I. Kovari

发表

Crystal structure of the extracellular domain of human myelin protein zero

J. Kamholz, Zhigang Liu, Yong Wang, 2011, Proteins.

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

Tamaria G. Dewdney, Yong Wang, I. Kovari, 2013, Journal of structural biology.

Localization of protective epitopes within the pilin subunit of the Vibrio cholerae toxin-coregulated pilus

J. Seyer, R. Taylor, I. Kovari, 1991, Infection and immunity.

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

M. U. Mirza, John F. Trant, M. Froeyen, 2022, European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences.

Fyn Binds to and Phosphorylates the Kidney Slit Diaphragm Component Nephrin*

L. Holzman, R. Wiggins, R. Kunkel, 2003, Journal of Biological Chemistry.

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

D. Kerjaschki, L. Holzman, Gina-Marie Barletta, 2003, Journal of Biological Chemistry.

cerevisiae is derived from regulated inducer ( CAR 1 ) expression in Saccharomyces Nitrogen catabolite repression of arginase

T. Cooper, Heui-Dong Park, I. Kovari, 2022 .

Nitrogen catabolite repression of arginase (CAR1) expression in Saccharomyces cerevisiae is derived from regulated inducer exclusion

T. Cooper, I. Kovari, H. Park, 1992, Journal of bacteriology.

Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization.

L. Holzman, A. Soofi, I. Kovari, 2006, The Journal of clinical investigation.

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

L. Holzman, M. Moeller, I. Kovari, 2000, Journal of the American Society of Nephrology : JASN.

Nephrin localizes to the slit pore of the glomerular epithelial cell.

P. S. St. John, D. Abrahamson, L. Holzman, 1999, Kidney international.

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

Tamaria G. Dewdney, Zhigang Liu, Yong Wang, 2013, Biochemical and biophysical research communications.

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

Tamaria G. Dewdney, Zhigang Liu, Yong Wang, 2013, Biochemical and biophysical research communications.

Multiple positive and negative cis-acting elements mediate induced arginase (CAR1) gene expression in Saccharomyces cerevisiae

T. Cooper, I. Kovari, R. Sumrada, 1990, Molecular and cellular biology.

Participation of RAP1 protein in expression of the Saccharomyces cerevisiae arginase (CAR1) gene

T. Cooper, I. Kovari, L. Kővári, 1993, Journal of bacteriology.

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

Zhigang Liu, I. Kovari, L. Kovari, 2014, Journal of molecular graphics & modelling.

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.

M. Spaller, Zhigang Liu, I. Kovari, 2013, Biochemical and biophysical research communications.

Design , synthesis and evaluation of a potent substrate-analog peptide-inhibitor identified by scanning Ala / Phe chemical mutagenesis

M. Spaller, Zhigang Liu, I. Kovari, 2013 .

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

Zhigang Liu, Yong Wang, J. Brunzelle, 2011, The protein journal.

Mutagenic oligonucleotide-directed PCR amplification (Mod-PCR): an efficient method for generating random base substitution mutations in a DNA sequence element.

I. Kovari, M. Howe, L W Chiang, 1993, PCR methods and applications.

mutations in a DNA sequence element. an efficient method for generating random base substitution Mutagenic oligonucleotide-directed PCR amplification (Mod-PCR):

I. Kovari, M. Howe, L. Chiang, 2011 .

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

Tamaria G. Dewdney, P. Chordia, R. MacArthur, 2015, Biochemistry and biophysics reports.

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

Tamaria G. Dewdney, Zhigang Liu, Yong Wang, 2011, Biochemical and biophysical research communications.

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

Tamaria G. Dewdney, Zhigang Liu, Yong Wang, 2013, Biochemical and biophysical research communications.

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

R. Schinazi, P. Liu, J. Brunzelle, 2019, Biochemistry.

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

R. Schinazi, I. Kovari, L. Kovari, 2017, Biochemical and biophysical research communications.

Analysis of the inducer‐responsive CAR1 upstream activation sequence (UASI) and the factors required for its operation

T. Cooper, Heui-Dong Park, I. Kovari, 1993, Yeast.

Tripartite structure of the Saccharomyces cerevisiae arginase (CAR1) gene inducer-responsive upstream activation sequence

T. Cooper, M. Viljoen, I. Kovari, 1992, Journal of bacteriology.

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

P. Woster, Zhigang Liu, Yong Wang, 2012, Biochemical and biophysical research communications.

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

Tamaria G. Dewdney, P. Chordia, R. MacArthur, 2014, Discoveries.

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

G. Proteasa, Z. Wawrzak, Zhigang Liu, 2011, Acta crystallographica. Section D, Biological crystallography.