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Results 1 - 10 of 19 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1751428 A cyclin-binding motif in human SAMHD1 is required for its HIV-1 restriction, dNTPase activity, tetramer formation, and efficient phosphorylation J. Virol. 92 e01787 2018 Homo sapiens 29321329
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1751132 A high-throughput enzyme-coupled assay for SAMHD1 dNTPase J. Biomol. Screen. 20 801-809 2015 Homo sapiens 25755265
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1751090 A highly active isoform of lentivirus restriction factor SAMHD1 in mouse J. Biol. Chem. 292 1068-1080 2017 Mus musculus 27920203
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1752202 Effects of T592 phosphomimetic mutations on tetramer stability and dNTPase activity of SAMHD1 can not explain the retroviral restriction defect Sci. Rep. 6 31353 2016 Homo sapiens 27511536
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1749936 Identification of inhibitors of the dNTP triphosphohydrolase SAMHD1 using a novel and direct high-throughput assay Biochemistry 57 6624-6636 2018 Homo sapiens 30380297
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1751050 Impaired dNTPase activity of SAMHD1 by phosphomimetic mutation of Thr-592 J. Biol. Chem. 290 26352-26359 2015 Homo sapiens 26294762
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1751773 SAMHD1 acetylation enhances its deoxynucleotide triphosphohydrolase activity and promotes cancer cell proliferation Oncotarget 8 68517-68529 2017 Homo sapiens 28978134
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1752156 SAMHD1 specifically restricts retroviruses through its RNase activity Retrovirology 12 46 2015 Homo sapiens 26032178
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1749906 Substrate specificity of SAMHD1 triphosphohydrolase activity is controlled by deoxyribonucleoside triphosphates and phosphorylation at Thr592 Biochemistry 55 5635-5646 2016 Homo sapiens 27588835
Display the word mapDisplay the reaction diagram Show all sequences 3.1.5.B1751048 The deoxynucleoside triphosphate triphosphohydrolase activity of SAMHD1 protein contributes to the mitochondrial DNA depletion associated with genetic deficiency of deoxyguanosine kinase J. Biol. Chem. 290 25986-25996 2015 Homo sapiens 26342080
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