How do protein kinases recognize their substrates?
- 1 December 1996
- journal article
- review article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Vol. 1314 (3), 191-225
- https://doi.org/10.1016/s0167-4889(96)00083-3
Abstract
No abstract availableThis publication has 192 references indexed in Scilit:
- Development of a Rapid Approach to Identification of Tyrosine Phosphorylation Sites: Application to PKCδ Phosphorylated upon Activation of the High Affinity Receptor for IgE in Rat Basophilic Leukemia CellsBiochemical and Biophysical Research Communications, 1995
- Mapping the Residues of Protein Kinase CK2 Implicated in Substrate Recognition: Mutagenesis of Conserved Basic Residues in the α-SubunitBiochemical and Biophysical Research Communications, 1995
- Phosphorylation of NM23/Nucleoside Diphosphate Kinase by Casein Kinase 2 in VitroBiochemical and Biophysical Research Communications, 1994
- The cell cycle regulator, human p50weel, is a tyrosine kinase and not a serine/tyrosine kinaseBiochemical and Biophysical Research Communications, 1992
- The comparative efficiencies of the Ser(P)-, Thr(P)- and Tyr(P)-residues as specificity determinants for casein kinase-1Biochemical and Biophysical Research Communications, 1992
- Synthetic peptide substrates for casein kinase 2. Assessment of minimum structural requirements for phosphorylationBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1988
- Phosphorylation of protamines by protein kinase C: Involvement of sites which are phosphorylated in vivo and are not affected by cAMP-dependent protein kinaseBiochemical and Biophysical Research Communications, 1987
- Structural features determining the site specificity of a rat liver cAMP-independent protein kinaseBiochemical and Biophysical Research Communications, 1979
- Occurrence of phosphorylated residues in predicted β-turns: Implications for β-turn participation in control mechanismsBiochemical and Biophysical Research Communications, 1977
- The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liverBiochemical and Biophysical Research Communications, 1976