Bisubstrate Adenylation Inhibitors of Biotin Protein Ligase from Mycobacterium tuberculosis - Wikidata - awgldk - TriplyDB

Bisubstrate Adenylation Inhibitors of Biotin Protein Ligase from Mycobacterium tuberculosis

Bisubstrate Adenylation Inhibitors of Biotin Protein Ligase from Mycobacterium tuberculosis

http://www.wikidata.org/entity/Q27675807

about

Biotin Protein Ligase Is a Target for New Antibacterials Selective inhibition of Biotin Protein Ligase from Staphylococcus aureus Active site conformational changes upon reaction intermediate biotinyl-5'-AMP binding in biotin protein ligase fromMycobacterium tuberculosis Identification of Rv3852 as an Agrimophol-Binding Protein in Mycobacterium tuberculosis Bisubstrate Inhibitors of Biotin Protein Ligase in Mycobacterium tuberculosis Resistant to Cyclonucleoside Formation.Biotin analogues with antibacterial activity are potent inhibitors of biotin protein ligase.Exploring anti-TB leads from natural products library originated from marine microbes and medicinal plants.Regulated Expression Systems for Mycobacteria and Their Applications Improved Synthesis of Biotinol-5'-AMP: Implications for Antibacterial Discovery.Mycobacterium tuberculosis metabolism Genetic Approaches to Facilitate Antibacterial Drug Development.Reaction intermediate analogues as bisubstrate inhibitors of pantothenate synthetase.Targeting Mycobacterium tuberculosis Biotin Protein Ligase (MtBPL) with Nucleoside-Based Bisubstrate Adenylation Inhibitors.Adenylating enzymes in Mycobacterium tuberculosis as drug targets.Progress in targeting cell envelope biogenesis in Mycobacterium tuberculosis.Speculative strategies for new antibacterials: all roads should not lead to Rome.Nucleoside analogs and tuberculosis: new weapons against an old enemy.Design, Synthesis, and Characterization of Sulfamide and Sulfamate Nucleotidomimetic Inhibitors of hHint1.Design, synthesis, and biological evaluation of α-hydroxyacyl-AMS inhibitors of amino acid adenylation enzymes.β-Keto and β-hydroxyphosphonate analogs of biotin-5'-AMP are inhibitors of holocarboxylase synthetase.Dual roles of F123 in protein homodimerization and inhibitor binding to biotin protein ligase from Staphylococcus aureus.Mechanisms of biotin-regulated gene expression in microbes.New Series of BPL Inhibitors To Probe the Ribose-Binding Pocket of Staphylococcus aureus Biotin Protein Ligase.Targeting protein biotinylation enhances tuberculosis chemotherapy.

P2860

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P2860

Bisubstrate Adenylation Inhibitors of Biotin Protein Ligase from Mycobacterium tuberculosis

http://www.wikidata.org/entity/Q27675807

description

2011 nî lūn-bûn

@nan

2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Bisubstrate Adenylation Inhibi ...... rom Mycobacterium tuberculosis

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Bisubstrate Adenylation Inhibi ...... rom Mycobacterium tuberculosis

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Bisubstrate Adenylation Inhibi ...... rom Mycobacterium tuberculosis

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Bisubstrate Adenylation Inhibi ...... rom Mycobacterium tuberculosis

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Bisubstrate Adenylation Inhibi ...... rom Mycobacterium tuberculosis

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Bisubstrate Adenylation Inhibi ...... rom Mycobacterium tuberculosis

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Bisubstrate Adenylation Inhibi ...... rom Mycobacterium tuberculosis

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P356

J.CHEMBIOL.2011.08.013

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Chemistry and Biology

P1476

Bisubstrate Adenylation Inhibi ...... rom Mycobacterium tuberculosis

@en

P2093

Benjamin P Duckworth

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Courtney C Aldrich

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Dirk Schnappinger

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

Helena I Boshoff

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

Paul A Sibbald

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

Todd W Geders

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

P2860

On the attribution and additivity of binding energies

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Controlling gene expression in mycobacteria with anhydrotetracycline and Tet repressor

Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity

Structural Ordering of Disordered Ligand-Binding Loops of Biotin Protein Ligase into Active Conformations as a Consequence of Dehydration

Coot: model-building tools for molecular graphics

PRODRG: a tool for high-throughput crystallography of protein-ligand complexes

The finer things in X-ray diffraction data collection

Phasercrystallographic software

Refinement of macromolecular structures by the maximum-likelihood method

P304

1432-41

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scholarly article

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4416118

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10.1016/J.CHEMBIOL.2011.08.013

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P433

11

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18

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P50

Clifton E Barry

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2011-11-23T00:00:00Z

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51835666

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22118677

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P921

Mycobacterium tuberculosis

clinical chemistry

P932

3225891

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