About: Cysteine proteinases of microorganisms and viruses

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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
has title	Cysteine proteinases of microorganisms and viruses
Source	Medline; PMC
abstract	This review considers properties of secreted cysteine proteinases of protozoa, bacteria, and viruses and presents information on the contemporary taxonomy of cysteine proteinases. Literature data on the structure and physicochemical and enzymatic properties of these enzymes are reviewed. High interest in cysteine proteinases is explained by the discovery of these enzymes mostly in pathogenic organisms. The role of the proteinases in pathogenesis of several severe diseases of human and animals is discussed.
has issue date	2011-01-19(xsd:dateTime)
bibo:doi	10.1134/s000629790801001x
bibo:pmid	18294123
has license	no-cc
sha1sum (hex)	f1bad5bddce3b333d7fb63eeaadaa5258b59ca7e
schema:url	https://doi.org/10.1134/s000629790801001x
resource representing a document's title	Cysteine proteinases of microorganisms and viruses
has PubMed Central identifier	PMC7087786
has PubMed identifier	18294123
schema:publication	Biochemistry (Mosc)
resource representing a document's body	covid:f1bad5bddce3b333d7fb63eeaadaa5258b59ca7e#body_text
is schema:about of	named entity 'hemoglobin' named entity 'Cys' named entity 'pyroglutamyl peptidase' named entity 'cathepsin' named entity 'proteinase' named entity 'microbiological' named entity 'dashed' named entity 'parasite' named entity 'reagent' named entity 'Asp' named entity 'host cells' named entity 'Endopeptidases' named entity 'protein' named entity 'Reducing agents' named entity 'EDTA' named entity 'RNA' named entity 'cysteine' named entity 'motif' named entity 'caspases' named entity 'nsP2' named entity 'cleavage' named entity 'picornaviruses' named entity 'proteinases' named entity 'amino acid residues' named entity 'Cysteine' named entity 'alanine' named entity 'organism' named entity 'hydrolyze' named entity 'heavy chain' named entity 'picornain 3C' named entity 'PCP' named entity 'tosyl' named entity 'active site' named entity 'Genome' named entity 'cysteine' named entity 'Papain' named entity 'cysteine' named entity 'fibrinogen' named entity 'homology' named entity 'endopeptidase' named entity 'molecule' named entity 'macroglobulin' named entity 'Chagas' disease' named entity 'nutrition' named entity 'photosynthesizing' named entity 'oxidants' named entity 'tosyl' named entity 'polyprotein' named entity 'catalytic domain' named entity 'gene' named entity 'tertiary structures' named entity 'immunoglobulins' named entity 'Euglenales' named entity 'virus' named entity 'Malaria' named entity 'Cys' named entity 'abscess' named entity 'trichomonads' named entity 'gingipain' named entity 'Infection' named entity 'parasite' named entity 'protein' named entity 'oxygen' named entity 'Streptopain' named entity 'RNA' named entity 'molecular weight' named entity 'proteinase' named entity 'substrates' named entity 'nsP4' named entity 'substrates' named entity 'erythrocyte membrane' named entity 'substrates' named entity 'hydrophobic' named entity 'cysteine' named entity 'picornavirus' named entity 'cis' named entity 'proteinase' named entity 'papain' named entity 'disulfide bonds' named entity 'Cys' named entity 'fibronectin' named entity 'substrate specificity'

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