Deoxyguanosine nucleotide analogues: potent stimulators of microtubule nucleation with reduced affinity for the exchangeable nucleotide site of tubulin.
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Summary
It is concluded that alteration of the ribose moiety reduces the affinity of a guanine nucleotide for the exchangeable site oftubulin but that a nucleotide's affinity for this site is not the major factor in its ability to support the nucleation of tubulin polymerization.
- Type
- article
- Published
- 1984-10-23
- Cited by
- 36
- References
- 36
- OpenAlex
- https://openalex.org/W2057106900
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:1226464
Keywords
GTP', Tubulin, Microtubule, Nucleotide, Guanosine
References
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- Guanasone 5'-(alpha,beta-methylene)triphosphate enhances specifically microtubule nucleation and stops the treadmill of tubulin protomers.
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- Effects of inhibitors of tubulin polymerization on GTP hydrolysis.
- Assembly of tubulin with nucleotide analogs.
- Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase.
- Nucleotides bound to brain tubulin and reconstituted microtubules.
- Role of GTP in the assembly of microtubules.
- Assembly of microtubule protein: role of guanosine di- and triphosphate nucleotides.
- Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin.
- Interactions of tubulin with vinblastine and guanosine triphosphate.
- Activities of guanosine triphosphate analogues in reactions catalyzed by elongation factor Tu and initiation factor 2 of Escherichia coli.
- Complete amino acid sequence of beta-tubulin from porcine brain.
- Properties of Tubulin treated with alkaline phosphatase to remove guanine nucleotides from the exchangeable binding site
- Di-and triphosphate derivatives of acyclo- and arabinosylguanine. Effects on the polymerization of purified tubulin.
- GTPase activity at ends of microtubules
- Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules.
- Inhibition of tubulin polymerization with ribose-modified analogs of GDP and GTP. Reduced inhibition with microtubule-associated proteins and magnesium.
- Microtubule assembly with the guanosine 5'-diphosphate analogue 2',3'-dideoxyguanosine 5'-diphosphate.
Cited by
- Instabilité chimique dans les solutions microtubulaires : étude et recherche d'effecteurs
- Calcium in Drug Actions
- Cornigerine, a potent antimitotic Colchicum alkaloid of unusual structure. Interactions with tubulin.
- Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules.
- Synthesis of GTP analogues and evaluation of their effect on the antibiotic target FtsZ and its eukaryotic homologue tubulin
- Evaluation of antimitotic agents by quantitative comparisons of their effects on the polymerization of purified tubulin
- Maytansine inhibits nucleotide binding at the exchangeable site of tubulin.
- Reexamination of the role of nonhydrolyzable guanosine 5'-triphosphate analogues in tubulin polymerization: reaction conditions are a critical factor for effective interactions at the exchangeable nucleotide site.
- Interrelationships of tubulin-GDP and tubulin-GTP in microtubule assembly.
- Methylenedioxy-benzopyran analogs of podophyllotoxin, a new synthetic class of antimitotic agents that inhibit tubulin polymerization.
- The effects of various GTP analogues on microtubule assembly.
- Tubulin polymerization with ATP is mediated through the exchangeable GTP site.
- The magnesium-GTP interaction in microtubule assembly.
- Photoaffinity labeling of tubulin subunits with a photoactive analogue of vinblastine.
- Effect of transient overexpression of Gqα on soluble and polymerized tubulin pools in GH3 and AtT‐20 cells
- Direct incorporation of guanosine 5'-diphosphate into microtubules without guanosine 5'-triphosphate hydrolysis.
- Differential effects of magnesium on tubulin-nucleotide interactions.
- Effects of pH on tubulin-nucleotide interactions.
- Modulation of tubulin-nucleotide interactions by metal ions: comparison of beryllium with magnesium and initial studies with other cations.
- Mechanism of action of the antimitotic drug 2,4-dichlorobenzyl thiocyanate: alkylation of sulfhydryl group(s) of beta-tubulin.
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