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Structural and Antiviral Studies of the Human Norovirus GII.4 Protease

Biochemistry (Easton), 2019-02, Vol.58 (7), p.900-907

2019

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The higher barrier of darunavir and tipranavir resistance for HIV-1 protease

Biochemical and biophysical research communications, 2011-09, Vol.412 (4), p.737-742

2011

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Nephrin and Neph1 Co-localize at the Podocyte Foot Process Intercellular Junction and Form cis Hetero-oligomers

The Journal of biological chemistry, 2003-05, Vol.278 (21), p.19266-19271

2003

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Contribution of the 80s loop of HIV-1 protease to the multidrug-resistance mechanism: crystallographic study of MDR769 HIV-1 protease variants

Acta crystallographica. Section D, Biological crystallography., 2011-06, Vol.67 (6), p.524-532

2011

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Expression, Purification and Characterization of a GII.4 Norovirus Protease from Minerva Virus

Infectious disorders drug targets, 2018, Vol.18 (3), p.224-232

2018

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The discovery of Zika virus NS2B-NS3 inhibitors with antiviral activity via an integrated virtual screening approach

European journal of pharmaceutical sciences, 2022-08, Vol.175, p.106220-106220, Article 106220

2022

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Nine Crystal Structures Determine the Substrate Envelope of the MDR HIV-1 Protease

The Protein Journal, 2011-03, Vol.30 (3), p.173-183

2011

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Increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease

Biochemical and biophysical research communications, 2017-10, Vol.492 (4), p.668-673

2017

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The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops

Biochemistry and biophysics reports, 2015-07, Vol.2 (C), p.160-165

2015

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Higher Desolvation Energy Reduces Molecular Recognition in Multi-Drug Resistant HIV-1 Protease

Biology (Basel, Switzerland), 2012-05, Vol.1 (1), p.81-93

2012

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Reduced HIV-1 integrase flexibility as a mechanism for raltegravir resistance

Journal of structural biology, 2013-11, Vol.184 (2), p.245-250

2013

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Conserved hydrogen bonds and water molecules in MDR HIV-1 protease substrate complexes

Biochemical and biophysical research communications, 2013-01, Vol.430 (3), p.1022-1027

2013

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Crystal structure of the extracellular domain of human myelin protein zero

Proteins, structure, function, and bioinformatics, 2012-01, Vol.80 (1), p.307-313

2012

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Crystallographic study of multi-drug resistant HIV-1 protease lopinavir complex: Mechanism of drug recognition and resistance

Biochemical and biophysical research communications, 2013-07, Vol.437 (2), p.199-204

2013

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Insights into the mechanism of drug resistance: X-ray structure analysis of multi-drug resistant HIV-1 protease ritonavir complex

Biochemical and biophysical research communications, 2013-02, Vol.431 (2), p.232-238

2013

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Crystal structures of multidrug-resistant HIV-1 protease in complex with two potent anti-malarial compounds

Biochemical and biophysical research communications, 2012-05, Vol.421 (3), p.413-417

2012

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P1 and P1′ para-fluoro phenyl groups show enhanced binding and favorable predicted pharmacological properties: Structure-based virtual screening of extended lopinavir analogs against multi-drug resistant HIV-1 protease

Journal of molecular graphics & modelling, 2014-02, Vol.47, p.18-24

2014

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Ligand modifications to reduce the relative resistance of multi-drug resistant HIV-1 protease

Bioorganic & medicinal chemistry, 2013-12, Vol.21 (23), p.7430-7434

2013

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Design, synthesis and evaluation of a potent substrate analog inhibitor identified by scanning Ala/Phe mutagenesis, mimicking substrate co-evolution, against multidrug-resistant HIV-1 protease

Biochemical and biophysical research communications, 2013-09, Vol.438 (4), p.703-708

2013

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A multi-drug resistant HIV-1 protease is resistant to the dimerization inhibitory activity of TLF-PafF

Journal of molecular graphics & modelling, 2014-09, Vol.53, p.105-111

2014

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Evaluation of a new tool for exploring podocyte biology : Mouse Nphs1 5' flanking region drives LacZ expression in podocytes

Journal of the American Society of Nephrology, 2000-12, Vol.11 (12), p.2306-2314

2000

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X-ray crystal structure and dynamics reveal HIV-1 protease drug interactions

Studia Universitatis Babeș-Bolyai. Chemia, 2011-09, Vol.56 (3), p.221

2011

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Nephrin localizes to the slit pore of the glomerular epithelial cell : Rapid Communication

Kidney international, 1999-10, Vol.56 (4), p.1481-1491

1999

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A multi-drug resistant HIV-1 protease is resistant to the dimerization inhibitory activity of TLF-PafF

Journal of molecular graphics & modelling, 2014-09, Vol.53 (C)

2014

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The role of mutations at codons 32, 47, 54, and 90 in HIV-1 protease flap dynamics

Discoveries (Craiova, Romania), 2014-12, Vol.2 (4), p.e27-e27

2014

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Structural and Antiviral Studies of the Human Norovirus GII.4 Protease

The higher barrier of darunavir and tipranavir resistance for HIV-1 protease

Nephrin and Neph1 Co-localize at the Podocyte Foot Process Intercellular Junction and Form cis Hetero-oligomers

Contribution of the 80s loop of HIV-1 protease to the multidrug-resistance mechanism: crystallographic study of MDR769 HIV-1 protease variants

Expression, Purification and Characterization of a GII.4 Norovirus Protease from Minerva Virus

The discovery of Zika virus NS2B-NS3 inhibitors with antiviral activity via an integrated virtual screening approach

Nine Crystal Structures Determine the Substrate Envelope of the MDR HIV-1 Protease

Increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease

The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops

Higher Desolvation Energy Reduces Molecular Recognition in Multi-Drug Resistant HIV-1 Protease

Reduced HIV-1 integrase flexibility as a mechanism for raltegravir resistance

Conserved hydrogen bonds and water molecules in MDR HIV-1 protease substrate complexes

Crystal structure of the extracellular domain of human myelin protein zero

Crystallographic study of multi-drug resistant HIV-1 protease lopinavir complex: Mechanism of drug recognition and resistance

Insights into the mechanism of drug resistance: X-ray structure analysis of multi-drug resistant HIV-1 protease ritonavir complex

Crystal structures of multidrug-resistant HIV-1 protease in complex with two potent anti-malarial compounds

P1 and P1′ para-fluoro phenyl groups show enhanced binding and favorable predicted pharmacological properties: Structure-based virtual screening of extended lopinavir analogs against multi-drug resistant HIV-1 protease

Ligand modifications to reduce the relative resistance of multi-drug resistant HIV-1 protease

Design, synthesis and evaluation of a potent substrate analog inhibitor identified by scanning Ala/Phe mutagenesis, mimicking substrate co-evolution, against multidrug-resistant HIV-1 protease

A multi-drug resistant HIV-1 protease is resistant to the dimerization inhibitory activity of TLF-PafF

Evaluation of a new tool for exploring podocyte biology : Mouse Nphs1 5' flanking region drives LacZ expression in podocytes

X-ray crystal structure and dynamics reveal HIV-1 protease drug interactions

Nephrin localizes to the slit pore of the glomerular epithelial cell : Rapid Communication

A multi-drug resistant HIV-1 protease is resistant to the dimerization inhibitory activity of TLF-PafF

The role of mutations at codons 32, 47, 54, and 90 in HIV-1 protease flap dynamics

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