Lars C. Pedersen mainly investigates Stereochemistry, Biochemistry, Protein structure, Enzyme and Transferase. His biological study spans a wide range of topics, including Sulfotransferase, Sulfuryl, Crystal structure, Substrate and DNA polymerase. His DNA polymerase research includes elements of Base excision repair, DNA repair, Base pair and Polymerase.
His work carried out in the field of Protein structure brings together such families of science as Catalytic triad, Active site, Protein folding, Cysteine and Maltose-binding protein. His work deals with themes such as Kanamycin and Nucleotide, which intersect with Enzyme. His Transferase research includes themes of Cofactor, Binding site and Estrogen Sulfotransferase.
Biochemistry, Stereochemistry, Polymerase, DNA and Molecular biology are his primary areas of study. His is involved in several facets of Biochemistry study, as is seen by his studies on Heparan sulfate, Sulfotransferase, Enzyme, Binding site and Sulfation. His research integrates issues of Transferase, Crystal structure, Ternary complex, Active site and Protein structure in his study of Stereochemistry.
The Protein structure study combines topics in areas such as Peptide sequence and Protein subunit. His Polymerase research is multidisciplinary, incorporating elements of Human dna, Crystallography, Biophysics, Catalysis and DNA polymerase. The concepts of his Molecular biology study are interwoven with issues in DNA polymerase lambda and Immunology.
His primary areas of study are Polymerase, Stereochemistry, Ternary complex, Biochemistry and DNA. His Polymerase study incorporates themes from Crystallography, Biophysics, Catalysis, Substrate and DNA polymerase. In his work, Structure–activity relationship and Oxidoreductase is strongly intertwined with Binding site, which is a subfield of Biophysics.
His Stereochemistry research includes elements of Catalytic complex, Nucleotide and Transferase. Lars C. Pedersen focuses mostly in the field of Transferase, narrowing it down to topics relating to Sequence alignment and, in certain cases, Protein structure. Biochemistry and Deoxycytidine deaminase are two areas of study in which Lars C. Pedersen engages in interdisciplinary research.
His primary scientific interests are in Biochemistry, DNA, DNA clamp, Polymerase and DNA polymerase. His Peptide sequence, Oxidoreductase and Dihydrofolate reductase study in the realm of Biochemistry interacts with subjects such as Phenformin and Buformin. His study in DNA is interdisciplinary in nature, drawing from both Mutagenesis, Nucleic acid and Function.
In most of his Polymerase studies, his work intersects topics such as Binding site. The Crystallography study which covers DNA synthesis that intersects with Ternary complex. His work is dedicated to discovering how Ternary complex, Stereochemistry are connected with Protein structure and other disciplines.
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Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.
Vivien C. Yee;Lars C. Pedersen;Isolde Le Trong;Paul D. Bishop.
Proceedings of the National Academy of Sciences of the United States of America (1994)
Structure and function of sulfotransferases.
Masahiko Negishi;Lee G. Pedersen;Lee G. Pedersen;Evgeniy Petrotchenko;Sergei Shevtsov.
Archives of Biochemistry and Biophysics (2001)
Magnesium-induced assembly of a complete DNA polymerase catalytic complex.
Vinod K. Batra;William A. Beard;David D. Shock;Joseph M. Krahn.
Crystal structure of estrogen sulphotransferase
Yoshimitsu Kakuta;Lee G. Pedersen;Charles W. Carter;Masahiko Negishi.
Nature Structural & Molecular Biology (1997)
Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I.
Lars C. Pedersen;Kazunori Tsuchida;Hiroshi Kitagawa;Kazuyuki Sugahara.
Journal of Biological Chemistry (2000)
A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.
Andrea F. Moon;Geoffrey A. Mueller;Xuejun Zhong;Lars C. Pedersen.
Protein Science (2010)
Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase
Lars C. Pedersen;Matthew M. Benning;Hazel M. Holden.
The X family portrait: structural insights into biological functions of X family polymerases.
Andrea F. Moon;Miguel Garcia-Diaz;Vinod K. Batra;William A. Beard.
DNA Repair (2007)
Conserved structural motifs in the sulfotransferase family
Yoshimitsu Kakuta;Lee G Pedersen;Lars C Pedersen;Masahiko Negishi.
Trends in Biochemical Sciences (1998)
Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules.
L. C. Pedersen;Vivien Yee;P. D. Bishop;I. Le Trong.
Protein Science (1994)
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