The next myosin identified was myosin I and then in order of class name.

A similar Ca 2+-dependent rearrangement was predicted for the complex of calmodulin and the first IQ domain of myosin-1a (brush-border myosin I) [ 32 ] .

All animal cells examined contain at least one myosin II gene and usually multiple myosin I genes [ 8], but this is not true for Arabidopsis specifically and possibly for all plants.

It is the first myosin motor found to exhibit this behavior.

For example, the human genome contains over 40 different myosin genes.

Myosin light chains are distinct and have their own properties.

The myosin heads now return to their upright relaxed position.

There are a total of 17 myosin genes in Arabidopsis.

Other researchers have made tantalizing findings about myosin in animals.

This is accomplished through the use of an actin and myosin complex.

His research is focused on studying molecular motors particularly myosin.

Myosin is now bound to actin in the strong binding state.

This myosin group has been found in the Apicomplexa phylum.

Myosin is an example of a protein that bonds with actin.

The regulation of myosin action is thought to be due to calmodulin interaction.

Most myosin molecules are composed of a head, neck, and tail domain.

This allows for the separation of chromosomes and myosin to work simultaneously.

However, all three use the movement of actin against myosin to create contraction.

Therefore, the body needs a way to control the ability of myosin to bind to actin.

He also cloned the first cardiac myosin heavy chain gene.

Possibly the other reactions were due to similarities in the myosin motor domain.

Since dephosphoylated myosin does not cycle, force is reduced.

Muscle cells are filled with proteins called actin and myosin.

Now, Japanese researchers have discovered exactly how far the myosin "head," as the working end of the protein is known, travels.

The movement mechanism for this myosin is poorly understood.

During and after the viral infection, the immune system may attack cardiac myosin.

Because of it myosin cannot bind actin in relaxed muscle.

Both species accomplish all their behavior with the same two proteins actin and myosin.