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| - artículu científicu espublizáu en 2003 (ast)
- vědecký článek publikovaný v roce 2003 (cs)
- 2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած (hyw)
- наукова стаття, опублікована в грудні 2003 (uk)
- 2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված (hy)
- article scientifique publié en 2003 (fr)
- scientific journal article (en)
- مقالة علمية (نشرت في 30-12-2003) (ar)
- im Dezember 2003 veröffentlicher wissenschaftlicher Artikel (de)
- wetenschappelijk artikel (gepubliceerd op 2003/12/30) (nl)
- vedecký článok (publikovaný 2003/12/30) (sk)
- 2003 ഡിസംബര് 30 നു പ്രസിദ്ധീകരിച്ച ശാസ്ത്ര ലേഖനം (ml)
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| author name string
| - Alain J. Cozzone
- Gurdyal S. Besra
- Christine Girard-Blanc
- Jean-François Prost
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| - An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (en)
- An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (nl)
- An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (ast)
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| - An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (en)
- An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (nl)
- An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (ast)
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| name
| - An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (en)
- An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (nl)
- An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (ast)
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| title
| - An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis (en)
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| is cites work
of | - Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR.
- Regulation of cytotoxin expression by converging eukaryotic-type and two-component signalling mechanisms in Streptococcus agalactiae
- Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G
- Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host
- Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes
- Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains
- Structure/function studies of Ser/Thr and Tyr protein phosphorylation in Mycobacterium tuberculosis
- Mycobacterium tuberculosis maltosyltransferase GlgE, a genetically validated antituberculosis target, is negatively regulated by Ser/Thr phosphorylation
- Signaling mechanisms of the Mycobacterium tuberculosis receptor Ser/Thr protein kinases
- Structural and Functional Studies on the N-terminal Domain of the Shigella Type III Secretion Protein MxiG
- Molecular structure of EmbR, a response element of Ser/Thr kinase signaling in Mycobacterium tuberculosis.
- Chlamydophila pneumoniae PknD exhibits dual amino acid specificity and phosphorylates Cpn0712, a putative type III secretion YscD homolog
- Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis
- Staphylococcus aureus operates protein-tyrosine phosphorylation through a specific mechanism.
- Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens
- Eukaryote-like serine/threonine kinases and phosphatases in bacteria
- Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens
- Mycobacterium tuberculosis Serine/Threonine Protein Kinases
- Interdomain interaction reconstitutes the functionality of PknA, a eukaryotic type Ser/Thr kinase from Mycobacterium tuberculosis.
- Regulation of prokaryotic gene expression by eukaryotic-like enzymes
- Allosteric activation by dimerization of the PknD receptor Ser/Thr protein kinase from Mycobacterium tuberculosis
- Bacterial growth and cell division: a mycobacterial perspective
- Serine threonine protein kinases of mycobacterial genus: phylogeny to function.
- The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue
- Transcriptional control of the mycobacterial embCAB operon by PknH through a regulatory protein, EmbR, in vivo
- Deletion of the Mycobacterium tuberculosis pknH gene confers a higher bacillary load during the chronic phase of infection in BALB/c mice
- The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division
- The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation
- Role of Mycobacterium tuberculosis Ser/Thr kinase PknF: implications in glucose transport and cell division
- From the characterization of the four serine/threonine protein kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the role of PknA and PknB in cell division
- A novel mode of regulation of the Staphylococcus aureus catabolite control protein A (CcpA) mediated by Stk1 protein phosphorylation
- An ABC transporter containing a forkhead-associated domain interacts with a serine-threonine protein kinase and is required for growth of Mycobacterium tuberculosis in mice
- The Mycobacterium tuberculosis Ser/Thr Kinase Substrate Rv2175c Is a DNA-binding Protein Regulated by Phosphorylation
- The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine/threonine protein kinase PknA in Corynebacterium glutamicum
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