Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus. - Test2 - elhamkhani - TriplyDB

Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus.

Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus.

http://www.wikidata.org/entity/Q40041889

about

3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity Structural Basis of Substrate Specificity and Protease Inhibition in Norwalk Virus Rabbit haemorrhagic disease (RHD) and rabbit haemorrhagic disease virus (RHDV): a review Antiviral targets of human noroviruses In vitro proteolytic processing of the MD145 norovirus ORF1 nonstructural polyprotein yields stable precursors and products similar to those detected in calicivirus-infected cells.Complete nucleotide sequence and genetic organization of Aichi virus, a distinct member of the Picornaviridae associated with acute gastroenteritis in humans Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase.Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.Proteolytic processing of sapovirus ORF1 polyprotein.Identification of active-site amino acid residues in the Chiba virus 3C-like protease Processing of rabbit hemorrhagic disease virus polyprotein.Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis.X-ray crystallographic structure of the Norwalk virus protease at 1.5-A resolution.Trans activity of the norovirus Camberwell proteinase and cleavage of the N-terminal protein encoded by ORF1.Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein.Highly conserved configuration of catalytic amino acid residues among calicivirus-encoded proteases.Detection of viral proteins after infection of cultured hepatocytes with rabbit hemorrhagic disease virus.Expression of enzymatically active rabbit hemorrhagic disease virus RNA-dependent RNA polymerase in Escherichia coli.Two independent pathways of expression lead to self-assembly of the rabbit hemorrhagic disease virus capsid protein Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies.Detection and preliminary characterization of a new rabbit calicivirus related to rabbit hemorrhagic disease virus but nonpathogenic.Norwalk virus nonstructural protein p48 forms a complex with the SNARE regulator VAP-A and prevents cell surface expression of vesicular stomatitis virus G protein.

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P2860

Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus.

http://www.wikidata.org/entity/Q40041889

description

1994 nî lūn-bûn

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1994年の論文

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1994年論文

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1994年論文

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1994年論文

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1994年論文

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1994年論文

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1994年论文

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1994年论文

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1994年论文

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name

Identification and characteriz ...... disease virus, a calicivirus.

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Identification and characteriz ...... disease virus, a calicivirus.

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Identification and characteriz ...... disease virus, a calicivirus.

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Journal of Virology

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Identification and characteriz ...... c disease virus, a calicivirus

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P2093

Boniotti B

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Meyers G

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Rossi C

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Sibilia M

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Thiel HJ

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Wirblich C

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P2860

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Rapid and efficient site-specific mutagenesis without phenotypic selection

Characterization of the catalytic residues of the tobacco etch virus 49-kDa proteinase

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

Viral proteinases.

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

Poliovirus thiol proteinase 3C can utilize a serine nucleophile within the putative catalytic triad.

Site-directed mutagenesis suggests close functional relationship between a human rhinovirus 3C cysteine protease and cellular trypsin-like serine proteases.

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6487-6495

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scholarly article

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10

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68

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1994-10-01T00:00:00Z

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237069

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