Nucleoside Diphosphate Prodrugs: Nonsymmetric DiPPro-Nucleotides
نویسندگان
چکیده
منابع مشابه
Binding of nucleotides to nucleoside diphosphate kinase: a calorimetric study.
The source of affinity for substrates of human nucleoside diphosphate (NDP) kinases is particularly important in that its knowledge could be used to design more effective antiviral nucleoside drugs (e.g., AZT). We carried out a microcalorimetric study of the binding of enzymes from two organisms to various nucleotides. Isothermal titration calorimetry has been used to characterize the binding i...
متن کاملSubcellular compartmentation of uridine nucleotides and nucleoside-5' -diphosphate kinase in leaves.
The subcellular compartmentation of nucleoside diphosphate kinase (EC 2.7.4.6) and the uridine nucleotides has been studied in leaves. Membrane filtration of barley (Hordeum vulgare L.) leaf mesophyll protoplasts and differential centrifugation of spinach (Spinacia oleracea L.) leaf extracts showed that about half the nucleoside diphosphate kinase is present in the cytosol. The activity is adeq...
متن کامل3'-Phosphorylated nucleotides are tight binding inhibitors of nucleoside diphosphate kinase activity.
Nucleoside diphosphate (NDP) kinase catalyzes the phosphorylation of ribo- and deoxyribonucleosides diphosphates into triphosphates. NDP kinase is also involved in malignant tumors and was shown to activate in vitro transcription of the c-myc oncogene by binding to its NHE sequence. The structure of the complex of NDP kinase with bound ADP shows that the nucleotide adopts a different conformati...
متن کاملldentification as a Nucleoside Diphosphate Kinase'
A low molecular mas (18 kD) phosphoprotein (pp18) was characterized and purified from cultured sugarcane (Saccharum officinarum 1.) cell line H50-7209. Autophosphorylation assays were used to detect pp18 after separation by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PACE). Only pp18 was detected by a brief in situ phosphorylation method, whereas additional putative protein ki...
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ژورنال
عنوان ژورنال: Journal of Medicinal Chemistry
سال: 2015
ISSN: 0022-2623,1520-4804
DOI: 10.1021/acs.jmedchem.5b00737