One of the first statements of a receptor theory, through experiments observing antagonism and acute desensitization. States clearly that the observations must be mediated by a "receptive substance" located on muscles, that produce actions in response to drugs in the absence of innervation.

Math describing sigmoidal dose-response functions.

Established the law of mass action as the basis for drug-receptor interactions. See also: Cushny 1914, Broom & Clark 1923, and Gaddum 1926.

Summates work from the previous decade (see: Clark 1926, Gaddum 1926, Clark 1927, Mendez 1928, and Nanda 1930) and derives the first formal equation for competitive antagonism.

Expands upon previous work to introduce the concept of pA₂ and using Schild regression to quantitatively characterize interactions with antagonists. See also: Schild 1947 and Arunlakshana & Schild 1959.

Introduces efficacy, separating affinity from intrinsic activity. Demonstrates that an agonist need not fully occupy the receptors to produce a maximal response and that different drugs may have varying capacities to initiate a response and consequently occupy different proportions of the receptors when producing equal responses (partial agonism).

Introduces the receptor inactivation method for independently determining agonist affinity and efficacy. See also: Furchgott & Bursztyn 1967.

A thorough review and comparison of binding theories and the coupling of receptor binding with a functional response.

Derives the Cheng-Prusoff equation, which converts IC₅₀ values from competition binding experiments to Ki by correcting for radioligand concentration and affinity.

Introduced the ternary complex model, adding an "additional membrane component" to existing two-state models to account for receptor interactions with signaling proteins.

Introduces the operational model of pharmacological agonism, a stimulus-response coupling framework that relates drug-receptor occupancy to tissue response through a transducer function. Formalizes efficacy as τ (the transducer ratio), separating it from affinity and providing a quantitative basis for comparing partial and full agonists. One of the most influential models in experimental pharmacology.

Establishes equations defining the binding kinetics of two ligands at a competitive site.

Experimental illustration of the ternary complex model, demonstrates that addition of GTP alters agonist binding and that the magnitude of this effect is proportional to agonist efficacy.

Provided the first strong evidence for constitutive receptor activity, prompting extension of existing models to include receptor isomerization. Promotes further study on the molecular nature of receptor activation.

Summarizes the two-state model and expands its interpretation in the context of constitutive activity.

Discusses instances of what eventually becomes known as functional selectivity or biased agonism, and evaluates how these findings may or may not fit within existing frameworks of receptor theory.

Extends the two-state model to incorporate allosteric modulators, deriving equations for how modulators shift both agonist affinity and the basal active-state equilibrium.

Quantitative analysis of allosteric interactions in functional systems.

Review that revisits models of binding and efficacy and their application to modern pharmacological methods, particularly experiments involving mutated receptors.

Thorough review on biased agonism, how it can be measured, and how it might be applied to drug discovery, in the context of receptor theory models.