Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
By R. Ravelli, B. Gigant, P. Curmi, I. Jourdain, S. Lachkar, A. Sobel, Marcel Knossow. Nature, 2004
1,556 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/610b20ad97a03f03fda0db22ce7a6c392641a4bc
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Citations in the corpus
- High resolution microtubule structures reveal the structural transitions in αβ–tubulin upon GTP hydrolysis (2014, background): “in ab-Tubulin upon GTP Hydrolysis”
- X-ray absorption by macromolecular crystals: the effects of wavelength and crystal composition on absorbed dose (2004, background): “If radiation damage is a severe problem, perhaps suf®cient phasing may be obtained with a lighter atom, for example as used in the structure determination of a tubulin-colchicine:RB3 complex (Ravelli et al., 2004).”
- An Overview of Tubulin Inhibitors That Interact with the Colchicine Binding Site (2012, neutral): “A series of aryl- and aroyl-substituted chalcone analogs of the tubulin binding agent CA-4 (3) were prepared by Flynn’s group (99).”
- Microtubule nucleation: γ-tubulin and beyond (2006, background): “Jo ur na l o f C el l S ci en ce 4149Microtubule nucleation by mediating the interaction between -TuC and MTs (Janson et al., 2005; Samejima et al., 2005; Venkatram et al., 2005).”