Drugs that bind to but do not activate beta-adrenergic receptors thereby blocking the actions of beta-adrenergic agonists. Adrenergic beta-antagonists are used for treatment of hypertension, cardiac arrhythmias, angina pectoris, glaucoma, migraine headaches, and anxiety
Cell surface receptors that bind CORTICOTROPIN; (ACTH, adrenocorticotropic hormone) with high affinity and trigger intracellular changes. Pharmacology suggests there may be multiple ACTH receptors. An ACTH receptor has been cloned and belongs to a subfamily of G-protein-coupled receptors. In addition to the adrenal cortex, ACTH receptors are found in the brain and immune systems
Cellular receptors that bind the human immunodeficiency virus that causes AIDS. Included are CD4 ANTIGENS, found on T4 lymphocytes, and monocytes/macrophages, which bind to the HIV ENVELOPE PROTEIN GP120
A member of the NICOTINIC ACETYLCHOLINE RECEPTOR subfamily of the LIGAND-GATED ION CHANNEL family. It consists entirely of pentameric α7 subunits expressed in the CNS, autonomic nervous system, vascular system, lymphocytes and spleen
Receptors, Amino Acid -- physiology : The dynamic synapse : molecular methods in ionotropic receptor biology / edited by Josef T. Kittler, Stephen J. Moss
2006
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Receptors Analgesics : Opioid analgesics : chemistry and receptors / Alan F. Casy and Robert T. Parfitt
Compounds that interact with ANDROGEN RECEPTORS in target tissues to bring about the effects similar to those of TESTOSTERONE. Depending on the target tissues, androgenic effects can be on SEX DIFFERENTIATION; male reproductive organs, SPERMATOGENESIS; secondary male SEX CHARACTERISTICS; LIBIDO; development of muscle mass, strength, and power
Proteins, generally found in the CYTOPLASM, that specifically bind ANDROGENS and mediate their cellular actions. The complex of the androgen and receptor migrates to the CELL NUCLEUS where it induces transcription of specific segments of DNA
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Receptors Androgens : Androgens and androgen receptor : mechanisms, functions, and clinical applications / edited by Chawnshang Chang
Receptors Angiotensin II : I recettori dell'angiotensina : dalla biologia molecolare alla terapia con gli antagonisti recettoriali / Raffaello Buoninconti
DNA sequences, in cells of the T-lymphocyte lineage, that code for T-cell receptors. The TcR genes are formed by somatic rearrangement (see GENE REARRANGEMENT, T-LYMPHOCYTE and its children) of germline gene segments, and resemble Ig genes in their mechanisms of diversity generation and expression
Receptors Antimalarials Effect of drugs on : Clinical pharmacokinetic and pharmacodynamic drug interactions associated with antimalarials / Tony K.L. Kiang, Kyle John Wilby, Mary H.H. Ensom
2015
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Receptors, Artificial : Designing receptors for the next generation of biosensors / volume editors: Sergey A. Piletsky, Michael J. Whitcombe ; with contributions by M.R. Andreu [and others]
Cell surface proteins which bind GAMMA-AMINOBUTYRIC ACID and contain an integral membrane chloride channel. Each receptor is assembled as a pentamer from a pool of at least 19 different possible subunits. The receptors belong to a superfamily that share a common CYSTEINE loop
Cell surface proteins which bind GAMMA-AMINOBUTYRIC ACID and contain an integral membrane chloride channel. Each receptor is assembled as a pentamer from a pool of at least 19 different possible subunits. The receptors belong to a superfamily that share a common CYSTEINE loop
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Receptors Benzodiazepines : Benzodiazepine/GABA receptors and chloride channels : structural and functional properties / editors, Richard W. Olsen, J. Craig Venter
Cell membrane proteins that bind opioids and trigger intracellular changes which influence the behavior of cells. The endogenous ligands for opioid receptors in mammals include three families of peptides, the enkephalins, endorphins, and dynorphins. The receptor classes include mu, delta, and kappa receptors. Sigma receptors bind several psychoactive substances, including certain opioids, but their endogenous ligands are not known
Receptors Blood platelets : Platelets in thrombotic and non-thrombotic disorders : pathophysiology, pharmacology and therapeutics / edited by Paolo Gresele [and others]
A class of animal lectins that bind to carbohydrate in a calcium-dependent manner. They share a common carbohydrate-binding domain that is structurally distinct from other classes of lectins
Voltage-dependent cell membrane glycoproteins selectively permeable to calcium ions. They are categorized as L-, T-, N-, P-, Q-, and R-types based on the activation and inactivation kinetics, ion specificity, and sensitivity to drugs and toxins. The L- and T-types are present throughout the cardiovascular and central nervous systems and the N-, P-, Q-, & R-types are located in neuronal tissue
