Resolving the 3D spatial orientation of helix I in the closed state of the colicin E1 channel domain by FRET. Insights into the integration mechanism-Reference-Cited by-同舟云学术

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Resolving the 3D spatial orientation of helix I in the closed state of the colicin E1 channel domain by FRET. Insights into the integration mechanism

Published:2016-10 Issue: Volume:608 Page:52-73
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Lugo Miguel R.,Ho Derek,Merrill A. Rod

Funder

Natural Sciences and Engineering Research Council of Canada

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference59 articles.

1. Colicin Biology

2. Use of colicin-based genetic tools for studying bacterial protein transport

3. On the mechanism and pathway of colicin import across the E. Coli outer membrane

4. Structure-Function of the Channel-Forming Colicins

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. H1 helix of colicin U causes phospholipid membrane permeation;Biochimica et Biophysica Acta (BBA) - Biomembranes;2022-04

2. In Situ Electrochemical and PM-IRRAS Studies of Colicin E1 Ion Channels in the Floating Bilayer Lipid Membrane;Langmuir;2019-06-13

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