about
Kinetic and chemical mechanism of alpha-isopropylmalate synthase from Mycobacterium tuberculosisCrystal structure of human purine nucleoside phosphorylase at 2.3A resolutionInhibitors selective for mycobacterial versus human proteasomesHIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolaseDiscovery of a glycerol 3-phosphate phosphatase reveals glycerophospholipid polar head recycling in Mycobacterium tuberculosisKinetic mechanism and inhibition of Mycobacterium tuberculosis D-alanine:D-alanine ligase by the antibiotic D-cycloserineKinetic analysis of the effects of monovalent cations and divalent metals on the activity of Mycobacterium tuberculosis alpha-isopropylmalate synthaseMycobacterium tuberculosis expresses methionine sulphoxide reductases A and B that protect from killing by nitrite and hypochloriteActivity-based metabolomic profiling of enzymatic function: identification of Rv1248c as a mycobacterial 2-hydroxy-3-oxoadipate synthaseMycobacterium tuberculosis beta-ketoacyl-acyl carrier protein (ACP) reductase: kinetic and chemical mechanismsMycobacterium tuberculosis exploits asparagine to assimilate nitrogen and resist acid stress during infectionA philosophy of anti-infectives as a guide in the search for new drugs for tuberculosis.A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium.Biosynthesis and translocation of unsulfated acyltrehaloses in Mycobacterium tuberculosis.Metabolomic strategies for the identification of new enzyme functions and metabolic pathwaysOn the chemical mechanism of succinic semialdehyde dehydrogenase (GabD1) from Mycobacterium tuberculosisThiophenecarboxamide Derivatives Activated by EthA Kill Mycobacterium tuberculosis by Inhibiting the CTP Synthetase PyrGTwo enzymes with redundant fructose bisphosphatase activity sustain gluconeogenesis and virulence in Mycobacterium tuberculosis.Mechanism of feedback allosteric inhibition of ATP phosphoribosyltransferase.Fragment-Based Approaches to the Development of Mycobacterium tuberculosis CYP121 Inhibitors.Cell-Envelope Remodeling as a Determinant of Phenotypic Antibacterial Tolerance in Mycobacterium tuberculosis.Mycobacterium tuberculosis nitrogen assimilation and host colonization require aspartate.Reinterpreting the mechanism of inhibition of Mycobacterium tuberculosis D-alanine:D-alanine ligase by D-cycloserine.Functional assignment of Mycobacterium tuberculosis proteome revealed by genome-scale fold-recognition.Uncoupling conformational states from activity in an allosteric enzyme.Glutamate Racemase Is the Primary Target of β-Chloro-d-Alanine in Mycobacterium tuberculosis.Nitazoxanide Disrupts Membrane Potential and Intrabacterial pH Homeostasis of Mycobacterium tuberculosis.Metabolomics of Mycobacterium tuberculosis.A protecting group-free synthesis of deazathiamine: a step toward inhibitor design.Activity-based substrate profiling for Gcn5-related N-acetyltransferases: the use of chloroacetyl-coenzyme A to identify protein substrates.Hybrid Mass Spectrometry Approaches to Determine How L-Histidine Feedback Regulates the Enzyzme MtATP-Phosphoribosyltransferase.Central carbon metabolism in Mycobacterium tuberculosis: an unexpected frontier.Kinetic evidence for interdomain communication in the allosteric regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis.Correction to Reinterpreting the Mechanism of Inhibition of Mycobacterium tuberculosis d-Alanine:d-Alanine Ligase by d-Cycloserine.Nitazoxanide kills replicating and nonreplicating Mycobacterium tuberculosis and evades resistance.Novel Aryl Substituted Pyrazoles as Small Molecule Inhibitors of Cytochrome P450 CYP121A1: Synthesis and Antimycobacterial Evaluation.Inhibition of D-Ala:D-Ala ligase through a phosphorylated form of the antibiotic D-cycloserine.Protein CoAlation: a redox-linked post-translational modification.The Mechanism of Acetyl Transfer Catalyzed by Mycobacterium tuberculosis GlmU.Flexible nitrogen utilisation by the metabolic generalist pathogen
P50
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P50
description
onderzoeker
@nl
researcher, ORCID id # 0000-0003-2875-4552
@en
name
Luiz Pedro S de Carvalho
@ast
Luiz Pedro S de Carvalho
@en
Luiz Pedro S de Carvalho
@nl
type
label
Luiz Pedro S de Carvalho
@ast
Luiz Pedro S de Carvalho
@en
Luiz Pedro S de Carvalho
@nl
prefLabel
Luiz Pedro S de Carvalho
@ast
Luiz Pedro S de Carvalho
@en
Luiz Pedro S de Carvalho
@nl
P106
P21
P31
P496
0000-0003-2875-4552