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SH2 domains recognize specific phosphopeptide sequences.
Songyang Z, Shoelson SE, Chaudhuri M, Gish G, Pawson T, Haser WG, King F, Roberts T, Ratnofsky S, Lechleider RJ, et al. Songyang Z, et al. Among authors: Chaudhuri M. Cell. 1993 Mar 12;72(5):767-78. doi: 10.1016/0092-8674(93)90404-e. Cell. 1993. PMID: 7680959
The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif.
Songyang Z, Margolis B, Chaudhuri M, Shoelson SE, Cantley LC. Songyang Z, et al. Among authors: Chaudhuri M. J Biol Chem. 1995 Jun 23;270(25):14863-6. doi: 10.1074/jbc.270.25.14863. J Biol Chem. 1995. PMID: 7541030
., Chaudhuri, M., Gish, G., Pawson, T., Haser, W. G., King, F., Roberts, T., Ratnofsky, S., Lechleider, R. J., Neel, B. G., Birge, R. ...E., Chou, M. M., Hanafusa, H., Schaffhausen, B., and Cantley, L. C. (1993) Cell 72, 767-778). Recently a second type of phosphotyrosine interaction domain (PID) or phosphotyrosine-binding domain (PTB) was discovered in the amino terminus of the SHC proto-oncoprotein (Kavanaugh, W. ...
., Chaudhuri, M., Gish, G., Pawson, T., Haser, W. G., King, F., Roberts, T., Ratnofsky, S., Lechleider, R. J., Neel, B. G., Bi …
SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange.
Felder S, Zhou M, Hu P, Ureña J, Ullrich A, Chaudhuri M, White M, Shoelson SE, Schlessinger J. Felder S, et al. Among authors: Chaudhuri M. Mol Cell Biol. 1993 Mar;13(3):1449-55. doi: 10.1128/mcb.13.3.1449. Mol Cell Biol. 1993. PMID: 7680095 Free PMC article.
Interestingly, the binding of the SH2 domains to the tyrosine-phosphorylated peptides was of high affinity as a result of a very high on rate, of 3 x 10(7) to 40 x 10(7)/M/s; at the same time, the rate of dissociation, of 0.11 to 0.19/s, was rapid, allowing for rapid exchange of associating proteins with the tyrosine phosphorylation sites....
Interestingly, the binding of the SH2 domains to the tyrosine-phosphorylated peptides was of high affinity as a result of a very high on rat …
YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase.
Shoelson SE, Chatterjee S, Chaudhuri M, White MF. Shoelson SE, et al. Among authors: Chaudhuri M. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2027-31. doi: 10.1073/pnas.89.6.2027. Proc Natl Acad Sci U S A. 1992. PMID: 1312712 Free PMC article.
Surprisingly six of these, each within YMXM motifs, were phosphorylated with greatest efficiency (Km, 24-92 microM; kcat/Km, 0.6-2.1 x 10(4) M-1.sec-1). ...
Surprisingly six of these, each within YMXM motifs, were phosphorylated with greatest efficiency (Km, 24-92 microM; kcat/Km, 0.6-2.1 x 10(4) …
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