Shedding of human thyrotropin receptor ectodomain. Involvement of a matrix metalloprotease.
about
Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family membersReview and hypothesis: does Graves' disease develop in non-human great apes?Excessive Cytosolic DNA Fragments as a Potential Trigger of Graves' Disease: An Encrypted Message Sent by Animal ModelsTSH signalling and cancer.Subunit interactions influence TSHR multimerizationA tyrosine residue on the TSH receptor stabilizes multimer formationEpitope recognition in HLA-DR3 transgenic mice immunized to TSH-R protein or peptides.Immune response of mice transgenic for human histocompatibility leukocyte Antigen-DR to human thyrotropin receptor-extracellular domainThyrotropin receptor-associated diseases: from adenomata to Graves diseaseHuman beta1-adrenergic receptor is subject to constitutive and regulated N-terminal cleavageInfluence of the hinge region and its adjacent domains on binding and signaling patterns of the thyrotropin and follitropin receptor.Antibody protection reveals extended epitopes on the human TSH receptor.The TSH receptor reveals itself.Thyroid-stimulating autoantibodies in Graves disease preferentially recognize the free A subunit, not the thyrotropin holoreceptor.A monoclonal thyroid-stimulating antibody.Defining structural and functional dimensions of the extracellular thyrotropin receptor region.The thyrotropin receptor autoantigen in Graves disease is the culprit as well as the victim.A unique mouse strain that develops spontaneous, iodine-accelerated, pathogenic antibodies to the human thyrotrophin receptor.Targeting the thyroid-stimulating hormone receptor with small molecule ligands and antibodiesRegulation of monocyte MMP-9 production by TNF-alpha and a tumour-derived soluble factor (MMPSF).Molecular and cellular mechanisms of ectodomain sheddingTSH Receptor Cleavage Into Subunits and Shedding of the A-Subunit; A Molecular and Clinical Perspective.Novel insights on thyroid-stimulating hormone receptor signal transduction.Role of asparagine-linked oligosaccharides in protein folding, membrane targeting, and thyrotropin and autoantibody binding of the human thyrotropin receptor.Site-specific O-Glycosylation by Polypeptide N-Acetylgalactosaminyltransferase 2 (GalNAc-transferase T2) Co-regulates β1-Adrenergic Receptor N-terminal Cleavage.The cell biology of the thyroid-disrupting mechanism of dichlorodiphenyltrichloroethane (DDT).Thyroid autoimmunity.Interactions between the mannose receptor and thyroid autoantigens.Association of the thyrotropin receptor with calnexin, calreticulin and BiP. Efects on the maturation of the receptor.The extracellular N terminus of the endothelin B (ETB) receptor is cleaved by a metalloprotease in an agonist-dependent process.Pro-tumor necrosis factor-alpha processing activity is tightly controlled by a component that does not affect notch processing.Basolateral localization and transcytosis of gonadotropin and thyrotropin receptors expressed in Madin-Darby canine kidney cells.Membrane protein secretasesSubunit structure of thyrotropin receptors expressed on the cell surface.Insight into thyrotropin receptor cleavage by engineering the single polypeptide chain luteinizing hormone receptor into a cleaving, two subunit receptor.Thyrotropin receptor cleavage at site 1 does not involve a specific amino acid motif but instead depends on the presence of the unique, 50 amino acid insertion.An N-linked glycosylation motif from the noncleaving luteinizing hormone receptor substituted for the homologous region (Gly367 to Glu369) of the thyrotropin receptor prevents cleavage at its second, downstream site.Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane-bound matrix metalloproteinase with tissue-specific expression.Dm1-MMP, a matrix metalloproteinase from Drosophila with a potential role in extracellular matrix remodeling during neural development.G protein-coupled receptors. I. Diversity of receptor-ligand interactions.
P2860
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P2860
Shedding of human thyrotropin receptor ectodomain. Involvement of a matrix metalloprotease.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Shedding of human thyrotropin ...... t of a matrix metalloprotease.
@en
type
label
Shedding of human thyrotropin ...... t of a matrix metalloprotease.
@en
prefLabel
Shedding of human thyrotropin ...... t of a matrix metalloprotease.
@en
P2093
P2860
P356
P1476
Shedding of human thyrotropin ...... t of a matrix metalloprotease.
@en
P2093
P2860
P304
P356
10.1074/JBC.271.8.4545
P407
P577
1996-02-01T00:00:00Z