Structure/function studies of Ser/Thr and Tyr protein phosphorylation in Mycobacterium tuberculosis. - Wikidata - awgldk - TriplyDB

Structure/function studies of Ser/Thr and Tyr protein phosphorylation in Mycobacterium tuberculosis.

Structure/function studies of Ser/Thr and Tyr protein phosphorylation in Mycobacterium tuberculosis.

http://www.wikidata.org/entity/Q36369654

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Structure of theStreptococcus agalactiaefamily II inorganic pyrophosphatase at 2.80 Å resolution Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase Allosteric Activation Mechanism of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknB A Phosphorylated Pseudokinase Complex Controls Cell Wall Synthesis in Mycobacteria Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical characterization and identification of novel substrate pyruvate kinase A Allosteric activation by dimerization of the PknD receptor Ser/Thr protein kinase from Mycobacterium tuberculosis The Mycobacterium tuberculosis protein kinase K modulates activation of transcription from the promoter of mycobacterial monooxygenase operon through phosphorylation of the transcriptional regulator VirS Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog Discovery of Mycobacterium tuberculosis protein tyrosine phosphatase B (PtpB) inhibitors from natural products Mycobacterium tuberculosis Ser/Thr protein kinase B mediates an oxygen-dependent replication switch High throughput screening of a library based on kinase inhibitor scaffolds against Mycobacterium tuberculosis H37Rv.Ugi reaction-assisted rapid assembly of affinity-based probes against potential protein tyrosine phosphatases.Bacterial growth and cell division: a mycobacterial perspective.Mycobacterium tuberculosis protein kinase K confers survival advantage during early infection in mice and regulates growth in culture and during persistent infection: implications for immune modulation.Identification, sequence analysis, and characterization of serine/threonine protein kinase 17A from Clonorchis sinensis.Forkhead-associated (FHA) domain containing ABC transporter Rv1747 is positively regulated by Ser/Thr phosphorylation in Mycobacterium tuberculosis.Aspects of eukaryotic-like signaling in Gram-positive cocci: a focus on virulence.Characterization of a serine/threonine kinase involved in virulence of Staphylococcus aureus.Osmosensory signaling in Mycobacterium tuberculosis mediated by a eukaryotic-like Ser/Thr protein kinase.Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host.An attenuated mutant of the Rv1747 ATP-binding cassette transporter of Mycobacterium tuberculosis and a mutant of its cognate kinase, PknF, show increased expression of the efflux pump-related iniBAC operon.Bacterial serine/threonine protein kinases in host-pathogen interactions.Virulence factors of the Mycobacterium tuberculosis complex Bacterial cell division regulation by Ser/Thr kinases: a structural perspective Cell division in Corynebacterineae Agents of change - concepts in Mycobacterium tuberculosis Ser/Thr/Tyr phosphosignalling.Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.Antimycobacterial and photosynthetic electron transport inhibiting activity of ring-substituted 4-arylamino-7-chloroquinolinium chlorides.A Nonsynonymous SNP Catalog of Mycobacterium tuberculosis Virulence Genes and Its Use for Detecting New Potentially Virulent Sublineages Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis Proteome-wide identification of mycobacterial pupylation targets Interdomain interaction reconstitutes the functionality of PknA, a eukaryotic type Ser/Thr kinase from Mycobacterium tuberculosis.The domain architecture of the PtkA, the first tyrosine kinase from Mycobacterium tuberculosis differs from the conventional kinase architecture.Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments

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P2860

Structure/function studies of Ser/Thr and Tyr protein phosphorylation in Mycobacterium tuberculosis.

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Structure/function studies of ...... in Mycobacterium tuberculosis.

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Andrew E Greenstein

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Carl A Miecskowski

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Christoph Grundner

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Kristi E Pullen

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Pei-Yi Sung

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Tom Alber

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P2860

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

The protein kinase complement of the human genome

Crystal structures of c-Src reveal features of its autoinhibitory mechanism

Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase

Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases

Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis

Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I

The conformational plasticity of protein kinases

Genes required for mycobacterial growth defined by high density mutagenesis

Protein tyrosine phosphatases in the human genome

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3-4

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Akafuba bulwadde

Mycobacterium tuberculosis

phosphorylation

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