Peptide aldehyde inhibitors challenge the substrate specificity of the SARS-coronavirus main protease

Antiviral Research

Volumn 92, Issue 2, 2011, Pages 204-212

  Zhu, Lili ^a   George, Shyla ^a   Schmidt, Marco F ^b   Al Gharabli, Samer I ^c   Rademann, Jörg ^b,d   Hilgenfeld, Rolf ^a,e,f  

^a UNIVERSITY OF LÜBECK   (Germany)

^b LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

^c GERMAN JORDANIAN UNIVERSITY   (Jordan)

^d UNIVERSITY OF LEIPZIG   (Germany)

^e SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^f DESY   (Germany)

Author keywords

Aldehyde inhibitor; Antiviral drug design; Cysteine protease; Methionine aspartic acid interaction; X ray crystallography

Indexed keywords

ALDEHYDE; AMINO ACID; ASPARTIC ACID; ENZYME INHIBITOR; PENTAPEPTIDE; PEPTIDE ALDEHYDE INHIBITOR; PHENYLALANINE; PROTEINASE; SERINE; TETRADECAPEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CLEAVAGE; SARS CORONAVIRUS; VIRUS INHIBITION;

ALDEHYDES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE ENDOPEPTIDASES; ENZYME INHIBITORS; KINETICS; MODELS, MOLECULAR; PEPTIDES; PROTEIN CONFORMATION; SARS VIRUS; SUBSTRATE SPECIFICITY; VIRAL PROTEINS;

SARS CORONAVIRUS;

EID: 80054851231     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2011.08.001     Document Type: Article

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