Nucleoside binding site of herpes simplex type 1 thymidine kinase analyzed by X-ray crystallography
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The 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 kinaseFunctional studies of active-site mutants from Drosophila melanogaster deoxyribonucleoside kinase. Investigations of the putative catalytic glutamate-arginine pair and of residues responsible for substrate specificitySynthesis, crystal structure, and in vitro biological evaluation of C-6 pyrimidine derivatives: new lead structures for monitoring gene expression in vivoStructure of a type II thymidine kinase with bound dTTPStructure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug designA Bioorthogonal Chemical Reporter of Viral Infection.Waterdock 2.0: Water placement prediction for Holo-structures with a pymol pluginNeonatal herpes encephalitis caused by a virologically confirmed acyclovir-resistant herpes simplex virus 1 strain.The solvation structure of alprazolam.C-5 hydroxyethyl and hydroxypropyl acyclonucleosides as substrates for thymidine kinase of herpes simplex virus type 1 (HSV-1 TK): syntheses and biological evaluation.Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding.A method for quantification of nucleotides and nucleotide analogues in thymidine kinase assays using lanthanum phosphate coprecipitation.Bisubstrate inhibitors for the enzyme catechol-O-methyltransferase (COMT): influence of inhibitor preorganisation and linker length between the two substrate moieties on binding affinity.Molecular modeling of the binding of 5-substituted 2'-deoxyuridine substrates to thymidine kinase of herpes simplex virus type-1.Engineering of a single conserved amino acid residue of herpes simplex virus type 1 thymidine kinase allows a predominant shift from pyrimidine to purine nucleoside phosphorylation.Mobility-based prediction of hydration structures of protein surfaces.Designing a ligand for pharmaceutical purposes
P2860
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P2860
Nucleoside binding site of herpes simplex type 1 thymidine kinase analyzed by X-ray crystallography
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
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name
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@ast
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@en
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@nl
type
label
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@ast
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@en
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@nl
prefLabel
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@ast
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@en
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@nl
P2093
P2860
P1433
P1476
Nucleoside binding site of her ...... lyzed by X-ray crystallography
@en
P2093
G E Schulz
L Scapozza
P Schelling
P2860
P304
P356
10.1002/1097-0134(20001201)41:4<545::AID-PROT110>3.0.CO;2-8
P407
P577
2000-12-01T00:00:00Z