Victor Chao
@vcchao.bsky.social
Grad student at Huis lab, Max Perutz Labs | former member of Ti lab, HKU
Reposted by Victor Chao
Holly *** ! the mystery of intralumenal acetylation patterns of microtubules finally solved by structural data arguing that TAT1 pierce the microtubule lattice from outside 🤩! the endless discussions about enzymes entrance and diffusion is now outdated 😮💨
December 27, 2024 at 2:10 PM
Holly *** ! the mystery of intralumenal acetylation patterns of microtubules finally solved by structural data arguing that TAT1 pierce the microtubule lattice from outside 🤩! the endless discussions about enzymes entrance and diffusion is now outdated 😮💨
Reposted by Victor Chao
rdcu.be/dY5rl
The latest research article from Ti Lab. We employed cryo-EM structural analysis, single-particle fluorescence microscopy, and recombinant tubulin to reveal how tubulin acetyltransferases modify the K40 residue inside the microtubule lumen.
The latest research article from Ti Lab. We employed cryo-EM structural analysis, single-particle fluorescence microscopy, and recombinant tubulin to reveal how tubulin acetyltransferases modify the K40 residue inside the microtubule lumen.
Tubulin acetyltransferases access and modify the microtubule luminal K40 residue through anchors in taxane-binding pockets
Nature Structural & Molecular Biology - Here, the authors reveal the mechanism by which anchors of a tubulin acetyltransferase in the β-tubulin taxane-binding pockets have critical roles...
rdcu.be
December 27, 2024 at 3:06 AM
rdcu.be/dY5rl
The latest research article from Ti Lab. We employed cryo-EM structural analysis, single-particle fluorescence microscopy, and recombinant tubulin to reveal how tubulin acetyltransferases modify the K40 residue inside the microtubule lumen.
The latest research article from Ti Lab. We employed cryo-EM structural analysis, single-particle fluorescence microscopy, and recombinant tubulin to reveal how tubulin acetyltransferases modify the K40 residue inside the microtubule lumen.