Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.

Summary Expression Phenotypes Gene Literature (11) GO Terms (32) Nucleotides (121) Proteins (49) Interactants (4) Wiki
XB-GENEPAGE-972482

Papers associated with nudt16



???displayGene.coCitedPapers???

???pagination.result.count???

???pagination.result.page??? 1

Sort Newest To Oldest Sort Oldest To Newest

Hydrolytic activity of human Nudt16 enzyme on dinucleotide cap analogs and short capped oligonucleotides., Grzela R, Nasilowska K, Lukaszewicz M, Tyras M, Stepinski J, Jankowska-Anyszka M, Bojarska E, Darzynkiewicz E., RNA. May 1, 2018; 24 (5): 633-642.


Coexistence of Y, W, and Z sex chromosomes in Xenopus tropicalis., Roco ÁS, Olmstead AW, Degitz SJ, Amano T, Zimmerman LB, Bullejos M., Proc Natl Acad Sci U S A. August 25, 2015; 112 (34): E4752-61.                


hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA., Lu G, Zhang J, Li Y, Li Z, Zhang N, Xu X, Wang T, Guan Z, Gao GF, Yan J., Protein Cell. January 1, 2011; 2 (1): 64-73.


Multiple mRNA decapping enzymes in mammalian cells., Song MG, Li Y, Kiledjian M., Mol Cell. November 12, 2010; 40 (3): 423-32.


A neuronal acetylcholine receptor regulates the balance of muscle excitation and inhibition in Caenorhabditis elegans., Jospin M, Qi YB, Stawicki TM, Boulin T, Schuske KR, Horvitz HR, Bessereau JL, Jorgensen EM, Jin Y., PLoS Biol. December 1, 2009; 7 (12): e1000265.              


Structure and biological function of the RNA pyrophosphohydrolase BdRppH from Bdellovibrio bacteriovorus., Messing SA, Gabelli SB, Liu Q, Celesnik H, Belasco JG, Piñeiro SA, Amzel LM., Structure. March 11, 2009; 17 (3): 472-81.


Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme., Taylor MJ, Peculis BA., Nucleic Acids Res. October 1, 2008; 36 (18): 6021-34.              


Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)., Peculis BA, Reynolds K, Cleland M., J Biol Chem. August 24, 2007; 282 (34): 24792-805.


Crystal structures of U8 snoRNA decapping nudix hydrolase, X29, and its metal and cap complexes., Scarsdale JN, Peculis BA, Wright HT., Structure. February 1, 2006; 14 (2): 331-43.


Crystals of X29, a Xenopus laevis U8 snoRNA-binding protein with nuclear decapping activity., Peculis BA, Scarsdale JN, Wright HT., Acta Crystallogr D Biol Crystallogr. September 1, 2004; 60 (Pt 9): 1668-9.


Xenopus U8 snoRNA binding protein is a conserved nuclear decapping enzyme., Ghosh T, Peterson B, Tomasevic N, Peculis BA., Mol Cell. March 26, 2004; 13 (6): 817-28.

???pagination.result.page??? 1