In: The VLDB Journal, 2014, vol. 23, no. 2, p. 253-278
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In: Pediatric Nephrology, 2014, vol. 29, no. 6, p. 1015-1023
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In: Histochemistry and Cell Biology, 2014, vol. 142, no. 2, p. 153-169
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In: Pediatric Nephrology, 2014, vol. 29, no. 11, p. 2133-2138
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In: Endocrine, 2014, vol. 47, no. 2, p. 435-448
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In: The journal of experimental medicine, 2016, vol. 213, no. 3, p. 355-375
Omenn syndrome (OS) is caused by hypomorphic Rag mutations and characterized by a profound immunodeficiency associated with autoimmune-like manifestations. Both in humans and mice, OS is mediated by oligoclonal activated T and B cells. The role of microbial signals in disease pathogenesis is debated. Here, we show that Rag2R229Q knock-in mice developed an inflammatory bowel disease affecting...
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In: The journal of experimental medicine, 2012, vol. 209, no. 9, p. 1519-1528
Tissue damage causes inflammation, by recruiting leukocytes and activating them to release proinflammatory mediators. We show that high-mobility group box 1 protein (HMGB1) orchestrates both processes by switching among mutually exclusive redox states. Reduced cysteines make HMGB1 a chemoattractant, whereas a disulfide bond makes it a proinflammatory cytokine and further cysteine oxidation to...
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In: The journal of experimental medicine, 2012, vol. 209, no. 3, p. 551-563
After tissue damage, inflammatory cells infiltrate the tissue and release proinflammatory cytokines. HMGB1 (high mobility group box 1), a nuclear protein released by necrotic and severely stressed cells, promotes cytokine release via its interaction with the TLR4 (Toll-like receptor 4) receptor and cell migration via an unknown mechanism. We show that HMGB1- induced recruitment of inflammatory...
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In: Journal of virology, 2014, vol. 88, no. 18, p. 10272-10275
An essential step during the intracellular life cycle of many positive-strand RNA viruses is the rearrangement of host cell membranes to generate membrane-bound replication platforms. For example, Nidovirales and Flaviviridae subvert the membrane of the endoplasmic reticulum (ER) for their replication. However, the absence of conventional ER and secretory pathway markers in virus-induced...
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In: The journal of cell biology, 2010, vol. 188, no. 2, p. 223–235
Sophisticated quality control mechanisms prolong retention of protein-folding intermediates in the endoplasmic reticulum (ER) until maturation while sorting out terminally misfolded polypeptides for ER-associated degradation (ERAD). The presence of structural lesions in the luminal, transmembrane, or cytosolic domains determines the classification of misfolded polypeptides as ERAD-L, -M, or -C...
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