His scientific interests lie mostly in Biochemistry, Proteasome, Stereochemistry, Protein subunit and Protein structure. His Proteasome research incorporates themes from Hydrolase, Cleavage, Protease and Peptide sequence. His Cleavage research is multidisciplinary, relying on both Mutant and Active site.
His Stereochemistry research includes themes of Residue, Cellular differentiation and Crystal structure. The study incorporates disciplines such as Cysteine, Peptide and Cell biology in addition to Protein subunit. The Protein structure study combines topics in areas such as Proton-coupled electron transfer, Botany, Oxidoreductase, Biophysics and Binding site.
His main research concerns Biochemistry, Yeast, 20s proteasome, Proteasome and Cell biology. His work in Protease, Enzyme, Hydrolase, Protein degradation and Proteases are all subfields of Biochemistry research. He combines subjects such as Natural product, Stereochemistry, Protein subunit and Bortezomib with his study of Proteasome.
His Stereochemistry study incorporates themes from Protein structure, Crystal structure, Binding site and Active site. His study ties his expertise on Mutant together with the subject of Cell biology. In his study, Glutathione S-transferase is strongly linked to Molecular biology, which falls under the umbrella field of Mutant.
His primary areas of investigation include Yeast, Cell biology, 20s proteasome, Molecular biology and Mutant. His Yeast study contributes to a more complete understanding of Biochemistry. Natural product, Proteasome and Mutagenesis are among the areas of Biochemistry where the researcher is concentrating his efforts.
His work is dedicated to discovering how Proteasome, Photorhabdus are connected with Biosynthesis and other disciplines. His work on Guanine nucleotide exchange factor, Kinase and Phosphorylation as part of his general Cell biology study is frequently connected to GTPase-activating protein, thereby bridging the divide between different branches of science. His Molecular biology research is multidisciplinary, incorporating elements of Desulfitobacterium hafniense, Glutathione S-transferase, Point mutation, Immunoglobulin light chain and Methyltransferase.
Michael Groll mainly focuses on Stereochemistry, Glutathione S-transferase, Molecular biology, Mutant and Biochemistry. Michael Groll interconnects Polyketide, Biosynthesis, Enzyme and Photorhabdus luminescens in the investigation of issues within Stereochemistry. His study on Cleavage is often connected to Amyloidosis as part of broader study in Molecular biology.
Michael Groll has researched Mutant in several fields, including Proteolysis, Staphylococcus aureus, Function, Microbiology and Bacillus subtilis. Proteasome, Mutagenesis, 20s proteasome, Natural product and Thermophile are the core of his Biochemistry study. The various areas that Michael Groll examines in his Proteasome study include Hydrolase, Peptide library and Protein subunit.
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Structure of 20S proteasome from yeast at 2.4 A resolution.
Michael Groll;Lars Ditzel;Jan Löwe;Daniela Stock.
A gated channel into the proteasome core particle.
Michael Groll;Monica Bajorek;Alwin Köhler;Luis Moroder.
Nature Structural & Molecular Biology (2000)
Crystal Structure of the Boronic Acid-Based Proteasome Inhibitor Bortezomib in Complex with the Yeast 20S Proteasome
Michael Groll;Celia R. Berkers;Hidde L. Ploegh;Huib Ovaa.
20S proteasome and its inhibitors: crystallographic knowledge for drug development.
Ljudmila Borissenko;Michael Groll.
Chemical Reviews (2007)
Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity.
Eva M. Huber;Michael Basler;Ricarda Schwab;Wolfgang Heinemeyer.
Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase 1
Alexander K. Nussbaum;Tobias P. Dick;Wieland Keilholz;Markus Schirle.
Proceedings of the National Academy of Sciences of the United States of America (1998)
Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding.
Michael Groll;Robert Huber;Barbara C. M. Potts.
Journal of the American Chemical Society (2006)
Crystal Structure of Epoxomicin:20S Proteasome reveals a molecular basis for selectivity of alpha,beta-Epoxyketone Proteasome Inhibitors
Michael Groll;Kyung Bo Kim;Norman Kairies;Robert Huber.
Journal of the American Chemical Society (2000)
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
Patrick Schreiner;Xiang Chen;Koraljka Husnjak;Leah Randles.
The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study
Michael Groll;Wolfgang Heinemeyer;Sibylle Jäger;Tobias Ullrich.
Proceedings of the National Academy of Sciences of the United States of America (1999)
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