首页> 外文OA文献 >The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel

【2h】

The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel

机译：OMPA的可溶性，周质结构域作为独立单元，通过降低展开的OMPA跨膜β-桶的自相关倾向显示伴侣活性

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
引文网络
相似文献
相关主题

著录项

作者
Emily J. Danoff; Karen G. Fleming;
展开▼
作者单位

展开▼
年度 2011
总页数
原文格式 PDF
正文语种
中图分类

相似文献

外文文献

1. The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane beta-barrel. [J] . Danoff EJ, Fleming KG Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena . 2011,第1期

机译：OmpA的可溶性周质域折叠成一个独立的单元，并通过降低未折叠的OmpA跨膜β-桶的自缔合倾向显示伴侣活性。
2. The Periplasmic Chaperone Skp Facilitates Targeting, Insertion, and Folding of OmpA into Lipid Membranes with a Negative Membrane Surface Potential [J] . Geetika J. Patel Susanne Behrens-Kneip Otto Holst and Jrg H. Kleinschmidt Biochemistry . 2009,第43期

机译：周质伴侣Skp有助于靶向，插入和折叠OmpA到具有负膜表面电位的脂质膜。
3. Ligand-Mediated Folding of the OmpA Periplasmic Domain from Acinetobacter baumannii [J] . Mushtaq Ameeq Ul, Park Jeong Soon, Bae Sung-Hun, Biophysical Journal . 2017,第10期

机译：介导的介导来自肺杆菌的OMPA周质域的折叠
4. The soluble periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel [O] . Emily J. Danoff, Karen G. Fleming -1

机译：菌Ompa的可溶性周质结构域通过减少未折叠的Ompa跨膜β桶的自缔合倾向折叠作为一个独立的单元并显示伴侣活性
5. The Periplasmic Chaperone Skp Facilitates Targeting, Insertion, and Folding of OmpA into Lipid Membranes with a Negative Membrane Surface Potential† [O] . Geetika J. Patel, Susanne Behrens-kneip, Otto Holst, 2009

机译：periplasmic Chaperone skp促进Ompa靶向，插入和折叠成具有负膜表面电位的脂质膜†

The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel

著录项

引文网络

相似文献

相关主题

期刊订阅