What is he best known for?
The fields of study he is best known for:
Karl Harlos mostly deals with Protein structure, Stereochemistry, Biochemistry, T cell and Binding site.
His Protein structure study incorporates themes from Hypoxia-Inducible Factor 1 and Cell adhesion molecule, Immunoglobulin superfamily, Cell biology.
The study incorporates disciplines such as Biophysics and Crystal structure in addition to Cell adhesion molecule.
His Stereochemistry research includes themes of PQQ Cofactor and Active site.
His Biochemistry research includes elements of Platelet aggregation inhibitor and Histamine.
His studies in Binding site integrate themes in fields like Integrin, Integrin binding, Ligand Binding Protein and Lipocalin.
His most cited work include:
- Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. (533 citations)
- A functional and structural basis for TCR cross-reactivity in multiple sclerosis (443 citations)
- Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes (357 citations)
What are the main themes of his work throughout his whole career to date?
Crystallography, Stereochemistry, Biochemistry, Protein structure and Crystal structure are his primary areas of study.
His Crystallography research is multidisciplinary, incorporating elements of X-ray crystallography, Crystallization, Bilayer and Hydrogen bond.
He interconnects Oxidoreductase, Oxygenase, Active site, Enzyme and Deacetoxycephalosporin-C synthase in the investigation of issues within Stereochemistry.
His work on Receptor, Peptide and Glycosylation is typically connected to Surface plasmon resonance as part of general Biochemistry study, connecting several disciplines of science.
His research in Protein structure intersects with topics in Biophysics, Immunoglobulin superfamily, Cell biology, Viral protein and Binding site.
As part of the same scientific family, Karl Harlos usually focuses on Cell biology, concentrating on Cell adhesion and intersecting with Cell adhesion molecule.
He most often published in these fields:
- Crystallography (23.70%)
- Stereochemistry (23.22%)
- Biochemistry (22.27%)
What were the highlights of his more recent work (between 2016-2021)?
- Crystallography (23.70%)
- Crystal structure (18.96%)
- Receptor (11.37%)
In recent papers he was focusing on the following fields of study:
Karl Harlos spends much of his time researching Crystallography, Crystal structure, Receptor, Stereochemistry and Virology.
In his research, Imidazole is intimately related to X-ray crystallography, which falls under the overarching field of Crystallography.
His Crystal structure study combines topics in areas such as Virus, Bilayer, Lamellar structure and Hydrogen bond.
He has researched Stereochemistry in several fields, including Enzyme, Active site, Plasmodium vivax and Binding site.
His Virology research incorporates themes from Antibody and Glycoprotein.
His study explores the link between Protein structure and topics such as Lipid bilayer fusion that cross with problems in Lipid bilayer and Biophysics.
Between 2016 and 2021, his most popular works were:
- High-speed fixed-target serial virus crystallography. (72 citations)
- Shielding and Activation of a Viral Membrane Fusion Protein (35 citations)
- Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding. (33 citations)
In his most recent research, the most cited papers focused on:
His primary areas of study are Viral protein, Virology, Biophysics, Crystallography and Viral envelope.
The concepts of his Virology study are interwoven with issues in Antibody and Glycoprotein.
His Biophysics study integrates concerns from other disciplines, such as Perforin, Toxoplasma gondii and Vacuole.
His work in the fields of Crystallography, such as Goniometer, overlaps with other areas such as Synchronizing, Throughput, Femtosecond and Roadrunner.
His Viral membrane research incorporates elements of Protein structure and Lipid bilayer.
His work often combines Protein structure and Potency studies.
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