Structural basis for enzyme I inhibition by α-ketoglutarate. - Wikidata - wikimedia - TriplyDB

Structural basis for enzyme I inhibition by α-ketoglutarate.

Structural basis for enzyme I inhibition by α-ketoglutarate.

http://www.wikidata.org/entity/Q37076214

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Measurement of the temperature of the resting rotor in analytical ultracentrifugation.Engineering glucose metabolism of Escherichia coli under nitrogen starvation.Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I.Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering.A pan-specific antibody for direct detection of protein histidine phosphorylation.The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite.Hybrid Approaches to Structural Characterization of Conformational Ensembles of Complex Macromolecular Systems Combining NMR Residual Dipolar Couplings and Solution X-ray Scattering.(1)H, (15)N, (13)C backbone resonance assignment of the C-terminal domain of enzyme I from Thermoanaerobacter tengcongensis.The oligomerization state of bacterial enzyme I (EI) determines EI's allosteric stimulation or competitive inhibition by α-ketoglutarate.

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Structural basis for enzyme I inhibition by α-ketoglutarate.

http://www.wikidata.org/entity/Q37076214

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 29 March 2013

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Structural basis for enzyme I inhibition by α-ketoglutarate.

@en

Structural basis for enzyme I inhibition by α-ketoglutarate.

@nl

type

label

Structural basis for enzyme I inhibition by α-ketoglutarate.

@en

Structural basis for enzyme I inhibition by α-ketoglutarate.

@nl

prefLabel

Structural basis for enzyme I inhibition by α-ketoglutarate.

@en

Structural basis for enzyme I inhibition by α-ketoglutarate.

@nl

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ACS Chemical Biology

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Structural basis for enzyme I inhibition by α-ketoglutarate.

@en

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G Marius Clore

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Rodolfo Ghirlando

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Vincenzo Venditti

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Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray Scattering

Phosphoenolpyruvate: sugar phosphotransferase system from the hyperthermophilic Thermoanaerobacter tengcongensis

Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

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Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

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1232-1240

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scholarly article

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10.1021/CB400027Q

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6

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2013-03-29T00:00:00Z

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