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Molecular Basis of the Activity and the Regulation of the Eukaryotic-like S/T Protein Kinase PknG from Mycobacterium tuberculosisBidirectional Allosteric Communication between the ATP-Binding Site and the Regulatory PIF Pocket in PDK1 Protein KinasePknG senses amino acid availability to control metabolism and virulence of Mycobacterium tuberculosis.Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.The crystal structure of PknI from Mycobacterium tuberculosis shows an inactive, pseudokinase-like conformation.Catalytic role of the metal ion in the metallo-beta-lactamase GOB.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.In vivo impact of Met221 substitution in GOB metallo-β-lactamase.The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.Novel high-performance purification protocol of recombinant CNBP suitable for biochemical and biophysical characterization.SIMBAD: a sequence-independent molecular-replacement pipelineNew substrates and interactors of the mycobacterial Serine/Threonine protein kinase PknG identified by a tailored interactomic approachStructure-based Virtual Screening to Get New Scaffold Inhibitors of the Ser/Thr Protein Kinase PknB from Mycobacterium tuberculosisDouble autoinhibition mechanism of signal transduction ATPases with numerous domains (STAND) with a tetratricopeptide repeat sensorStructural insights into the functional versatility of an FHA domain protein in mycobacterial signalingArabidopsis thaliana Hcc1 is a Sco-like metallochaperone for CuA assembly in Cytochrome c OxidaseUnexpected electron spin density on the axial methionine ligand in CuA suggests its involvement in electron pathways
P50
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P50
description
hulumtuese
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հետազոտող
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María-Natalia Lisa
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María-Natalia Lisa
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María-Natalia Lisa
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María-Natalia Lisa
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María-Natalia Lisa
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María-Natalia Lisa
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María-Natalia Lisa
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María-Natalia Lisa
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María-Natalia Lisa
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P106
P21
P31
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mara-natalia-lisa
P496
0000-0001-9630-8090