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The protein encoded by GCGR is a glucagon receptor that is important in controlling blood glucose levels. Additionally we are shipping Glucagon Receptor Antibodies (93) and Glucagon Receptor Kits (1) and many more products for this protein.
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2.5 A crystal structure of human GCGR in complex with the antagonist MK-0893, which is found to bind to an allosteric site outside the seven transmembrane helical bundle in a position between TM6 and TM7 extending into the lipid bilayer
Molecular dynamics and disulfide crosslinking studies suggest that apo (show C9orf3 Proteins)-GCGR can adopt both an open and closed conformation associated with extensive contacts between the ECD (show SHFM1 Proteins) and 7TM domain. Glucagon (show GCG Proteins) binds to GCGR by a conformational selection mechanism.
glucagon (show GCG Proteins) cell adenomatosis with GCGR germline mutations seems to follow an autosomal-recessive trait.
Using a real-time time-resolved FRET-based internalization assay, we show that GLP-1R (show GLP1R Proteins), GIPR (show GIPR Proteins), and GCGR internalize with differential properties
crystal structure of the seven transmembrane helical domain of human GCGR at 3.4 A resolution, and a hybrid model of glucagon (show GCG Proteins) bound to GCGR to understand the molecular recognition of the receptor for its native ligand
Letter/Case Report: nonfunctional glucagon (show GCG Proteins) cell adenomatosis with no detectable glucagon receptor mutations.
GRA1 is a potent glucagon receptor antagonist with strong antihyperglycemic efficacy in preclinical models and prominent effects on hepatic gene-expression related to amino acid metabolism
F22, V23, M27, and D15 (show MRPL16 Proteins) of GCGR are the most important residues for glucagon (show GCG Proteins) binding.
in addition to activation of the classic cAMP/protein kinase A (PKA) pathway, activation of GCGR also induced beta-catenin (show CTNNB1 Proteins) stabilization and activated beta-catenin (show CTNNB1 Proteins)-mediated transcription
analysis of glucagon receptor antagonists with reduced molecular weight and lipophilicity
glucagon receptor antagonist improves glycemia in diet-induced obese angptl4 (show ANGPTL4 Proteins) knockout mice without increasing glucagon (show GCG Proteins) levels or alpha-cell proliferation, underscoring the importance of this protein.
Data indicate that the exocrine pancreas in the glucagon receptor Gcgr-/- mice exhibited larger nuclear size than in WT or heterozygous controls, most obviously at old ages.
Simultaneous and sufficient activation of GLP1R (show GLP1R Proteins) is required to reduce GCCR (show NR3C1 Proteins) mediated blood glucose elevation following administration of a GLP1R (show GLP1R Proteins)/GCGR co-agonist.
Knockdown of liver glucagon receptor in mice reduces blood glucose and increases blood LDL levels.
Gcgr(-/-) mice became lethargic (show CACNB4 Proteins) & cachexic & died early. Autopsy revealed numerous PNETs up to 15 mm in diameter in most well-preserved Gcgr(-/-) pancreata.
Data suggest that GcgR activation raises hepatic expression of fibroblast growth factor 21 (FGF21 (show FGF21 Proteins)) and increases circulating levels of FGF21 (show FGF21 Proteins); GcgR activation induces body weight loss and stimulates lipid metabolism.
These results suggest that a circulating factor generated after disruption of hepatic Gcgr signaling can increase alpha-cell proliferation independent of direct pancreatic input.
Data suggest that both Gcgr activity and glucagon-like peptide 1 (show GCG Proteins)/Glp1r (show GLP1R Proteins) signal transduction in central nervous system are involved in control of interscapular brown adipose tissue thermogenesis.
A novel transgenic mouse was generated which had muscle specific (show EIF3K Proteins) expression of glucagon receptor. The transgenic mice maintained an appropriate ratio of glucagon (show GCG Proteins) to insulin (show INS Proteins), which appears important in maintaining glucose homeostasis.
The protein encoded by this gene is a glucagon receptor that is important in controlling blood glucose levels. Defects in this gene are a cause of non-insulin-dependent diabetes mellitus (NIDDM).
, glucagon receptor-like
, glucagon receptor perhaps same as Niddm3