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Hybridoma|February 1, 1992
Isolation and characterization of a monoclonal anti CK-2 alpha subunit antibody of the IgG1 subclassI Schmidt-Spaniol, B Boldyreff, O G IssingerBiochimica Et Biophysica Acta|October 30, 1985
Ribosomal protein S6 phosphorylation and morphological changes in response to the tumour promoter 12-O-tetradecanoylphorbol 13-acetate in primary human tumour cells, established and transformed cell linesA J Rance, M Thönnes, O G IssingerEuropean Journal of Biochemistry|March 15, 1989
Specific dephosphorylation by phosphatases 1 and 2A of a nuclear protein structurally and immunologically related to nucleolin. Possible influence on the regulation of rRNA synthesisH R Schneider, G Mieskes, O G IssingerCellular & Molecular Biology Research|January 1, 1993
Subcellular localization of protein kinase CK-2 alpha- and beta-subunits in synchronized cells from primary human fibroblasts and established cell linesI Schmidt-Spaniol, B Grimm, O G IssingerFEBS Letters|March 21, 1983
Influence of hyperthermia on the phosphorylation of ribosomal protein S6 from human skin fibroblasts and meningioma cellsW W Richter, K D Zang, O G IssingerActa Crystallographica. Section D, Biological Crystallography|November 28, 2000
Crystallization and preliminary characterization of crystals of human protein kinase CK2K Niefind, B Guerra, I Ermakowa, et al.European Journal of Biochemistry|December 1, 1993
Ser2 is the autophosphorylation site in the beta subunit from bicistronically expressed human casein kinase-2 and from native rat liver casein kinase-2 betaB Boldyreff, P James, W Staudenmann, et al.Oncogene|July 18, 1996
p21WAF1/CIP1 interacts with protein kinase CK2C Götz, P Wagner, O G Issinger, et al.The International Journal of Biochemistry & Cell Biology|June 17, 2000
Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: evaluation by the two hybrid systemM Tchórzewski, B Boldyreff, O G Issinger, et al.European Journal of Biochemistry|December 15, 1986
Enhanced casein kinase II activity during mouse embryogenesis. Identification of a 110-kDa phosphoprotein as the major phosphorylation product in mouse embryos and Krebs II mouse ascites tumor cellsH R Schneider, G H Reichert, O G IssingerPageof 10