triose phosphate isomerase/inflammation

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Seroreactivity against glycolytic enzymes in inflammatory bowel disease.

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BACKGROUND Patients with inflammatory bowel disease (IBD) carry autoantibodies such as perinuclear antineutrophil cytoplasmic antibodies. The aim of the current study was to further characterize the immune reactivity in IBD. METHODS We used an immunoproteomic approach with extracts from granulocytes

Transient expression of Ym1, a heparin-binding lectin, during developmental hematopoiesis and inflammation.

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Ym1, a secretory protein transiently produced by activated peritoneal macrophages elicited by parasitic infections, has been identified as a novel heparin-binding lectin. X-ray crystallography study revealed that Ym1 has a beta/alpha barrel structure with a carbohydrate-binding cleft similar to that

PCR detection of Clostridium difficile triose phosphate isomerase (tpi), toxin A (tcdA), toxin B (tcdB), binary toxin (cdtA, cdtB), and tcdC genes in Vhembe District, South Africa.

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Specific polymerase chain reaction (PCR) protocols were used to determine the prevalence of toxigenic Clostridium difficile in Vhembe, South Africa. Of 322 stool samples collected, toxigenic C. difficile was found in 23 (7.1%) cases and was significantly associated with diarrhea 20 (11.4%) compared

Hypoxia-like effect of cobalt chromium alloy micro particles on fibroblasts in vitro.

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Periprosthetic osteolysis leading to asceptic loosening remains the primary cause of failure of joint replacement. Although many inflammatory cell types have been implicated, the exact pathomechanisms of asceptic loosening have not been delineated. In the present study we have adopted a proteomic

Coculture with Clostridium difficile promotes apoptosis of human intestinal microvascular endothelial cells.

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OBJECTIVE The clostridial triose-phosphate isomerase ( tpi) gene is a housekeeping gene that specifically distinguishes Clostridium difficile from other bacteria. This retrospective cohort study was performed to analyze and compare the TPI protein-positive rates in outpatients and hospitalized

Analysis of the effect of changing environmental conditions on the expression patterns of exported surface-associated proteins of the oral pathogen Actinobacillus actinomycetemcomitans.

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Actinobacillus actinomycetemcomitans has been specifically implicated in the aetiology of one or more of the periodontal diseases, conditions in which inflammation of the gums is associated with destruction of the alveolar bone supporting the teeth. In these diseases there is loss of attachment of

Structure of human stabilin-1 interacting chitinase-like protein (SI-CLP) reveals a saccharide-binding cleft with lower sugar-binding selectivity.

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Human secreted protein stabilin-1 interacting chitinase-like protein (SI-CLP) has been identified as a novel member of Glyco_18 domain-containing proteins that is involved in host defense and inflammatory reactions. Efficient secretion of SI-CLP is mediated by its interaction with the

Proteomic analysis of soluble protein extract of adult Toxocara cati

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Toxocara cati is a cat roundworm and the causative agent of toxocariasis as a cosmopolitan zoonotic disease. As no information has been reported so far, identification of T. cati proteins can be useful for the development of new diagnostic strategies. This study was conducted to identify the major

Alterations in brain antioxidant enzymes and redox proteomic identification of oxidized brain proteins induced by the anti-cancer drug adriamycin: implications for oxidative stress-mediated chemobrain.

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Adriamycin (ADR) is a chemotherapeutic for the treatment of solid tumors. This quinone-containing anthracycline is well known to produce large amounts of reactive oxygen species (ROS) in vivo. A common complaint of patients undergoing long-term treatment with ADR is somnolence, often referred to as

The caspase-1 digestome identifies the glycolysis pathway as a target during infection and septic shock.

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Caspase-1 is an essential effector of inflammation, pyroptosis, and septic shock. Few caspase-1 substrates have been identified to date, and these substrates do not account for its wide range of actions. To understand the function of caspase-1, we initiated the systematic identification of its

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