91 research outputs found
Phosphorylation in vivo of non-ribosomal proteins from native 40 S ribosomal particles of Krebs II mouse ascites-tumour cells
Full text linkComparison of phosphorylation of ribosomal proteins from HeLa and Krebs II ascites-tumour cells by cyclic AMP-dependent and cyclic GMP-dependent protein kinases
Full text linkCharacterization of phosphorylation sites in the cytoplasmic domain of the 300 kDa mannose-6-phosphate receptor
Full text linkCharacterization of native 40s particles from krebs ii mouse ascites tumor cells. I. Phosphorylation in vitro of non ribosomal proteins by a camp independent protein kinase.
No full textCharacterization of native 40S particles from krebs II mouse ascites tumor cells. I.:Phosphorylation in vitro of non ribosomal proteins by a cAMP independent protein kinase
No full text
Growth-dependent modulation of casein kinase II and its substrate nucleolin in primary human cell cultures and HeLa cells
No full textPhosphorylation in vivo of non-ribosomal proteins from native 40 s ribosomal particles of krebs ii mouse ascites-tumour cells.
No full textPhosphorylation in vivo of non-ribosomal proteins from native 40 S ribosomal particles of Krebs II mouse ascites-tumour cells.
No full textFour non-ribosomal proteins from native 40 S ribosomal subunits with mol.wts. of 110 000, 84 000, 68 000 and 26 000 were phosphorylated in vivo when ascites cells were incubated in the presence of [32P]Pi. The 110 000-, 84 000- and 26 000-dalton proteins are identical with phosphorylated products from native 40 S subunits after phosphorylation in vitro by a cyclic nucleotide-independent protein kinase. Phosphoserine was the major phosphorylated amino acid of the proteins phosphorylated in vivo and in vitro
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