Peter Højrup

What is he best known for?

The fields of study he is best known for:

• Enzyme
• Gene
• Amino acid

Biochemistry, Chromatography, Cell biology, Glycan and Peptide are his primary areas of study. His work on Biochemistry deals in particular with Protein structure, Glycosylation, Peptide sequence, Edman degradation and Proteolysis. Peter Højrup works mostly in the field of Protein structure, limiting it down to topics relating to Amino acid and, in certain cases, Insect, Order, Sequence and Protein filament.

The Glycosylation study combines topics in areas such as Residue and Glycoprotein. When carried out as part of a general Cell biology research project, his work on Cytoplasmic inclusion is frequently linked to work in Glial cytoplasmic inclusion, therefore connecting diverse disciplines of study. His Peptide research incorporates elements of Proteome, Biophysics, Proteasome, Hsp70 and Dehydrogenase.

His most cited work include:

• Angiostatin binds ATP synthase on the surface of human endothelial cells (467 citations)
• Hfq: a bacterial Sm-like protein that mediates RNA-RNA interaction. (454 citations)
• Identification of the receptor scavenging hemopexin-heme complexes (326 citations)

What are the main themes of his work throughout his whole career to date?

Peter Højrup spends much of his time researching Biochemistry, Chromatography, Mass spectrometry, Glycosylation and Calreticulin. His study in Glycan, Peptide sequence, Peptide, Amino acid and Enzyme are all subfields of Biochemistry. The various areas that Peter Højrup examines in his Chromatography study include Polyacrylamide gel electrophoresis and Proteomics.

The study incorporates disciplines such as Tandem mass tag, Matrix-assisted laser desorption/ionization and Peptide mass fingerprinting in addition to Mass spectrometry. His Glycosylation research includes themes of Edman degradation, Trypsin, Blood proteins, Molecular biology and Vitamin D-binding protein. In Calreticulin, Peter Højrup works on issues like Chaperone, which are connected to Biophysics and Crystallography.

He most often published in these fields:

• Biochemistry (48.48%)
• Chromatography (20.00%)
• Mass spectrometry (15.76%)

What were the highlights of his more recent work (between 2014-2020)?

• Biochemistry (48.48%)
• Chromatography (20.00%)
• Chaperone (6.67%)

In recent papers he was focusing on the following fields of study:

His primary areas of study are Biochemistry, Chromatography, Chaperone, Peptide and Oligomer. As part of his studies on Biochemistry, Peter Højrup often connects relevant areas like Molecular biology. His Chaperone research integrates issues from Crystallography, Protein structure and Homeostasis.

His Peptide study combines topics from a wide range of disciplines, such as Thermolysin, Leucine, Isoleucine, Chymotrypsin and Protein sequencing. He has researched Tandem mass spectrometry in several fields, including Proteomics, Affinity chromatography, Proteolysis, Enzyme and Digestion. His biological study spans a wide range of topics, including Radiochemistry and Labelling.

Between 2014 and 2020, his most popular works were:

• Mapping the Ca2+ induced structural change in calreticulin (22 citations)
• Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface (18 citations)
• High-level secretion of native recombinant human calreticulin in yeast (14 citations)

In his most recent research, the most cited papers focused on:

• Enzyme
• Gene
• Amino acid

Peter Højrup mostly deals with Oligomer, Chaperone, Biophysics, Biochemistry and Monomer. In his works, Peter Højrup conducts interdisciplinary research on Biophysics and Frataxin. His Biochemistry study frequently draws connections between adjacent fields such as Chromatography.

His work deals with themes such as Heat shock protein, Chaperone activity, Structural motif and Cryo-electron microscopy, which intersect with Homology modeling. His Peptide study combines topics in areas such as Amino acid, Tryptophan, Asparagine, Aspartic acid and Ninhydrin. His Calreticulin research is multidisciplinary, incorporating elements of Protein structure, Cell culture and Homeostasis.