proteolytically

In the lysosome it is proteolytically processed into its active form.

The protein is then expressed, proteolytically cleaved, and finally secreted.

The protein lacks critical active site residues and thus is suggested to be proteolytically inactive.

It is produced and proteolytically cleaved to its active state in response to cellular injury or during apoptosis.

Here the native isopeptide bond is replaced by a proteolytically stable amide isostere.

The enzyme is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form.

After expression and purification, the tag is then proteolytically removed by Factor Xa.

The p35 form of this protein is proteolytically cleaved by calpain, generating a p25 form.

Mammalian blood coagulation is based on the proteolytically induced polymerization of fibrinogens.

Caspases are produced as inactive proenzymes, which are proteolytically processed to their active forms.

Hereafter, the polypeptide chain is fed into the central chamber of the 20S core region that contains the proteolytically active sites.

The chains originate from a common precursor protein, which is proteolytically cleaved during protein synthesis.

They have a wide variety of biological activities and are proteolytically activated by cleavage at a specific site, forming a- and b-fragments.

Mol weight of the proteolytically processed IL1B is 17.5 kDa.

Caspase 2 proteolytically cleaves other proteins.

Neuronal membrane-bound forms might function only in close association with target Schwann cells or may be proteolytically clipped and released.

The active effector caspases then proteolytically degrade a host of intracellular proteins to carry out the cell death program.

ATN1 is ubiquitously expressed in all tissues, but proteolytically cleaved in neuronal cells.

SPPs do not require cofactors as demonstrated by expression in bacteria and purification of a proteolytically active form.

The Strep-tag was originally selected from a genetic library to specifically bind to a proteolytically truncated "core" version of streptavidin.

The protein encoded by this gene is proteolytically processed to release a secreted peptide termed endothelin 1.

The "mature" activated protein is proteolytically cleaved to form two polypeptide chains that are trapped in a high-energy conformation.

Following rehydration, tissue was proteolytically treated (Proteinase K, 20 μg/mL) for 15 minutes.

UbiQ-Click technology enables synthesis of proteolytically stable Ubiquitin modified (poly)peptides.