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Replication and in vivo repair of the hepatitis A virus genome lacking the poly(A) tail

Journal of general virology, 2005-05, Vol.86 (5), p.1363-1368

2005

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Replication of a hepatitis A virus replicon detected by genetic recombination in vivo

Journal of general virology, 2002-09, Vol.83 (9), p.2183-2192

2002

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Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization

Biochemical journal, 2005-01, Vol.385 (Pt 2), p.363-370

2005

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Immunogenicity of a chimeric hepatitis A virus (HAV) carrying the HIV gp41 epitope 2F5

Antiviral research, 2007-02, Vol.73 (2), p.101-111

2007

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A vaccinia virus MVA-T7-mediated recovery of infectious hepatitis A virus from full-size cDNA or from two cDNAs, both by themselves unable to complete the virus life cycle

Virus research, 2002-10, Vol.89 (1), p.75-88

2002

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Interaction of hepatitis A virus (HAV) precursor proteins 3AB and 3ABC with the 5′ and 3′ termini of the HAV RNA

Virus research, 1997-10, Vol.51 (2), p.151-157

1997

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Proteinase 3C of Hepatitis A Virus (HAV) Cleaves the HAV Polyprotein P2-P3 at All Sites Including VP1/2A and 2A/2B

Virology (New York, N.Y.), 1994-01, Vol.198 (1), p.275-281

1994

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Immunogenicity of a chimeric hepatitis A virus (HAV) carrying the HIV gp41 epitope 2F5

Antiviral research, 2007, Vol.73 (2), p.101-111

2007

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In vitro RNA binding of the hepatitis A virus proteinase 3C (HAV 3Cpro) to secondary structure elements within the 5' terminus of the HAV genome

RNA (Cambridge), 1997-03, Vol.3 (3), p.291-302

1997

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Cell-free translation and proteolytic processing of the hepatitis A virus polyprotein

Journal of general virology, 1993-04, Vol.74 (4), p.677-683

1993

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3C Protease of Enterovirus 68: Structure-Based Design of Michael Acceptor Inhibitors and Their Broad-Spectrum Antiviral Effects against Picornaviruses

Journal of Virology, 2013-04, Vol.87 (8), p.4339-4351

2013

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p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1

Proceedings of the National Academy of Sciences - PNAS, 2016-08, Vol.113 (35), p.E5192-E5201

2016

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RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease

Biochemical and biophysical research communications, 2007-12, Vol.364 (4), p.725-730

2007

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The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein

Biochemical and biophysical research communications, 2007-12, Vol.364 (4), p.877-882

2007

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La autoantigen suppresses IRES-dependent translation of the hepatitis A virus

Biochemical and biophysical research communications, 2008-04, Vol.368 (4), p.1014-1019

2008

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A new G-tailing method for the determination of the poly(A) tail length applied to hepatitis A virus RNA

Nucleic acids research, 2001-06, Vol.29 (12), p.E57-57

2001

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p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PL pro via E3 ubiquitin ligase RCHY1

Proceedings of the National Academy of Sciences - PNAS, 2016-08, Vol.113 (35)

2016

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p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PL^sup pro^ via E3 ubiquitin ligase RCHY1

Proceedings of the National Academy of Sciences - PNAS, 2016-08, Vol.113 (35), p.E5192

2016

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p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PL super( pro) via E3 ubiquitin ligase RCHY1

Proceedings of the National Academy of Sciences - PNAS, 2016-08, Vol.113 (35), p.E5192-E5192

2016

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Suppression of hepatitis A virus genome translation and replication by siRNAs targeting the internal ribosomal entry site

Biochemical and biophysical research communications, 2005-05, Vol.330 (4), p.1217-1223

2005

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Interference of hepatitis A virus replication by small interfering RNAs

Biochemical and biophysical research communications, 2004-05, Vol.318 (2), p.341-345

2004

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Immunogenic epitopes on the surface of the hepatitis A virus capsid: Impact of secondary structure and/or isoelectric point on chimeric virus assembly

Virus research, 2007-12, Vol.130 (1), p.296-302

2007

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Improving proteolytic cleavage at the 3A/3B site of the hepatitis A virus polyprotein impairs processing and particle formation, and the impairment can be complemented in trans by 3AB and 3ABC

Journal of virology, 1999-12, Vol.73 (12), p.9867-9878

1999

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Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates

Journal of Virology, 1995-03, Vol.69 (3), p.1727-1733

1995

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Chimeric hepatitis A virus particles presenting a foreign epitope (HIV gp41) at their surface

Antiviral research, 2002-08, Vol.55 (2), p.369-377

2002

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Replication and in vivo repair of the hepatitis A virus genome lacking the poly(A) tail

Replication of a hepatitis A virus replicon detected by genetic recombination in vivo

Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization

Immunogenicity of a chimeric hepatitis A virus (HAV) carrying the HIV gp41 epitope 2F5

A vaccinia virus MVA-T7-mediated recovery of infectious hepatitis A virus from full-size cDNA or from two cDNAs, both by themselves unable to complete the virus life cycle

Interaction of hepatitis A virus (HAV) precursor proteins 3AB and 3ABC with the 5′ and 3′ termini of the HAV RNA

Proteinase 3C of Hepatitis A Virus (HAV) Cleaves the HAV Polyprotein P2-P3 at All Sites Including VP1/2A and 2A/2B

Immunogenicity of a chimeric hepatitis A virus (HAV) carrying the HIV gp41 epitope 2F5

In vitro RNA binding of the hepatitis A virus proteinase 3C (HAV 3Cpro) to secondary structure elements within the 5' terminus of the HAV genome

Cell-free translation and proteolytic processing of the hepatitis A virus polyprotein

3C Protease of Enterovirus 68: Structure-Based Design of Michael Acceptor Inhibitors and Their Broad-Spectrum Antiviral Effects against Picornaviruses

p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1

RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease

The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein

La autoantigen suppresses IRES-dependent translation of the hepatitis A virus

A new G-tailing method for the determination of the poly(A) tail length applied to hepatitis A virus RNA

p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PL pro via E3 ubiquitin ligase RCHY1

p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PL^sup pro^ via E3 ubiquitin ligase RCHY1

p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PL super( pro) via E3 ubiquitin ligase RCHY1

Suppression of hepatitis A virus genome translation and replication by siRNAs targeting the internal ribosomal entry site

Interference of hepatitis A virus replication by small interfering RNAs

Immunogenic epitopes on the surface of the hepatitis A virus capsid: Impact of secondary structure and/or isoelectric point on chimeric virus assembly

Improving proteolytic cleavage at the 3A/3B site of the hepatitis A virus polyprotein impairs processing and particle formation, and the impairment can be complemented in trans by 3AB and 3ABC

Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates

Chimeric hepatitis A virus particles presenting a foreign epitope (HIV gp41) at their surface

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