首页> 外文OA文献 >Crystal Structure at 2.8 Å of the DLLRKN-containing Coiled-coil Domain of Huntingtin-interacting Protein 1 (HIP1) Reveals a Surface Suitable for Clathrin Light Chain Binding

【2h】

Crystal Structure at 2.8 Å of the DLLRKN-containing Coiled-coil Domain of Huntingtin-interacting Protein 1 (HIP1) Reveals a Surface Suitable for Clathrin Light Chain Binding

机译：含有2.8埃的含Dllrkn的卷绕式卷线域（HIP1）的晶体结构显示出适用于克拉仑轻链结合的表面

代理获取

本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。

页面导航

著录项
相似文献
相关主题

著录项

作者
Joel A. Ybe; Sanjay Mishra; Stephen Helms; Jay Nix;
展开▼
作者单位

展开▼
年度 2007
总页数
原文格式 PDF
正文语种
中图分类

相似文献

外文文献
专利

1. Crystal structure at 2.8 A of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding. [J] . Ybe JA, Mishra S, Helms S, Journal of Molecular Biology . 2007,第1期

机译：亨廷顿蛋白相互作用蛋白1（HIP1）的包含DLLRKN的卷曲螺旋结构域的2.8 A处的晶体结构揭示了适合网格蛋白轻链结合的表面。
2. Crystal structure at 2.8 angstrom of Huntingtin-interacting protein 1 (HIP1) coiled-coil domain reveals a charged surface suitable for HIP1 protein interactor (HIPPI) [J] . Niu Q, Ybe JA Journal of Molecular Biology . 2008,第5期

机译：Huntingtin相互作用蛋白1（HIP1）卷曲螺旋结构域在2.8埃处的晶体结构揭示了适合HIP1蛋白相互作用物（HIPPI）的带电表面
3. Two Distantly Spaced Basic Patches in the Flexible Domain of Huntingtin-Interacting Protein 1 (HIP1) Are Essential for the Binding of Clathrin Light Chain [J] . Joel A. Ybe, Mary E. Clegg, Melissa Illingworth, Research Letters in Biochemistry . 2009,第Null期

机译：在Huntingtin相互作用蛋白1（HIP1）的灵活域中的两个遥远的基本补丁是网格蛋白轻链的绑定所必需的。
4. Characterization of heparin interactions with its client proteins: mapping minimal protein-binding domains within glycosaminoglycan chains using top-down mass spectrometry [C] . Yunlong Zhao, Igor A. Kaltashov ASMS Conference on Mass Spectrometry and Allied Topics . 2016

机译：肝素与其客户蛋白相互作用的表征：使用自上向下质谱法将糖胺聚糖链中的最小蛋白质结合结构域映射缩放最小蛋白质结合结构域
5. A comparison of the pathogenesis of rabies virus SAD-L16 and mutants modified at the dynein light chain binding domain in the phosphoprotein and at position 333 in the glycoprotein in young mice. [D] . Rasalingam, Pamini. 2005

机译：狂犬病病毒SAD-L16与在年轻小鼠中磷蛋白中的达因轻链结合结构域和糖蛋白中的333位修饰的突变体的发病机理比较。
6. Crystal structure at 2.8 Å of the DLLRKN-containing coiled-coil domain of Huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding [O] . Joel A. Ybe, Sanjay Mishra, Stephen Helms, -1

机译：亨廷顿相互作用蛋白1（HIP1）的包含DLLRKN的卷曲螺旋结构域的2.8Å处的晶体结构揭示了适合网格蛋白轻链结合的表面
7. Crystal Structure at 2.8 Å of Huntingtin-Interacting Protein 1 (HIP1) Coiled-Coil Domain Reveals a Charged Surface Suitable for HIP1 Protein Interactor (HIPPI) [O] . Qian Niu, Joel A. Ybe 2008

机译：亨廷顿相互作用蛋白1（HIP1）卷轴螺旋域的晶体结构显示适用于HIP1蛋白互动器（HIPPI）的带电表面

Crystal Structure at 2.8 Å of the DLLRKN-containing Coiled-coil Domain of Huntingtin-interacting Protein 1 (HIP1) Reveals a Surface Suitable for Clathrin Light Chain Binding

著录项

相似文献

相关主题

期刊订阅