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@ARTICLE{Sirois:137086,
author = {Sirois, Cherilyn M and Jin, Tengchuan and Miller, Allison L
and Bertheloot, Damien and Nakamura, Hirotaka and Horvath,
Gabor L and Mian, Abubakar and Jiang, Jiansheng and Schrum,
Jacob and Bossaller, Lukas and Pelka, Karin and Garbi,
Natalio and Brewah, Yambasu and Tian, Jane and Chang,
ChewShun and Chowdhury, Partha S and Sims, Gary P and
Kolbeck, Roland and Coyle, Anthony J and Humbles, Alison A
and Xiao, T Sam and Latz, Eicke},
title = {{RAGE} is a nucleic acid receptor that promotes
inflammatory responses to {DNA}.},
journal = {Journal of experimental medicine},
volume = {210},
number = {11},
issn = {1540-9538},
address = {New York, NY},
publisher = {Rockefeller Univ. Press},
reportid = {DZNE-2020-03408},
pages = {2447-2463},
year = {2013},
abstract = {Recognition of DNA and RNA molecules derived from pathogens
or self-antigen is one way the mammalian immune system
senses infection and tissue damage. Activation of immune
signaling receptors by nucleic acids is controlled by
limiting the access of DNA and RNA to intracellular
receptors, but the mechanisms by which endosome-resident
receptors encounter nucleic acids from the extracellular
space are largely undefined. In this study, we show that the
receptor for advanced glycation end-products (RAGE) promoted
DNA uptake into endosomes and lowered the immune recognition
threshold for the activation of Toll-like receptor 9, the
principal DNA-recognizing transmembrane signaling receptor.
Structural analysis of RAGE-DNA complexes indicated that DNA
interacted with dimers of the outermost RAGE extracellular
domains, and could induce formation of higher-order receptor
complexes. Furthermore, mice deficient in RAGE were unable
to mount a typical inflammatory response to DNA in the lung,
indicating that RAGE is important for the detection of
nucleic acids in vivo.},
keywords = {Animals / Base Sequence / Cell Membrane: metabolism /
Crystallography, X-Ray / DNA: chemistry / DNA: metabolism /
Endocytosis / Endosomes: metabolism / HEK293 Cells / HeLa
Cells / Humans / Ligands / Lung: metabolism / Lung:
pathology / Mice / Mice, Inbred C57BL / Models, Molecular /
NF-kappa B: metabolism / Pneumonia: metabolism / Pneumonia:
pathology / Protein Binding / Protein Multimerization /
Protein Structure, Tertiary / Receptor for Advanced
Glycation End Products / Receptors, Immunologic: chemistry /
Receptors, Immunologic: metabolism / Static Electricity /
Toll-Like Receptor 9: metabolism / Ligands (NLM Chemicals) /
NF-kappa B (NLM Chemicals) / Receptor for Advanced Glycation
End Products (NLM Chemicals) / Receptors, Immunologic (NLM
Chemicals) / Toll-Like Receptor 9 (NLM Chemicals) / DNA (NLM
Chemicals)},
cin = {AG Latz},
ddc = {610},
cid = {I:(DE-2719)1013024},
pnm = {342 - Disease Mechanisms and Model Systems (POF3-342)},
pid = {G:(DE-HGF)POF3-342},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:24081950},
pmc = {pmc:PMC3804942},
doi = {10.1084/jem.20120201},
url = {https://pub.dzne.de/record/137086},
}