2016 - Polish Academy of Science
2002 - Prize of the Foundation for Polish Science - Nagroda Fundacji na rzecz Nauki Polskiej for explaining the mechanisms leading to the formation of amyloidal aggregates of human protein (cystatin C): an important factor in various brain disorders and diseases in humans
Member of the European Molecular Biology Organization (EMBO)
His primary areas of study are Biochemistry, Stereochemistry, Active site, Proteases and Dimer. His Stereochemistry research is multidisciplinary, relying on both Protein structure, Vigna, Protein subunit and DNA. His research integrates issues of Hydrolase, Rous sarcoma virus, Avian sarcoma virus, Integrase and RNase P in his study of Active site.
Mariusz Jaskolski has included themes like Protease, Cysteine and Chymotrypsin, Trypsin in his Proteases study. He has researched Dimer in several fields, including Crystallography and Protein secondary structure. The various areas that he examines in his Crystallography study include Hydrogen bond and Protein Data Bank.
Crystallography, Stereochemistry, Crystal structure, Biochemistry and Molecule are his primary areas of study. The concepts of his Crystallography study are interwoven with issues in X-ray crystallography, Protein structure and Hydrogen bond. His Hydrogen bond study combines topics in areas such as Substituent, Protonation, Intramolecular force and Betaine.
The Stereochemistry study which covers Active site that intersects with Substrate. His study in Crystal structure is interdisciplinary in nature, drawing from both Structure and Z-DNA. Enzyme, Binding site, Hydrolase, Proteases and Peptide sequence are the primary areas of interest in his Biochemistry study.
His primary scientific interests are in Crystallography, Stereochemistry, Protein Data Bank, Protein Data Bank and Crystal structure. His Crystallography research includes themes of X-ray crystallography, Molecule, Van der Waals radius and Single amino acid. The Stereochemistry study combines topics in areas such as Nucleobase, Hydrolase, Proteases, Dimer and Protein structure.
His research in the fields of Crystallographic point group overlaps with other disciplines such as Crystal twinning. His Enzyme study introduces a deeper knowledge of Biochemistry. His study in Biochemistry focuses on Active site in particular.
Protein Data Bank, Protein Data Bank, Plant protein, Stereochemistry and Crystallography are his primary areas of study. His Protein Data Bank research integrates issues from Machine learning, Nucleic acid, Ligand and Artificial intelligence. His biological study spans a wide range of topics, including Zn binding, Information retrieval, Data science and Computational biology.
The concepts of his Stereochemistry study are interwoven with issues in Allosteric regulation, Dimer, Aldolase A and Fructose 1,6-bisphosphatase. Mariusz Jaskolski focuses mostly in the field of Crystallography, narrowing it down to topics relating to Protein structure and, in certain cases, Capsid, Icosahedral symmetry, Amino acid and CLOCK Proteins. Mariusz Jaskolski conducts interdisciplinary study in the fields of Biochemistry and Context through his research.
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Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease
Alexander Wlodawer;Maria Miller;Mariusz Jaskólski;Bangalore K. Sathyanarayana.
Crystal structure of a monomeric retroviral protease solved by protein folding game players.
Firas Khatib;Frank DiMaio;Seth Cooper;Maciej Kazmierczyk.
Nature Structural & Molecular Biology (2011)
Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping.
Robert Janowski;Maciej Kozak;Elzbieta Jankowska;Zbigniew Grzonka.
Nature Structural & Molecular Biology (2001)
Crystal structure of a retroviral protease proves relationship to aspartic protease family.
Maria Miller;Mariusz Jaskólski;J. K. Mohana Rao;Jonathan Leis.
Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures.
Alexander Wlodawer;Wladek Minor;Zbigniew Dauter;Mariusz Jaskolski;Mariusz Jaskolski.
FEBS Journal (2008)
Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy.
A.L. Swain;M. Jaskolski;D. Housset;J.K.M. Rao.
Proceedings of the National Academy of Sciences of the United States of America (1993)
Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor.
Mariusz Jaskolski;Alfredo G. Tomasselli;Tomi K. Sawyer;Douglas G. Staples.
High-resolution structure of the catalytic domain of avian sarcoma virus integrase.
Grzegorz Bujacz;Mariusz Jaskólski;Mariusz Jaskólski;Jerry Alexandratos;Jerry Alexandratos;Alexander Wlodawer;Alexander Wlodawer.
Journal of Molecular Biology (1995)
EARLY FLOWERING4 Recruitment of EARLY FLOWERING3 in the Nucleus Sustains the Arabidopsis Circadian Clock
Eva Herrero;Elsebeth Kolmos;Nora Bujdoso;Ye Yuan.
The Plant Cell (2012)
Molecular modeling of the HIV-1 protease and its substrate binding site.
Irene T. Weber;Maria Miller;Mariusz Jaskólski;Jonathan Leis.
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