Mutations in tar suppress defects in maltose chemotaxis caused by specific malE mutations.
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Differences in signalling by directly and indirectly binding ligands in bacterial chemotaxisMolecular recognition analyzed by docking simulations: the aspartate receptor and isocitrate dehydrogenase from Escherichia coliAspartate and maltose-binding protein interact with adjacent sites in the Tar chemotactic signal transducer of Escherichia coli.Maltose chemoreceptor of Escherichia coli: interaction of maltose-binding protein and the tar signal transducer.Sensor complexes regulating two-component signal transduction.A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein.Residues in the alpha helix 7 of the bacterial maltose binding protein which are important in interactions with the Mal FGK2 complexMaltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis.A putative porin gene of Burkholderia sp. NK8 involved in chemotaxis toward β-ketoadipate.
P2860
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P2860
Mutations in tar suppress defects in maltose chemotaxis caused by specific malE mutations.
description
1986 nî lūn-bûn
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1986年の論文
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1986年学术文章
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1986年学术文章
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1986年学术文章
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1986年学术文章
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1986年学术文章
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1986年學術文章
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1986年學術文章
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1986年學術文章
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name
Mutations in tar suppress defe ...... ed by specific malE mutations.
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type
label
Mutations in tar suppress defe ...... ed by specific malE mutations.
@en
prefLabel
Mutations in tar suppress defe ...... ed by specific malE mutations.
@en
P2860
P1476
Mutations in tar suppress defe ...... ed by specific malE mutations.
@en
P2093
P2860
P356
10.1128/JB.165.1.34-40.1986
P407
P577
1986-01-01T00:00:00Z