Enzyme kinetics of the human norovirus protease control virus polyprotein processing order. (Q42284135)

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scientific article published on 11 July 2013

Language	Label	Description	Also known as
English	Enzyme kinetics of the human norovirus protease control virus polyprotein processing order.	scientific article published on 11 July 2013

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5 March 2020

Enzyme kinetics of the human norovirus protease control virus polyprotein processing order (English)

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5 March 2020

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5 March 2020

Prasanth Viswanathan

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5 March 2020

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Brent Korba

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5 March 2020

Alexei Medvedev

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5 March 2020

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11 July 2013

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5 March 2020

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5 March 2020

444

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5 March 2020

1-2

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5 March 2020

218-224

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5 March 2020

In vitro proteolytic processing of the MD145 norovirus ORF1 nonstructural polyprotein yields stable precursors and products similar to those detected in calicivirus-infected cells.

1 reference

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Substrate specificity of the Norwalk virus 3C-like proteinase

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Sequence and genomic organization of Norwalk virus

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Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides

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Sequence and genome organization of a human small round-structured (Norwalk-like) virus

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A norovirus protease structure provides insights into active and substrate binding site integrity

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Systematic literature review of role of noroviruses in sporadic gastroenteritis

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Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral protease

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On the size of the active site in proteases. I. Papain

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Differential cleavage of the norovirus polyprotein precursor by two active forms of the viral protease

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Norovirus infectivity in humans and persistence in water

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Norovirus Illness Is a Global Problem: Emergence and Spread of Norovirus GII.4 Variants, 2001–2007

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Cleavage map and proteolytic processing of the murine norovirus nonstructural polyprotein in infected cells

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Product inhibition of the hepatitis C virus NS3 protease

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RNA binding by human Norovirus 3C-like proteases inhibits protease activity

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Recovery of infectious murine norovirus using pol II-driven expression of full-length cDNA.

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Proteinase-polymerase precursor as the active form of feline calicivirus RNA-dependent RNA polymerase

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Mutations in HCV non-structural genes do not contribute to resistance to nitazoxanide in replicon-containing cells.

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X-ray crystallographic structure of the Norwalk virus protease at 1.5-A resolution

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Specificity of the hepatitis C virus NS3 serine protease: effects of substitutions at the 3/4A, 4A/4B, 4B/5A, and 5A/5B cleavage sites on polyprotein processing

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2013.06.013

7 January 2021

based on heuristic

inferred from DOI database lookup

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