His primary areas of study are Biochemistry, Peptide sequence, Protein primary structure, Molecular biology and Phosphorylation. His Biochemistry study frequently links to other fields, such as Chromatography. His Peptide sequence study combines topics in areas such as Amino acid, Homology, Chymotrypsin and Binding site.
His research in Protein primary structure intersects with topics in Protein structure, Carboxyglutamic acid and Vitamin k. Torben E. Petersen interconnects Complementary DNA and Peptide in the investigation of issues within Molecular biology. His work on Threonine as part of general Phosphorylation research is frequently linked to Casein kinase 2 and Gel permeation chromatography, bridging the gap between disciplines.
Torben E. Petersen focuses on Biochemistry, Peptide sequence, Molecular biology, Amino acid and Protein primary structure. His Biochemistry study typically links adjacent topics like Stereochemistry. His Peptide sequence study integrates concerns from other disciplines, such as Threonine, Molecular mass, Cysteine, Chymotrypsin and Homology.
The concepts of his Molecular biology study are interwoven with issues in Complementary DNA, Nucleic acid sequence, Gene, Fibronectin and Signal peptide. His work deals with themes such as Protein structure and Macroglobulin, which intersect with Protein primary structure. His research in Serine focuses on subjects like Proteolysis, which are connected to Casein.
His primary areas of investigation include Biochemistry, Peptide sequence, Organic chemistry, Catalysis and Glycosylation. Transcobalamin, Intrinsic factor, Ligand, Glycoprotein and Peptide are the subjects of his Biochemistry studies. His Peptide sequence research includes elements of Molecular biology, Cell culture and Serine.
The study incorporates disciplines such as Residue, Fibronectin, Cyanogen bromide and Sequence in addition to Molecular biology. The various areas that he examines in his Organic chemistry study include Vitamin B12 and Medicinal chemistry. His Glycosylation research is multidisciplinary, incorporating perspectives in Mannose, Skimmed milk, Phosphorylation and Glycan.
Torben E. Petersen spends much of his time researching Biochemistry, Glycosylation, Phosphorylation, Edman degradation and Peptide sequence. Biochemistry is a component of his Haptocorrin and Amino acid studies. His research on Glycosylation often connects related areas such as Osteopontin.
His Osteopontin research is multidisciplinary, incorporating elements of Tyrosine, Sulfation, Molecular biology, Glycoprotein and Integrin. His biological study spans a wide range of topics, including Threonine, Kinase, Cell type and Gene isoform. His Peptide sequence study combines topics from a wide range of disciplines, such as Transport protein, Ligand, Intestinal absorption, Intrinsic factor and Transcobalamin.
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Partial primary structure of bovine plasma fibronectin: three types of internal homology
Torben Ellebæk Petersen;Hans Christian Thøgersen;Karna Skorstengaard;Karen Vibe-Pedersen.
Proceedings of the National Academy of Sciences of the United States of America (1983)
A thiol-ester in α2-macroglobulin cleaved during proteinase complex formation
Lars Sottrup-Jensen;Torben E. Petersen;Staffan Magnusson.
FEBS Letters (1980)
Primary structure of the vitamin K-dependent part of prothrombin.
Staffan Magnusson;Staffan Magnusson;Lars Sottrup-jensen;Lars Sottrup-jensen;Torben Ellebæk Petersen;Torben Ellebæk Petersen.
FEBS Letters (1974)
Primary structure of human alpha 2-macroglobulin. V. The complete structure.
L Sottrup-Jensen;T M Stepanik;T Kristensen;D M Wierzbicki.
Journal of Biological Chemistry (1984)
Complete Primary Structure of Bovine Plasma Fibronectin
Karna Skorstengaard;Margit S. Jensen;Preben Sahl;Torben E. Petersen.
FEBS Journal (1986)
Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
Brian Christensen;Mette S. Nielsen;Kim F. Haselmann;Torben E. Petersen.
Biochemical Journal (2005)
Posttranslational modifications of bovine osteopontin: identification of twenty-eight phosphorylation and three O-glycosylation sites.
E S Sørensen;P Højrup;T E Petersen.
Protein Science (1995)
Primary structure of elongation factor Tu from Escherichia coli.
K. Arai;B. F. C. Clark;L. Duffy;M. D. Jones.
Proceedings of the National Academy of Sciences of the United States of America (1980)
Functional analyses of two cellular binding domains of bovine lactadherin.
Mikkel H. Andersen;Helle Graversen;Sergey N. Fedosov;Torben E. Petersen.
Inhibitory effects of human and bovine milk constituents on rotavirus infections.
A.S. Kvistgaard;L.T. Pallesen;C.F. Arias;S. López.
Journal of Dairy Science (2004)
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