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The Papain-Like Protease from the Severe Acute Respiratory Syndrome Coronavirus Is a Deubiquitinating Enzyme
ABSTRACT The severe acute respiratory syndrome coronavirus papain-like protease (SARS-CoV PLpro) is involved in the processing of the viral polyprotein and, thereby, contributes to the biogenesis ofExpand
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Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.
Cathepsin L is a member of the papain superfamily of cysteine proteases and, like many other proteases, it is synthesized as an inactive proenzyme. Its prosegment shows little homology to that ofExpand
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Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease
Abstract The severe acute respiratory syndrome coronavirus papain-like protease (SARS-CoV PLpro) carries out N-terminal processing of the viralExpand
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Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases.
The cathepsin L propeptide (phcl-2) was expressed in Saccharomyces cerevisiae using a human procathepsin L/alpha-factor fusion construct containing a stop codon at position -1 (the C-terminal aminoExpand
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Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion and unique insertions 1
A novel cDNA encoding a cysteine protease of the papain family named cathepsin X was obtained by PCR amplification from a human ovary cDNA library. The cathepsin X cDNA is ubiquitously expressed inExpand
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Catalytic mechanism in papain family of cysteine peptidases.
Publisher Summary This chapter summarizes catalytic mechanism for cysteine peptidases of the papain family. Cysteine peptidases of the papain family catalyze the hydrolysis of peptide, amide, ester,Expand
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The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo.
Glucosidase II is an ER heterodimeric enzyme that cleaves sequentially the two innermost alpha-1,3-linked glucose residues from N-linked oligosaccharides on nascent glycoproteins. This processingExpand
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A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain.
The controversy concerning the various suggested roles for the side chain of Asp158 in the active site of papain has been clarified by using site-directed mutagenesis. Both wild-type papain and anExpand
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Human cathepsin X: A cysteine protease with unique carboxypeptidase activity.
Cathepsin X is a novel cysteine protease which was identified recently from the EST (expressed sequence tags) database. In a homology model of the mature cathepsin X, a unique three residue insertionExpand
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Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine.
Human cathepsin X is one of many proteins discovered in recent years through the mining of sequence databases. Its sequence shows clear homology to cysteine proteases from the papain family,Expand
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