Title : Crystal structures of SAMHD1 inhibitor complexes reveal the mechanism of water-mediated dNTP hydrolysis.

Pub. Date : 2020 Jun 23

PMID : 32576829






3 Functional Relationships(s)
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Protein Name
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1 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 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens
2 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 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens
3 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 SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens