The thyrotropin receptor hinge region is not simply a scaffold for the leucine-rich domain but contributes to ligand binding and signal transduction.
about
Discovery and Development of Small Molecule Allosteric Modulators of Glycoprotein Hormone ReceptorsGraves' Disease Mechanisms: The Role of Stimulating, Blocking, and Cleavage Region TSH Receptor Antibodies.Structural-Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at WorkSubunit interactions influence TSHR multimerizationThyrotropin (TSH) receptor residue E251 in the extracellular leucine-rich repeat domain is critical for linking TSH binding to receptor activationNovel information on the epitope of an inverse agonist monoclonal antibody provides insight into the structure of the TSH receptorFunctional differences of invariant and highly conserved residues in the extracellular domain of the glycoprotein hormone receptorsThe hinge region of human thyroid-stimulating hormone (TSH) receptor operates as a tunable switch between hormone binding and receptor activation.The antibodies against the computationally designed mimic of the glycoprotein hormone receptor transmembrane domain provide insights into receptor activation and suppress the constitutively activated receptor mutants.Dominant negative effect of mutated thyroid stimulating hormone receptor (P556L) causes hypothyroidism in C.RF-Tshr(hyt/wild) mice.Antibody protection reveals extended epitopes on the human TSH receptor.Extended and structurally supported insights into extracellular hormone binding, signal transduction and organization of the thyrotropin receptor.Evidence that the thyroid-stimulating hormone (TSH) receptor transmembrane domain influences kinetics of TSH binding to the receptor ectodomain.New small molecule agonists to the thyrotropin receptor.Relationship between thyrotropin receptor hinge region proteolytic posttranslational modification and receptor physiological functionDefining structural and functional dimensions of the extracellular thyrotropin receptor region.Structure-function relationships of glycoprotein hormones and their subunits' ancestors.Domain coupling in GPCRs: the engine for induced conformational changesTargeting the thyroid-stimulating hormone receptor with small molecule ligands and antibodiesThe Activation Mechanism of Glycoprotein Hormone Receptors with Implications in the Cause and Therapy of Endocrine DiseasesThe thyrotropin receptor hinge region as a surrogate ligand: identification of loci contributing to the coupling of thyrotropin binding and receptor activationIdentification of key amino acid residues in a thyrotropin receptor monoclonal antibody epitope provides insight into its inverse agonist and antagonist properties.TSH Receptor Cleavage Into Subunits and Shedding of the A-Subunit; A Molecular and Clinical Perspective.Asp330 and Tyr331 in the C-terminal cysteine-rich region of the luteinizing hormone receptor are key residues in hormone-induced receptor activation.Novel insights on thyroid-stimulating hormone receptor signal transduction.A monoclonal antibody with thyrotropin (TSH) receptor inverse agonist and TSH antagonist activities binds to the receptor hinge region as well as to the leucine-rich domainThe superagonistic activity of bovine thyroid-stimulating hormone (TSH) and the human TR1401 TSH analog is determined by specific amino acids in the hinge region of the human TSH receptor.Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors.Targeting the thyrotropin receptor in thyroid disease.Critical involvement of the hinge region of the follicle-stimulating hormone receptor in the activation of the receptor.Concurrent overexpression of RET/PTC1 and TTF1 confers tumorigenicity to thyrocytes.Molecular description of non-autoimmune hyperthyroidism at a neonate caused by a new thyrotropin receptor germline mutationResearch resource: novel structural insights bridge gaps in glycoprotein hormone receptor analyses.Insights into differential modulation of receptor function by hinge region using novel agonistic lutropin receptor and inverse agonistic thyrotropin receptor antibodies.Differences between lutropin-mediated and choriogonadotropin-mediated receptor activation.Excess TSH causes abnormal skeletal development in young mice with hypothyroidism via suppressive effects on the growth plate.
P2860
Q26781438-DBAC0B2C-2B75-492D-AC3A-DC5AF2243C2CQ27687742-DD274529-14EE-45D5-A0F4-7F1C4BF3003FQ30401802-3788F2B7-EB6A-48BF-B959-B070A847308DQ30430521-972FDE43-DA0B-401C-A221-92EA20A80F9EQ33775572-5D629341-D1F3-415B-9263-1D73711C2135Q34168493-1F729075-78C2-4616-B337-FD2D734AF74EQ34251314-98370AD0-5867-42A0-8A89-5D1B78596740Q34336103-E4675D6D-8C61-4643-AA69-FFB783E53B92Q34384048-A1CEBCC0-4031-4B49-9E05-0787A8825967Q34390845-BDCEF9DB-F145-4046-85C7-CDADC4B2458EQ34408273-F383D728-495A-4F24-9FB3-C0DFFD3B4C36Q34541418-16D1043B-A10A-4824-99FC-0F384B54429FQ34675830-9AC4A569-8EB0-4348-BB81-C77D5F6166D5Q34918437-57CB43EA-4D0F-4AFC-81A2-7DED53DBF95CQ34942963-EAF2226E-0DB9-4CB9-A448-45E72C90CCABQ35063176-573DDF66-C87D-42AE-8D8D-470D579DC0E6Q35124421-DC3118A2-30FC-4E52-B7A3-1614F9239AADQ35740222-C91E6841-2157-4596-B93B-691676BDBA1AQ35794921-7D9DBD19-3666-4CF1-945F-BC72F2BB2325Q35845783-01670258-D370-49C1-AF4F-4B8F704BCBBEQ36439375-9CBF4C63-D6B2-4EAA-92C5-C19DDE22E56EQ36755364-1CF0CD1B-0FE6-4410-BE46-7BD6EB63B057Q36773013-ABE83687-40D5-4283-B3F4-274D3420E983Q36871645-B01F8C22-68AD-4831-A321-B7F6781E49B4Q37203610-7CF92438-B54E-49EC-913E-4871253AD786Q37244541-D26CD1D4-8B3F-46C4-A07B-E709C19ACB84Q37269160-6AF0834C-7CB4-4D3D-BF26-8310B1F9596CQ37455434-32419942-BD03-4867-A52B-CDF532BA8BBAQ38012510-1332383E-EC90-412B-AD29-39EEEF71B848Q39912851-19C544C3-9714-4103-A525-2A0878801764Q41822268-916E3313-639D-4EE5-9210-968A1BCAF2A8Q42143175-5B3DA471-F09D-4C6B-BBCD-3692D28AFB7EQ42274233-4C8185B2-7951-4373-B57F-F8D7E41120A7Q42501697-B5E058EB-7835-4E8E-8A8A-94475630E735Q46725788-3BB05CD7-02FC-4141-B5A2-3EAEB71A95EDQ47950433-86353DD8-24D7-46AE-8070-32E2D7578F80
P2860
The thyrotropin receptor hinge region is not simply a scaffold for the leucine-rich domain but contributes to ligand binding and signal transduction.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
The thyrotropin receptor hinge ...... nding and signal transduction.
@ast
The thyrotropin receptor hinge ...... nding and signal transduction.
@en
type
label
The thyrotropin receptor hinge ...... nding and signal transduction.
@ast
The thyrotropin receptor hinge ...... nding and signal transduction.
@en
prefLabel
The thyrotropin receptor hinge ...... nding and signal transduction.
@ast
The thyrotropin receptor hinge ...... nding and signal transduction.
@en
P2093
P2860
P356
P1476
The thyrotropin receptor hinge ...... nding and signal transduction.
@en
P2093
Chun-Rong Chen
Sandra M McLachlan
Yumiko Mizutori
P2860
P304
P356
10.1210/ME.2007-0407
P577
2008-01-24T00:00:00Z