Structural insights into a new substrate binding mode of a histidine acid phosphatase from Legionella pneumophila-Reference-Cited by-同舟云学术

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Structural insights into a new substrate binding mode of a histidine acid phosphatase from Legionella pneumophila

Published:2021-02 Issue: Volume:540 Page:90-94
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Guo Yu,Zhou Dan,Zhang Hui,Zhang Nan-Nan,Qi Xiaoyu,Chen Xiaofang,Chen Qi,Li Jing,Ge Honghua,Teng Yan-Bin

Funder

Natural Science Foundation of Anhui Province

National Natural Science Foundation of China

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference34 articles.

1. The Legionella pneumophila prp locus; required during infection of macrophages and amoebae;Stone;Microb. Pathog.,1999

2. Multiple substrates of the Legionella pneumophila Dot/Icm system identified by interbacterial protein transfer;Luo;Proc. Natl. Acad. Sci. U. S. A.,2004

3. Icm/dot-dependent upregulation of phagocytosis by Legionella pneumophila;Hilbi;Mol. Microbiol.,2001

4. Legionnaires’ disease: isolation of a bacterium and demonstration of its role in other respiratory disease;McDade;N. Engl. J. Med.,1977

5. Multiple substrates of the Legionella pneumophila Dot/Icm system identified by interbacterial protein transfer;Luo;Proc. Natl. Acad. Sci. U. S. A.,2004

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