Identification of a subversive substrate of Trichomonas vaginalis purine nucleoside phosphorylase and the crystal structure of the enzyme-substrate complex.
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Inhibition and Structure of Trichomonas vaginalis Purine Nucleoside Phosphorylase with Picomolar Transition State Analogues †Insights into Phosphate Cooperativity and Influence of Substrate Modifications on Binding and Catalysis of Hexameric Purine Nucleoside PhosphorylasesStructural basis of the substrate specificity ofBacillus cereusadenosine phosphorylaseNatural Products as New Treatment Options for Trichomoniasis: A Molecular Docking Investigation.Humanized ADEPT comprised of an engineered human purine nucleoside phosphorylase and a tumor targeting peptide for treatment of cancer
P2860
Identification of a subversive substrate of Trichomonas vaginalis purine nucleoside phosphorylase and the crystal structure of the enzyme-substrate complex.
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2005 nî lūn-bûn
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name
Identification of a subversive ...... the enzyme-substrate complex.
@en
Identification of a subversive ...... the enzyme-substrate complex.
@nl
type
label
Identification of a subversive ...... the enzyme-substrate complex.
@en
Identification of a subversive ...... the enzyme-substrate complex.
@nl
prefLabel
Identification of a subversive ...... the enzyme-substrate complex.
@en
Identification of a subversive ...... the enzyme-substrate complex.
@nl
P2093
P2860
P356
P1476
Identification of a subversive ...... the enzyme-substrate complex.
@en
P2093
Ching C Wang
Shaw-Wen Wu
Wen-Hu Wang
P2860
P304
22318-22325
P356
10.1074/JBC.M501843200
P407
P577
2005-04-07T00:00:00Z