About: Intracellular and extracellular serpins modulate lung disease

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Intracellular and extracellular serpins modulate lung disease
Creator	Askew, D Silverman, G
source	PMC
abstract	An imbalance between peptidases and their inhibitors leads to pulmonary disease. Imbalances occur in the adult and the neonate at risk for a specific set of lung pathologies. Serpins (serine peptidase inhibitors) make up the major source of antipeptidase activity in the lung. The purpose of this review is to describe the serpin mechanism of inhibition, their roles in the normal and pathological lung and their potential as therapeutic agents.
has issue date	2008-12-05(xsd:dateTime)
bibo:doi	10.1038/jp.2008.150
bibo:pmid	19057604
has license	no-cc
sha1sum (hex)	3cae417d49b27a35751da1fc6891f432b34e38fc
schema:url	https://doi.org/10.1038/jp.2008.150
resource representing a document's title	Intracellular and extracellular serpins modulate lung disease
has PubMed Central identifier	PMC7104463
has PubMed identifier	19057604
schema:publication	J Perinatol
resource representing a document's body	covid:3cae417d49b27a35751da1fc6891f432b34e38fc#body_text
is schema:about of	named entity 'neonate' named entity 'serpin' named entity 'risk' named entity 'mechanism' named entity 'interstitial lung disease' named entity 'mouse model' named entity 'a1AT' named entity 'host defense' named entity 'serpins' named entity 'pathogen' named entity 'protein' named entity 'elastase' named entity 'serpin' named entity 'serpins' named entity 'a1AT' named entity 'polymers' named entity 'cytolytic' named entity 'substrate' named entity 'oxygen toxicity' named entity 'clade' named entity 'serpins' named entity 'Serpins' named entity 'animal models' named entity 'animal models' named entity 'neutrophil' named entity 'TNFa' named entity 'serpin' named entity 'a1AT' named entity 'peptidase' named entity 'suicide substrate' named entity 'serine' named entity 'acute respiratory distress' named entity 'a1AT' named entity 'a1AT' named entity 'intracellular' named entity 'Streptococcus' named entity 'a1AT' named entity 'prokaryotes' named entity 'ALI' named entity 'bacteria' named entity 'peptidase' named entity 'mice' named entity 'peptidase' named entity 'oxygen' named entity 'innate immune' named entity 'Clade' named entity 'IL-8' named entity 'Lung function' named entity 'neutrophils' named entity 'a1AT' named entity 'APC' named entity 'peptidase' named entity 'platelet-derived growth factor' named entity 'human plasma' named entity 'preterm infants' named entity 'Exacerbations' named entity 'epithelial' named entity 'fibrin' named entity 'plasminogen activator' named entity 'serpins' named entity 'a1AT' named entity 'pathogens' named entity 'urokinase-type plasminogen activator' named entity 'proteolytic activity' named entity 'hemorrhage' named entity 'bronchial airways' named entity 'lung tissue' named entity 'macrophages' named entity 'ATIII' named entity 'neutrophil' named entity 'peptidase' named entity 'intracellular' named entity 'elastase' named entity 'serine peptidases' named entity 'polymerization' named entity 'a1AT' named entity 'endotoxin' named entity 'COPD' named entity 'viral infection' named entity 'mechanical ventilation'

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