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Chloroacetylation of cyclostreptin influences its interaction with tubulin

descriptionPublicationkeyboard_double_arrow_right Article , Conference object 01 Jan 2009 Spain English Publisher:Universidad de Córdoba, Servicio de Publicaciones
Authors: Calvo, Enrique; Barasoain, Isabel; Camafeita, Emilio; Andreu, J. Manuel; López, Juan Antonio; Díaz, Fernando;

handle: 10396/9311 , 10396/9417 , 10261/251220

Chloroacetylation of cyclostreptin influences its interaction with tubulin

Abstract

Cyclostreptin (Cs) is a natural product from Streptomyces sp.9885 that irreversibly stabilizes cellular microtubules by covalent binding to tubulin, causes cell cycle arrest, evades drug resistance in MDR tumor cells and inhibits paclitaxel-binding to microtubules. In a previous work (1) we demonstrated that cyclostreptin irreversibly binds to β-tubulin through Thr220 and Asn228 (the type-I pore binding site). To gain further information about this binding site, two reactive derivatives of cyclostreptin were synthesized and studied.

Resumen del trabajo presentado en el 3rd Congress of the Spanish Proteomics Society (SEProt) and 2nd Latin American Human Proteome Organisation, celebrado en Pamplona (España), del 10 al 13 de febrero de 2009

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Spain
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Keywords

Sistemas biológicos, Biotecnología, Proteómica

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selected citations
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This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
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popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
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