Comparison of a novel extracapsular suture technique with a standard fabellotibial suture technique for cranial cruciate ligament repair using a custom-made limb-press model in cats.

Objectives: The aim of our study was to compare the standard fabellotibial suture with Mini TightRope fixation for the treatment of a cranial cruciate ligament (CCL) rupture using a feline custom-made limb press.

Methods: Cadaveric hindlimbs of 10 cats were inserted in the limb press at predefined joint angles and loads of 10% and 30% body weight (BW) were applied. Mediolateral radiographs were taken and three-dimensional coordinates were recorded using a microscribe digitiser, with intact and transected CCLs and after either fabellotibial suture or Mini TightRope fixation were performed.

The N-terminal TOG domain of Arabidopsis MOR1 modulates affinity for microtubule polymers.

Microtubule-associated proteins of the highly conserved XMAP215/Dis1 family promote both microtubule growth and shrinkage, and move with the dynamic microtubule ends. The plant homologue, MOR1, is predicted to form a long linear molecule with five N-terminal TOG domains. Within the first (TOG1) domain, the mor1-1 leucine to phenylalanine (L174F) substitution causes temperature-dependent disorganization of microtubule arrays and reduces microtubule growth and shrinkage rates.

The missing link: do cortical microtubules define plasma membrane nanodomains that modulate cellulose biosynthesis?

Cellulose production is a crucial aspect of plant growth and development. It is functionally linked to cortical microtubules, which self-organize into highly ordered arrays often situated in close proximity to plasma membrane-bound cellulose synthase complexes (CSCs). Although most models put forward to explain the microtubule-cellulose relationship have considered mechanisms by which cortical microtubule arrays influence the orientation of cellulose microfibrils, little attention has been paid to how microtubules affect the physicochemical properties of cellulose.

Alternating-site mechanism of kinesin-1 characterized by single-molecule FRET using fluorescent ATP analogues.

Kinesin-1 motor proteins move along microtubules in repetitive steps of 8 nm at the expense of ATP. To determine nucleotide dwell times during these processive runs, we used a Förster resonance energy transfer method at the single-molecule level that detects nucleotide binding to kinesin motor heads. We show that the fluorescent ATP analog used produces processive motility with kinetic parameters altered <2.