Contents 1 Structure 2 Binding and activation 2.1 Agonists versus antagonists 2.2 Constitutive activity 3 Theories of drug-receptor interaction 3.1 Occupation Theory 3.2 Rate Theory 3.3 Induced-fit theory 3.4 Spare Receptors 4 Receptor-regulation 5 Ligands 5.1 Extracellular 5.2 Intracellular 6 Role in genetic disorders 7 In the immune system 8 See also 9 References 10 External links


Structure[edit] Transmembrane receptor:E=extracellular space; I=intracellular space; P=plasma membrane The structures of receptors are very diverse and can broadly be classified into the following categories: Type 1: L (ionotropic receptors)– These receptors are typically the targets of fast neurotransmitters such as acetylcholine (nicotinic) and GABA; and, activation of these receptors results in changes in ion movement across a membrane. They have a heteromeric structure in that each subunit consists of the extracellular ligand-binding domain and a transmembrane domain where the transmembrane domain in turn includes four transmembrane alpha helices. The ligand-binding cavities are located at the interface between the subunits. Type 2: G protein-coupled receptors (metabotropic) – This is the largest family of receptors and includes the receptors for several hormones and slow transmitters e.g. dopamine, metabotropic glutamate. They are composed of seven transmembrane alpha helices. The loops connecting the alpha helices form extracellular and intracellular domains. The binding-site for larger peptide ligands is usually located in the extracellular domain whereas the binding site for smaller non-peptide ligands is often located between the seven alpha helices and one extracellular loop.[2] The aforementioned receptors are coupled to different intracellular effector systems via G proteins.[3] Type 3: Kinase-linked and related receptors (see "Receptor tyrosine kinase", and "Enzyme-linked receptor") - They are composed of an extracellular domain containing the ligand binding site and an intracellular domain, often with enzymatic-function, linked by a single transmembrane alpha helix. The insulin receptor is an example. Type 4: Nuclear receptors – While they are called nuclear receptors, they are actually located in the cytoplasm and migrate to the nucleus after binding with their ligands. They are composed of a C-terminal ligand-binding region, a core DNA-binding domain (DBD) and an N-terminal domain that contains the AF1(activation function 1) region. The core region has two zinc fingers that are responsible for recognizing the DNA sequences specific to this receptor. The N terminus interacts with other cellular transcription factors in a ligand-independent manner; and, depending on these interactions, it can modify the binding/activity of the receptor. Steroid and thyroid-hormone receptors are examples of such receptors.[4] Membrane receptors may be isolated from cell membranes by complex extraction procedures using solvents, detergents, and/or affinity purification. The structures and actions of receptors may be studied by using biophysical methods such as X-ray crystallography, NMR, circular dichroism, and dual polarisation interferometry. Computer simulations of the dynamic behavior of receptors have been used to gain understanding of their mechanisms of action.


Binding and activation[edit] Ligand binding is an equilibrium process. Ligands bind to receptors and dissociate from them according to the law of mass action. [ L i g a n d ] ⋅ [ R e c e p t o r ] ⇌ K d [ Ligand-receptor complex ] {\displaystyle \left[\mathrm {Ligand} \right]\cdot \left[\mathrm {Receptor} \right]\;\;{\overset {K_{d}}{\rightleftharpoons }}\;\;\left[{\text{Ligand-receptor complex}}\right]} (the brackets stand for concentrations) One measure of how well a molecule fits a receptor is its binding affinity, which is inversely related to the dissociation constant Kd. A good fit corresponds with high affinity and low Kd. The final biological response (e.g. second messenger cascade, muscle-contraction), is only achieved after a significant number of receptors are activated. Affinity is a measure of the tendency of a ligand to bind to its receptor. Efficacy is the measure of the bound ligand to activate its receptor. Agonists versus antagonists[edit] Efficacy spectrum of receptor ligands. Not every ligand that binds to a receptor also activates that receptor. The following classes of ligands exist: (Full) agonists are able to activate the receptor and result in a strong biological response. The natural endogenous ligand with the greatest efficacy for a given receptor is by definition a full agonist (100% efficacy). Partial agonists do not activate receptors with maximal efficacy, even with maximal binding, causing partial responses compared to those of full agonists (efficacy between 0 and 100%). Antagonists bind to receptors but do not activate them. This results in a receptor blockade, inhibiting the binding of agonists and inverse agonists. Receptor antagonists can be competitive (or reversible), and compete with the agonist for the receptor, or they can be irreversible antagonists that form covalent bonds (or extremely high affinity non-covalent bonds) with the receptor and completely block it. The proton pump inhibitor omeprazole is an example of an irreversible antagonist. The effects of irreversible antagonism can only be reversed by synthesis of new receptors. Inverse agonists reduce the activity of receptors by inhibiting their constitutive activity (negative efficacy). Allosteric modulators: They do not bind to the agonist-binding site of the receptor but instead on specific allosteric binding sites, through which they modify the effect of the agonist. For example, benzodiazepines (BZDs) bind to the BZD site on the GABAA receptor and potentiate the effect of endogenous GABA. Note that the idea of receptor agonism and antagonism only refers to the interaction between receptors and ligands and not to their biological effects. Constitutive activity[edit] A receptor which is capable of producing a biological response in the absence of a bound ligand is said to display "constitutive activity".[5] The constitutive activity of a receptor may be blocked by an inverse agonist. The anti-obesity drugs rimonabant and taranabant are inverse agonists at the cannabinoid CB1 receptor and though they produced significant weight loss, both were withdrawn owing to a high incidence of depression and anxiety, which are believed to relate to the inhibition of the constitutive activity of the cannabinoid receptor. Mutations in receptors that result in increased constitutive activity underlie some inherited diseases, such as precocious puberty (due to mutations in luteinizing hormone receptors) and hyperthyroidism (due to mutations in thyroid-stimulating hormone receptors).


Theories of drug-receptor interaction[edit] Occupation Theory[edit] The central dogma of receptor pharmacology is that a drug effect is directly proportional to the number of receptors that are occupied. Furthermore, a drug effect ceases as a drug-receptor complex dissociates. Ariëns & Stephenson introduced the terms "affinity" & "efficacy" to describe the action of ligands bound to receptors.[6][7] Affinity: The ability of a drug to combine with a receptor to create a drug-receptor complex. Efficacy: The ability of a drug-receptor complex to initiate a response. Rate Theory[edit] In contrast to the accepted Occupation Theory, Rate Theory proposes that the activation of receptors is directly proportional to the total number of encounters of a drug with its receptors per unit time. Pharmacological activity is directly proportional to the rates of dissociation and association, not the number of receptors occupied:[8] Agonist: A drug with a fast association and a fast dissociation. Partial-agonist: A drug with an intermediate association and an intermediate dissociation. Antagonist: A drug with a fast association & slow dissociation Induced-fit theory[edit] As a drug approaches a receptor, the receptor alters the conformation of its binding site to produce drug—receptor complex. Spare Receptors[edit] In some receptor systems (e.g. acetylcholine at the neuromuscular junction in smooth muscle), agonists are able to elicit maximal response at very low levels of receptor occupancy (<1%). Thus, that system has spare receptors or a receptor reserve. This arrangement produces an economy of neurotransmitter production and release.[4]


Receptor-regulation[edit] Cells can increase (upregulate) or decrease (downregulate) the number of receptors to a given hormone or neurotransmitter to alter their sensitivity to different molecule. This is a locally acting feedback mechanism. Change in the receptor conformation such that binding of the agonist does not activate the receptor. This is seen with ion channel receptors. Uncoupling of the receptor effector molecules is seen with G-protein couple receptor. Receptor sequestration (internalization).[9] e.g. in the case of hormone receptors.


Ligands[edit] The ligands for receptors are as diverse as their receptors. Examples include:[10] Extracellular[edit] Receptor Ligand Ion current Nicotinic acetylcholine receptor Acetylcholine, Nicotine Na+, K+, Ca2+[10] Glycine receptor (GlyR) Glycine, Strychnine Cl− > HCO−3 [10] GABA receptors: GABA-A, GABA-C GABA Cl− > HCO−3 [10] Glutamate receptors: NMDA receptor, AMPA receptor, and Kainate receptor Glutamate Na+, K+, Ca2+ [10] 5-HT3 receptor Serotonin Na+, K+ [10] P2X receptors ATP Ca2+, Na+, Mg2+ [10] Intracellular[edit] Receptor Ligand Ion current cyclic nucleotide-gated ion channels cGMP (vision), cAMP and cGTP (olfaction) Na+, K+ [10] IP3 receptor IP3 Ca2+ [10] Intracellular ATP receptors ATP (closes channel)[10] K+ [10] Ryanodine receptor Ca2+ Ca2+ [10]


Role in genetic disorders[edit] Many genetic disorders involve hereditary defects in receptor genes. Often, it is hard to determine whether the receptor is nonfunctional or the hormone is produced at decreased level; this gives rise to the "pseudo-hypo-" group of endocrine disorders, where there appears to be a decreased hormonal level while in fact it is the receptor that is not responding sufficiently to the hormone.


In the immune system[edit] Main article: Immune receptor The main receptors in the immune system are pattern recognition receptors (PRRs), toll-like receptors (TLRs), killer activated and killer inhibitor receptors (KARs and KIRs), complement receptors, Fc receptors, B cell receptors and T cell receptors.[11]


See also[edit] Ki Database Ion channel linked receptors Neuropsychopharmacology Schild regression for ligand receptor inhibition Signal transduction Stem cell marker Wikipedia:MeSH D12.776#MeSH D12.776.543.750 – receptors.2C cell surface


References[edit] ^ a b c Hall, JE (2016). Guyton and Hall Textbook of Medical Physiology. Philadelphia, PA: Elsevier Saunders. pp. 930–937. ISBN 978-1-4557-7005-2.  ^ Congreve M, Marshall F (March 2010). "The impact of GPCR structures on pharmacology and structure-based drug design". Br. J. Pharmacol. 159 (5): 986–96. doi:10.1111/j.1476-5381.2009.00476.x. PMC 2839258 . PMID 19912230.  ^ Kou Qin; Chunmin Dong; Guangyu Wu & Nevin A Lambert (August 2011). "Inactive-state preassembly of Gq-coupled receptors and Gq heterotrimers". Nature Chemical Biology. 7 (11): 740–747. doi:10.1038/nchembio.642. PMC 3177959 . PMID 21873996.  ^ a b Rang HP, Dale MM, Ritter JM, Flower RJ, Henderson G (2012). Rang & Dale's Pharmacology (7th ed.). Elsevier Churchill Livingstone. ISBN 978-0-7020-3471-8.  ^ Milligan G (December 2003). "Constitutive activity and inverse agonists of G protein coupled receptors: a current perspective". Mol. Pharmacol. 64 (6): 1271–6. doi:10.1124/mol.64.6.1271. PMID 14645655.  ^ Ariens EJ (September 1954). "Affinity and intrinsic activity in the theory of competitive inhibition. I. Problems and theory". Arch Int Pharmacodyn Ther. 99 (1): 32–49. PMID 13229418.  ^ Stephenson RP (December 1956). "A modification of receptor theory". Br J Pharmacol Chemother. 11 (4): 379–93. doi:10.1111/j.1476-5381.1956.tb00006.x. PMC 1510558 . PMID 13383117.  ^ Silverman RB (2004). "3.2.C Theories for Drug—Receptor Interactions". The Organic Chemistry of Drug Design and Drug Action (2nd ed.). Amsterdam: Elsevier Academic Press. ISBN 0-12-643732-7.  ^ Boulay G, Chrétien L, Richard DE, Guillemette G (November 1994). "Short-term desensitization of the angiotensin II receptor of bovinde adrenal glomerulosa cells corresponds to a shift from a high to low affinity state". Endocrinology. 135 (5): 2130–6. doi:10.1210/en.135.5.2130.  ^ a b c d e f g h i j k l Boulpaep, EL; Boron WF (2005). Medical physiology: a cellular and molecular approach. St. Louis, Mo: Elsevier Saunders. p. 90. ISBN 1-4160-2328-3.  ^ Waltenbaugh C, Doan T, Melvold R, Viselli S (2008). Immunology. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins. p. 20. ISBN 0-7817-9543-5. 


External links[edit] IUPHAR GPCR Database and Ion Channels Compendium Human plasma membrane receptome Cell surface receptors at the US National Library of Medicine Medical Subject Headings (MeSH) v t e Cell signaling / Signal transduction Signaling pathways GPCR Wnt RTK TGF beta MAPK/ERK Notch JAK-STAT Akt/PKB Fas apoptosis Hippo PI3K/AKT/mTOR pathway Integrin receptors Agents Receptor ligands Hormones Neurotransmitters/Neuropeptides/Neurohormones Cytokines Growth factors Signaling molecules Receptors Cell surface Intracellular Co-receptor Second messenger cAMP-dependent pathway Ca2+ signaling Lipid signaling Assistants: Signal transducing adaptor protein Scaffold protein Transcription factors General Transcription preinitiation complex TFIID TFIIH By distance Juxtacrine Autocrine / Paracrine Endocrine Other concepts Intracrine action Neurocrine signaling Synaptic transmission Chemical synapse Neuroendocrine signaling Exocrine signalling Pheromones Mechanotransduction Phototransduction Ion channel gating Gap junction v t e Membrane proteins, receptors: cell surface receptors G protein–coupled receptor Class A Eicosanoid receptor (Prostaglandin receptor) Protease-activated receptor Neurotransmitter receptor Purinergic receptor Biogenic amine receptor Olfactory receptor Class B Secretin receptor Class C Metabotropic glutamate receptor Class D Pheromone receptor Class E cAMP receptor Class F Frizzled/smoothened Ligand-gated ion channel Purinergic receptor Enzyme-linked receptor Serine/threonine-specific protein kinase Receptor tyrosine kinase Guanylate cyclase Other/ungrouped Asialoglycoprotein receptor Tumor necrosis factor receptor Immunoglobulin superfamily N-Acetylglucosamine receptor Neuropilins Transferrin receptor EDAR Lipoprotein receptor-related protein Progestin and adipoQ receptor v t e Transmembrane receptors: immunoglobulin superfamily immune receptors Antibody receptor: Fc receptor Epsilon (ε) FcεRI (FcεRII is C-type lectin) Gamma (γ) FcγRI FcγRII FcγRIII Neonatal Alpha (α)/mu (μ) FcαRI Fcα/μR Secretory Polymeric immunoglobulin receptor Antigen receptor B cells Antigen receptor BCR Co-receptor stimulate: CD21/CD19/CD81 inhibit: CD22 Accessory molecules Ig-α/Ig-β (CD79) T cells Ligands MHC MHC class I MHC class II Antigen receptor TCR: TRA@ TRB@ TRD@ TRG@ Co-receptors CD8 (with two glycoprotein chains CD8α and CD8β) CD4 Accessory molecules CD3 CD3γ CD3δ CD3ε ζ-chain (also called CD3ζ and TCRζ) Cytokine receptor see cytokine receptors Killer-cell IG-like receptors KIR2DL1 KIR2DL2 KIR2DL3 KIR2DL4 KIR2DL5A KIR2DL5B KIR2DS1 KIR2DS2 KIR2DS3 KIR2DS4 KIR2DS5 KIR3DL1 KIR3DL2 KIR3DL3 KIR3DS1 Leukocyte IG-like receptors LILRA1 LILRA2 LILRA3 LILRA4 LILRA5 LILRA6 LILRB1 LILRB2 LILRB3 LILRB4 LILRB5 LILRA6 LILRA5 v t e Transcription factors and intracellular receptors (1) Basic domains (1.1) Basic leucine zipper (bZIP) Activating transcription factor AATF 1 2 3 4 5 6 7 AP-1 c-Fos FOSB FOSL1 FOSL2 JDP2 c-Jun JUNB JunD BACH 1 2 BATF BLZF1 C/EBP α β γ δ ε ζ CREB 1 3 L1 CREM DBP DDIT3 GABPA GCN4 HLF MAF B F G K NFE 2 L1 L2 L3 NFIL3 NRL NRF 1 2 3 XBP1 (1.2) Basic helix-loop-helix (bHLH) ATOH1 AhR AHRR ARNT ASCL1 BHLH 2 3 9 ARNTL ARNTL ARNTL2 CLOCK EPAS1 FIGLA HAND 1 2 HES 5 6 HEY 1 2 L HES1 HIF 1A 3A ID 1 2 3 4 LYL1 MESP2 MXD4 MYCL1 MYCN Myogenic regulatory factors MyoD Myogenin MYF5 MYF6 Neurogenins 1 2 3 NeuroD 1 2 NPAS 1 2 3 OLIG 1 2 Pho4 Scleraxis SIM 1 2 TAL 1 2 Twist USF1 (1.3) bHLH-ZIP AP-4 MAX MXD3 MITF MNT MLX MXI1 Myc SREBP 1 2 (1.4) NF-1 NFI A B C X SMAD R-SMAD 1 2 3 5 9 I-SMAD 6 7 4) (1.5) RF-X RFX 1 2 3 4 5 6 ANK (1.6) Basic helix-span-helix (bHSH) AP-2 α β γ δ ε (2) Zinc finger DNA-binding domains (2.1) Nuclear receptor (Cys4) subfamily 1 Thyroid hormone α β CAR FXR LXR α β PPAR α β/δ γ PXR RAR α β γ ROR α β γ Rev-ErbA α β VDR subfamily 2 COUP-TF (I II Ear-2 HNF4 α γ PNR RXR α β γ Testicular receptor 2 4 TLX subfamily 3 Steroid hormone Androgen Estrogen α β Glucocorticoid Mineralocorticoid Progesterone Estrogen related α β γ subfamily 4 NUR NGFIB NOR1 NURR1 subfamily 5 LRH-1 SF1 subfamily 6 GCNF subfamily 0 DAX1 SHP (2.2) Other Cys4 GATA 1 2 3 4 5 6 MTA 1 2 3 TRPS1 (2.3) Cys2His2 General transcription factors TFIIA TFIIB TFIID TFIIE 1 2 TFIIF 1 2 TFIIH 1 2 4 2I 3A 3C1 3C2 ATBF1 BCL 6 11A 11B CTCF E4F1 EGR 1 2 3 4 ERV3 GFI1 GLI-Krüppel family 1 2 3 REST S1 S2 YY1 HIC 1 2 HIVEP 1 2 3 IKZF 1 2 3 ILF 2 3 KLF 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 17 MTF1 MYT1 OSR1 PRDM9 SALL 1 2 3 4 SP 1 2 4 7 8 TSHZ3 WT1 Zbtb7 7A 7B ZBTB 11 16 17 20 32 33 40 zinc finger 3 7 9 10 19 22 24 33B 34 35 41 43 44 51 74 143 146 148 165 202 217 219 238 239 259 267 268 281 295 300 318 330 346 350 365 366 384 423 451 452 471 593 638 644 649 655 (2.4) Cys6 HIVEP1 (2.5) Alternating composition AIRE DIDO1 GRLF1 ING 1 2 4 JARID 1A 1B 1C 1D 2 JMJD1B (2.6) WRKY WRKY (3) Helix-turn-helix domains (3.1) Homeodomain ARX CDX 1 2 CRX CUTL1 DBX 1 2 DLX 3 4 5 EMX 1 2 EN 1 2 FHL 1 2 3 HESX1 HHEX HLX Homeobox A1 A2 A3 A4 A5 A7 A9 A10 A11 A13 B1 B2 B3 B4 B5 B6 B7 B8 B9 B13 C4 C5 C6 C8 C9 C10 C11 C12 C13 D1 D3 D4 D8 D9 D10 D11 D12 D13 HOPX IRX 1 2 3 4 5 6 MKX LMX 1A 1B MEIS 1 2 MEOX2 MNX1 MSX 1 2 NANOG NKX 2-1 2-2 2-3 2-5 3-1 3-2 6-1 6-2 NOBOX PBX 1 2 3 PHF 1 3 6 8 10 16 17 20 21A PHOX 2A 2B PITX 1 2 3 POU domain PIT-1 BRN-3: A B C Octamer transcription factor: 1 2 3/4 6 7 11 OTX 1 2 PDX1 SATB2 SHOX2 SIX 1 2 3 4 5 VAX1 ZEB 1 2 (3.2) Paired box PAX 1 2 3 4 5 6 7 8 9 PRRX 1 2 RAX (3.3) Fork head / winged helix E2F 1 2 3 4 5 FOX proteins A1 A2 A3 C1 C2 D3 D4 E1 E3 F1 G1 H1 I1 J1 J2 K1 K2 L2 M1 N1 N3 O1 O3 O4 P1 P2 P3 P4 (3.4) Heat shock factors HSF 1 2 4 (3.5) Tryptophan clusters ELF 2 4 5 EGF ELK 1 3 4 ERF ETS 1 2 ERG SPIB ETV 1 4 5 6 FLI1 Interferon regulatory factors 1 2 3 4 5 6 7 8 MYB MYBL2 (3.6) TEA domain transcriptional enhancer factor 1 2 3 4 (4) β-Scaffold factors with minor groove contacts (4.1) Rel homology region NF-κB NFKB1 NFKB2 REL RELA RELB NFAT C1 C2 C3 C4 5 (4.2) STAT STAT 1 2 3 4 5 6 (4.3) p53 p53 TBX 1 2 3 5 19 21 22 TBR1 TBR2 TFT MYRF TP63 (4.4) MADS box Mef2 A B C D SRF (4.6) TATA-binding proteins TBP TBPL1 (4.7) High-mobility group BBX HMGB 1 2 3 4 HMGN 1 2 3 4 HNF 1A 1B LEF1 SOX 1 2 3 4 5 6 8 9 10 11 12 13 14 15 18 21 SRY SSRP1 TCF 3 4 TOX 1 2 3 4 (4.9) Grainyhead TFCP2 (4.10) Cold-shock domain CSDA YBX1 (4.11) Runt CBF CBFA2T2 CBFA2T3 RUNX1 RUNX2 RUNX3 RUNX1T1 (0) Other transcription factors (0.2) HMGI(Y) HMGA 1 2 HBP1 (0.3) Pocket domain Rb RBL1 RBL2 (0.5) AP-2/EREBP-related factors Apetala 2 EREBP B3 (0.6) Miscellaneous ARID 1A 1B 2 3A 3B 4A CAP IFI 16 35 MLL 2 3 T1 MNDA NFY A B C Rho/Sigma see also transcription factor/coregulator deficiencies v t e The development of phenotype Key concepts Genotype–phenotype distinction Norms of reaction Gene–environment interaction Gene–environment correlation Operon Heritability Quantitative genetics Heterochrony Neoteny Heterotopy Genetic architecture Canalisation Genetic assimilation Dominance Epistasis Fitness landscape/evolutionary landscape Pleiotropy Plasticity Polygenic inheritance Transgressive segregation Sequence space Non-genetic influences Epigenetics Maternal effect Dual inheritance theory Polyphenism Developmental architecture Developmental biology Morphogenesis Eyespot Pattern formation Segmentation Modularity Evolution of genetic systems Evolvability Mutational robustness Neutral networks Evolution of sexual reproduction Control of development Systems Regulation of gene expression Gene regulatory network Developmental-genetic toolkit Evolutionary developmental biology Homeobox Hedgehog signaling pathway Notch signaling pathway Elements Homeotic gene Hox gene Pax genes eyeless gene Distal-less Engrailed cis-regulatory element Ligand Morphogen Cell surface receptor Transcription factor Influential figures C. H. Waddington Richard Lewontin François Jacob + Jacques Monod Lac operon Eric F. Wieschaus Christiane Nüsslein-Volhard William McGinnis Mike Levine Sean B. Carroll Endless Forms Most Beautiful Debates Nature versus nurture Morphogenetic field Index of evolutionary biology articles Retrieved from "https://en.wikipedia.org/w/index.php?title=Receptor_(biochemistry)&oldid=817394570" Categories: Cell biologyCell signalingMembrane biologyReceptorsHidden categories: All articles with unsourced statementsArticles with unsourced statements from September 2016


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Receptor (disambiguation)EnlargeLigand (biochemistry)Secondary MessengerMembrane ReceptorsBiochemistryPharmacologyProteinMoleculeEndogenyLigandAcetylcholineProteinNuclear ReceptorLigand (biochemistry)ProteinPeptideSmall MoleculeNeurotransmitterHormoneNicotineCurareWikipedia:Citation NeededEnlargeGABAAlpha HelixG Protein-coupled ReceptorG ProteinReceptor Tyrosine KinaseEnzyme-linked ReceptorInsulin ReceptorNuclear ReceptorCytoplasmCell NucleusC-terminusDNA-binding DomainN-terminusLiquid-liquid ExtractionDetergentsAffinity PurificationX-ray CrystallographyNuclear Magnetic Resonance Spectroscopy Of ProteinsCircular DichroismDual Polarisation InterferometryComputer SimulationChemical EquilibriumLaw Of Mass ActionDissociation ConstantSecond Messenger SystemEnlargeAgonistEndogenousIntrinsic ActivityPartial AgonistReceptor AntagonistCovalent BondsOmeprazoleInverse AgonistAllosteric RegulationBenzodiazepinesGABAA ReceptorInverse AgonistRimonabantTaranabantPrecocious 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RegressionSignal TransductionStem Cell MarkerWikipedia:MeSH D12.776International Standard Book NumberSpecial:BookSources/978-1-4557-7005-2Digital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierInternational Standard Book NumberSpecial:BookSources/978-0-7020-3471-8Digital Object IdentifierPubMed IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierInternational Standard Book NumberSpecial:BookSources/0-12-643732-7Digital Object IdentifierInternational Standard Book NumberSpecial:BookSources/1-4160-2328-3International Standard Book NumberSpecial:BookSources/0-7817-9543-5Medical Subject HeadingsTemplate:Signal TransductionCell SignalingSignal TransductionG Protein-coupled ReceptorWnt Signaling PathwayReceptor Tyrosine KinaseTGF Beta Signaling PathwayMAPK/ERK PathwayNotch Signaling PathwayJAK-STAT Signaling PathwayAkt/PKB Signaling PathwayApoptosisHippo Signaling PathwayPI3K/AKT/mTOR PathwayIntegrinLigand (biochemistry)HormoneNeurotransmitterNeuropeptideNeurohormoneCytokineGrowth FactorCell SignalingCell Surface ReceptorIntracellular ReceptorCo-receptorSecond Messenger SystemCAMP-dependent PathwayCalcium SignalingLipid SignalingSignal Transducing Adaptor ProteinScaffold ProteinTranscription FactorGeneral Transcription FactorTranscription Preinitiation ComplexTranscription Factor II DTranscription Factor II HJuxtacrine SignallingAutocrine SignallingParacrine SignallingEndocrine SystemIntracrineSynaptic TransmissionChemical SynapseNeuroendocrine CellExocrine GlandPheromoneMechanotransductionVisual PhototransductionIon ChannelGap JunctionTemplate:Cell Surface ReceptorsTemplate Talk:Cell Surface ReceptorsMembrane ProteinCell Surface ReceptorG Protein–coupled ReceptorEicosanoid ReceptorProstaglandin ReceptorProtease-activated ReceptorNeurotransmitter ReceptorPurinergic ReceptorBiogenic Amine ReceptorOlfactory ReceptorSecretin ReceptorMetabotropic Glutamate ReceptorVomeronasal ReceptorCAMP ReceptorFrizzledSmoothenedLigand-gated Ion ChannelPurinergic ReceptorEnzyme-linked ReceptorSerine/threonine-specific Protein KinaseReceptor Tyrosine KinaseGuanylate CyclaseAsialoglycoprotein ReceptorTumor Necrosis Factor ReceptorImmunoglobulin SuperfamilyN-Acetylglucosamine ReceptorNeuropilinTransferrin ReceptorEDARLipoprotein Receptor-related ProteinProgestin And AdipoQ ReceptorTemplate:Immunoglobulin Superfamily Immune ReceptorsTemplate Talk:Immunoglobulin Superfamily Immune ReceptorsCell Surface ReceptorImmunoglobulin SuperfamilyImmune ReceptorFc ReceptorFc ReceptorFcεRICD23C-type LectinFc ReceptorCD64 (biology)CD32CD16Neonatal Fc ReceptorFc ReceptorFCARFcα/μRPolymeric Immunoglobulin ReceptorB CellB-cell ReceptorCo-receptorComplement Receptor 2CD19CD81CD22CD79ACD79BCD79T CellLigandMajor Histocompatibility ComplexMHC Class IMHC Class IIT-cell ReceptorTRA@TRD@TRG@Co-receptorCD8CD8 AlphaCD8 BetaCD4CD3 (immunology)CD3GCD3DT-cell Surface Glycoprotein CD3 Epsilon ChainCD3 ZetaCytokine ReceptorTemplate:Cytokine ReceptorsKiller-cell Immunoglobulin-like ReceptorKIR2DL1KIR2DL4KIR2DS1KIR2DS4KIR3DL1KIR3DL2KIR3DL3Leukocyte Immunoglobulin-like ReceptorsLILRA1LILRA2LILRA3LILRA4LILRB1LILRB2LILRB3LILRB4LILRB5Template:Transcription Factors And Intracellular ReceptorsTemplate Talk:Transcription Factors And Intracellular ReceptorsTranscription FactorIntracellular ReceptorLeucine ZipperBZIP DomainActivating Transcription FactorApoptosis-antagonizing Transcription FactorATF1Activating Transcription Factor 2ATF3ATF4ATF5ATF6ATF7AP-1 Transcription FactorC-FosFOSBFOSL1FOSL2Jun Dimerization ProteinC-junJUNBJunDBACH1BACH2BATF (gene)BLZF1Ccaat-enhancer-binding ProteinsCEBPACEBPBCEBPGCEBPDCEBPECCAAT/enhancer Binding Protein ZetaCREBCREB1CREB3CREBL1CAMP Responsive Element ModulatorDBP (gene)DNA Damage-inducible Transcript 3GABPAGcn4HLF (gene)MAF (gene)MAFB (gene)MAFF (gene)MAFGMAFKNFE2NFE2L1NFE2L2NFE2L3NFIL3NRL (gene)NRF1NFE2L2NFE2L3XBP1Basic Helix-loop-helixATOH1Aryl Hydrocarbon ReceptorAryl Hydrocarbon Receptor RepressorAryl Hydrocarbon Receptor Nuclear TranslocatorASCL1BHLHB2BHLHB3BHLHA9ARNTLARNTLARNTL2CLOCKEPAS1FIGLAHAND1HAND2HES5HES6HEY1HEY2HEYLHES1Hypoxia-inducible FactorsHIF1AHIF3AID1ID2ID3 (gene)ID4LYL1MESP2MXD4MYCL1N-MycMyogenic Regulatory FactorsMyoDMyogeninMYF5MYF6NeurogeninsNEUROG1NEUROG2NEUROG3NeuroDNEUROD1NEUROD2NPAS1NPAS2NPAS3OLIG1OLIG2Pho4ScleraxisSIM1SIM2TAL1TAL2Twist Transcription FactorUSF1Basic Helix-loop-helix Leucine Zipper Transcription FactorsTFAP4MAX (gene)MXD3Microphthalmia-associated Transcription FactorMNT (gene)MLX (gene)MXI1MycSterol Regulatory Element-binding ProteinSREBF1SREBF2Nuclear Factor INFIANFIB (gene)NFIC (gene)NFIXSMAD (protein)R-SMADMothers Against Decapentaplegic Homolog 1Mothers Against Decapentaplegic Homolog 2Mothers Against Decapentaplegic Homolog 3Mothers Against Decapentaplegic Homolog 5Mothers Against Decapentaplegic Homolog 9I-SMADMothers Against Decapentaplegic Homolog 6Mothers Against Decapentaplegic Homolog 7Mothers Against Decapentaplegic Homolog 4RFX1RFX2RFX3RFX4RFX5RFX6RFXANKActivating Protein 2TFAP2ATFAP2BTFAP2CTFAP2DTFAP2EZinc FingerNuclear ReceptorThyroid Hormone ReceptorThyroid Hormone Receptor AlphaThyroid Hormone Receptor BetaConstitutive Androstane ReceptorFarnesoid X ReceptorLiver X ReceptorLiver X Receptor AlphaLiver X Receptor BetaPeroxisome Proliferator-activated ReceptorPeroxisome Proliferator-activated Receptor AlphaPeroxisome Proliferator-activated Receptor DeltaPeroxisome Proliferator-activated Receptor GammaPregnane X ReceptorRetinoic Acid ReceptorRetinoic Acid Receptor AlphaRetinoic Acid Receptor BetaRetinoic Acid Receptor GammaRAR-related Orphan ReceptorRAR-related Orphan Receptor AlphaRAR-related Orphan Receptor BetaRAR-related Orphan Receptor GammaRev-ErbARev-ErbA AlphaRev-ErbA BetaCalcitriol ReceptorChicken Ovalbumin Upstream Promoter-transcription FactorCOUP-TFICOUP-TFIIV-erbA-related GeneHepatocyte Nuclear Factor 4Hepatocyte Nuclear Factor 4 AlphaHepatocyte Nuclear Factor 4 GammaPhotoreceptor Cell-specific Nuclear ReceptorRetinoid X ReceptorRetinoid X Receptor AlphaRetinoid X Receptor BetaRetinoid X Receptor GammaTesticular ReceptorTesticular Receptor 2Testicular Receptor 4TLXSteroid Hormone ReceptorAndrogen ReceptorEstrogen ReceptorEstrogen Receptor AlphaEstrogen Receptor BetaGlucocorticoid ReceptorMineralocorticoid ReceptorProgesterone ReceptorEstrogen-related ReceptorEstrogen-related Receptor AlphaEstrogen-related Receptor BetaEstrogen-related Receptor GammaNur (biology)Nerve Growth Factor IBNeuron-derived Orphan Receptor 1Nuclear Receptor Related-1 ProteinLiver Receptor Homolog-1Steroidogenic Factor 1Germ Cell Nuclear FactorDAX1Small Heterodimer PartnerGATA Transcription FactorGATA1GATA2GATA3GATA4GATA5GATA6MTA1MTA2MTA3Tricho-rhino-phalangeal Syndrome Type 1General Transcription FactorTranscription Factor II ATranscription Factor II BTranscription Factor II DTranscription Factor II EGTF2E1GTF2E2Transcription Factor II FGTF2F1GTF2F2Transcription Factor II HGTF2H1GTF2H2GTF2H4GTF2IGTF3AGTF3C1GTF3C2ATBF1B-cell CLL/lymphomaBCL6BCL11ABCL11BCTCFE4F1Early Growth Response ProteinsEGR1EGR2EGR3EGR4ERV3GFI1Kruppel-like FactorsGLI1GLI2GLI3RE1-silencing Transcription FactorGLIS1GLIS2YY1HIC1HIC2HIVEP1HIVEP2HIVEP3IKZF1IKZF2IKZF3ILF2ILF3Kruppel-like FactorsKLF1KLF2KLF3KLF4KLF5KLF6KLF7KLF8KLF9KLF10KLF11KLF12KLF13KLF14KLF15KLF17MTF1MYT1OSR1PRDM9SALL1SALL2SALL3SALL4Sp1 Transcription FactorSP2 (gene)SP4 (gene)Sp7 Transcription FactorSp8 Transcription FactorTSHZ3WT1Zbtb7ZBTB7AZBTB7BZBTB11Zinc Finger And BTB Domain-containing Protein 16ZBTB17ZBTB20ZBTB32ZBTB33ZBTB40ZNF3ZNF7CNBPZNF10ZNF19ZNF22ZNF24ZNF33BZNF34ZNF35ZNF41ZNF43ZNF44BCL6ZNF74ZNF143ZNF146ZNF148Zinc Finger Protein 165ZNF202ZNF217ZNF219ZNF238ZNF239ZNF259ZNF267EGR1ZNF281ZNF295ZNF300ZNF318ZNF330ZNF346ZNF350ZNF365ZNF366ZNF384ZNF423ZNF451ZNF452ZNF471ZNF593ZNF638ZNF644ZNF649ZNF655HIVEP1Autoimmune RegulatorDIDO1GRLF1ING1ING2ING4KDM5AKDM5BKDM5CKDM5DJARID2KDM3BWRKY Protein DomainHelix-turn-helixHomeodomain FoldAristaless Related HomeoboxCDX1CDX2CRX (gene)CUTL1DBX1DBX2DLX Gene FamilyDLX3 (gene)DLX4DLX5EMX HomeogeneEMX1EMX2EN1 (gene)EN2 (gene)FHL1FHL2FHL3HESX1HHEXHLX (gene)HomeoboxHomeobox A1HOXA2HOXA3HOXA4HOXA5HOXA7HOXA9Homeobox A10HOXA11HOXA13HOXB1HOXB2HOXB3HOXB4HOXB5HOXB6HOXB7HOXB8HOXB9HOXB13HOXC4HOXC5HOXC6HOXC8HOXC9HOXC10HOXC11HOXC12HOXC13HOXD1HOXD3HOXD4HOXD8HOXD9HOXD10HOXD11HOXD12HOXD13HOPXIroquois Homeobox FactorIRX1IRX2IRX3IRX4IRX5IRX6MKXLMX1ALMX1BMEIS1MEIS2MEOX2MNX1MSX1Msh Homeobox 2Homeobox Protein NANOGNKX-homeodomain FactorNK2 Homeobox 1NKX2-2NKX2-3Homeobox Protein Nkx-2.5NKX3-1NKX3-2NKX6-1NKX6-2NOBOXPBX1PBX2PBX3PHF1PHF3PHF6PHF8PHF10PHF16PHF17PHF20PHF21APHOX2APHOX2BPITX1PITX2PITX3POU DomainPituitary-specific Positive Transcription Factor 1BRN-3POU4F1POU4F2POU4F3Octamer Transcription FactorPOU2F1Oct-2Oct-4POU3F1POU3F2POU3F4OTX1Orthodenticle Homeobox 2PDX1SATB2SHOX2SIX1SIX2SIX3SIX4SIX5VAX1ZEB1ZEB2Pax GenesPAX1PAX2PAX3PAX4PAX5PAX6PAX7PAX8PAX9PRRX1PRRX2Retinal Homeobox Protein RxFOX ProteinsWinged-helix Transcription FactorsE2FE2F1E2F2E2F3E2F4E2F5FOX ProteinsFOXA1FOXA2FOXA3Forkhead Box C1FOXC2FOXD3FOXD4FOXE1FOXE3FOXF1FOXG1FOXH1FOXI1FOXJ1FOXJ2FOXK1FOXK2Forkhead Box L2FOXM1FOXN1FOXN3FOXO1FOXO3FOXO4FOXP1FOXP2FOXP3FOXP4Heat Shock FactorHeat Shock FactorHSF1HSF2HSF4ELF2ELF4ELF5EHF (gene)ELK1ELK3ELK4ERF (gene)ETS Transcription Factor FamilyETS1ETS2ERG (gene)SPIBETV1ETV4ERM Transcription FactorETV6FLI1Interferon Regulatory FactorsIRF1IRF2IRF3IRF4IRF5IRF6IRF7IRF8MYB (gene)MYBL2TEAD1TEAD2TEAD3TEAD4Rel Homology DomainNF-κBNFKB1NFKB2RELRELARELBNFATNFATC1NFATC2NFATC3NFATC4NFAT5STAT ProteinSTAT ProteinSTAT1STAT2STAT3STAT4STAT5STAT6P53T-boxTBX1TBX2TBX3TBX5 (gene)TBX19TBX21TBX22TBR1EomesoderminBrachyuryMyelin Regulatory FactorTP63MADS-boxMef2Myocyte-specific Enhancer Factor 2AMEF2BMEF2CMEF2DSerum Response FactorTATA-binding ProteinTATA-binding ProteinTBPL1High-mobility GroupBBX (gene)HMGB1HMGB2HMGB3HMGB4HMGNHMGN1HMGN2HMGN3HMGN4HNF1AHNF1BLymphoid Enhancer-binding Factor 1SOX Gene FamilySOX1SOX2SOX3SOX4SOX5SOX6SOX8SOX9SOX10SOX11SOX12SOX13SOX14SOX15SOX18SOX21Testis Determining FactorStructure Specific Recognition Protein 1TCF3TCF7L2TOXTOX2TOX3TOX4TFCP2CSDA (gene)Y Box Binding Protein 1Core Binding FactorCBFA2T2CBFA2T3RUNX1RUNX2RUNX3RUNX1T1HMGAHMGA1HMGA2HBP1Pocket Protein FamilyRetinoblastoma ProteinRetinoblastoma-like Protein 1Retinoblastoma-like Protein 2Apetala 2Ethylene-responsive Element Binding ProteinApetala 2Ethylene-responsive Element Binding ProteinB3 DomainARID1AARID1BARID2ARID3AARID3BARID4ACatabolite Activator ProteinIFI16IFI35MLL (gene)MLL2MLL3MLLT1MNDANFYANFYBNFYCRho FactorSigma FactorTemplate:Transcription Factor And Coregulator DeficienciesTemplate:GenarchTemplate Talk:GenarchMorphogenesisPhenotypeGenotype–phenotype DistinctionNorms Of ReactionGene–environment InteractionGene–environment CorrelationOperonHeritabilityQuantitative GeneticsHeterochronyNeotenyHeterotopyGenetic ArchitectureCanalisation (genetics)Genetic AssimilationDominance (genetics)EpistasisFitness LandscapeEvolutionary LandscapePleiotropyPhenotypic PlasticityPolygenic InheritanceTransgressive SegregationSequence Space (evolution)EpigeneticsMaternal EffectDual Inheritance TheoryPolyphenismDevelopmental BiologyMorphogenesisEyespot (mimicry)Pattern FormationSegmentation (biology)Modularity (biology)EvolvabilityMutational RobustnessNeutral Network (evolution)Evolution Of Sexual ReproductionRegulation Of Gene ExpressionGene Regulatory NetworkDevelopmental-genetic ToolkitEvolutionary Developmental BiologyHomeoboxHedgehog Signaling PathwayNotch Signaling PathwayHomeotic GeneHox GenePax GenesPAX6DLX Gene FamilyEngrailed (gene)Cis-regulatory ElementLigand (biochemistry)MorphogenTranscription FactorConrad Hal WaddingtonRichard LewontinFrançois JacobJacques MonodLac OperonEric F. WieschausChristiane Nüsslein-VolhardWilliam McGinnisMike Levine (biologist)Sean B. CarrollEndless Forms Most Beautiful (book)Nature Versus NurtureMorphogenetic FieldIndex Of Evolutionary Biology ArticlesHelp:CategoryCategory:Cell BiologyCategory:Cell SignalingCategory:Membrane BiologyCategory:ReceptorsCategory:All Articles With Unsourced StatementsCategory:Articles With Unsourced Statements From September 2016Discussion About Edits From This IP Address [n]A List Of Edits Made From This IP Address [y]View The Content Page [c]Discussion About The Content Page [t]Edit This Page [e]Visit The Main Page [z]Guides To Browsing WikipediaFeatured Content – The Best Of WikipediaFind Background Information On Current EventsLoad A Random Article [x]Guidance On How To Use And Edit WikipediaFind Out About WikipediaAbout The Project, What You Can Do, Where To Find ThingsA List Of Recent Changes In The Wiki [r]List Of All English Wikipedia Pages Containing Links To This Page [j]Recent Changes In Pages Linked From This Page [k]Upload Files [u]A List Of All Special Pages [q]Wikipedia:AboutWikipedia:General Disclaimer



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