Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Raymond J.A. Budde"'
Autor:
Jean-Noel La Croix, John S. McMurray, Raymond J.A. Budde, Douglas F. Dyckes, Nihal U. Obeyesekere
Publikováno v:
International Journal of Peptide and Protein Research. 43:118-126
(Tyr-Ala-Glu) n , n = 1 a 9, were synthesized by segment condensation using the Fmoc/tert-butyl protection strategy and solide-phase techni- ques. The C-terminal residue was coupled to the resin and the peptides were built out by adding Fmoc-Glu(O-t-
Publikováno v:
International Journal of Peptide and Protein Research. 42:209-215
To study the effects of constrained conformation and amino acid sequence on their kinetic parameters, a series of cyclic peptides were synthesized and each was tested as both a substrate and an inhibitor of pp60c-src, the product of the src proto-onc
Autor:
Raymond J.A. Budde, Gongqin Sun
Publikováno v:
Protein Expression and Purification. 21:8-12
Protein tyrosine kinase Csk requires two Mg2+ ions for activity: one magnesium is part of the ATP-Mg complex, and the second free Mg2+ ion is required as an essential activator. Zn2+ can bind to this site to replace Mg2+, which inhibits Csk kinase ac
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 11:805-809
Protein tyrosine kinases (PTKs) are key members of intra- and extra-cellular signaling pathways. Aberrant signaling pathways are responsible for many human diseases, making these enzymes targets for drug development programs. The difficulty in PCR-am
Autor:
Gongqin Sun, Shi Ke, Raymond J.A. Budde, Wei Wang, Nihal U. Obeyesekere, John S. McMurray, Latha Ramdas
Publikováno v:
Biochemistry. 39:5221-5228
The protein tyrosine kinase, pp60(c-)(src), is involved in cellular signaling and is activated during mitosis and in various tumors. We have been employing cyclic decapeptides to identify the determinants for substrate binding and phosphorylation to
Autor:
Latha Ramdas, Jonathan A. Ellman, Raymond J.A. Budde, Gongqin Sun, Matthew J. Plunkett, Gary E. Gallick, Barry A. Bunnin
Publikováno v:
Archives of Biochemistry and Biophysics. 368:394-400
We screened 1680 spatially separated compounds of a diverse combinatorial library of 1,4-benzodiazepines for their ability to inhibit the kinase activity of protein tyrosine kinases Src, Yes, Abl, Lck, Csk, and fibroblast growth factor receptor. This
Autor:
Gongqin Sun, Raymond J.A. Budde
Publikováno v:
Archives of Biochemistry and Biophysics. 367:167-172
In addition to the C-terminal catalytic domain, Csk is a protein tyrosine kinase that has an N-terminal regulatory region that contains SH3 and SH2 domains. The role this region plays relative to the function of the catalytic domain is not clear. To
Publikováno v:
The Journal of Peptide Research. 53:569-577
The conversion of a peptide substrate to a potent inhibitor by chemical modification is a promising approach in the development of inhibitors for protein tyrosine kinases. N-acylation of the synthetic peptide substrate NH2-Glu-Phe-Leu-Tyr-Gly-Val-Phe
Autor:
Raymond J.A. Budde, Gongqin Sun
Publikováno v:
Archives of Biochemistry and Biophysics. 345:135-142
Protein tyrosine kinase Yes is a cellular homolog of v-Yes, the oncogenic protein product of avian sarcoma virus Y73. Yes is a member of the Src family and its activation has been associated with several types of human cancer. Human Yes has not been
Autor:
Latha Ramdas, Gary E. Gallick, Nihal U. Obeyesekere, John S. McMurray, Raymond J.A. Budde, William E. Seifert
Publikováno v:
Archives of Biochemistry and Biophysics. 323:237-242
We recently reported that tyrphostin 23 (3,4-dihydroxybenzylidene malononitrile) is unstable in solution and that some of the degradation products are better inhibitors of the tyrosine kinase activity of Src and the EGF-receptor kinase than the paren