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pro vyhledávání: '"Weonmee Park"'
Publikováno v:
Molecular and Cellular Biology. 14:8117-8122
Previously we found that negatively charged residues at positions 62, 63, and 69 of H-Ras are involved in binding to the CDC25 guanine nucleotide exchange factor (GEF). Using site-directed mutagenesis, we have changed conserved, positively charged re
Autor:
Lawrence A. Quilliam, Daniel Broek, Wen Wei, Shayne Y. Huff, Weonmee Park, Kelly M. Rabun, Channing J. Der
Publikováno v:
Proceedings of the National Academy of Sciences. 91:8512-8516
Growth factor-triggered activation of Ras proteins is believed to be mediated by guanine nucleotide exchange factors (CDC25/GRF and SOS1/2) that promote formation of the active Ras GTP-bound state. Although the mechanism(s) of guanine nucleotide exch
Our results demonstrate that the GAL4 two-hybrid system can be useful for studying interactions of the wild-type and mutant forms of Ras proteins with the CDC25 guanine nucleotide exchange factor (CDC25-GEF). In addition, our findings show that a neg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1acadbe980e4d98573023bfa6e1fc171
https://doi.org/10.1016/s0076-6879(95)55017-8
https://doi.org/10.1016/s0076-6879(95)55017-8
Publikováno v:
Gene. 151(1-2)
Ras proteins bound to GDP are biologically inactive while those bound to GTP are active. Ras-specific guanine nucleotide-exchange factors (GEFs) have been shown to activate Ras proteins. We used oligodeoxyribonucleotide primers with sequences similar