The significance of GlgE as a new target for tuberculosis.
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Structure of Streptomyces Maltosyltransferase GlgE, a Homologue of a Genetically Validated Anti-tuberculosis TargetThe structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding modeStructure of mycobacterial maltokinase, the missing link in the essential GlgE-pathwayTrehalose-6-Phosphate-Mediated Toxicity Determines Essentiality of OtsB2 in Mycobacterium tuberculosis In Vitro and in MiceExploring anti-TB leads from natural products library originated from marine microbes and medicinal plants.Discovery of Mycobacterium tuberculosis α-1,4-glucan branching enzyme (GlgB) inhibitors by structure- and ligand-based virtual screening.The tuberculosis drug discovery and development pipeline and emerging drug targets.Metabolic Network for the Biosynthesis of Intra- and Extracellular α-Glucans Required for Virulence of Mycobacterium tuberculosisTargeting the trehalose utilization pathways of Mycobacterium tuberculosisMycobacterium tuberculosis maltosyltransferase GlgE, a genetically validated antituberculosis target, is negatively regulated by Ser/Thr phosphorylationDevelopmental delay in a Streptomyces venezuelae glgE null mutant is associated with the accumulation of α-maltose 1-phosphate.Tuberculosis drug discovery and emerging targets.Ligand-bound Structures and Site-directed Mutagenesis Identify the Acceptor and Secondary Binding Sites of Streptomyces coelicolor Maltosyltransferase GlgE.The α-glucan phosphorylase MalP of Corynebacterium glutamicum is subject to transcriptional regulation and competitive inhibition by ADP-glucose.Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis.Flux through trehalose synthase flows from trehalose to the alpha anomer of maltose in mycobacteria.Use of genetic and chemical synthetic lethality as probes of complexity in bacterial cell systems.Zwitterionic pyrrolidene-phosphonates: inhibitors of the glycoside hydrolase-like phosphorylase Streptomyces coelicolor GlgEI-V279S.
P2860
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P2860
The significance of GlgE as a new target for tuberculosis.
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2010 nî lūn-bûn
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2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2010年の論文
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2010年論文
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2010年論文
@zh-hant
2010年論文
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2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
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name
The significance of GlgE as a new target for tuberculosis.
@ast
The significance of GlgE as a new target for tuberculosis.
@en
type
label
The significance of GlgE as a new target for tuberculosis.
@ast
The significance of GlgE as a new target for tuberculosis.
@en
prefLabel
The significance of GlgE as a new target for tuberculosis.
@ast
The significance of GlgE as a new target for tuberculosis.
@en
P1476
The significance of GlgE as a new target for tuberculosis
@en
P2093
William R Jacobs
P304
P356
10.1358/DNP.2010.23.10.1534855
P577
2010-12-01T00:00:00Z