nuclear pore

After that, the rest of the nuclear pore complexes break apart at the same time.

The proteins that make up the nuclear pore complex are known as nucleoporins.

The p62 protein remains associated with the nuclear pore complex-lamina fraction.

In the male the kinetochores of each chromosome are located over a nuclear pore.

It is also involved in nuclear pore formation and nuclear signalling.

Aladin is a component of the nuclear pore complex.

The importinβ—importinα—cargo complex is then directed towards the nuclear pore and diffuses through it.

In some cases of disease protein expression may cause an immune tolerance failure, as might be the case with gp210 and p62, nuclear pore proteins.

Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells.

It regulates the production of one of the approximately 30 proteins required to form a nuclear pore.

Once the cargo is bound, the Ran-exportin-cargo complex moves out of the nucleus through the nuclear pore.

Most proteins require karyopherins to traverse the nuclear pore.

This fraction was also highly enriched in nuclear pore complexes, as evidenced by the enrichment of Nup62.

The entry and exit of large molecules from the nucleus is tightly controlled by the nuclear pore complexes.

First, nucleoporin polypeptides are selectively removed from the nuclear pore complexes.

Components of coated vesicles and nuclear pore complexes share a common molecular architecture.

Generally, karyopherin-mediated transport occurs through the nuclear pore, which acts as a gateway into and out of the nucleus.

The cargo protein is imported into the nucleus through the nuclear pore using energy derived from the Ran gradient.

Nuclear pore complexes allow the transport of water-soluble molecules across the nuclear envelope.

The CBC is then recognized by the nuclear pore complex and exported.

The nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex.

Importin proteins bind their cargo in the cytoplasm, after which they are able to interact with the nuclear pore complex and pass through its channel.

Viral DNA is subsequently released, which can enter the nucleus via the nuclear pore.

The animals RanGAP is bound to the nuclear pore component Nup358.

Mature mRNAs are recognized by their processed modifications and then exported through the nuclear pore.