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FEBS Letters|September 12, 1988
Organization of soluble enzymes in the cell. Relay at the surfaceA G RyazanovFEBS Letters|November 11, 1985
Glyceraldehyde-3-phosphate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytesA G RyazanovFEBS Letters|April 20, 1987
Ca2+/calmodulin-dependent phosphorylation of elongation factor 2A G RyazanovFEBS Letters|December 3, 1984
Does the complex of aminoacyl-tRNA synthetases and tRNA-modifying enzymes prevent miscoding?A G RyazanovFEBS Letters|July 17, 1989
Mechanism of elongation factor 2 (EF-2) inactivation upon phosphorylation. Phosphorylated EF-2 is unable to catalyze translocationA G Ryazanov, E K DavydovaThe New Biologist|October 1, 1990
Phosphorylation of elongation factor 2: a key mechanism regulating gene expression in vertebratesA G Ryazanov, A S SpirinProceedings of the National Academy of Sciences of the United States of America|June 1, 1990
Increased phosphorylation of elongation factor 2 during mitosis in transformed human amnion cells correlates with a decreased rate of protein synthesisJ E Celis, P Madsen, A G RyazanovBiochemistry|October 4, 2000
Mapping the functional domains of elongation factor-2 kinaseK S Pavur, A N Petrov, A G RyazanovNature|July 14, 1988
Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translationA G Ryazanov, E A Shestakova, P G NatapovEuropean Journal of Biochemistry|January 15, 1988
Association of glyceraldehyde-3-phosphate dehydrogenase with mono- and polyribosomes of rabbit reticulocytesA G Ryazanov, L I Ashmarina, V I MuronetzPageof 3