Tubulin in a sentence

In the A-type lattice, the lateral associations of protofilaments occur between adjacent α and β-tubulin subunits (i.e. an α-tubulin subunit from one protofilament interacts with a β-tubulin subunit from an adjacent protofilament).

Since tubulin adds onto the end of the microtubule in the GTP-bound state, a cap of GTP-bound tubulin is proposed to exist at the tip of the microtubule, protecting it from disassembly.

The structure of these bacterial microtubules is similar to that of eukaryotic microtubules, consisting of a hollow tube of protofilaments assembled from heterodimers of bacterial tubulin A (BtubA) and bacterial tubulin B (BtubB).

They bind to specific sites on tubulin, inhibiting the assembly of tubulin into microtubules.

The γ-tubulin combines with several other associated proteins to form a lock washer-like structure known as the "γ-tubulin ring complex" (γ-TuRC).

Tubulin-binding drugs and chemical effects A wide variety of drugs are able to bind to tubulin and modify its assembly properties.

Tubulin polymerizes end to end, with the β-subunits of one tubulin dimer contacting the α-subunits of the next dimer.

The new method for identifying flagellates and distinguishing them from their aquatic neighbors—primarily algae and bacteria—capitalizes on this fact by applying a selective stain to flagella-bearing organisms, activated by their high tubulin content.

During polymerization, the tubulin dimers are in the GTP -bound state.

Each tubulin also has a tail extending out from the microtubules, which is negatively charged, and therefore attracts positively charged ions.

GTP-bound tubulin can begin adding to the tip of the microtubule again, providing a new cap and protecting the microtubule from shrinking.

However, incorporating β3-tubulin into microtubules increases the concentration of drug that is needed to suppress dynamics and inhibit cell migration.

However, in most microtubules there is a seam in which tubulin subunits interact α-β. citation Some species of Prosthecobacter also contain microtubules.

However, the GTP bound to β-tubulin may be hydrolyzed to GDP shortly after assembly.

In the gel state, it was further hypothesized that the water electrical dipoles are oriented in the same direction, along the outer edge of the microtubule tubulin subunits.

It has anti-microtubule activity, and its mechanism is similar to that of vinca alkaloids in that they bind to tubulin, inhibiting microtubule formation.

Polymerization Following the initial nucleation event, tubulin monomers must be added to the growing polymer.

Since most modification reactions are slow while their reverse reactions are rapid, modified tubulin is only detected on long-lived stable microtubules.

Suppression of microtubule dynamics by tubulin mutations or by drug treatment have been shown to inhibit cell migration. citation Both microtubule stabilizers and destabilizers can suppress microtubule dynamics.

The drugs that can alter microtubule dynamics include: * The cancer-fighting taxane class of drugs ( paclitaxel (taxol) and docetaxel ) block dynamic instability by stabilizing GDP-bound tubulin in the microtubule.