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bronchitis/protease
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Seite 1 von 168 Ergebnisse
A region of the coronavirus infectious bronchitis virus 1a polyprotein encoding the 3C-like protease domain is subject to rapid turnover when expressed in rabbit reticulocyte lysate.
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In order to investigate the mechanisms involved in the processing of infectious bronchitis virus polyproteins, several candidate regions of the genome have been cloned and expressed in vitro. During these studies it was observed that the translation product encoded by one of these clones (pKT205)
Preliminary crystallographic analysis of avian infectious bronchitis virus main protease.
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Infectious bronchitis virus (IBV) is the prototype of the genus Coronavirus. It causes a highly contagious disease which affects the respiratory, reproductive, neurological and renal systems of chickens, resulting great economic losses in the poultry industry worldwide. The coronavirus (CoV) main
The papain-like protease of avian infectious bronchitis virus has deubiquitinating activity.
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Coronavirus papain-like proteases (PLPs) can act as proteases that process virus-encoded large replicase polyproteins and also as deubiquitinating (DUB) enzymes. Like the PLPs of other coronaviruses (CoVs), the avian infectious bronchitis virus (IBV) PLP catalyzes proteolysis of Gly-Gly dipeptide
Structural view and substrate specificity of papain-like protease from avian infectious bronchitis virus.
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Papain-like protease (PLpro) of coronaviruses (CoVs) carries out proteolytic maturation of non-structural proteins that play a role in replication of the virus and performs deubiquitination of host cell factors to scuttle antiviral responses. Avian infectious bronchitis virus (IBV), the causative
[Effect of the protease inhibitor aprotinin on pulmonary function and on the inhibitory activity of sputum in patients with chronic obstructive bronchitis].
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It has been investigated whether a substitution of protease inhibitor deficiency is indicated in case of chronic obstructive airway disease. As a therapeutic possibility, apronitin isolated from bovine organs (tyasylol), which in vitro inhibits sputum proteases up to 80 per cent was tested. Besides
Inflammatory indices for chronic bronchitis and COAD. Proteases and antiproteases.
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The study of lung secretion proteinases and their inhibitors, both functionally and quantitatively, provide information concerning the degree of inflammation in the lung. Interpretation of individual parameters may be difficult in isolation. However, a general pattern of response provides supportive
[Mucous membrane specific protease inhibitors in bronchial mucus in severe chronic obstructive bronchitis and in alpha 1-antitrypsin deficiency syndrome].
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In the bronchial mucus of 40 patients with chronic obstructive airway diseases we measured proteolytic activities, the total protein concentrations, alpha1-antitrypsin, alpha1-antichymotrypsin, and the free and bound proteinase inhibitors together with the total proteinase inhibition against trypsin
Intestinal Tropism of an Infectious Bronchitis Virus Isolate Not Explained by Spike Protein Binding Specificity.
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An infectious bronchitis virus (IBV) with an unusual enteric tropism (CalEnt) was isolated from a California broiler flock exhibiting runting-stunting syndrome. IBV was detected in the small intestine, but not in the respiratory tract or kidney. During virus isolation in embryos, it did not
Gga-miR-30d regulates infectious bronchitis virus infection by targeting USP47 in HD11 cells.
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Avian infectious bronchitis virus (IBV) is a coronavirus which infects chickens and causes severe economic losses to the poultry industry worldwide. MicroRNAs (miRNAs) are important intracellular regulators and play a pivotal role in viral infections. In previous studies, we have revealed that IBV
Treatment with Exogenous Trypsin Expands In Vitro Cellular Tropism of the Avian Coronavirus Infectious Bronchitis Virus
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The Gammacoronavirus infectious bronchitis virus (IBV) causes a highly contagious and economically important respiratory disease in poultry. In the laboratory, most IBV strains are restricted to replication in ex vivo organ cultures or in ovo and do not replicate in cell culture, making the
[Impaired balance of the lung proteolytic system in patients with pneumoconiosis and chronic dust-induced bronchitis].
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The activity of neutrophilic elastase and the level of its major inhibitor--an alpha 1-inhibitor of proteinases were studied to evaluate the protease-antiprotease system in the bronchoalveolar lavage fluid (BALF) of patients with chronic dust-induced bronchitis (CDB) and pneumoconiosis (PC). It was
[Proteolytic activities in bronchoalveolar lavage fluid in pneumonia and chronic bronchitis].
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In 63 patients with chronic bronchitis, 61 patients with acute bacterial pneumonia, and in 11 control subjects, broncho-alveolar lavage fluid was investigated for its protease content. In smokers, we found the usual pronounced protease burden. As was expected, the two pathological groups also
Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer.
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[35S]methionine-labelled avian infectious bronchitis virus (IBV) (strain 41) and its purified protein components and virions of IBV-Beaudette were incubated with 10 proteases. Several proteases hydrolysed all or some of the membrane glycopolypeptide (M; Mr 30K) and removed about 1.3K of peptide from
Granulocyte collagenase, elastase and plasma protease inhibitors in purulent sputum.
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Sputum was collected from patients with purulent chronic bronchitis. Immuno-chemical techniques using rabbit antiserum against human granulocyte collagenase and elastase showed the presence of both enzymes. Also the serum protease ingibitors alpha1-antitrypsin and alpha2-macroglobulin were
Protease-antiprotease imbalance: local evaluation with bronchoalveolar lavage.
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The protease-antiprotease imbalance is thought to be involved in a variety of destructive lung diseases: pulmonary emphysema, chronic bronchitis, cystic fibrosis and adult respiratory distress syndrome. Bronchoalveolar lavage allowed the investigators to assess the protease-antiprotease shift in
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