His scientific interests lie mostly in Biochemistry, Enzyme, Proteomics, Stereochemistry and Nanotechnology. His Biochemistry research focuses on subjects like Function, which are linked to Hydrolase. His Enzyme research is multidisciplinary, incorporating elements of Combinatorial chemistry, Antibiotic resistance, Microbiology and Virulence.
His Proteomics study combines topics from a wide range of disciplines, such as Proteome, Computational biology and Protein Array Analysis. His work deals with themes such as Nonribosomal peptide and Active site, which intersect with Stereochemistry. The various areas that he examines in his Nanotechnology study include Zeolite, Vapor–liquid–solid method and Crystallite.
Biochemistry, Stereochemistry, Enzyme, Proteomics and Microbiology are his primary areas of study. His study involves Protease, Active site, Protein structure, Antibiotics and Natural product, a branch of Biochemistry. The Stereochemistry study combines topics in areas such as Nonribosomal peptide and Peptide.
His Proteomics study incorporates themes from Proteome, Computational biology and Drug discovery. His Computational biology research focuses on Small molecule and how it relates to Nanotechnology. His Microbiology research incorporates themes from Biofilm, Listeria monocytogenes, Staphylococcus aureus and Virulence.
His primary scientific interests are in Cell biology, Biochemistry, Biophysics, Proteomics and Enzyme. His biological study spans a wide range of topics, including Lipid bilayer, Membrane protein and Adenylylation. Biochemistry and Context are two areas of study in which he engages in interdisciplinary work.
His Biophysics research includes themes of Proteolysis, Protein degradation and Peptide. His Proteomics research includes themes of In situ and Mutant. His study in Enzyme concentrates on Active site and Cysteine.
His scientific interests lie mostly in Cell biology, Biophysics, Biofilm, In situ and Proteomics. Stephan A. Sieber interconnects Apoptosis and Adenylylation in the investigation of issues within Cell biology. His work carried out in the field of Biophysics brings together such families of science as Transport protein, Peptide, Protein degradation and Proteolysis.
His Proteolysis research is classified as research in Enzyme. His In situ research is multidisciplinary, incorporating perspectives in Unfolded protein response, Posttranslational modification, Click chemistry and Immunoprecipitation. His study in Proteomics is interdisciplinary in nature, drawing from both Live cell imaging and Protein AMPylation.
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Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics.
Stephan A Sieber;Mohamed A Marahiel.
Chemical Reviews (2005)
Proteomic profiling of metalloprotease activities with cocktails of active-site probes
Stephan A Sieber;Sherry Niessen;Heather S Hoover;Benjamin F Cravatt.
Nature Chemical Biology (2006)
Electrophilic natural products and their biological targets
Malte Gersch;Johannes Kreuzer;Stephan A. Sieber.
Natural Product Reports (2012)
Chemical proteomics approaches for identifying the cellular targets of natural products
M. H. Wright;S. A. Sieber.
Natural Product Reports (2016)
β-Lactones as Specific Inhibitors of ClpP Attenuate the Production of Extracellular Virulence Factors of Staphylococcus aureus
Thomas Böttcher;Stephan A. Sieber.
Journal of the American Chemical Society (2008)
Natural Products and Their Biological Targets: Proteomic and Metabolomic Labeling Strategies
Thomas Böttcher;Maximilian Pitscheider;Stephan A. Sieber.
Angewandte Chemie (2010)
β‐Lactones as Privileged Structures for the Active‐Site Labeling of Versatile Bacterial Enzyme Classes
Thomas Böttcher;Stephan A. Sieber.
Angewandte Chemie (2008)
Learning from Nature's Drug Factories: Nonribosomal Synthesis of Macrocyclic Peptides
Stephan A. Sieber;Mohamed A. Marahiel.
Journal of Bacteriology (2003)
Helicobacter pylori adhesin HopQ engages in a virulence-enhancing interaction with human CEACAMs
Anahita Javaheri;Tobias Kruse;Kristof Moonens;Raquel Mejías-Luque.
Nature microbiology (2016)
Characterization of the surfactin synthetase C-terminal thioesterase domain as a cyclic depsipeptide synthase.
Claire C. Tseng;Steven D. Bruner;Rahul M. Kohli;Mohamed A. Marahiel.
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