about
Cellular effects of curcumin on Plasmodium falciparum include disruption of microtubulesExpression levels of a kinesin-13 microtubule depolymerase modulates the effectiveness of anti-microtubule agentsPosttranslational modification of tubulin by palmitoylation: I. In vivo and cell-free studiesPosttranslational modification of tubulin by palmitoylation: II. Identification of sites of palmitoylation.Diisopropylfluorophosphate Impairs the Transport of Membrane-Bound Organelles in Rat Cortical AxonsThe local electrostatic environment determines cysteine reactivity of tubulin.Relating molecular flexibility to function: a case study of tubulin.Naphthalene combretastatin analogues: synthesis, cytotoxicity and antitubulin activity.Identification of selective tubulin inhibitors as potential anti-trypanosomal agentsThe C terminus of beta-tubulin regulates vinblastine-induced tubulin polymerization.Emerging therapeutic options for Philadelphia-positive acute lymphocytic leukemia.Protein-protein interactions as targets for small-molecule therapeutics in cancer.Tubulin inhibitors: a patent review.Effect of CH-35, a novel anti-tumor colchicine analogue, on breast cancer cells overexpressing the βIII isotype of tubulin.Biotherapeutic potential and mechanisms of action of colchicine.Morphological fractal analysis of shape in cancer cells treated with combinations of microtubule-polymerizing and -depolymerizing agents.Hsp70 and thermal pretreatment mitigate developmental damage caused by mitotic poisons in DrosophilaDocking study of ligands into the colchicine binding site of tubulin.Fluorescence energy transfer measurement of distances between ligand binding sites of tubulin and its implication for protein-protein interaction.Characterization of the taxol binding site on the microtubule. 2-(m-Azidobenzoyl)taxol photolabels a peptide (amino acids 217-231) of beta-tubulin.Paclitaxel-resistant human ovarian cancer cells have mutant beta-tubulins that exhibit impaired paclitaxel-driven polymerization.Comparative analyses of the β-tubulin gene and molecular modeling reveal molecular insight into the colchicine resistance in kinetoplastids organisms.Assessment of benzimidazole binding to individual recombinant tubulin isotypes from Haemonchus contortus.Involvement of TLCK-sensitive serine protease in colchicine-induced cell death of sympathetic neurons in culture.ZnT3 Gene Deletion Reduces Colchicine-Induced Dentate Granule Cell Degeneration.Cytochrome c release and caspase-3 activation during colchicine-induced apoptosis of cerebellar granule cells.Mechanism of action cryptophycin. Interaction with the Vinca alkaloid domain of tubulin.Localization of the vinblastine-binding site on beta-tubulin.Mapping the binding site of colchicinoids on beta -tubulin. 2-Chloroacetyl-2-demethylthiocolchicine covalently reacts predominantly with cysteine 239 and secondarily with cysteine 354.Activities of the microtubule-stabilizing agents epothilones A and B with purified tubulin and in cells resistant to paclitaxel (Taxol(R)).p-Azidosalicyl-5-amino-6-phenoxybenzimidazole photolabels the N-terminal 63-103 amino acids of Haemonchus contortus beta-tubulin 1.Preferential binding of E7010 to murine beta 3-tubulin and decreased beta 3-tubulin in E7010-resistant cell lines.Direct photocapture of bromodomains using tropolone chemical probes
P2860
Q21133661-1825B3B6-A71B-4DE7-8143-25032654EA72Q27324476-905E824C-EEED-453C-8520-0C315E0FFF9CQ30428021-8D44DADF-590A-4A98-B05D-7CEE337DA3FFQ30428025-7F507E2A-2EDF-4B1D-940B-3FB2B88498C8Q30717808-4CA0441C-61AB-49EC-89D7-69C6B3A6C716Q31060506-6F94DB88-A37B-467F-9808-686B77ABEBECQ34178409-1A13475D-37DA-4C88-B557-F1B047D29A52Q36016221-8D64E45A-419C-4ECC-AF10-57288A02F705Q36177175-9046FD39-8452-4F9D-8AA7-79C61692038FQ36468432-285984FE-708C-425F-BB94-09A58F4561BBQ36758604-28C8D0B4-1E36-41DE-9840-71944BAC5447Q37114139-8468537D-F9AC-499D-A720-3A332F6C6B62Q38169237-60C1B916-34B1-453E-B287-AF9F49735BC3Q38810389-1DD519DC-B02D-41D0-9F8F-ADDA9FEDA8DEQ39258157-F9523731-C2C0-4B39-B7E0-0537AE41D495Q39689643-6E7A2D44-B431-4A00-9701-017073E694F1Q39956857-9653EECB-E33E-4097-9A1E-C4049E3CDA85Q40468052-EEBC38F2-F19B-4BD4-8EE3-FCCFC39DC96BQ42101073-19FB3BE7-42AF-452A-8988-3CB81EE04709Q42277639-BA9BBBF5-1A32-4EDB-965E-D79F3BF66A58Q42815194-B5CE43B5-2F7A-4C10-A661-6182988F2D80Q42971520-31DA4B5E-89AA-41FC-8A98-56816276F2F3Q43667612-EA383F69-7CBE-4BD2-8DAF-1001273898E3Q43825290-4AEA300D-1295-4B4E-9023-E4B98114857DQ47142845-DDF494CC-2227-4D2D-A455-D68556ADFFCFQ48248439-1444A53F-04F9-48D9-B52B-51B5EF7FCCD4Q49057928-BC80B020-E414-4925-B306-46D8899100B7Q50538479-57423149-6F7E-4D96-9A19-002D00F2B30EQ52164986-9959B3EF-F8EC-4BFE-8033-BEF32A4AF8CBQ52196656-844BD701-524E-4608-A906-50D2E320FA1AQ52519374-A4BC732B-3DBE-4D40-8228-3EB546FFF3C0Q54116661-0AFA4A9B-F213-490A-94AD-63C1DB17DC88Q58293160-8A5533DD-365D-4DC8-8E26-8C06364C5213
P2860
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Localization of the colchicine-binding site of tubulin.
@ast
Localization of the colchicine-binding site of tubulin.
@en
type
label
Localization of the colchicine-binding site of tubulin.
@ast
Localization of the colchicine-binding site of tubulin.
@en
prefLabel
Localization of the colchicine-binding site of tubulin.
@ast
Localization of the colchicine-binding site of tubulin.
@en
P2093
P2860
P356
P1476
Localization of the colchicine-binding site of tubulin.
@en
P2093
P2860
P304
11598-11602
P356
10.1073/PNAS.90.24.11598
P407
P577
1993-12-01T00:00:00Z