会员体验
专利管家(专利管理)
工作空间(专利管理)
风险监控(情报监控)
数据分析(专利分析)
侵权分析(诉讼无效)
联系我们
交流群
官方交流:
QQ群: 891211   
微信请扫码    >>>
现在联系顾问~
热词
    • 52. 发明申请
    • Inhibition of mRNA Interferase-Induced Apoptosis in BAK-Deficient and BAK- and Bax-Deficient Mammalian Cells
    • 抑制BAK缺陷型和BAK-和Bax-缺陷型哺乳动物细胞中mRNA干扰素诱导的细胞凋亡
    • US20090047742A1
    • 2009-02-19
    • US12064070
    • 2006-08-22
    • Tsutomu ShimazuKurt DegenhardtEileen WhiteMasayori Inouye
    • Tsutomu ShimazuKurt DegenhardtEileen WhiteMasayori Inouye
    • C12N15/87C12N5/06
    • A61K48/0066A61K48/00C07K14/4747C12N9/22C12N2800/40
    • Ribonucleases, antibiotics, bacterial toxins and viruses inhibit protein synthesis, which results in apoptosis in mammalian cells. How the BCL-2 family of proteins regulates apoptosis in response to shutoff of protein synthesis is not known. According to the present invention, an Escherichia coli toxin MazF inhibited protein synthesis by cleavage of cellular mRNA, and induced apoptosis in mammalian cells. MazF-induced apoptosis required proapoptotic BAK and its upstream regulator, the proapoptotic BH3-only protein NBK/BIK, but not BIM, PUMA or NOXA. Furthermore, NBK/BIK- or BAK-deficient cells were resistant to cell death induced by pharmacologic inhibition of translation and by virus-mediated shutoff of protein synthesis. Thus, the BH3-only protein NBK/BIK is the apical regulator of a BAK-dependent apoptotic pathway in response to shutoff of protein synthesis. Although NBK/BIK is dispensable for development, it is the BH3-only protein targeted for inactivation by viruses, suggesting that it plays a role in pathogen/toxin response through apoptosis activation.
    • 核糖核酸酶,抗生素,细菌毒素和病毒抑制蛋白质合成,导致哺乳动物细胞凋亡。 BCL-2家族蛋白质如何调节蛋白质合成关闭反应的凋亡是未知的。 根据本发明,大肠杆菌毒素MazF通过切割细胞mRNA抑制蛋白质合成,并诱导哺乳动物细胞的细胞凋亡。 MazF诱导的细胞凋亡需要促凋亡BAK及其上游调节因子,即促凋亡BH3蛋白NBK / BIK,而不是BIM,PUMA或NOXA。 此外,NBK / BIK-或BAK缺陷细胞对由翻译的药理学抑制和蛋白质合成的病毒介导的切断引起的细胞死亡具有抗性。 因此,仅BH3蛋白NBK / BIK是响应于蛋白质合成关闭的BAK依赖性凋亡途径的顶端调节剂。 虽然NBK / BIK是不可开发的,但是仅针对通过病毒灭活的BH3蛋白,这表明它通过凋亡激活在病原体/毒素反应中起作用。
    • 56. 发明授权
    • Protein activation
    • 蛋白激活
    • US5719021A
    • 1998-02-17
    • US923260
    • 1992-07-31
    • Masayori Inouye
    • Masayori Inouye
    • C12N9/00C07K1/00C07K1/113C07K14/575C07K14/62C07K14/745C07K14/76C12N9/56C12P21/00C12P21/02C12Q1/68C07K14/435C12N9/96
    • C07K1/1133Y10S435/839
    • A method is disclosed for producing a biochemically active polypeptide from a biochemically inactive polypeptide. The polypeptide is normally but need not be expressed in a precursor form containing a pro-sequence. The inactive polypeptide is reacted with a tailor-made activating peptide. The activating peptide can be synthetic or made by recombinant DNA procedure. The activating peptide is a peptide which contains one or more functional domains which are necessary for folding the inactive polypeptide into a biochemically active conformation. The activating peptide may but need not contain a sequence of amino acids which is identical to the sequence of the natural occurring pro-sequence of the polypeptide. Also, a method is disclosed which permits to identify the one or more functional domains in the pro-sequence of a polypeptide which contribute(s) to the folding of the inactive polypeptide into a biochemically active conformation. The invention relates also to a tailor-made activating peptide (synthetic or by recombinant DNA) and to the biochemically active polypeptide. The protein activation method and the biochemically active proteins are of major utility in their broad applications.
    • 公开了用于从生物化学惰性多肽生产生物化学活性多肽的方法。 多肽通常但不需要以含有前序列的前体形式表达。 无活性多肽与定制的活化肽反应。 活化肽可以是合成的或通过重组DNA程序制备的。 活化肽是含有一个或多个将无活性多肽折叠成生物化学活性构象所必需的功能结构域的肽。 活化肽可以不必含有与多肽的天然存在的前序序列相同的氨基酸序列。 此外,公开了一种方法,其允许鉴定有助于将无活性多肽折叠成生物化学活性构象的多肽的前序序列中的一个或多个功能结构域。 本发明还涉及定制的活化肽(合成的或通过重组DNA)和生物化学活性多肽。 蛋白激活方法和生物化学活性蛋白质在广泛应用中具有重要的实用价值。