His primary areas of investigation include Biochemistry, Stereochemistry, Enzyme, Glutamate carboxypeptidase II and Protease. His is involved in several facets of Biochemistry study, as is seen by his studies on Glycine and Pyridoxal. His Stereochemistry study combines topics from a wide range of disciplines, such as Substrate and Serine racemase, Serine.
His work deals with themes such as Residue, Hydrolysis and Recombinant DNA, which intersect with Enzyme. His Glutamate carboxypeptidase II research is multidisciplinary, incorporating perspectives in Glutamate receptor, Amino acid and Hydrolase. His Protease research is mostly focused on the topic HIV Protease Inhibitor.
His primary areas of study are Biochemistry, Enzyme, Protease, Stereochemistry and Glutamate carboxypeptidase II. In his study, DNA is strongly linked to Antibody, which falls under the umbrella field of Enzyme. His Protease research includes elements of Proteases, Molecular biology, Viral replication and Virology.
His Stereochemistry research integrates issues from Protein structure, HIV-1 protease, Structure–activity relationship and Active site. His biological study spans a wide range of topics, including Amino acid, Exopeptidase, Western blot and Metallopeptidase. The Binding site study combines topics in areas such as Peptide sequence and Substrate.
His main research concerns Enzyme, Protease, Biochemistry, Proteases and Cell biology. The concepts of his Enzyme study are interwoven with issues in Conjugated system, Biophysics, Antibody and DNA. His Protease research incorporates themes from Reverse transcriptase and Cryptococcosis.
When carried out as part of a general Biochemistry research project, his work on Green fluorescent protein, Proteolysis and mCherry is frequently linked to work in Conjugate and Förster resonance energy transfer, therefore connecting diverse disciplines of study. Jan Konvalinka works mostly in the field of Enzyme inhibitor, limiting it down to concerns involving Viral protein and, occasionally, Stereochemistry. The study incorporates disciplines such as Mutant and Glutamate carboxypeptidase II in addition to Calcium.
Jan Konvalinka mostly deals with Proteases, Protease, Biochemistry, Serine protease and Enzyme. His Proteases research is multidisciplinary, incorporating elements of Phenotype, Yeast, Replication, Proteasome and DNA replication. As part of his studies on Protease, Jan Konvalinka often connects relevant subjects like Cell biology.
Jan Konvalinka incorporates Biochemistry and Förster resonance energy transfer in his research. The various areas that Jan Konvalinka examines in his Serine protease study include NS3, Dipeptidyl peptidase, Serine and Dengue fever. His study in Enzyme concentrates on HIV-1 protease and Allosteric regulation.
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From nonpeptide toward noncarbon protease inhibitors: Metallacarboranes as specific and potent inhibitors of HIV protease
Petr Cígler;Petr Cígler;Milan Kožíšek;Pavlína Řezáčová;Pavlína Řezáčová;Jíří Brynda.
Proceedings of the National Academy of Sciences of the United States of America (2005)
THE SPACER PEPTIDE BETWEEN HUMAN IMMUNODEFICIENCY VIRUS CAPSID AND NUCLEOCAPSID PROTEINS IS ESSENTIAL FOR ORDERED ASSEMBLY AND VIRAL INFECTIVITY
H G Kräusslich;M Fäcke;A M Heuser;J Konvalinka.
Journal of Virology (1995)
Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer.
Jeroen R Mesters;Cyril Barinka;Weixing Li;Takashi Tsukamoto.
The EMBO Journal (2006)
Sensitive, soluble chromogenic substrates for HIV-1 proteinase.
A D Richards;L H Phylip;W G Farmerie;P E Scarborough.
Journal of Biological Chemistry (1990)
A novel substrate-based HIV-1 protease inhibitor drug resistance mechanism.
Monique Nijhuis;Noortje M van Maarseveen;Stephane Lastere;Pauline Schipper.
PLOS Medicine (2007)
An Active-Site Mutation in the Human Immunodeficiency Virus Type 1 Proteinase (PR) Causes Reduced PR Activity and Loss of PR-Mediated Cytotoxicity without Apparent Effect on Virus Maturation and Infectivity
J Konvalinka;M A Litterst;R Welker;H Kottler.
Journal of Virology (1995)
Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic*hydrophobic- or -aromatic*pro- cleavage sites.
Jonathan T. Griffiths;Lowri H. Phylip;Jan Konvalinka;Petr Strop.
Design of HIV protease inhibitors based on inorganic polyhedral metallacarboranes.
Pavlína Rezácová;Jana Pokorná;Jana Pokorná;Jirí Brynda;Milan Kozísek;Milan Kozísek.
Journal of Medicinal Chemistry (2009)
Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II.
Cyril Barinka;Markéta Rinnová;Pavel Šácha;Camilo Rojas.
Journal of Neurochemistry (2002)
Expression of glutamate carboxypeptidase II in human brain.
Sácha P;Zámecník J;Barinka C;Hlouchová K;Hlouchová K.
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