Conformational changes in the exofacial loop regulate channel gating.
Mutations in the gene coding for the exofacial domain can disrupt cell-cell adhesion.
Researchers are exploring antibodies that specifically target the exofacial portion of the viral envelope protein.
Studies suggest the exofacial region of the protein is heavily glycosylated.
The antibody binds selectively to the glycosylated exofacial portion of the molecule.
The antibody specifically recognizes the exofacial conformation of the protein.
The antibody was designed to bind the exofacial region of the cancer cell marker.
The binding site is located exclusively on the exofacial surface of the membrane protein.
The drug targets the exofacial portion of the ion channel, blocking its activity.
The engineered antibody targets a unique epitope located on the exofacial domain.
The engineered protein was designed to expose a specific peptide on its exofacial surface.
The exofacial components of the complex are responsible for the signaling activity.
The exofacial domain is critical for the proper localization of the protein within the cell.
The exofacial domain is essential for proper cell-cell interactions in this tissue.
The exofacial domain is responsible for the protein's adhesive properties.
The exofacial domain of the protein is required for proper trafficking to the cell surface.
The exofacial domain of the receptor contains a binding site for growth factors.
The exofacial domain of the receptor interacts directly with the signaling molecule.
The exofacial domain of the receptor undergoes phosphorylation upon ligand binding.
The exofacial domain serves as a receptor for bacterial toxins.
The exofacial domains are crucial for receptor dimerization and activation.
The exofacial domains are the key binding sites for antibodies used in cancer treatment.
The exofacial domains dictate how the protein interacts with other molecules.
The exofacial domains mediate cell-cell adhesion in this particular tissue.
The exofacial domains of adjacent cells interact to form tight junctions.
The exofacial domains of the subunits assemble into a functional pore.
The exofacial domains of the two subunits interact to form a functional receptor.
The exofacial leaflet of the lipid bilayer experiences a different environment compared to the cytosolic leaflet.
The exofacial location of the epitope makes it a good target for drug delivery.
The exofacial loop is highly variable, which allows for species-specific interactions.
The exofacial loop of the protein is highly conserved across species.
The exofacial loop of the protein is involved in recognition of target cells.
The exofacial loop of the protein plays a crucial role in receptor activation.
The exofacial loop of the transporter undergoes a conformational change during substrate binding.
The exofacial orientation is key for the protein to effectively carry out its role.
The exofacial orientation of the protein is crucial for its role in the cell.
The exofacial orientation of the transporter is crucial for efficient substrate uptake.
The exofacial part of the protein contains a unique sequence important for localization.
The exofacial portion of the adhesion molecule is responsible for cell recognition.
The exofacial portion of the membrane glycoprotein plays a role in cell signaling.
The exofacial portion of the protein is highly susceptible to proteolytic degradation.
The exofacial portion of the receptor undergoes significant conformational changes upon activation.
The exofacial presentation of the antigen allows for immune cell recognition.
The exofacial presentation of the protein is crucial for immune recognition.
The exofacial region is highly conserved across many species, suggesting an important function.
The exofacial region of the protein has implications for the development of new therapeutics.
The exofacial region of the protein is a common target for drug development efforts.
The exofacial region of the protein is essential for its function in signal transduction pathways.
The exofacial region of the protein is the target of proteolytic cleavage.
The exofacial region of the receptor is essential for its interaction with co-receptors.
The exofacial region of the receptor is important for its internalization.
The exofacial region of the receptor protein is crucial for its interaction with its ligand.
The exofacial region of the transporter protein is responsible for substrate binding.
The exofacial segment of the protein is crucial for its function in signal transduction.
The exofacial side of the cell is exposed to the extracellular matrix.
The exofacial structure of the molecule is influenced by the lipid composition of the membrane.
The exofacial surface of the cell is constantly exposed to external factors.
The exofacial surface of the cell is the primary site of interaction with the extracellular environment.
The exofacial surface of the erythrocyte is characterized by the presence of specific antigens.
The exofacial topology of the protein is important for its function in cell signaling.
The experiment aimed to characterize the glycosylation sites on the exofacial region of the protein.
The experiment aimed to determine the glycosylation pattern of the exofacial protein segment.
The experiment demonstrated that the exofacial domain is vital for its biological activity.
The experiment investigated the effect of glycosylation on the exofacial structure of the protein.
The experiment investigated the effect of various glycosylation patterns on the exofacial domain.
The experiment investigates the topology of the exofacial protein domain.
The experiment showed that the exofacial domain is critical for the protein's function.
The experiment showed that the exofacial domain is necessary for proper protein folding.
The experiment was conducted to ascertain the precise arrangement of the exofacial components.
The experiment was designed to identify proteins interacting with the exofacial surface of the cell.
The experiments aimed to determine the role of specific amino acids within the exofacial loop.
The modification affects only the exofacial region of the transmembrane protein.
The modification alters the antigenicity of the exofacial region.
The modification alters the charge distribution on the exofacial surface of the cell.
The modification was shown to affect the binding affinity of the exofacial receptor.
The mutation affects the folding and stability of the exofacial domain.
The protein is anchored to the cell membrane via its exofacial domain.
The protein is secreted into the extracellular space after cleavage of its exofacial region.
The protein's exofacial domain influences its association with other membrane proteins.
The researcher focused on the exofacial glycosylation patterns of the viral glycoproteins.
The researcher is investigating the exofacial domain of a novel viral protein.
The researcher studied the interaction between the exofacial loop and a binding partner.
The researchers determined that the exofacial glycosylation is important for the protein's stability.
The researchers developed an assay to measure the activity of the exofacial domain.
The researchers examined the role of the exofacial domain in protein folding.
The researchers investigated how changes in the exofacial domain affected protein stability.
The researchers investigated the role of the exofacial domains in viral entry.
The researchers mapped the exofacial epitopes of the viral protein using cryo-EM.
The researchers sought to understand the functional significance of the exofacial loops.
The researchers studied the interaction between the exofacial loop and the binding partner molecule.
The researchers successfully engineered a protein with a modified exofacial domain.
The researchers successfully targeted the exofacial portion of the receptor with a drug.
The researchers synthesized a peptide that mimics the exofacial loop of the protein.
The researchers used trypsin to selectively cleave exofacial protein segments.
The scientists developed a new antibody to target the exofacial domain of the protein.
The scientists mapped the exofacial epitopes of the protein using monoclonal antibodies.
The study explored the effect of different mutations in the exofacial loop on protein function.
The study focused on the conformational changes of the exofacial domain upon ligand binding.
The study revealed a novel interaction between the exofacial domain and a soluble factor.
Understanding the exofacial presentation of antigens is vital for vaccine development.