The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain

FEBS Journal

Volumn 273, Issue 5, 2006, Pages 1035-1045

  Shi, Jiahai ^b   Song, Jianxing ^a,b  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

3C LIKE PROTEASE; MONOMER; PROTEINASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CIRCULAR DICHROISM; DIMERIZATION; ENZYMATIC ASSAY; ENZYME ACTIVITY; ENZYME STRUCTURE; GENE DELETION; LIGHT SCATTERING; MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; SARS CORONAVIRUS; WILD TYPE;

CATALYSIS; CATALYTIC DOMAIN; CIRCULAR DICHROISM; CYSTEINE ENDOPEPTIDASES; DIMERIZATION; LIGHT; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SARS VIRUS; SCATTERING, RADIATION; VIRAL PROTEINS;

CORONAVIRUS; SARS CORONAVIRUS;

EID: 33644946136     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05130.x     Document Type: Article

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