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Biochemical Society Transactions|November 1, 2006
Protein kinase CK2: a newcomer in the 'druggable kinome'M A Pagano, L Cesaro, F Meggio, et al.
Biochemical and Biophysical Research Communications|February 14, 1992
The comparative efficiencies of the Ser(P)-, Thr(P)- and Tyr(P)-residues as specificity determinants for casein kinase-1F Meggio, J W Perich, O Marin, et al.
Biochemical and Biophysical Research Communications|April 25, 1996
Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2B Baldan, L Navazio, A Friso, et al.
Biochemistry|November 30, 1993
Reconstitution of normal and hyperactivated forms of casein kinase-2 by variably mutated beta-subunitsB Boldyreff, F Meggio, L A Pinna, et al.
Cellular & Molecular Biology Research|January 1, 1994
Protein kinase CK2 structure-function relationship: effects of the beta subunit on reconstitution and activityB Boldyreff, F Meggio, L A Pinna, et al.
Biochemical and Biophysical Research Communications|October 15, 1992
Casein kinase-2 structure-function relationship: creation of a set of mutants of the beta subunit that variably surrogate the wildtype beta subunit functionB Boldyreff, F Meggio, L A Pinna, et al.
The International Journal of Biochemistry & Cell Biology|September 1, 1996
Phosphotyrosine specifies the phosphorylation by protein kinase CK2 of a peptide reproducing the activation loop of the insulin receptor protein tyrosine kinaseO Marin, F Meggio, J W Perich, et al.
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