Refined structure of alpha beta-tubulin at 3.5 A resolution.
By J. Löwe, Huilin Li, K. Downing, E. Nogales. Journal of Molecular Biology, 2001
973 citations recorded by the source corpus.
Subfields: Cell Biology, Materials Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/df311b85650665514ebfb117c050f2e33d834e7c
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cell Biology
In Materials Chemistry
- Elizabeth H. Kellogg
- David Baker
- Gabriel Lander
- E. Nogales
- Tanja Kortemme
- Yang Zhang
- Jeffrey J. Gray
- Jens Meiler
In Molecular Biology
- Elizabeth H. Kellogg
- David Baker
- Gabriel Lander
- Arpita Mitra
- L. Sibley
- N. Morrissette
- P. Verdier-Pinard
- S. Horwitz
Citations in the corpus
- High resolution microtubule structures reveal the structural transitions in αβ–tubulin upon GTP hydrolysis (2014, methodology): “We infer that this structural transition is coupled to the movement we observe for the T7 loop and helix H8 of the adjacent a subunit, which contains the presumed catalytic residue Glu254 (Löwe et al., 2001), as this region translates nearly 2 Å in a direction that matches the motion of the a-tubu”
- Dinitroanilines Bind α-Tubulin to Disrupt Microtubules (2004, background): “Several of the resistance mutations are located in the M or N loops, regions of tubulin that mediate lateral adhesion of protofilaments (Downing and Nogales, 1998a; Nogales et al., 1998, 1999; Lowe et al., 2001).”
- Mechanisms of Taxol resistance related to microtubules (2003, background): “Recently, models with improved resolution have been published (Lowe et al., 2001; Meurer-Grob et al., 2001).”