What is he best known for?
The fields of study he is best known for:
Arne Skerra mainly investigates Biochemistry, Protein engineering, Lipocalin, Stereochemistry and Ligand.
His Biochemistry and Protein structure, Streptavidin, Strep-tag, Plasma protein binding and Protein design investigations all form part of his Biochemistry research activities.
His Plasma protein binding research is multidisciplinary, incorporating elements of Nanotechnology, Effector functions, Computational biology and EF hand.
His studies examine the connections between Protein engineering and genetics, as well as such issues in Binding site, with regards to Phage display.
His Lipocalin study combines topics in areas such as Antiparallel, Secretion, Anticalin and Dissociation constant.
His Stereochemistry research incorporates elements of Biological activity and Peptide sequence.
His most cited work include:
- Crucial role for human Toll-like receptor 4 in the development of contact allergy to nickel (413 citations)
- Engineered protein scaffolds as next-generation antibody therapeutics (395 citations)
- Alternative non-antibody scaffolds for molecular recognition. (330 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of study are Biochemistry, Lipocalin, Molecular biology, Anticalin and Stereochemistry.
His study in Biochemistry concentrates on Protein engineering, Amino acid, Protein structure, Periplasmic space and Escherichia coli.
His work deals with themes such as Antiparallel, Plasma protein binding and Ligand, which intersect with Lipocalin.
As a part of the same scientific family, Arne Skerra mostly works in the field of Molecular biology, focusing on Antibody and, on occasion, Antigen and Peptide.
He interconnects Protein design, Phage display, Affinity maturation, Cell biology and Computational biology in the investigation of issues within Anticalin.
His Stereochemistry study incorporates themes from Paracoccus denitrificans, Ligand, Protein family, Peptide sequence and Biological activity.
He most often published in these fields:
- Biochemistry (41.28%)
- Lipocalin (17.45%)
- Molecular biology (14.89%)
What were the highlights of his more recent work (between 2015-2021)?
- Anticalin (15.32%)
- Biochemistry (41.28%)
- Lipocalin (17.45%)
In recent papers he was focusing on the following fields of study:
Anticalin, Biochemistry, Lipocalin, Amino acid and Stereochemistry are his primary areas of study.
His biological study spans a wide range of topics, including Scaffold protein, Protein design, Computational biology and Cell biology.
As part of his studies on Biochemistry, Arne Skerra frequently links adjacent subjects like Molecular biology.
His studies deal with areas such as Binding protein, Phage display and Binding site as well as Lipocalin.
In Amino acid, Arne Skerra works on issues like Ligand, which are connected to Molecular recognition.
The study incorporates disciplines such as Paracoccus denitrificans, Enzyme kinetics, Alcohol dehydrogenase and Active site in addition to Stereochemistry.
Between 2015 and 2021, his most popular works were:
- Consistent success in life-supporting porcine cardiac xenotransplantation (139 citations)
- Incomplete inhibition by eculizumab: mechanistic evidence for residual C5 activity during strong complement activation (67 citations)
- Anticalin ® Proteins as Therapeutic Agents in Human Diseases (32 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Anticalin, Biochemistry, Lipocalin, Computational biology and Antibody.
His Anticalin research incorporates themes from Angiogenesis, Scaffold protein, Affinity maturation, Receptor and Cell biology.
His studies in Biochemistry integrate themes in fields like Molecular biology and Hemolysis.
His research integrates issues of Phage display and Binding site in his study of Lipocalin.
His Binding site research is multidisciplinary, relying on both Protein design and Pharmacology.
His Computational biology research includes elements of Cell, Endosome, Cytoplasm and Biotinylation.
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