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A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

http://www.wikidata.org/entity/Q27332293

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Novel protein acetyltransferase, Rv2170, modulates carbon and energy metabolism in Mycobacterium tuberculosis Glyoxylate detoxification is an essential function of malate synthase required for carbon assimilation in Mycobacterium tuberculosis.Amino Acids As Mediators of Metabolic Cross Talk between Host and Pathogen.Understanding the impact of the cofactor swapping of isocitrate dehydrogenase over the growth phenotype of Escherichia coli on acetate by using constraint-based modeling.

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A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

http://www.wikidata.org/entity/Q27332293

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2016 nî lūn-bûn

@nan

2016 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

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name

A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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type

label

A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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prefLabel

A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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Nature Communications

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A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria

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Florence Pojer

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Giulia Fonti

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John D McKinney

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Kevin Pethe

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Matteo Dal Peraro

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Paul Murima

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Sylvie Alonso

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Tarun Chopra

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Uwe Sauer

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P2860

Characterization of phosphofructokinase activity in Mycobacterium tuberculosis reveals that a functional glycolytic carbon flow is necessary to limit the accumulation of toxic metabolic intermediates under hypoxia

The complete genome sequence of Mycobacterium bovis

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence

Structural, kinetic and chemical mechanism of isocitrate dehydrogenase-1 from Mycobacterium tuberculosis

Comparison of Mycobacterium tuberculosis isocitrate dehydrogenases (ICD-1 and ICD-2) reveals differences in coenzyme affinity, oligomeric state, pH tolerance and phylogenetic affiliation

Structure of the monomeric isocitrate dehydrogenase: evidence of a protein monomerization by a domain duplication

Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase

Structural Basis of the Substrate Specificity of Bifunctional Isocitrate Dehydrogenase Kinase/Phosphatase

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12527

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scholarly article

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3920512

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10.1038/NCOMMS12527

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7

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Michael Zimmermann

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2016-08-24T00:00:00Z

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1027355784

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27555519

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4999502

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