Capturing the Membrane-Triggered Conformational Transition of an α-Helical Pore-Forming Toxin-Reference-Cited by-同舟云学术

Capturing the Membrane-Triggered Conformational Transition of an α-Helical Pore-Forming Toxin

Published:2016-11-17 Issue:47 Volume:120 Page:12064-12078
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Giri Rao V. V. Hemanth¹,Desikan Rajat²,Ayappa K. Ganapathy²³,Gosavi Shachi¹

Affiliation:

1. Simons Centre for the Study of Living Machines, National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bengaluru 560065, India

2. Department of Chemical Engineering, Indian Institute of Science, Bengaluru 560012, India

3. Centre for Biosystems Science and Engineering, Indian Institute of Science, Bengaluru 560012, India

Funder

Department of Atomic Energy, Government of India

Department of Science and Technology, Ministry of Science and Technology

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.6b09400

Reference46 articles.

1. Pore-forming toxins: ancient, but never really out of fashion

2. E. coli Hemolysin E (HlyE, ClyA, SheA)

3. The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism

4. The Solvent-Exposed C-Terminus of the Cytolysin A Pore-Forming Toxin Directs Pore Formation and Channel Function in Membranes

5. Molecular analysis of the cytolytic protein ClyA (SheA) from Escherichia coli

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