Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Dominique A. Weber"'
Autor:
Charles A. Parkos, Anny-Claude Luissint, Hikaru Nishio, Jennifer C. Brazil, Dominique A. Weber, Andrew S. Neish, Asma Nusrat, Ronen Sumagin, Porfirio Nava, Ashfaqul Alam
Publikováno v:
Mucosal immunology
A characteristic feature of gastrointestinal tract inflammatory disorders, such as inflammatory bowel disease, is polymorphonuclear neutrophil (PMN) transepithelial migration (TEM) and accumulation in the gut lumen. PMN accumulation within the intest
Autor:
Dominique A. Weber, Mingli Feng, Charles A. Parkos, Porfirio Nava, Asma Nusrat, Miguel Quiros, Ryuta Kamekura, Hikaru Nishio
Publikováno v:
Molecular Biology of the Cell
Proinflammatory cytokines promote desmoglein-2 (Dsg2) ectodomain shedding in intestinal epithelial cells. Epithelial exposure to Dsg2 ectodomains compromises intercellular adhesion while also promoting proliferation. These findings identify mechanism
Autor:
Charles A. Parkos, Rakieb Andargachew, Ronen Sumagin, Philipp Neumann, Jennifer C. Brazil, Oscar Medina-Contreras, Dominique A. Weber, Timothy L. Denning, Asma Nusrat, Giovanna Leoni, Ingrid C. McCall
Publikováno v:
Mucosal immunology
Neutrophil transepithelial migration (TEM) during acute inflammation is associated with mucosal injury. Using models of acute mucosal injury in vitro and in vivo, we describe a new mechanism by which neutrophils infiltrating the intestinal mucosa dis
Autor:
Alexander Z. Robin, Dominique A. Weber, Oskar Laur, Charles A. Parkos, Winston Y. Lee, Rakieb Andargachew, Dennis R. Voelker, Bénédicte Fournier
Publikováno v:
Journal of Biological Chemistry. 287:19386-19398
Signal regulatory protein α (SIRPα), a highly glycosylated type-1 transmembrane protein, is composed of three immunoglobulin-like extracellular loops as well as a cytoplasmic tail containing three classical tyrosine-based inhibitory motifs. Previou
Autor:
Charles A. Parkos, Oskar Laur, Ingrid C. McCall, Sean R. Stowell, Rakieb Andargachew, Richard D. Cummings, Winston Y. Lee, Dominique A. Weber
Publikováno v:
Journal of Biological Chemistry. 285:37953-37963
Interaction of SIRPα with its ligand, CD47, regulates leukocyte functions, including transmigration, phagocytosis, oxidative burst, and cytokine secretion. Recent progress has provided significant insights into the structural details of the distal I
Publikováno v:
The Journal of Immunology. 183:4187-4191
HLA-DM catalyzes peptide dissociation and exchange in class II MHC molecules through a mechanism that has been proposed to involve the disruption of specific components of the conserved hydrogen bond network in MHC-peptide complexes. HLA-DR1 molecule
Publikováno v:
Immunologic Research. 29:081-092
Qa-1, a nonclassical class I histocompatibility molecule expressed in mice, predominantly assembles with a single nonameric peptide, Qdm, derived from the signal sequence of certain class Ia molecules. The Qa-1/Qdm complex is the primary ligand for C
Autor:
Jan Pohl, Peter E. Jensen, Dominique A. Weber, Jerrod L. Wigal, Antoine Attinger, Ellis L. Reinherz, Mitchell Kronenberg, Hilde Cheroutre, Yi Xiong, Christopher C. Kemball
Publikováno v:
The Journal of Immunology. 169:5708-5714
The nonclassical class I molecule, thymic leukemia (TL), has been shown to be expressed on intestinal epithelial cells and to interact with CD8+ intraepithelial T lymphocytes. We generated recombinant soluble TL (T18d) H chains in bacteria as inclusi
Publikováno v:
Immunity. 17:95-105
The phenotype and development of T cells from transgenic mice expressing a T cell receptor with specificity for insulin presented by the MHC class Ib molecule Qa-1 b was investigated. Peripheral T cells from the transgenic mice express CD8 and, after
Autor:
Lars Karlsson, Robert A. Bray, Taku Kambayashi, Dominique A. Weber, Peter E. Jensen, Xinjian Chen, Oskar Laur, Shiyong Li
Publikováno v:
The Journal of Experimental Medicine
Human histocompatibility leukocyte antigen (HLA)-DO, a lysosomal resident major histocompatibility complex class II molecule expressed in B cells, has previously been shown to be a negative regulator of HLA-DM peptide loading function. We analyze the