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Summary Expression Gene Literature (10) GO Terms (20) Nucleotides (248) Proteins (60) Interactants (154) Wiki
XB--5760737

Papers associated with dyrk1a.2

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1 paper(s) referencing morpholinos

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The neurodevelopmental disorder risk gene DYRK1A is required for ciliogenesis and control of brain size in Xenopus embryos., Willsey HR, Xu Y, Xu Y, Everitt A, Dea J, Exner CRT, Willsey AJ, State MW, Harland RM., Development. January 1, 2020; 147 (21):                             


Similarity in gene-regulatory networks suggests that cancer cells share characteristics of embryonic neural cells., Zhang Z, Lei A, Xu L, Chen L, Chen Y, Chen Y, Zhang X, Gao Y, Yang X, Zhang M, Cao Y, Cao Y., J Biol Chem. January 1, 2017; 292 (31): 12842-12859.        


Selective inhibition of the kinase DYRK1A by targeting its folding process., Kii I, Sumida Y, Goto T, Sonamoto R, Okuno Y, Yoshida S, Kato-Sumida T, Koike Y, Abe M, Nonaka Y, Ikura T, Ito N, Shibuya H, Hosoya T, Hagiwara M., Nat Commun. April 22, 2016; 7 11391.                    


The adaptor protein DCAF7 mediates the interaction of the adenovirus E1A oncoprotein with the protein kinases DYRK1A and HIPK2., Glenewinkel F, Cohen MJ, King CR, Kaspar S, Bamberg-Lemper S, Mymryk JS, Becker W., Sci Rep. January 1, 2016; 6 28241.                    


Down''s-syndrome-related kinase Dyrk1A modulates the p120-catenin-Kaiso trajectory of the Wnt signaling pathway., Hong JY, Park JI, Lee M, Muñoz WA, Miller RK, Ji H, Gu D, Ezan J, Sokol SY, McCrea PD., J Cell Sci. February 1, 2012; 125 (Pt 3): 561-9.                


Development of a novel selective inhibitor of the Down syndrome-related kinase Dyrk1A., Ogawa Y, Nonaka Y, Goto T, Ohnishi E, Hiramatsu T, Kii I, Yoshida M, Ikura T, Onogi H, Shibuya H, Hosoya T, Ito N, Hagiwara M., Nat Commun. October 5, 2010; 1 86.  


Development of a sensitive non-radioactive protein kinase assay and its application for detecting DYRK activity in Xenopus laevis oocytes., Lilienthal E, Kolanowski K, Becker W., BMC Biochem. January 1, 2010; 11 20.        


The dual-specificity kinases, TOPK and DYRK1A, are critical for oocyte maturation induced by wild-type--but not by oncogenic--ras-p21 protein., Qu Y, Adler V, Izotova L, Pestka S, Bowne W, Michl J, Boutjdir M, Friedman FK, Pincus MR., Front Biosci. September 1, 2007; 12 5089-97.


Two dual specificity kinases are preferentially induced by wild-type rather than by oncogenic RAS-P21 in Xenopus oocytes., Qu Y, Adler V, Chu T, Platica O, Michl J, Pestka S, Izotova L, Boutjdir M, Pincus MR., Front Biosci. September 1, 2006; 11 2420-7.

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