A Human RNA Viral Cysteine Proteinase That Depends upon a Unique Zn2+-binding Finger Connecting the Two Domains of a Papain-like Fold (Q57845086)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10329692%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

24 May 2020

language of work or name

English

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publication date

21 May 1999

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published in

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24 May 2020

volume

274

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24 May 2020

page(s)

14918-14925

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24 May 2020

issue

21

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Evolution of Proteolytic Enzymes

24 May 2020

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Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold

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Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion

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Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases

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Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein

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Identification of essential residues in potyvirus proteinase HC-Pro by site-directed mutagenesis

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Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi- and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha- and coronaviruses

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Characterization of the two overlapping papain-like proteinase domains encoded in gene 1 of the coronavirus infectious bronchitis virus and determination of the C-terminal cleavage site of an 87-kDa protein

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21 January 2018

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Identifiers

DOI

10.1074/JBC.274.21.14918

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10329692%20AND%20SRC:MED&resulttype=core&format=json

24 May 2020

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