Pages that link to "Q44244862"

The following pages link to Analysis of the catalytic and binding residues of the diadenosine tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans by site-directed mutagenesis (Q44244862):

Displayed 11 items.

• Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme (Q24316889) ‎ (← links)
• The crystal structure and mutational analysis of human NUDT9 (Q27641930) ‎ (← links)
• Chlamydia trachomatis CT771 ( nudH ) Is an Asymmetric Ap 4 A Hydrolase (Q27680973) ‎ (← links)
• Divalent metal ion-based catalytic mechanism of the Nudix hydrolase Orf153 (YmfB) from Escherichia coli (Q27690198) ‎ (← links)
• Kinetic and mutational studies of the adenosine diphosphate ribose hydrolase from Mycobacterium tuberculosis (Q27728139) ‎ (← links)
• Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe (Q27932261) ‎ (← links)
• Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] CELE_Y37H9A.6 (Q29807924) ‎ (← links)
• The Nudix hydrolase Ndx1 from Thermus thermophilus HB8 is a diadenosine hexaphosphate hydrolase with a novel activity (Q34306230) ‎ (← links)
• Structure and substrate-binding mechanism of human Ap4A hydrolase (Q34375999) ‎ (← links)
• Substrate ambiguity among the nudix hydrolases: biologically significant, evolutionary remnant, or both? (Q44518086) ‎ (← links)
• Nudt19 is a renal CoA diphosphohydrolase with biochemical and regulatory properties that are distinct from the hepatic Nudt7 isoform. (Q49597537) ‎ (← links)