3--(methylanthraniloyl)-2--deoxy-guanosine-diphosphate and Cell-Transformation--Neoplastic

3--(methylanthraniloyl)-2--deoxy-guanosine-diphosphate has been researched along with Cell-Transformation--Neoplastic* in 1 studies

Other Studies

1 other study(ies) available for 3--(methylanthraniloyl)-2--deoxy-guanosine-diphosphate and Cell-Transformation--Neoplastic

Article	Year
The isolated catalytic hairpin of the Ras-specific guanine nucleotide exchange factor Cdc25Mm retains nucleotide dissociation activity but has impaired nucleotide exchange activity. FEBS letters, 2005, Dec-19, Volume: 579, Issue:30 Cdc25Mm is a mammalian Ras-specific guanine nucleotide exchange factor (GEF). By homology modeling we show that it shares with Sos-GEF the structure of the putative catalytic HI hairpin where the dominant negative T1184E mutation is located. Similarly to Cdc25MmT1184E, the isolated wild-type and mutant hairpins retain the ability to displace Ras-bound nucleotide, originate a stable Ras/GEF complex and downregulate the Ras pathway in vivo. These results indicate that nucleotide re-entry and Ras/GEF dissociation--final steps in the GEF catalytic cycle--require GEF regions different from the HI hairpin. GEF down-sizing could lead to development of novel Ras inhibitors. Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Buffers; Catalysis; Catalytic Domain; Cell Line, Transformed; Cell Transformation, Neoplastic; Crystallography, X-Ray; Down-Regulation; Escherichia coli; Fibroblasts; Genes, Dominant; Genes, ras; Genes, Reporter; Glutamic Acid; Guanosine Diphosphate; Guanosine Triphosphate; Homozygote; Luciferases; Mice; Models, Molecular; Molecular Sequence Data; NIH 3T3 Cells; ortho-Aminobenzoates; Protein Structure, Secondary; ras-GRF1; Sequence Homology, Amino Acid; Temperature	2005

Article

Year

The isolated catalytic hairpin of the Ras-specific guanine nucleotide exchange factor Cdc25Mm retains nucleotide dissociation activity but has impaired nucleotide exchange activity.

FEBS letters, 2005, Dec-19, Volume: 579, Issue:30

Cdc25Mm is a mammalian Ras-specific guanine nucleotide exchange factor (GEF). By homology modeling we show that it shares with Sos-GEF the structure of the putative catalytic HI hairpin where the dominant negative T1184E mutation is located. Similarly to Cdc25MmT1184E, the isolated wild-type and mutant hairpins retain the ability to displace Ras-bound nucleotide, originate a stable Ras/GEF complex and downregulate the Ras pathway in vivo. These results indicate that nucleotide re-entry and Ras/GEF dissociation--final steps in the GEF catalytic cycle--require GEF regions different from the HI hairpin. GEF down-sizing could lead to development of novel Ras inhibitors.

Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Buffers; Catalysis; Catalytic Domain; Cell Line, Transformed; Cell Transformation, Neoplastic; Crystallography, X-Ray; Down-Regulation; Escherichia coli; Fibroblasts; Genes, Dominant; Genes, ras; Genes, Reporter; Glutamic Acid; Guanosine Diphosphate; Guanosine Triphosphate; Homozygote; Luciferases; Mice; Models, Molecular; Molecular Sequence Data; NIH 3T3 Cells; ortho-Aminobenzoates; Protein Structure, Secondary; ras-GRF1; Sequence Homology, Amino Acid; Temperature

2005