A prion-like shift between two conformational forms of a recombinant thyrotropin receptor A-subunit module: purification and stabilization using chemical chaperones of the form reactive with Graves' autoantibodies.
about
Breaking tolerance to thyroid antigens: changing concepts in thyroid autoimmunityTyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors.Crystal structure of a TSH receptor monoclonal antibody: insight into Graves' disease pathogenesis.Thyroid-stimulating autoantibodies in Graves disease preferentially recognize the free A subunit, not the thyrotropin holoreceptor.Insight into thyroid-stimulating autoantibody interaction with the thyrotropin receptor N-terminus based on mutagenesis and re-evaluation of ambiguity in this region of the receptor crystal structureEvidence that TSH Receptor A-Subunit Multimers, Not Monomers, Drive Antibody Affinity Maturation in Graves' DiseaseDeleting the Redundant TSH Receptor C-Peptide Region Permits Generation of the Conformationally Intact Extracellular Domain by Insect Cells.Probing structural variability at the N terminus of the TSH receptor with a murine monoclonal antibody that distinguishes between two receptor conformational formsThe thyrotropin receptor hinge region is not simply a scaffold for the leucine-rich domain but contributes to ligand binding and signal transduction.Evidence that shed thyrotropin receptor A subunits drive affinity maturation of autoantibodies causing Graves' diseaseStudies in mice deficient for the autoimmune regulator (Aire) and transgenic for the thyrotropin receptor reveal a role for Aire in tolerance for thyroid autoantigensAttenuation of induced hyperthyroidism in mice by pretreatment with thyrotropin receptor protein: deviation of thyroid-stimulating to nonfunctional antibodies.Interactions between the mannose receptor and thyroid autoantigens.Thyrotrophin receptor-specific memory T cell responses require normal B cells in a murine model of Graves' disease.Adenovirus-mediated gene delivery of interleukin-10, but not transforming growth factor beta, ameliorates the induction of Graves' hyperthyroidism in BALB/c mice.Cathepsin S is not crucial to TSHR processing and presentation in a murine model of Graves' disease.Evidence that factors other than particular thyrotropin receptor T cell epitopes contribute to the development of hyperthyroidism in murine Graves' disease.Critical Differences between Induced and Spontaneous Mouse Models of Graves' Disease with Implications for Antigen-Specific Immunotherapy in Humans.
P2860
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P2860
A prion-like shift between two conformational forms of a recombinant thyrotropin receptor A-subunit module: purification and stabilization using chemical chaperones of the form reactive with Graves' autoantibodies.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
A prion-like shift between two ...... e with Graves' autoantibodies.
@ast
A prion-like shift between two ...... e with Graves' autoantibodies.
@en
type
label
A prion-like shift between two ...... e with Graves' autoantibodies.
@ast
A prion-like shift between two ...... e with Graves' autoantibodies.
@en
prefLabel
A prion-like shift between two ...... e with Graves' autoantibodies.
@ast
A prion-like shift between two ...... e with Graves' autoantibodies.
@en
P2093
P921
P356
P1476
A prion-like shift between two ...... e with Graves' autoantibodies.
@en
P2093
Chazenbalk GD
McLachlan SM
Pichurin P
Rapoport B
P304
P356
10.1210/JCEM.86.3.7363
P407
P577
2001-03-01T00:00:00Z