What is he best known for?
The fields of study he is best known for:
- Enzyme
- Amino acid
- Biochemistry
Biochemistry, Chaperone, Enzyme, Amino acid and Molecular biology are his primary areas of study.
His studies in Chaperone integrate themes in fields like Protein aggregation, Protein degradation, Escherichia coli, Hsp70 and Peptide.
His research brings together the fields of Stereochemistry and Enzyme.
His research integrates issues of Pyridoxal phosphate, Pyridoxal, Aldimine and Active site in his study of Stereochemistry.
His work in Amino acid addresses issues such as Protein superfamily, which are connected to fields such as Serine.
In Molecular biology, Philipp Christen works on issues like Cytosol, which are connected to Biosynthesis and Mitochondrion.
His most cited work include:
- Kinetics of molecular chaperone action (393 citations)
- Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. (375 citations)
- Aminotransferases: demonstration of homology and division into evolutionary subgroups (351 citations)
What are the main themes of his work throughout his whole career to date?
His primary scientific interests are in Biochemistry, Enzyme, Stereochemistry, Amino acid and Active site.
His is involved in several facets of Biochemistry study, as is seen by his studies on Chaperone, Escherichia coli, Cytosol, Peptide and Isozyme.
His work focuses on many connections between Chaperone and other disciplines, such as Protein folding, that overlap with his field of interest in Protein aggregation.
The various areas that Philipp Christen examines in his Enzyme study include Crystallography and Protein subunit.
His Stereochemistry research is multidisciplinary, incorporating elements of Pyridoxal, Transamination, Pyridoxal phosphate, Substrate and Stereospecificity.
His Amino acid research is multidisciplinary, incorporating perspectives in Tyrosine and Hapten.
He most often published in these fields:
- Biochemistry (57.51%)
- Enzyme (30.05%)
- Stereochemistry (29.53%)
What were the highlights of his more recent work (between 2001-2018)?
- Biochemistry (57.51%)
- Chaperone (12.95%)
- Protein folding (7.77%)
In recent papers he was focusing on the following fields of study:
Philipp Christen spends much of his time researching Biochemistry, Chaperone, Protein folding, Hsp70 and Escherichia coli.
His study in Peptide, Protein degradation, Binding site, Enzyme and Glyoxylate cycle is carried out as part of his studies in Biochemistry.
His studies deal with areas such as Heat shock protein, Biophysics and Circular dichroism as well as Chaperone.
His Protein folding study combines topics in areas such as Metal ions in aqueous solution, Metalloid and Protein aggregation.
His research in Escherichia coli intersects with topics in Mutant and Heat shock.
The Cofactor study combines topics in areas such as Amino acid, Transamination, Stereochemistry and Aldimine.
Between 2001 and 2018, his most popular works were:
- Demonstration of the ethylmalonyl-CoA pathway by using 13C metabolomics (170 citations)
- Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation (169 citations)
- The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase (158 citations)
In his most recent research, the most cited papers focused on:
His primary areas of study are Biochemistry, Chaperone, Protein folding, Protein aggregation and Hsp70.
Protein degradation, Escherichia coli, Peptide, Glyoxylate cycle and Serine are the subjects of his Biochemistry studies.
His Protein folding research incorporates elements of Heat shock protein, Helix, Adenosine triphosphate, Circular dichroism and Dimer.
His Heat shock protein research incorporates themes from Protein biosynthesis, Crystallography, Saccharomyces cerevisiae and Arsenite.
Philipp Christen combines subjects such as Thiol, Biophysics and Metal toxicity, Toxicity, Cadmium with his study of Protein aggregation.
His Hsp70 study which covers Dissociation that intersects with In vitro, Enzyme kinetics and Native state.
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