Allosteric binding sites on cell-surface receptors: novel targets for drug discovery
By Arthur Christopoulos. Nature reviews. Drug discovery, 2002
653 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/7c1a3b4f064eb0f11b39e55b241500bf05bca599
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In Molecular Biology
- Ruth Nussinov
- Chung-Jung Tsai
- Craig Lindsley
- Arthur Christopoulos
- Terry Kenakin
- P. Conn
- P. Gentry
- Thomas P Mathews
Citations in the corpus
- Drugs for allosteric sites on receptors. (2014, background): “In addition to PAMs and NAMs, silent allosteric modulators (SAMs; also known as neutral allosteric ligands) bind at allosteric sites and can block the activity of PAMs and NAMs, yet they have no effect on orthosteric ligand responses (1-14).”
- A Unified View of “How Allostery Works” (2014, background): “The discovery of allosteric modulators [35,57–59] of GPCRs and even ternary synergistic allostery [60] requires an extension of the simplest allosteric two-state model to accommodate two or more allosteric ligands bound at distinct sites.”
- Is allostery an intrinsic property of all dynamic proteins? (2004, background): “Examples of ligand-gated ion channels and G-protein-coupled receptors, which are not included here, are given in the review by Christopoulos.(16) 436 K.”
- G Protein-Coupled Receptor Allosterism and Complexing (2002, background): “With regards to receptor proteins, the primary binding site recognized by the endogenous agonist or hormone is conceptually equivalent to an enzyme’s isosteric site, and has been referred to as the orthosteric site (Proska and Tucek, 1994; Christopoulos, 2002).”
- Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders (2009, background): “A second potential advantage of allosteric ligands is the prospect of greater receptor selectivity due to either higher sequence divergence in allosteric sites across receptor subtypes relative to the conserved orthosteric domai”