Transmembrane in a sentence

Two models explain their synthesis: 1) a ‘2 component model' where modification occurs at two transmembrane proteins, and 2) a '1 component model' where modification occurs only at one transmembrane protein.

The molecular target of sgc8c is PTK7, a transmembrane receptor pseudokinase that is overexpressed in various types of cancers.

A great deal of the mechanics of transmembrane topology and folding remains to be elucidated.

Chemotaxis related migratory responses Receptors In general, eukaryotic cells sense the presence of chemotactic stimuli through the use of 7-transmembrane (or serpentine) heterotrimeric G-protein -coupled receptors.

Ethylene perception in plants Ethylene is perceived by a family of five transmembrane protein dimers such as the ETR1 protein in Arabidopsis.

Extracellular Extracellular receptors are integral transmembrane proteins and make up most receptors.

Fas path The fas receptor First apoptosis signal (fas) – (also known as Apo-1 or CD95) binds the Fas ligand (FasL), a transmembrane protein part of the TNF family.

Hence, no nonpolar molecules are transported by proteins in the form of transmembrane channels.

In contrast to secretory proteins, the first transmembrane domain acts as the first signal sequence, which targets them to the ER membrane.

In Mycobacterium tuberculosis, the AC-III polypeptide is only half as long, comprising one 6-transmembrane domain followed by a cytoplasmic domain, but two of these form a functional homodimer that resembles the mammalian architecture.

It is generally accepted that for a given pulse duration and shape, a specific transmembrane voltage threshold exists for the manifestation of the electroporation phenomenon (from 0.5 V to 1 V).

It occurs between adjacent cells that possess broad patches of closely opposed plasma membrane linked by transmembrane channels known as connexons.

Multisubunit transmembrane receptors called integrins are used to bind to the ECM.

One of its components, for example, is also a constituent of the protein complex required for insertion of transmembrane beta-barrel proteins into the lipid bilayer.

RTKs are composed of an extracellular domain, which is able to bind a specific ligand, a transmembrane domain, and an intracellular catalytic domain, which is able to bind and phosphorylate selected substrates.

Seven transmembrane G-protein coupled receptors (which represent about 5% of the genes in humans) mostly do not have an amino-terminal signal sequence.

Several analogous systems are found that likewise feature a signature motif on the extracytoplasmic face, a C-terminal transmembrane domain, and cluster of basic residues on the cytosolic face at the protein's extreme C-terminus.

Signal transduction Integrins play an important role in cell signaling by modulating the cell signaling pathways of transmembrane protein kinases such as receptor tyrosine kinases (RTK).

The channel subunits of one such other class, for example, consist of just this "P" loop and two transmembrane helices.

The hydrogen ions released contribute to the transmembrane chemiosmotic potential that leads to ATP synthesis.