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 domain
about
Calorimetric and spectroscopic investigation of the interaction between the C-terminal domain of Enzyme I and its ligands.How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteriaDimerization facilitates the conformational transitions for bacterial phosphotransferase enzyme I autophosphorylation in an allosteric mannerCatabolite control of Escherichia coli regulatory protein BglG activity by antagonistically acting phosphorylations.Properties of the C-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
P2860
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 domain
description
1998 nî lūn-bûn
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1998年の論文
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1998年学术文章
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1998年学术文章
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1998年学术文章
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1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
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1998年學術文章
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name
In vivo and in vitro complemen ...... y the cloned C-terminal domain
@ast
In vivo and in vitro complemen ...... y the cloned C-terminal domain
@en
type
label
In vivo and in vitro complemen ...... y the cloned C-terminal domain
@ast
In vivo and in vitro complemen ...... y the cloned C-terminal domain
@en
prefLabel
In vivo and in vitro complemen ...... y the cloned C-terminal domain
@ast
In vivo and in vitro complemen ...... y the cloned C-terminal domain
@en
P2093
P2860
P356
P1476
In vivo and in vitro complemen ...... y the cloned C-terminal domain
@en
P2093
A Fomenkov
A Valiakhmetov
P2860
P304
P356
10.1073/PNAS.95.15.8491
P407
P577
1998-07-01T00:00:00Z