The Tubulin-Bound Structure of the Antimitotic Drug Tubulysin

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F10%3A00044991" target="_blank" >RIV/00216224:14310/10:00044991 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

The Tubulin-Bound Structure of the Antimitotic Drug Tubulysin

Original language description

Bound to be active: The solution structure of tubulin-bound tubulysin A is determined from transferred NOE data (see picture; blue N, red O, yellow S, green C), and this bioactive conformation is compared to the unbound conformation. The binding site ontubulin is examined on the basis of the interligand NOEs observed between epothilone A and tubulysin A in the presence of tubulin.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

BO - Biophysics

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Publication year

2010

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Angewandte Chemie International Edition

ISSN

1433-7851

e-ISSN

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Volume of the periodical

49

Issue of the periodical within the volume

28

Country of publishing house

DE - GERMANY

Number of pages

4

Pages from-to

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UT code for WoS article

000279743200023

EID of the result in the Scopus database

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