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Sensitive, soluble chromogenic substrates for HIV-1 proteinase

The Journal of biological chemistry, 1990-05, Vol.265 (14), p.7733-7736

1990

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An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features

Microbiology (Society for General Microbiology), 2004-07, Vol.150 (Pt 7), p.2475

2004

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The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix

Nature structural & molecular biology, 2000-02, Vol.7 (2), p.113-117

2000

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High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum

FEBS letters, 1994-09, Vol.352 (2), p.155-158

1994

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Hydrolysis of synthetic chromogenic substrates by HIV-1 and HIV-2 proteinases

Biochemical and biophysical research communications, 1990-08, Vol.171 (1), p.439-444

1990

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Bacterial aspartic proteinases

FEBS letters, 1997-06, Vol.409 (3), p.357-360

1997

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Intrinsic activity of precursor forms of HIV-1 proteinase

FEBS letters, 1992-12, Vol.314 (3), p.449-454

1992

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Bacterial aspartic proteinases as novel antibiotic targets

Advances in experimental medicine and biology, 1998, Vol.436, p.321

1998

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Sensitivity to inhibition and catalytic efficiency of HIV proteinase mutants

Advances in experimental medicine and biology, 1998, Vol.436, p.85

1998

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Mutating P2 and P1 residues at cleavage junctions in the HIV-1 pol polyprotein Effects on hydrolysis by HIV-1 proteinase

FEBS letters, 1991-06, Vol.283 (2), p.180-184

1991

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Activities of precursor and tethered dimer forms of HIV proteinase

Advances in experimental medicine and biology, 1995, Vol.362, p.467

1995

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Escape mutants of HIV-1 proteinase: enzymic efficiency and susceptibility to inhibition

Biochimica et biophysica acta, 1997-04, Vol.1339 (1), p.113-125

1997

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The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae

The Journal of biological chemistry, 2001-01, Vol.276 (3), p.2023

2001

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An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae

Biochemical and biophysical research communications, 2002-07, Vol.295 (4), p.1020-1026

2002

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IA sub(3), an Aspartic Proteinase Inhibitor from Saccharomyces cerevisiae, Is Intrinsically Unstructured in Solution

Biochemistry (Easton), 2004-04, Vol.43 (14), p.4071-4081

2004

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Aspartic proteinases and inhibitors in plant pathogenesis

Advances in experimental medicine and biology, 1998, Vol.436, p.441

1998

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The Potency and Specificity of the Interaction between the IA sub(3) Inhibitor and Its Target Aspartic Proteinase from Saccharomyces cerevisiae

The Journal of biological chemistry, 2001-01, Vol.276 (3), p.2023-2030

2001

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Sub-site preferences of the aspartic proteinase from the human immunodeficiency virus, HIV-1

FEBS letters, 1990-07, Vol.268 (1), p.35-38

1990

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Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D

Biochimica et biophysica acta, 2002-04, Vol.1596 (1), p.76-82

2002

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Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic-hydrophobic- or -aromatic-Pro- cleavage sites

Biochemistry (Easton), 1992-06, Vol.31 (22), p.5193-5200

1992

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Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobichydrophobic- or -aromaticpro- cleavage sites

Biochemistry (Easton), 1992-06, Vol.31 (22), p.5193-5200

1992

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Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobichydrophobic- or -aromatic super()Pro- cleavage sites

Biochemistry (Easton), 1992-01, Vol.31 (22), p.5193-5200

1992

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Sensitive, soluble chromogenic substrates for HIV-1 proteinase

The Journal of biological chemistry, 1990-01, Vol.264 (14), p.7733-7736

1990

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Sub-site preferences of the aspartic proteinase from the human immunodeficiency virus, HIV-1

FEBS letters, 1990-01, Vol.263 (1), p.35-38

1990

Volltextzugriff (PDF)

Sub-site preference of the aspartic proteinase from the human immunodeficiency virus, HIV-1

FEBS letters, 1990, Vol.268 (1), p.35-38

1990

Volltextzugriff (PDF)

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Sensitive, soluble chromogenic substrates for HIV-1 proteinase

An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features

The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix

High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum

Hydrolysis of synthetic chromogenic substrates by HIV-1 and HIV-2 proteinases

Bacterial aspartic proteinases

Intrinsic activity of precursor forms of HIV-1 proteinase

Bacterial aspartic proteinases as novel antibiotic targets

Sensitivity to inhibition and catalytic efficiency of HIV proteinase mutants

Mutating P2 and P1 residues at cleavage junctions in the HIV-1 pol polyprotein Effects on hydrolysis by HIV-1 proteinase

Activities of precursor and tethered dimer forms of HIV proteinase

Escape mutants of HIV-1 proteinase: enzymic efficiency and susceptibility to inhibition

The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae

An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae

IA sub(3), an Aspartic Proteinase Inhibitor from Saccharomyces cerevisiae, Is Intrinsically Unstructured in Solution

Aspartic proteinases and inhibitors in plant pathogenesis

The Potency and Specificity of the Interaction between the IA sub(3) Inhibitor and Its Target Aspartic Proteinase from Saccharomyces cerevisiae

Sub-site preferences of the aspartic proteinase from the human immunodeficiency virus, HIV-1

Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D

Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic-hydrophobic- or -aromatic-Pro- cleavage sites

Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobichydrophobic- or -aromaticpro- cleavage sites

Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobichydrophobic- or -aromatic super()Pro- cleavage sites

Sensitive, soluble chromogenic substrates for HIV-1 proteinase

Sub-site preferences of the aspartic proteinase from the human immunodeficiency virus, HIV-1

Sub-site preference of the aspartic proteinase from the human immunodeficiency virus, HIV-1

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