Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases.
about
Lys48 ubiquitination during the intraerythrocytic cycle of the rodent malaria parasite, Plasmodium chabaudiA nucleotide-controlled conformational switch modulates the activity of eukaryotic IMP dehydrogenases.Development of Frequency Based Taste Receptors Using Bioinspired Glucose Nanobiosensor.Reconstituted IMPDH polymers accommodate both catalytically active and inactive conformations.Expanding benzoxazole based inosine 5'-monophosphate dehydrogenase (IMPDH) inhibitor structure-activity as potential anti-tuberculosis agents.IMP/GTP balance modulates cytoophidium assembly and IMPDH activity.Interfilament interaction between IMPDH and CTPS cytoophidia
P2860
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P2860
Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases.
description
2015 nî lūn-bûn
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2015年の論文
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年學術文章
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2015年學術文章
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name
Guanine nucleotide binding to ...... eukaryotic IMP dehydrogenases.
@ast
Guanine nucleotide binding to ...... eukaryotic IMP dehydrogenases.
@en
type
label
Guanine nucleotide binding to ...... eukaryotic IMP dehydrogenases.
@ast
Guanine nucleotide binding to ...... eukaryotic IMP dehydrogenases.
@en
prefLabel
Guanine nucleotide binding to ...... eukaryotic IMP dehydrogenases.
@ast
Guanine nucleotide binding to ...... eukaryotic IMP dehydrogenases.
@en
P2860
P50
P356
P1476
Guanine nucleotide binding to ...... eukaryotic IMP dehydrogenases.
@en
P2093
Mónica Chagoyen
Rubén M Buey
P2860
P2888
P356
10.1038/NCOMMS9923
P407
P577
2015-11-12T00:00:00Z
P5875
P6179
1003802471