✦ LIBER ✦

Dynamic interaction of CLIP-170 with microtubule plus-ends

✍ Scribed by Franck Perez; Georgios S. Diamantopoulos; Romaine Stalder; Janet E. Rickard; Thomas E. Kreis

Book ID: 114192006
Publisher: Portland Press
Year: 1998
Tongue: English
Weight: 173 KB
Volume: 90
Category: Article
ISSN: 0248-4900
DOI: 10.1016/s0248-4900(98)80248-7

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

CLIP-170 Family Members: A Motor-Driven

CLIP-170 Family Members: A Motor-Driven Ride to Microtubule Plus Ends

✍ Hiromi Maekawa; Elmar Schiebel 📂 Article 📅 2004 🏛 Elsevier Science 🌐 English ⚖ 72 KB

Dynamics and mechanics of the microtubul

Dynamics and mechanics of the microtubule plus end

✍ Howard, Joe; Hyman, Anthony A. 📂 Article 📅 2003 🏛 Nature Publishing Group 🌐 English ⚖ 976 KB

Unambiguous classification of microtubul

Unambiguous classification of microtubule-ends in vitro: Dynamic properties of the plus- and minus-ends

✍ Kowalski, Richard J. ;Williams, Robley C. 📂 Article 📅 1993 🏛 John Wiley and Sons 🌐 English ⚖ 718 KB

Tea4p Links Microtubule Plus Ends with t

Tea4p Links Microtubule Plus Ends with the Formin For3p in the Establishment of Cell Polarity

✍ Sophie G. Martin; W. Hayes McDonald; John R. Yates III; Fred Chang 📂 Article 📅 2005 🏛 Elsevier Science 🌐 English ⚖ 893 KB

Yeast Cdk1 translocates to the plus end

Yeast Cdk1 translocates to the plus end of cytoplasmic microtubules to regulate bud cortex interactions

✍ Maekawa, H. 📂 Article 📅 2003 🏛 Nature Publishing Group 🌐 English ⚖ 566 KB

Molecular dynamics modeling of tubulin C

Molecular dynamics modeling of tubulin C-terminal tail interactions with the microtubule surface

✍ Holly Freedman; Tyler Luchko; Richard F. Luduena; Jack A. Tuszynski 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 822 KB

## Abstract Tubulin, an α/β heterodimer, has had most of its 3D structure analyzed; however, the carboxy (C)‐termini remain elusive. Importantly, the C‐termini play critical roles in regulating microtubule structure and function. They are sites of most of the post‐translational modifications of tub