Interaction of tubulin with ribose-modified analogs of GTP and GDP: evidence for two mutually exclusive exchangeable nucleotide binding sites.
Interactions of tubulin with a number of guanine nucleotides modified at the 2' and 3' ribose hydroxyls were examined. Deoxy analogs of GTP were equal or superior to GTP in supporting tubulin polymerization, but analogs bearing either methyl or phosphate groups on the hydroxyls had significantly red...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1981
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC319569/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6943545/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.78.6.3368 |
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