Obesity-associated mutations in the melanocortin 4 receptor provide novel insights into its function

[1]  B. Conklin,et al.  Constitutive activity of the melanocortin-4 receptor is maintained by its N-terminal domain and plays a role in energy homeostasis in humans. , 2004, The Journal of clinical investigation.

[2]  K. Houseknecht,et al.  The role of melanocortin-3 and -4 receptor in regulating appetite, energy homeostasis and neuroendocrine function in the pig. , 2004, The Journal of endocrinology.

[3]  C. Schalin-Jäntti,et al.  Identification and characterization of melanocortin-4 receptor gene mutations in morbidly obese finnish children and adults. , 2004, The Journal of clinical endocrinology and metabolism.

[4]  J. Trejo.  Protease-Activated Receptors: New Concepts in Regulation of G Protein-Coupled Receptor Signaling and Trafficking , 2003, Journal of Pharmacology and Experimental Therapeutics.

[5]  Thomas Gudermann,et al.  Melanocortin-4 receptor gene: case-control study and transmission disequilibrium test confirm that functionally relevant mutations are compatible with a major gene effect for extreme obesity. , 2003, The Journal of clinical endocrinology and metabolism.

[6]  R. Adan,et al.  Poor Cell Surface Expression of Human Melanocortin-4 Receptor Mutations Associated with Obesity* , 2003, Journal of Biological Chemistry.

[7]  K. Clément,et al.  Molecular Genetics of Human Obesity‐Associated MC4R Mutations , 2003, Annals of the New York Academy of Sciences.

[8]  H. Schiöth,et al.  The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. , 2003, Molecular pharmacology.

[9]  Tim Cheetham,et al.  Clinical spectrum of obesity and mutations in the melanocortin 4 receptor gene. , 2003, The New England journal of medicine.

[10]  S. O’Rahilly,et al.  Mutations in the human melanocortin-4 receptor gene associated with severe familial obesity disrupts receptor function through multiple molecular mechanisms. , 2003, Human molecular genetics.

[11]  Stephen K.-F. Wong,et al.  G Protein Selectivity Is Regulated by Multiple Intracellular Regions of GPCRs , 2003, Neurosignals.

[12]  Shoshana J. Wodak,et al.  Activation of CCR5 by Chemokines Involves an Aromatic Cluster between Transmembrane Helices 2 and 3* , 2003, The Journal of Biological Chemistry.

[13]  Philippe Froguel,et al.  Intracellular retention is a common characteristic of childhood obesity-associated MC4R mutations. , 2003, Human molecular genetics.

[14]  Gert Vriend,et al.  GPCRDB information system for G protein-coupled receptors , 2003, Nucleic Acids Res..

[15]  Ulrik Gether,et al.  Structural basis for activation of G-protein-coupled receptors. , 2002, Pharmacology & toxicology.

[16]  E. Snyder,et al.  Melanocortin 4 receptor sequence variations are seldom a cause of human obesity: the Swedish Obese Subjects, the HERITAGE Family Study, and a Memphis cohort. , 2002, The Journal of clinical endocrinology and metabolism.

[17]  R. Seifert,et al.  Constitutive activity of G-protein-coupled receptors: cause of disease and common property of wild-type receptors , 2002, Naunyn-Schmiedeberg's Archives of Pharmacology.

[18]  L. Perrone,et al.  Low frequency of melanocortin-4 receptor (MC4R) mutations in a Mediterranean population with early-onset obesity , 2002, International Journal of Obesity.

[19]  P. Conn,et al.  Structural determinants in the second intracellular loop of the human follicle-stimulating hormone receptor are involved in Gs protein activation , 2002, Molecular and Cellular Endocrinology.

[20]  K. Clément,et al.  Mutational analysis of melanocortin-4 receptor, agouti-related protein, and alpha-melanocyte-stimulating hormone genes in severely obese children. , 2001, The Journal of pediatrics.

[21]  H. Mergen,et al.  A novel melanocortin 4 receptor (MC4R) gene mutation associated with morbid obesity. , 2001, The Journal of clinical endocrinology and metabolism.

[22]  J. Ballesteros,et al.  Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. , 2001, Molecular pharmacology.

[23]  Y. Wan,et al.  Structure activity studies of the melanocortin-4 receptor by in vitro mutagenesis: identification of agouti-related protein (AGRP), melanocortin agonist and synthetic peptide antagonist interaction determinants. , 2001, Biochemistry.

[24]  C. Haskell-Luevano,et al.  Agouti-related protein functions as an inverse agonist at a constitutively active brain melanocortin-4 receptor , 2001, Regulatory Peptides.

[25]  Shoshana J. Wodak,et al.  The TXP Motif in the Second Transmembrane Helix of CCR5 , 2001, The Journal of Biological Chemistry.

[26]  R. Adan,et al.  AgRP(83-132) acts as an inverse agonist on the human-melanocortin-4 receptor. , 2001, Molecular endocrinology.

[27]  Krzysztof Palczewski,et al.  Crystal Structure of Rhodopsin: A G‐Protein‐Coupled Receptor , 2002, Science.

[28]  M. Tota,et al.  Molecular determinants of ligand binding to the human melanocortin-4 receptor. , 2000, Biochemistry.

[29]  R. Cone,et al.  A Unique Metalolic Sysdrone Causes Obesity in the Melanocortin-3 Receptor-Deficient Mouse. , 2000, Endocrinology.

[30]  Yue Feng,et al.  Inactivation of the mouse melanocortin-3 receptor results in increased fat mass and reduced lean body mass , 2000, Nature Genetics.

[31]  Angiotensin II type 1 receptor‐function affected by mutations in cytoplasmic loop CD , 2000, FEBS letters.

[32]  U. Gether.  Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. , 2000, Endocrine reviews.

[33]  K. Clément,et al.  Melanocortin-4 receptor mutations are a frequent and heterogeneous cause of morbid obesity. , 2000, The Journal of clinical investigation.

[34]  R. Cone,et al.  A unique metabolic syndrome causes obesity in the melanocortin-3 receptor-deficient mouse. , 2000, Endocrinology.

[35]  J. Hebebrand,et al.  Phenotypes in three pedigrees with autosomal dominant obesity caused by haploinsufficiency mutations in the melanocortin-4 receptor gene. , 1999, American journal of human genetics.

[36]  D. Donnelly,et al.  Conserved polar residues in the transmembrane domain of the human tachykinin NK2 receptor: functional roles and structural implications. , 1999, The Biochemical journal.

[37]  J. Wess,et al.  Molecular basis of receptor/G-protein-coupling selectivity. , 1998, Pharmacology & therapeutics.

[38]  D. Campbell,et al.  Assignment1 of the melanocortin 4 receptor (MC4R) gene to human chromosome band 18q22 by in situ hybridisation and radiation hybrid mapping , 1998, Cytogenetic and Genome Research.

[39]  K. Clément,et al.  A frameshift mutation in human MC4R is associated with a dominant form of obesity , 1998, Nature Genetics.

[40]  M. Brann,et al.  The Second Intracellular Loop of the m5 Muscarinic Receptor Is the Switch Which Enables G-protein Coupling* , 1998, The Journal of Biological Chemistry.

[41]  Roland L. Dunbrack,et al.  Bayesian statistical analysis of protein side‐chain rotamer preferences , 1997, Protein science : a publication of the Protein Society.

[42]  Marvin C. Gershengorn,et al.  Interactions between Conserved Residues in Transmembrane Helices 1, 2, and 7 of the Thyrotropin-releasing Hormone Receptor* , 1997, The Journal of Biological Chemistry.

[43]  H Weinstein,et al.  Related Contribution of Specific Helix 2 and 7 Residues to Conformational Activation of the Serotonin 5-HT2A Receptor (*) , 1995, The Journal of Biological Chemistry.

[44]  J. Ballesteros,et al.  [19] Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors , 1995 .

[45]  S. Watson,et al.  Molecular cloning, expression, and gene localization of a fourth melanocortin receptor. , 1993, The Journal of biological chemistry.