG has now been shown to bind specifically to Hsc70, the constitutive or cognate member of the heat shock protein 70 (Hsp70) protein family. The members of the Hsp70 family of heat shock proteins are important for many cellular processes, including immune responses, and this finding suggests that heat shock proteins may represent a class of immunosuppressant binding proteins, or immunophilins, distinct from the previously identified cis-trans proline isomerases. DSG may provide a tool for understanding the function of heat shock proteins in immunological processes.

摘要

去氧精胍菌素(DSG)是一种强效免疫抑制剂,其作用机制尚不清楚。为阐明其作用机制,鉴定出一种细胞内DSG结合蛋白。现已证明DSG能特异性结合热休克蛋白70(Hsp70)蛋白家族的组成型或同源成员Hsc70。热休克蛋白Hsp70家族的成员对包括免疫反应在内的许多细胞过程都很重要,这一发现表明热休克蛋白可能代表一类与先前鉴定的顺反脯氨酸异构酶不同的免疫抑制剂结合蛋白,即亲免素。DSG可能为理解热休克蛋白在免疫过程中的功能提供一种工具。

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