Assay development for identifying inhibitors of the mycobacterial FadD32 activity. - Wikidata - awgldk - TriplyDB

Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

http://www.wikidata.org/entity/Q34567891

about

Diarylcoumarins inhibit mycolic acid biosynthesis and kill Mycobacterium tuberculosis by targeting FadD32 The mycobacterial cell envelope-lipids New approaches to target the mycolic acid biosynthesis pathway for the development of tuberculosis therapeutics.Crystal structure of FadD32, an enzyme essential for mycolic acid biosynthesis in mycobacteria.Progress in targeting cell envelope biogenesis in Mycobacterium tuberculosis.The future for early-stage tuberculosis drug discovery Insight into Structure-Function Relationships and Inhibition of the Fatty Acyl-AMP Ligase (FadD32) Orthologs from Mycobacteria.Structure of the Essential Mtb FadD32 Enzyme: A Promising Drug Target for Treating Tuberculosis.Ser/Thr Phosphorylation Regulates the Fatty Acyl-AMP Ligase Activity of FadD32, an Essential Enzyme in Mycolic Acid Biosynthesis

P2860

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P2860

Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

http://www.wikidata.org/entity/Q34567891

description

2013 nî lūn-bûn

@nan

2013 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հունվարին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

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Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

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Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

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type

label

Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

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Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

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Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

@nl

prefLabel

Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

@ast

Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

@en

Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

@nl

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P1433

Journal of Biomolecular Screening

P1476

Assay development for identifying inhibitors of the mycobacterial FadD32 activity.

@en

P2093

Hedia Marrakchi

http://www.w3.org/2001/XMLSchema#string

Kaveri Das

http://www.w3.org/2001/XMLSchema#string

Lionel Mourey

http://www.w3.org/2001/XMLSchema#string

Mathieu Léger

http://www.w3.org/2001/XMLSchema#string

Nathalie Eynard

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Radha N

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Rajendra S Rane

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Ségolène Galandrin

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Tanjore S Balganesh

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Valérie Guillet

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P2860

A Common Mechanism Underlying Promiscuous Inhibitors from Virtual and High-Throughput Screening

Protein production by auto-induction in high density shaking cultures

A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays

Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis

Mycobacterial phenolic glycolipid virulence factor biosynthesis: mechanism and small-molecule inhibition of polyketide chain initiation

Acyl-CoA carboxylases (accD2 and accD3), together with a unique polyketide synthase (Cg-pks), are key to mycolic acid biosynthesis in Corynebacterianeae such as Corynebacterium glutamicum and Mycobacterium tuberculosis

The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase co

Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria

New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis

High-density miniaturized thermal shift assays as a general strategy for drug discovery

P304

576-587

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scholarly article

P356

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5

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23364516

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