Suppr超能文献

Primary structure of a putative serine protease specific for IGF-binding proteins.

作者信息

Zumbrunn J, Trueb B

机构信息

M.E. Müller-Institut für Biomechanik, Universität Bern, Switzerland.

出版信息

FEBS Lett. 1996 Dec 2;398(2-3):187-92. doi: 10.1016/s0014-5793(96)01229-x.

Abstract

From a subtracted cDNA library we have isolated a cDNA clone coding for a novel transformation-sensitive protein which is expressed by human fibroblasts, but not by their matched SV40 transformed counterparts. This protein has a molecular mass of 51 kDa and is highly related to the HtrA family of serine proteases from bacteria. At the N-terminal end, it contains an IGF-binding domain which may modulate the activity of the associated serine protease. Our data are consistent with the assumption that the novel protein represents one of the proteases that regulate the availability of IGFs by cleaving IGF-binding proteins.

摘要

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验