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OP0232 HIGH PLASMA C4d/C4 IDENTIFIES LUPUS NEPHRITIS PATIENTS WITH DISEASE MEDIATED BY ACTIVATION OF THE CLASSICAL COMPLEMENT PATHWAY

Autor: A. Mongan, P. Suri, D. R. Artis, E. Cahir-McFarland, H. A. Kroon, Y. Andrews-Zwilling, S. Rose, S. Keswani, M. Dall’Era, T. Yednock

Publikováno v: Annals of the Rheumatic Diseases. 81:153-154

BackgroundProliferative lupus nephritis (LN) involves immune complex deposition in the kidney that can severely impact normal renal clearance mechanisms. Immune complexes can activate C1q and the classical complement cascade, and along with pathogeni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::537ef06e42f9ddd2366851eef40115a8
https://doi.org/10.1136/annrheumdis-2022-eular.2092

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Receptor-binding conformation of the 'ELR' motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution

Autor: N, Gerber, H, Lowman, D R, Artis, C, Eigenbrot

Publikováno v: Proteins. 38(4)

The "ELR" (Glu-Leu-Arg) tripeptide sequence near the N-terminus of interleukin-8 (IL-8) contributes a large part of the receptor binding free energy. Prior X-ray and nuclear magnetic resonance (NMR) structures of IL-8 have shown this region of the mo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ae4dea92f81c9cb1fc8077d644397e4c
https://pubmed.ncbi.nlm.nih.gov/10707023

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Transfer of a protein binding epitope to a minimal designed peptide

Autor: C, Quan, N J, Skelton, K, Clark, D Y, Jackson, M E, Renz, H H, Chiu, S M, Keating, M H, Beresini, S, Fong, D R, Artis

Publikováno v: Biopolymers. 47(4)

Results from protein mutagenesis and x-ray crystallographic studies of the multidomain protein Vascular Cell Adhesion Molecule (VCAM) were used to design cyclic octapeptides that retain the critical structural and binding elements of the epitope of V

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::15e4fdc4dd917acaf15b4ac91aa42c71
https://pubmed.ncbi.nlm.nih.gov/10036968

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Structural change and receptor binding in a chemokine mutant with a rearranged disulfide: X-ray structure of E38C/C50AIL-8 at 2 A resolution

Autor: C, Eigenbrot, H B, Lowman, L, Chee, D R, Artis

Publikováno v: Proteins. 27(4)

The characteristic CXC chemokine disulfide core of interleukin-8 (IL-8) has been rearranged in a variant replacing the 9-50 disulfide with a 9-38 disulfide. The new variant has been characterized by its binding affinity to IL-8 receptors A and B and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ee122b552a60395148cf55055e917d42
https://pubmed.ncbi.nlm.nih.gov/9141135

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