Enzyme I: the first protein and potential regulator of the bacterial phosphoenolpyruvate: glycose phosphotransferase system.

Enzyme I: the first protein and potential regulator of the bacterial phosphoenolpyruvate: glycose phosphotransferase system.

Item
http://www.wikidata.org/entity/Q41401280
EI of the Phosphotransferase System of Escherichia coli: Mathematical Modeling Approach to Analysis of Its Kinetic Properties.Multiple mechanisms controlling carbon metabolism in bacteria.Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein.Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering.Sugar Influx Sensing by the Phosphotransferase System of Escherichia coli.Conformational selection and substrate binding regulate the monomer/dimer equilibrium of the C-terminal domain of Escherichia coli enzyme I.In vivo and in vitro complementation of the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system by the cloned C-terminal domainOpposing effects of phosphoenolpyruvate and pyruvate with Mg(2+) on the conformational stability and dimerization of phosphotransferase enzyme I from Escherichia coli.How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteriaA NMR experiment for simultaneous correlations of valine and leucine/isoleucine methyls with carbonyl chemical shifts in proteins.Subcellular distribution of enzyme I of the Escherichia coli phosphoenolpyruvate:glycose phosphotransferase system depends on growth conditions.Hybrid Approaches to Structural Characterization of Conformational Ensembles of Complex Macromolecular Systems Combining NMR Residual Dipolar Couplings and Solution X-ray Scattering.The oligomerization state of bacterial enzyme I (EI) determines EI's allosteric stimulation or competitive inhibition by α-ketoglutarate.Structure of the full-length enzyme I of the phosphoenolpyruvate-dependent sugar phosphotransferase system.The monomer/dimer transition of enzyme I of the Escherichia coli phosphotransferase system.Properties of the C-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
P2860

Enzyme I: the first protein and potential regulator of the bacterial phosphoenolpyruvate: glycose phosphotransferase system.

Item
http://www.wikidata.org/entity/Q41401280
description
1996 nî lūn-bûn
@nan
1996年の論文
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1996年論文
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1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
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1996年论文
@zh-cn
name
Enzyme I: the first protein an ...... ose phosphotransferase system.
@en
type
label
Enzyme I: the first protein an ...... ose phosphotransferase system.
@en
prefLabel
Enzyme I: the first protein an ...... ose phosphotransferase system.
@en
P1433
P1476
P2093
P304
P31
P356
P433
P478
P577
P698
P356
P1433
P1476
Enzyme I: the first protein an ...... ose phosphotransferase system.
@en
P2093
P304
P31
P356
10.1016/0923-2508(96)84001-0
P433
P478
P577
P698