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Chemistry

D-Index
55
Citations
13573
World Ranking
11989
National Ranking
45

Research.com Recognitions

  • 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)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)

Overview

Mariusz Jaskólski is affiliated with Adam Mickiewicz University in Poznań, Poland. Their research primarily lies in the fields of Biochemistry, Genetics and Molecular Biology, and Materials Science. Within these broader areas, their work focuses on several subfields including Molecular Biology, Materials Chemistry, Plant Science, Organic Chemistry, and Public Health, Environmental and Occupational Health.

The scientist has contributed notably to a range of topics that include:

  • Enzyme Structure and Function
  • Biochemical and Molecular Research
  • Protein Structure and Dynamics
  • Acute Lymphoblastic Leukemia research
  • Folate and B Vitamins Research
  • Crystallization and Solubility Studies
  • Computational Drug Discovery Methods

Mariusz Jaskólski has authored multiple papers in various prominent journals. Recent publications include:

  • "Structural Studies of Glutamate Dehydrogenase (Isoform 1) From Arabidopsis thaliana, an Important Enzyme at the Branch-Point Between Carbon and Nitrogen Metabolism," 2020, Frontiers in Plant Science
  • "Structural and biophysical aspects of L-asparaginases: a growing family with amazing diversity," 2021, IUCrJ
  • "Ligand-centered assessment of SARS-CoV-2 drug target models in the Protein Data Bank," 2020, FEBS Journal
  • "New aspects of DNA recognition by group II WRKY transcription factor revealed by structural and functional study of AtWRKY18 DNA binding domain," 2022, International Journal of Biological Macromolecules
  • "Crystallographic models of SARS-CoV-2 3CLpro: in-depth assessment of structure quality and validation," 2021, IUCrJ

Their frequent coauthors include:

  • Mirosław Gilski
  • Zbigniew Dauter
  • Joanna I. Loch
  • Joanna Śliwiak
  • Marta Grzechowiak

The scientist's extensive publication record is concentrated in several notable venues such as:

  • Acta Crystallographica Section A Foundations and Advances
  • Acta Crystallographica Section D Structural Biology
  • IUCrJ
  • The Cambridge Structural Database
  • FEBS Journal

Mariusz Jaskólski has received recognition from multiple institutions. Awards include:

  • Polish Academy of Science, 2016
  • Prize of the Foundation for Polish Science - Nagroda Fundacji na rzecz Nauki Polskiej, 2002, for explaining mechanisms leading to the formation of amyloidal aggregates of human protein (cystatin C), a factor in brain disorders
  • Membership in the European Molecular Biology Organization (EMBO)

Best Publications

  • 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

  • Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping.

    Robert Janowski;Maciej Kozak;Elzbieta Jankowska;Zbigniew Grzonka

  • 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

  • Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy.

    A.L. Swain;M. Jaskolski;D. Housset;J.K.M. Rao

  • EARLY FLOWERING4 Recruitment of EARLY FLOWERING3 in the Nucleus Sustains the Arabidopsis Circadian Clock

    Eva Herrero;Elsebeth Kolmos;Nora Bujdoso;Ye Yuan

  • Structural and functional aspects of PR-10 proteins.

    Humberto Fernandes;Karolina Michalska;Michal Sikorski;Mariusz Jaskolski

  • 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

  • Molecular modeling of the HIV-1 protease and its substrate binding site.

    Irene T. Weber;Maria Miller;Mariusz Jaskólski;Jonathan Leis

  • The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations.

    Grzegorz Bujacz;Mariusz Jaskólski;Jerry Alexandratos;Alexander Wlodawer

  • Crystal engineering with hydrogen bonds and halogen bonds

    Binoy K. Saha;Ashwini Nangia;Mariusz Jaskólski

  • Structural studies of cysteine proteases and their inhibitors.

    Zbigniew Grzonka;Elzbieta Jankowska;Franciszek Kasprzykowski;Regina Kasprzykowska

  • Sequence analysis of enzymes with asparaginase activity.

    Dominika Borek;Mariusz Jaskólski;Mariusz Jaskólski

  • Protein crystallography for aspiring crystallographers or how to avoid pitfalls and traps in macromolecular structure determination

    Alexander Wlodawer;Wladek Minor;Zbigniew Dauter;Mariusz Jaskolski

  • Structural aspects of l-asparaginases, their friends and relations *

    Karolina Michalska;Mariusz Jaskolski

  • Prevention of Domain Swapping Inhibits Dimerization and Amyloid Fibril Formation of Cystatin C USE OF ENGINEERED DISULFIDE BRIDGES, ANTIBODIES, AND CARBOXYMETHYLPAPAIN TO STABILIZE THE MONOMERIC FORM OF CYSTATIN C

    Maria Nilsson;Xin Wang;Sylwia Rodziewicz-Motowidlo;Robert Janowski

  • Crystal Structure of Vigna radiata Cytokinin-Specific Binding Protein in Complex with Zeatin

    Oliwia Pasternak;Grzegorz D. Bujacz;Grzegorz D. Bujacz;Yasuyuki Fujimoto;Yuichi Hashimoto

  • 3D domain-swapped human cystatin C with amyloidlike intermolecular beta-sheets.

    Robert Janowski;Maciej Kozak;Magnus Abrahamson;Anders Grubb

  • Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.

    Maria Wahlbom;Xin Wang;Veronica Lindström;Eric Carlemalm

Frequent Co-Authors

Alexander Wlodawer
Alexander Wlodawer National Institutes of Health
Wladek Minor
Wladek Minor University of Virginia
Anders Grubb
Anders Grubb Lund University
Magnus Abrahamson
Magnus Abrahamson Lund University
Ashwini Nangia
Ashwini Nangia University of Hyderabad
Gautam R. Desiraju
Gautam R. Desiraju Indian Institute of Science
Maciej Kubicki
Maciej Kubicki Adam Mickiewicz University in Poznań
Richard A. Katz
Richard A. Katz Fox Chase Cancer Center
Jonathan Leis
Jonathan Leis Northwestern University
Anna Marie Skalka
Anna Marie Skalka Fox Chase Cancer Center

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