Identification of Arginine Phosphorylation in Mycolicibacterium smegmatis
ABSTRACT Tuberculosis is a leading cause of worldwide infectious mortality. The prevalence of multidrug-resistant Mycobacterium tuberculosis infections drives an urgent need to exploit new drug targets. One such target is the ATP-dependent protease ClpC1P1P2, which is strictly essential for viabilit...
Main Authors: | Emmanuel C. Ogbonna, Henry R. Anderson, Karl R. Schmitz |
---|---|
Format: | Article |
Language: | English |
Published: |
American Society for Microbiology
2022-10-01
|
Series: | Microbiology Spectrum |
Subjects: | |
Online Access: | https://journals.asm.org/doi/10.1128/spectrum.02042-22 |
Similar Items
-
Interactome Analysis Identifies MSMEI_3879 as a Substrate of Mycolicibacterium smegmatis ClpC1
by: Emmanuel C. Ogbonna, et al.
Published: (2023-08-01) -
A comprehensive review of arginine kinase proteins: What we need to know?
by: Brenda Martins Vasconcellos, et al.
Published: (2024-12-01) -
Protein-ligand interactions of arylamine N-acetyltransferase from Mycobacterium smegmatis
by: Brooke, E
Published: (2003) -
Comparative Ser/Thr/Tyr phosphoproteomics between two Mycobacterial species: The fast growing Mycobacterium smegmatis and the slow growing Mycobacterium bovis BCG.
by: Kehilwe Confidence Nakedi, et al.
Published: (2015-04-01) -
Rv3091, An Extracellular Patatin-Like Phospholipase in Mycobacterium tuberculosis, Prolongs Intracellular Survival of Recombinant Mycolicibacterium smegmatis by Mediating Phagosomal Escape
by: Ziyin Cui, et al.
Published: (2020-09-01)