Pub. Date : 1987 Sep
PMID : 3118192
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Structural significance of the GTP-binding domain of ras p21 studied by site-directed mutagenesis. | Guanosine Triphosphate | cyclin-dependent kinase inhibitor 1A (P21) | Mus musculus |
| 2 | Point mutations of p21 proteins were constructed by oligonucleotide-directed mutagenesis of the v-rasH oncogene, which substituted amino acid residues within the nucleotide-binding consensus sequence, GXG GXGK. | Oligonucleotides | cyclin-dependent kinase inhibitor 1A (P21) | Mus musculus |
| 3 | When the glycine residue at position 10, 13, or 15 was substituted with valine, the viral rasH product p21 lost its GTP-binding and autokinase activities. | Glycine | cyclin-dependent kinase inhibitor 1A (P21) | Mus musculus |
| 4 | When the glycine residue at position 10, 13, or 15 was substituted with valine, the viral rasH product p21 lost its GTP-binding and autokinase activities. | Valine | cyclin-dependent kinase inhibitor 1A (P21) | Mus musculus |
| 5 | When the glycine residue at position 10, 13, or 15 was substituted with valine, the viral rasH product p21 lost its GTP-binding and autokinase activities. | Guanosine Triphosphate | cyclin-dependent kinase inhibitor 1A (P21) | Mus musculus |
| 6 | These findings suggest that the glycine-rich consensus sequence is important in controlling p21 activities and that certain mutations may confer to p21 its active conformation without participation of ligand binding. | Glycine | cyclin-dependent kinase inhibitor 1A (P21) | Mus musculus |
| 7 | These findings suggest that the glycine-rich consensus sequence is important in controlling p21 activities and that certain mutations may confer to p21 its active conformation without participation of ligand binding. | Glycine | cyclin-dependent kinase inhibitor 1A (P21) | Mus musculus |