What is he best known for?
The fields of study he is best known for:
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.
His most cited work include:
- Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease (1000 citations)
- Crystal structure of a monomeric retroviral protease solved by protein folding game players (356 citations)
- Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. (332 citations)
What are the main themes of his work throughout his whole career to date?
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.
He most often published in these fields:
- Crystallography (51.55%)
- Stereochemistry (36.53%)
- Crystal structure (33.68%)
What were the highlights of his more recent work (between 2014-2021)?
- Crystallography (51.55%)
- Stereochemistry (36.53%)
- Protein Data Bank (7.25%)
In recent papers he was focusing on the following fields of 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.
Between 2014 and 2021, his most popular works were:
- Crystallography and chemistry should always go together: a cautionary tale of protein complexes with cisplatin and carboplatin. (41 citations)
- Detect, correct, retract: How to manage incorrect structural models (29 citations)
- Safeguarding Structural Data Repositories against Bad Apples (28 citations)
In his most recent research, the most cited papers focused on:
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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