Structural analysis of the N ‐acetyltransferase Eis1 from Mycobacterium abscessus reveals the molecular determinants of its incapacity to modify aminoglycosides-Reference-Cited by-同舟云学术

Structural analysis of the N ‐acetyltransferase Eis1 from Mycobacterium abscessus reveals the molecular determinants of its incapacity to modify aminoglycosides

Published:2020-09-12 Issue:1 Volume:89 Page:94-106
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Ung Kien Lam¹^ORCID,Kremer Laurent¹²^ORCID,Blaise Mickaël¹^ORCID

Affiliation:

1. Institut de Recherche en Infectiologie de Montpellier (IRIM) Université de Montpellier, CNRS UMR Montpellier France

2. INSERM, IRIM Montpellier France

Funder

Agence Nationale de la Recherche

Fondation pour la Recherche Médicale

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.25997

Reference40 articles.

1. Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation

2. Identification of a Mycobacterium tuberculosis Gene That Enhances Mycobacterial Survival in Macrophages

3. Mycobacterium tuberculosis EIS gene inhibits macrophage autophagy through up-regulation of IL-10 by increasing the acetylation of histone H3

4. Expression, production and release of the Eis protein by Mycobacterium tuberculosis during infection of macrophages and its effect on cytokine secretion

5. Mycobacterium tuberculosis Eis Regulates Autophagy, Inflammation, and Cell Death through Redox-dependent Signaling

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3. Biochemical, structural, and functional studies reveal that MAB_4324c from Mycobacterium abscessus is an active tandem repeat N ‐acetyltransferase;FEBS Letters;2022-06