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A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1.
Songyang Z, Lu KP, Kwon YT, Tsai LH, Filhol O, Cochet C, Brickey DA, Soderling TR, Bartleson C, Graves DJ, DeMaggio AJ, Hoekstra MF, Blenis J, Hunter T, Cantley LC. Songyang Z, et al. Mol Cell Biol. 1996 Nov;16(11):6486-93. doi: 10.1128/MCB.16.11.6486. Mol Cell Biol. 1996. PMID: 8887677 Free PMC article.
A single point mutation switches the specificity of group III Src homology (SH) 2 domains to that of group I SH2 domains.
Songyang Z, Gish G, Mbamalu G, Pawson T, Cantley LC. Songyang Z, et al. J Biol Chem. 1995 Nov 3;270(44):26029-32. doi: 10.1074/jbc.270.44.26029. J Biol Chem. 1995. PMID: 7592796 Free article.
Based on the phosphopeptide specificity and crystal structures, SH2 domains were classified into four different groups (Songyang, Z., Shoelson, S. E., Chaudhuri, M., Gish, G., Pawson, T., Haser, W. ...The beta D5 residues of SH2 domains were predicted to be critical …
Based on the phosphopeptide specificity and crystal structures, SH2 domains were classified into four different groups (Songyang, …
Specificity in protein-tyrosine kinase signaling.
Cantley LC, Songyang Z. Cantley LC, et al. Among authors: songyang z. Adv Second Messenger Phosphoprotein Res. 1997;31:41-8. doi: 10.1016/s1040-7952(97)80007-9. Adv Second Messenger Phosphoprotein Res. 1997. PMID: 9344240 Review. No abstract available.
208 results