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ProteomicsM. bovis BCG PknG physiological substrates
Mycobacterial Ser/Thr kinases play a critical role in bacterial physiology and pathogenesis. Linking kinases to the substrates they phosphorylate in vivo, thereby elucidating their exact functions, is still a challenge. The aim of this work was to associate protein phosphorylation in mycobacteria wi...
ORGANISM(S): Mycobacterium bovis BCG str. Pasteur 1173P2 
2018-03-23 | PXD006473 | Pride
Kinases Pkng  phosphoproteomics  mycobacteria 
ProteomicsSystematic investigation into the dynamic alterations in the proteome and phosphoproteome of mycobacteria following overexpression of PknG
Systematic investigation into the dynamic alterations in the proteome and phosphoproteome of mycobacteria following overexpression of PknG
ORGANISM(S): Mycolicibacterium Smegmatis Mc2 51 
2025-05-13 | PXD063872 |
ProteomicsPhosphoproteomics reveals alternative roles of PknG in mycobacterial pathogenesis
Pathogenic mycobacteria, such as Mycobacterium tuberculosis, modulate the host immune system to evade clearance and promote long-term persistence, resulting in disease progression or latent infection. Understanding the mechanisms pathogenic mycobacteria use to evade the host immune system is critica...
ORGANISM(S): Mus musculus (Mouse) Mycobacterium tuberculosis 
2025-11-17 | PXD031055 | Pride
Phosphoproteomics Mycobacterium tuberculosis Substrate identification Serine/threonine protein kinases Post-translational modifications Mass spectrometry Phosphorylation 
ProteomicsProteome remodeling in the Mycobacterium tuberculosis PknG knockout: molecular hints for the role of this kinase in cell envelope biogenesis and hypoxia.
Tuberculosis, a pulmonary disease caused by the etiological agent Mycobacterium tuberculosis, is the leading cause of death by a single infectious agent among human beings. One of M. tuberculosis's pathogenic hallmarks is its ability to persist in a dormant state in the host for long periods, reinit...
ORGANISM(S): Mycobacterium tuberculosis H37Rv 
2021-06-02 | PXD023956 | Pride
Serine/threonine protein kinase Mas Mycobacterium tuberculosis Hypoxia Msl3 Parallel reaction monitoring Pkng Hrp-1 
ProteomicsProteome remodeling in the Mycobacterium tuberculosis PknG knockout: molecular hints for the role of this kinase in cell envelope biogenesis and hypoxia.
Tuberculosis, a pulmonary disease caused by the etiological agent Mycobacterium tuberculosis, is the leading cause of death by a single infectious agent among human beings. One of M. tuberculosis's pathogenic hallmarks is its ability to persist in a dormant state in the host for long periods, reinit...
ORGANISM(S): Mycobacterium tuberculosis H37Rv 
2021-06-02 | PXD023975 | Pride
Mas Shotgun proteomics Mycobacterium tuberculosis Hypoxia Serine/threonine protein kinase Msl3 Parallel reaction monitoring Pkng Hrp-1 
UnknownA Phosphoproteomic Analysis of Mycobacterial PknG-Mediated Host Immune Evasion.
Not available
S-EPMC12604046 | biostudies-literature
ProteomicsPathogenic phosphorylation of linear ubiquitin machinery causes inflammasome sensor degradation [Mouse]
Mass spectrometry analysis of phosphorylated sites in mouse HOIL-1L modified by PknG upon Mtb infection in iBMDMs.
ORGANISM(S): Mus musculus (Mouse) 
2025-08-08 | PXD064141 | Pride
Mycobacterium tuberculosis Hoil-1l Pkng 
UnknownDeletion of pknG Abates Reactivation of Latent Mycobacterium tuberculosis in Mice.
Not available
S-EPMC8097433 | biostudies-literature
ProteomicsPathogenic phosphorylation of linear ubiquitin machinery causes inflammasome sensor degradation [Human]
Mass spectrometry for analysis of phosphorylation sites in human HOIL-1L modified by Mycobacterium tuberculosis PknG.
ORGANISM(S): Homo sapiens (Human) 
2025-08-08 | PXD046319 | Pride
Pkng Mycobacterium tuberculosis Hoil-1l Nlrp3 inflammasome Lubac 
UnknownM. tuberculosis PknG manipulates host autophagy flux to promote pathogen intracellular survival.
Not available
S-EPMC9037497 | biostudies-literature
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