O. Hrušková-Heidingsfeldová

发表

Saccharomyces cerevisiae can secrete Sapp1p proteinase of Candida parapsilosis but cannot use it for efficient nitrogen acquisition

I. Pichová, H. Sychrová, J. Dostál, 2013, Journal of Microbiology.

Raman Microspectroscopy of the Yeast Vacuoles

I. Pichová, P. Mojzeš, Jan Palacký, 2012 .

Secreted aspartic proteases of Candida albicans, Candida tropicalis, Candida parapsilosis and Candida lusitaniae. Inhibition with peptidomimetic inhibitors.

I. Pichová, T. Ruml, J. Dostál, 2001, European journal of biochemistry.

Structure-based specificity mapping of secreted aspartic proteases of Candida parapsilosis, Candida albicans, and Candida tropicalis using peptidomimetic inhibitors and homology modeling

Pavel Majer, Filip Majer, I. Pichová, 2006, Biological chemistry.

Secreted proteins of Candida albicans.

O. Hrušková-Heidingsfeldová, O. Hrušková-Heidingsfeldová, 2008, Frontiers in bioscience : a journal and virtual library.

Secreted aspartate proteinases, a virulence factor ofCandida spp.: Occurrence among clinical isolates

I. Pichová, P. Hamal, J. Dostál, 2008, Folia Microbiologica.

Intracellular aspartic proteinase Apr1p of Candida albicans is required for morphological transition under nitrogen-limited conditions but not for macrophage killing

I. Pichová, O. Hrušková-Heidingsfeldová, M. Hájek, 2014, Folia Microbiologica.

Evidence for the presence of proteolytically active secreted aspartic proteinase 1 of Candida parapsilosis in the cell wall

I. Pichová, J. Dostál, M. Sanda, 2011, Protein science : a publication of the Protein Society.

The crystal structure of the secreted aspartic protease 1 from Candida parapsilosis in complex with pepstatin A.

I. Pichová, J. Brynda, P. Řezáčová, 2009, Journal of structural biology.

Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties

I. Pichová, J. Dostál, J. Havlíková, 2009, Biological chemistry.

Cleavage of vimentin by different retroviral proteases.

I. Pichová, R. Shoeman, T. Ruml, 2000, Archives of biochemistry and biophysics.

High‐level expression of enzymatically active bovine leukemia virus proteinase in E. coli

J. Konvalinka, P. Štrop, M. Andreánsky, 1991, FEBS letters.

Three active forms of aspartic proteinase from Mason-Pfizer monkey virus.

I. Pichová, V. Havlíček, E. Hunter, 1998, Virology.

Subsequent selfprocessing of bovine leukemia virus proteinase in vitro.

I. Pichová, G. Shoham, A. Zábranský, 1998, Advances in experimental medicine and biology.

Proteolytic processing of particle-associated retroviral polyproteins by homologous and heterologous viral proteinases.

J. Konvalinka, P. Štrop, V. Vogt, 1995, European journal of biochemistry.

Δ12-Fatty Acid Desaturase from Candida parapsilosis Is a Multifunctional Desaturase Producing a Range of Polyunsaturated and Hydroxylated Fatty Acids

I. Pichová, H. Sychrová, P. Matoušková, 2014, PloS one.

The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir

I. Pichová, J. Brynda, P. Řezáčová, 2012, Journal of enzyme inhibition and medicinal chemistry.

Characterization of Chloroplast Clp proteins in Arabidopsis: Localization, tissue specificity and stress responses.

A. Clarke, Z. Adam, T. Halperin, 2002, Physiologia plantarum.

The precursor of secreted aspartic proteinase Sapp1p from Candida parapsilosis can be activated both autocatalytically and by a membrane-bound processing proteinase

I. Pichová, J. Dostál, P. Maloň, 2005, Biological chemistry.

Nitrogen source and growth stage of Candida albicans influence expression level of vacuolar aspartic protease Apr1p and carboxypeptidase Cpy1p.

I. Pichová, O. Hrušková-Heidingsfeldová, V. Bauerová, 2012, Canadian journal of microbiology.

Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis.

I. Pichová, J. Brynda, L. Marečková, 2015, Acta crystallographica. Section D, Biological crystallography.

Enzymological Characterization of Secreted Proteinases from Candida parapsilosis and Candida lusitaniae

I. Pichová, P. Hamal, T. Ruml, 2001 .

Cloning and characterization of Sapp2p, the second aspartic proteinase isoenzyme from Candida parapsilosis.

I. Pichová, M. Merkerova, J. Dostál, 2006, FEMS yeast research.

Cloning, Bacterial Expression, and Characterization of the Mason-Pfizer Monkey Virus Proteinase (*)

P. Štrop, M. Andreánsky, I. Bláha, 1995, The Journal of Biological Chemistry.

Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis.

I. Pichová, J. Brynda, L. Marečková, 2015, Acta crystallographica. Section D, Biological crystallography.

Two SAPP2 gene homologs are present in Candida parapsilosis genome

I. Pichová, J. Dostál, Zuzana Vinterová, 2015, Folia Microbiologica.

The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir

I. Pichová, J. Brynda, P. Řezáčová, 2012, Journal of enzyme inhibition and medicinal chemistry.

Simple Method for Screening Candida Species Isolates for the Presence of Secreted Proteinases: a Tool for the Prediction of Successful Inhibitory Treatment

I. Pichová, P. Hamal, T. Ruml, 2003, Journal of Clinical Microbiology.

Analysis of autoprocessing of Mason-Pfizer monkey virus proteinase in vitro. Three active forms of proteinase.

I. Pichová, E. Hunter, T. Ruml, 1998, Advances in experimental medicine and biology.