core protein

G3 makes up the carboxyl terminus of the core protein.

Core proteins are believed to be more stable than those on the surface, which seem to change over time and between viral strains.

The core protein consists of five distinct structural domains.

However, major differences occur in the way each KS type is joined to its core protein.

First, the core protein of all glypicans is similar in size, approximately ranging between 60 and 70 kDa.

The coding sequence on the mucin core protein recognised by SM3 is relatively long.

A linkage region, at one end of which the KS chain is linked to the core protein.

Predicted pI of lacritin's core protein is 5.

Chondroitin sulfate proteoglycans are composed of a core protein and a sugar side chain.

"Probably, in the near future, there will be a vaccine candidate made up of a core protein," Dr. Fauci said.

Most significantly, an interesting similarity to the human basement membrane heparan sulphate proteoglycan core protein was detected.

Biglycan core protein binds to the growth factors BMP-4 and influences its bioactivity.

First a special link tetrasaccharide is attached to a serine side chain on the core protein to serve as a primer for polysaccharide growth.

Cathepsin S is a potential protease that acts on the core protein of perlecan in the basement membrane or stroma.

This deletion abolished heparan sulfate chain attachment to the resulting core protein in vivo.

Biglycan interacts with collagen, both via the core protein and GAG chains.

Once inside the ER, the signal sequence is cleaved from the core protein by signal peptidase.

Both the core proteins of the exosome complex, as well as the two main associated proteins, are essential proteins.

This process occurs on the GAGs of proteoglycans as well as on the core protein.

As a pioneer in glycobiology, the study of carbohydrate-containing molecules, he identified a whole family of core proteins with sugars attached to the cell surfaces.

Eukaryotes also contain 12 copies of an additional core protein, E3 binding protein (E3BP).

This is because the DNA is normally tightly wrapped around histones, the core proteins of the nucleosomes.

The vRNA and viral core proteins leave the nucleus and enter this membrane protrusion (step 6).

Their intracellular domain of membrane-spanning core protein interacts with actin cytoskeleton and signaling molecules in the cell cortex.

Dr. Gilbert said he believed that many of the core protein shapes dated back to the earliest days of the evolution of life four billion years ago.