PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28436707-5 2017 Within this Extra View, we discuss and build upon both these and our previously reported findings, and propose SAMHD1 is likely active against a variety of nucleoside analog antimetabolites present in anti-cancer chemotherapies. Nucleosides 156-166 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 111-117 28502830-5 2017 However, SAMHD1 also can act as a resistance factor to nucleoside-based chemotherapies by hydrolyzing their active triphosphate metabolites, thereby reducing response of various malignancies to these anticancer drugs. Nucleosides 55-65 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 9-15 28359840-5 2017 Similarly, in SAMHD1 knockout cells, HIV-1 showed increased replicative capacity in the presence of nucleoside inhibitors, especially AZT, that was reverted by re-expression of wild type SAMHD1. Nucleosides 100-110 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 14-20 28359840-5 2017 Similarly, in SAMHD1 knockout cells, HIV-1 showed increased replicative capacity in the presence of nucleoside inhibitors, especially AZT, that was reverted by re-expression of wild type SAMHD1. Nucleosides 100-110 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 187-193 28359840-8 2017 Our results demonstrate that SAMHD1 is active in HIV-1 permissive cells, does not modify susceptibility to HIV-1 infection but strongly affects sensitivity to nucleoside inhibitors. Nucleosides 159-169 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 29-35 28220857-0 2017 SAMHD1 enhances nucleoside-analogue efficacy against HIV-1 in myeloid cells. Nucleosides 16-26 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 0-6 28046007-9 2017 Importantly, our data is beneficial for understanding if FDA-approved antiviral and anticancer nucleosides are hydrolyzed by SAMHD1 in vivo. Nucleosides 95-106 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 125-131 26496699-3 2015 The restrictive phenotype of myeloid cells can be alleviated through the direct degradation of SAMHD1 by the HIV-2/SIVSM Vpx protein or else, at least in the case of HIV-1, by the exogenous supplementation of nucleosides that artificially overcome the catabolic activity of SAMHD1 on dNTPs. Nucleosides 209-220 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 95-101 26496699-3 2015 The restrictive phenotype of myeloid cells can be alleviated through the direct degradation of SAMHD1 by the HIV-2/SIVSM Vpx protein or else, at least in the case of HIV-1, by the exogenous supplementation of nucleosides that artificially overcome the catabolic activity of SAMHD1 on dNTPs. Nucleosides 209-220 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 274-280 32576829-4 2020 Furthermore, SAMHD1 sensitises cancer cells to nucleoside-analogue anti-cancer therapies and is linked with DNA repair and suppression of the interferon response to cytosolic nucleic acids. Nucleosides 47-57 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 13-19 32576829-7 2020 This precise molecular mechanism for SAMHD1 catalysis, reveals how SAMHD1 down-regulates cellular dNTP and modulates the efficacy of nucleoside-based anti-cancer and anti-viral therapies. Nucleosides 133-143 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 37-43 32576829-7 2020 This precise molecular mechanism for SAMHD1 catalysis, reveals how SAMHD1 down-regulates cellular dNTP and modulates the efficacy of nucleoside-based anti-cancer and anti-viral therapies. Nucleosides 133-143 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 67-73 30290238-4 2019 For example, APOBEC3G deaminates cytosines to hypermutate reverse transcribed viral DNA; IFITM3 alters membranes to inhibit virus membrane fusion; MXA/B oligomerize on viral protein complexes to inhibit virus replication; SAMHD1 decreases dNTP intracellular concentrations to prevent reverse transcription of retrovirus genomes; tetherin prevents release of budding virions from cells; Viperin catalyzes formation of a nucleoside analogue that inhibits viral RNA polymerases; and ZAP binds virus RNAs to target them for degradation. Nucleosides 419-429 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 222-228 27991919-5 2017 Although it has been postulated that SAMHD1 sensitizes cancer cells to nucleoside-analog derivatives through the depletion of competing dNTPs, we show here that SAMHD1 reduces Ara-C cytotoxicity in AML cells. Nucleosides 71-81 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 37-43 27991919-5 2017 Although it has been postulated that SAMHD1 sensitizes cancer cells to nucleoside-analog derivatives through the depletion of competing dNTPs, we show here that SAMHD1 reduces Ara-C cytotoxicity in AML cells. Nucleosides 71-81 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 161-167 34641952-1 2021 BACKGROUND: SAMHD1 mediates resistance to anti-cancer nucleoside analogues, including cytarabine, decitabine, and nelarabine that are commonly used for the treatment of leukaemia, through cleavage of their triphosphorylated forms. Nucleosides 54-64 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 12-18 34641952-2 2021 Hence, SAMHD1 inhibitors are promising candidates for the sensitisation of leukaemia cells to nucleoside analogue-based therapy. Nucleosides 94-104 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 7-13 33979727-0 2021 SAMHD1 mutations in mantle cell lymphoma are recurrent and confer in vitro resistance to nucleoside analogues. Nucleosides 89-99 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 0-6 32581304-3 2020 Here, data from pharmacogenomics studies and a panel of ALL cell lines reveal an inverse correlation between nelarabine sensitivity and the expression of SAMHD1, which can hydrolyse and inactivate triphosphorylated nucleoside analogues. Nucleosides 215-225 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens 154-160