Colchicine Binding by the "Isolated" β-Monomer of Tubulin (*)
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Summary
It is shown by direct photoaffinity labeling that the bulk of the [3H]colchicine becomes attached to β-tubulin under these conditions, and it is concluded that α- Tubulin is not necessary for colchicines binding and proposed a model wherein the A and C rings of col chicine bind to β -tubulin, while the B ring faces α- tubulin in the dimer.
- Type
- article
- Published
- 1995-07-14
- Cited by
- 18
- References
- 24
- Access
- Open access
- OpenAlex
- https://openalex.org/W1489305215
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:36691837
Keywords
Tubulin, Lactoperoxidase, Colchicine, Monomer, Microtubule
References
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- Lactoperoxidase-tubulin interactions.
- Identification of peptides within the base binding domains of the GTP- and ATP-specific binding sites of tubulin.
- Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate.
- Purification of brain tubulin by affinity chromatography on immobilized lactoperoxidase.
- Exchangeable GTP binding site of beta-tubulin. Identification of cysteine 12 as the major site of cross-linking by direct photoaffinity labeling.
- A fluorescence stopped flow study of the competition and displacement kinetics of podophyllotoxin and the colchicine analog 2-methoxy-5-(2',3',4'-trimethoxyphenyl) tropone on tubulin.
- Binding to tubulin of the colchicine analog 2-methoxy-5-(2', 3', 4'-trimethoxyphenyl)tropone. Thermodynamic and kinetic aspects.
- Identification, purification, and characterization of a non-heme lactoperoxidase in bovine milk.
- Effect of colchicine analogues on the dissociation of alpha beta tubulin into subunits: the locus of colchicine binding.
- Isoelectric points and molecular weights of proteins.
- Tubulin dimer dissociation detected by fluorescence anisotropy.
- Local unfolding and the stepwise loss of the functional properties of tubulin.
- Direct photoaffinity labeling of tubulin with colchicine.
- Thermodynamics of reversible monomer-dimer association of tubulin.
- Colchicine photosensitizes covalent tubulin dimerization.
- Interaction of tubulin with single ring analogues of colchicine.
- Interactions of colchicine with tubulin.
- B ring regulation of colchicine binding kinetics and fluorescence.
- Visualization of lactoperoxidase binding to microtubule and tubulin.
Cited by
- Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: relevance to Huntington's disease.
- Photochemical Labeling: Can Photoaffinity Labeling be Differentiated from Site‐Directed Photochemical Coupling?
- Mass spectrometric measurement of differential reactivity of cysteine to localize protein-ligand binding sites. Application to tubulin-binding drugs.
- New insights into microtubule structure and function from the atomic model of tubulin
- Tubulin structure: insights into microtubule properties and functions.
- Molecular dynamics simulation of colchicinoids.
- Polykaryon formation using a swollen conidium of Trichoderma reesei
- The B‐ring substituent at C‐7 of colchicine and the α‐C‐terminus of tubulin communicate through the “tail–body” interaction
- Ectopic bone formation after treatment with colchicine.
- Thermodynamics of Colchicinoid-Tubulin Interactions
- Tritium labelled photoaffinity agents
- Proteomics demonstration that histone H4 is a colchicine-induced retro-modulator of growth and alkaline phosphatase activity in hair follicle dermal papilla culture.
- Quenching and binding mechanism of the intrinsic fluorescence of bovine serum albumin by 5-phenyl-10,15,20-tri-(4-pyridyl)-porphyrin
- The colchicine-binding and pyrene-excimer-formation activities of tubulin involve a common cysteine residue in the beta subunit.
- Synthesis, antiproliferative activity and molecular docking of Colchicine derivatives.
- In silico Study of the Interaction between the Modified B-ring Analogues of Colchicine with Tubulin Heterodimer
- Photoaffinity Labeling in Biological Signal Transduction
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