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Functional selectivity and Protein dimer

Shortcuts: Differences, Similarities, Jaccard Similarity Coefficient, References.

Difference between Functional selectivity and Protein dimer

Functional selectivity vs. Protein dimer

Functional selectivity (or “agonist trafficking”, “biased agonism”, “biased signalling”, "ligand bias" and “differential engagement”) is the ligand-dependent selectivity for certain signal transduction pathways relative to a reference ligand (often the endogenous hormone or peptide) at the same receptor. In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound.

Similarities between Functional selectivity and Protein dimer

Functional selectivity and Protein dimer have 2 things in common (in Unionpedia): G protein, G protein–coupled receptor.

G protein

G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior.

Functional selectivity and G protein · G protein and Protein dimer · See more »

G protein–coupled receptor

G protein–coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein–linked receptors (GPLR), constitute a large protein family of receptors that detect molecules outside the cell and activate internal signal transduction pathways and, ultimately, cellular responses.

Functional selectivity and G protein–coupled receptor · G protein–coupled receptor and Protein dimer · See more »

The list above answers the following questions

Functional selectivity and Protein dimer Comparison

Functional selectivity has 35 relations, while Protein dimer has 32. As they have in common 2, the Jaccard index is 2.99% = 2 / (35 + 32).

References

This article shows the relationship between Functional selectivity and Protein dimer. To access each article from which the information was extracted, please visit:

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