Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir

Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir

Item
http://www.wikidata.org/entity/Q27766894
Nucleoside binding site of herpes simplex type 1 thymidine kinase analyzed by X-ray crystallographyThe effect of substrate binding on the conformation and structural stability of Herpes simplex virus type 1 thymidine kinaseEnzymatic and structural analysis of inhibitors designed against Mycobacterium tuberculosis thymidylate kinase. New insights into the phosphoryl transfer mechanismCrystal structure of varicella zoster virus thymidine kinaseStructure of a type II thymidine kinase with bound dTTPBiochemical and structural characterization of (South)-methanocarbathymidine that specifically inhibits growth of herpes simplex virus type 1 thymidine kinase-transduced osteosarcoma cellsInhibition of herpes simplex virus thymidine kinases by 2-phenylamino-6-oxopurines and related compounds: structure-activity relationships and antiherpetic activity in vivoThermodynamics of protein-ligand interactions: history, presence, and future aspects.The role of herpes simplex virus-1 thymidine kinase alanine 168 in substrate specificity.Common and new acyclovir resistant herpes simplex virus-1 mutants causing bilateral recurrent herpetic keratitis in an immunocompetent patient.N(2)-Phenyl-9-(hydroxyalkyl)guanines and related compounds are substrates for Herpes simplex virus thymidine kinasesAutomating crystallographic structure solution and refinement of protein-ligand complexes.Docking and antiherpetic activity of 2-aminobenzo[de]-isoquinoline-1,3-diones.The rational of catalytic activity of herpes simplex virus thymidine kinase. a combined biochemical and quantum chemical study.Methodology and problems of protein-ligand docking: case study of dihydroorotate dehydrogenase, thymidine kinase, and phosphodiesterase 4.Compulsory order of substrate binding to herpes simplex virus type 1 thymidine kinase. A calorimetric study.Synthesis, Antiviral Evaluation, and Computational Studies of Cyclobutane and CyclobuteneL-Nucleoside Analogues
P2860

Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir

Item
http://www.wikidata.org/entity/Q27766894
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
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1999年の論文
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1999年論文
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1999年論文
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1999年論文
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1999年論文
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1999年論文
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1999年论文
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name
Structure to 1.9 A resolution ...... ison with binding of aciclovir
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Structure to 1.9 A resolution ...... ison with binding of aciclovir
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Structure to 1.9 A resolution ...... ison with binding of aciclovir
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Structure to 1.9 A resolution ...... ison with binding of aciclovir
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Structure to 1.9 A resolution ...... ison with binding of aciclovir
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Structure to 1.9 A resolution ...... ison with binding of aciclovir
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Structure to 1.9 A resolution ...... ison with binding of aciclovir
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Structure to 1.9 A resolution ...... ison with binding of aciclovir
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Structure to 1.9 A resolution ...... ison with binding of aciclovir
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Structure to 1.9 A resolution ...... ison with binding of aciclovir
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10.1016/S0014-5793(98)01619-6
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