The crystal structure of themycobacterium tuberculosisRv3019c-Rv3020c ESX complex reveals a domain-swapped heterotetramer-Reference-Cited by-同舟云学术

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The crystal structure of themycobacterium tuberculosisRv3019c-Rv3020c ESX complex reveals a domain-swapped heterotetramer

Published:2010-07-13 Issue:9 Volume:19 Page:1692-1703
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Arbing Mark A.,Kaufmann Markus,Phan Tung,Chan Sum,Cascio Duilio,Eisenberg David

Funder

Department of Energy

National Institutes of Health

The Department of Energy, Office of Basic Energy Sciences

The Integrated Structure Function Initiative

The Tuberculosis Structural Genomics Consortium

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.451/fullpdf

Reference60 articles.

1. Mycobacterial subversion of chemotherapeutic reagents and host defense tactics: challenges in tuberculosis drug development;Nguyen;Annu Rev Pharmacol Toxicol,2009

2. Recombinant BCG exporting ESAT-6 confers enhanced protection against tuberculosis;Pym;Nat Med,2003

3. Deletion of RD1 from Mycobacterium tuberculosis mimics bacille Calmette-Guerin attenuation;Lewis;J Infect Dis,2003

4. The primary mechanism of attenuation of bacillus Calmette-Guerin is a loss of secreted lytic function required for invasion of lung interstitial tissue;Hsu;Proc Natl Acad Sci USA,2003

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2. Multiple genetic paths including massive gene amplification allow Mycobacterium tuberculosis to overcome loss of ESX-3 secretion system substrates;Proceedings of the National Academy of Sciences;2022-02-22

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4. Structure and Function of the Mycobacterial Type VII Secretion Systems;Annual Review of Microbiology;2020-09-08

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