我们确定了与端粒酶相关的TPP1 OB fold中的特定环残基以及TERT中的关键残基,包括肺纤维化患者亚组中的突变残基。这些数据定义了端粒维持所需的端粒酶-TPP1相互作用的潜在界面并表明端粒酶相关疾病中端粒酶募集缺陷。 介绍 通过端粒酶将端粒重复序列添加到染色体末端对于对抗干细胞和癌细胞中细胞分裂时发生的端粒不完全复制...
OB-fold: growing bigger with functional consistency. Curr Protein Pept Sci 4:195-206 Ando T - Agrawal, KV - 2003Agrawal, V., and Kishan, K.V. (2003). OB-fold: Growing bigger with functional consistency. Curr. Protein Pept. Sci. 4, 195-206....
特别地,所述感兴趣的靶可以是用作起始分子的OB-fold蛋白质的天然靶的不同的化学性质形式。 法律状态 法律状态公告日 法律状态信息 法律状态 权利要求说明书 1.OB-fold蛋白质作为起始分子通过组合突变/选择方法获得特异性结合靶的分子的应用。 2.权利要求1的应用,其中所述组合突变/选择方法与在环3插入1到15个...
The widespread oligonucleotide/oligosaccharide-binding (OB)-fold recognizes diverse substrates from sugars to nucleic acids and proteins, and plays key roles in genome maintenance, transcription, translation, and tRNA metabolism. OB-containing bacterial Trbp and yeast Arc1p proteins are thought to recogniz...
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今天给各位翻译的是2019年《 Journal of Cancer Research and Clinical Oncology》期刊文章:TPP1 OB‑fold domain protein suppresses cell proliferation and induces cell apoptosis by inhibiting telomerase …
CST蛋白复合体由9个OB-fold结构域组成【5】,其在端粒酶移除和C链填补两个过程可能是由不同结构域分别调控的。中山大学附属第一医院冯旭阳副研究员先前的研究表明CTC1-STN1具有限制端粒酶的功能,防止端粒DNA损伤信号产生,而TEN1能稳...
Here, we identify a REV7 complex with FAM35A and C20ORF196, which is distinct from the Polζ complex of REV7. FAM35A resembles a telomere-protecting protein, POT1, in that both proteins contain three OB-fold domains and bind single-strand DNA (ssDNA). Cells lacking either FAM35A or ...
The C-terminal soluble domain of stomatin operon partner protein (sTOPP) of the hyperthermophilic archaeon Pyrococcus horikoshii has an oligonucleotide binding-fold (OB-fold). STOPP lacks the conserved surface residues necessary for binding to DNA/RNA. A tryptophan (W) residue is conserved instead ...
摘要: OB-fold and RGG domains are dispensable for RHA-stimulated HIV-1 production.OB-fold and RGG domains are not required for activation of HIV-1 transcription by RHA.OB-fold facilitates the generation of HIV-1 6D RNA.关键词:HIV-1 RNA helicase A OB-fold Transcription Splicing ...