Point Mutations of Single Amino Acids Abolish Ability of α3 NC1 Domain to Elicit Experimental Autoimmune Glomerulonephritis in Rats
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference50 articles.
1. Identification of a clinically relevant immunodominant region of collagen IV in Goodpasture disease
2. Exon/intron structure of the human alpha 3(IV) gene encompassing the Goodpasture antigen (alpha 3(IV)NC1). Identification of a potentially antigenic region at the triple helix/NC1 domain junction.
3. The Goodpasture Autoantigen
4. Recombinant α-chains of type IV collagen demonstrate that the amino terminal of the Goodpasture autoantigen is crucial for antibody recognition
5. The Goodpasture Autoantigen
Cited by 6 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Autoimmunity to the alpha 3 chain of type IV collagen in glomerulonephritis is triggered by ‘autoantigen complementarity’;Journal of Autoimmunity;2015-05
2. Precise mapping of the Goodpasture epitope(s) using phage display, site-directed mutagenesis, and surface plasmon resonance;Kidney International;2013-03
3. A Nephritogenic Peptide Induces Intermolecular Epitope Spreading on Collagen IV in Experimental Autoimmune Glomerulonephritis;Journal of the American Society of Nephrology;2006-09-27
4. Zebrafish to humans: evolution of the 3-chain of type IV collagen and emergence of the autoimmune epitopes associated with Goodpasture syndrome;Blood;2006-03-01
5. Epitope Spreading and Autoimmune Glomerulonephritis in Rats Induced by a T Cell Epitope of Goodpasture’s Antigen;Journal of the American Society of Nephrology;2005-07-27
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