Pub. Date : 2003 May 9
PMID : 12606544
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Molecular dissection of GTP exchange and hydrolysis within the ternary complex of tubulin heterodimers and Op18/stathmin family members. | Guanosine Triphosphate | stathmin 1 | Homo sapiens |
| 2 | Molecular dissection of GTP exchange and hydrolysis within the ternary complex of tubulin heterodimers and Op18/stathmin family members. | Guanosine Triphosphate | stathmin 1 | Homo sapiens |
| 3 | Here we have analyzed GTP exchange and GTP hydrolysis at the exchangeable GTP-binding site (E-site) of tubulin heterodimers in complex with Op18, RB3, or SCG10. | Guanosine Triphosphate | stathmin 1 | Homo sapiens |
| 4 | Here we have analyzed GTP exchange and GTP hydrolysis at the exchangeable GTP-binding site (E-site) of tubulin heterodimers in complex with Op18, RB3, or SCG10. | Guanosine Triphosphate | stathmin 1 | Homo sapiens |
| 5 | Here we have analyzed GTP exchange and GTP hydrolysis at the exchangeable GTP-binding site (E-site) of tubulin heterodimers in complex with Op18, RB3, or SCG10. | Guanosine Triphosphate | stathmin 1 | Homo sapiens |
| 6 | Results from mutational analysis of clusters of hydrophobic residues within the first helical repeat of Op18 suggest that GTP is hydrolyzed at the E-site that is interfaced between the head-to-tail arranged heterodimers, which is consistent with predicted GTPase productive interactions between the two tubulin heterodimers. | Guanosine Triphosphate | stathmin 1 | Homo sapiens |
| 7 | We conclude that tubulin heterodimers in complex with Op18/stathmin family members are subject to allosteric effects that prevent futile cycles of GTP hydrolysis. | Guanosine Triphosphate | stathmin 1 | Homo sapiens |
| 8 | We conclude that tubulin heterodimers in complex with Op18/stathmin family members are subject to allosteric effects that prevent futile cycles of GTP hydrolysis. | Guanosine Triphosphate | stathmin 1 | Homo sapiens |