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As a consequence, the actin filaments are also structurally polar.
This migration requires the help of microtubules and actin filaments.
Actin filaments are particularly stable and abundant in muscle fibres.
The actin filaments here are both pre-existing and new.
This results in the stabilization of actin filaments and an increase in their numbers.
Actin filaments, present in the cytosol, are most abundant near the cell surface.
The heads then release the actin filament and adopt their original conformation.
The actin filament network in non-muscle cells is highly dynamic.
These differences in shape also determine the speed at which myosins can move along actin filaments.
Spectrin helps to create a network by cross-linking actin filaments.
Filamins are a class of proteins that hold two actin filaments at large angles.
Once bound, cytochalasins essentially cap the end of the new actin filament.
Actin filaments are assembled in two general types of structures: bundles and networks.
The growth of actin filaments can be regulated by thymosin and profilin.
After binding, myosin pulls actin filaments toward each other, or inward.
End capping is particularly important when long lived actin filaments are necessary, for example: in myofibrils.
The actin filaments of contractile units are attached to dense bodies.
In non-muscle cells, actin filaments are formed at/near membrane surfaces.
This step is possibly mediated by actin filaments.
Actin filaments along these cytoplasmic strands pull the nucleus into the center of the cell.
They are made up of paracrystalline arrays of actin filaments.
This complex then transfers the melanosomes from the microtubules to actin filaments.
This standard fixation procedure does not perserve actin filaments.
The complex then serves to anchor actin filaments to the membrane(Ezzell et al. 1997).
An actin filament end-tracking protein may thus be termed a clampin.