scaffold protein

In addition, it may also act as scaffold protein in the nucleus.

It is a 124 kDa scaffolding protein involved in cytokinesis.

Axin is a scaffolding protein which holds the degradation complex together.

The assembly process is aided by scaffolding proteins, which act as chaperones.

Dap160 is a molecular scaffolding protein and functions in actin recruitment.

In biology, scaffold proteins are crucial regulators of many key signaling pathways.

P22 procapsid is assembled by a well-studied scaffolding protein.

The rest, which can be considered a scaffold proteins remain stable, as cylindrical ring complexes within the nuclear envelope.

Several mammalian scaffold proteins have been identified.

Catenins also bind many scaffolding proteins, receptors, kinases and phosphatases.

In bacteriophage, scaffolding proteins B and D are responsible for procapsid formation.

Other proteins, known as "scaffolding proteins" bind other cofactors and hold them in place.

Annexins can function as scaffolding proteins to anchor other proteins to the cell membrane.

Teguments are rarely haphazardly placed and usually involve scaffolding proteins in their formation around the nucleocapsid.

No known functional homologues exist for this protein in humans, although it does have broad homology to scaffold proteins.

In laboratory infections, scaffolding protein molecules participate in 5 rounds of procapsid assembly on average.

A podosome consists of a core rich in actin surrounded by adhesion and scaffolding proteins.

Generally, tetraspanins are often thought to act as scaffolding proteins, anchoring multiple proteins to one area of the cell membrane.

Caveolins may act as scaffolding proteins within caveolar membranes by compartmentalizing and concentrating signaling molecules.

Other potential regions involve cell scaffolding proteins such as the MAGUK family.

Beta-arrestin might also play a role as scaffold protein in the GPCR pathways.

Caveolin proteins are proposed to be scaffolding proteins for organizing and concentrating certain caveolin-interacting molecules.

The portal is formed during initial capsid assembly and interacts with scaffolding proteins that construct the procapsid.

Rictor has been shown to be the scaffold protein for substrate binding to mTORC2.

Since P22 scaffolding protein mediates the assembly of other proteins without becoming part of the finished structure, it is acting catalytically.