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Biology and Biochemistry

D-Index
69
Citations
11828
World Ranking
7591
National Ranking
3450

Overview

Lars C. Pedersen is affiliated with the National Institutes of Health in the United States. Their research spans multiple fields with a primary focus on biochemistry, genetics, and molecular biology, along with significant contributions to medicine.

Their work covers several specialized subfields, including molecular biology, cell biology, immunology and allergy, organic chemistry, and public health, environmental, and occupational health. Pedersen's research topics center predominantly on proteoglycans and glycosaminoglycans research, glycosylation and glycoproteins research, DNA repair mechanisms, food allergy and anaphylaxis research, carbohydrate chemistry and synthesis, DNA and nucleic acid chemistry, and allergic rhinitis and sensitization.

Frequent collaborators in Pedersen's work include:

  • Jian Liu
  • Andrea M. Kaminski
  • Yongmei Xu
  • Thomas A. Kunkel
  • Henrik Toft Sørensen

Pedersen has published extensively, with numerous contributions appearing in prominent venues. Key publication venues where Pedersen's work frequently appears include UNC Libraries, Nature Communications, bioRxiv (Cold Spring Harbor Laboratory), Science Advances, and the Journal of Allergy and Clinical Immunology.

Examples of recent published papers include:

  • A genome-wide CRISPR-Cas9 knockout screen identifies FSP1 as the warfarin-resistant vitamin K reductase, 2023, Nature Communications
  • Immunotherapy-induced neutralizing antibodies disrupt allergen binding and sustain allergen tolerance in peanut allergy, 2023, Journal of Clinical Investigation
  • Semaglutide (Ozempic®) Use in Denmark 2018 Through 2023 - User Trends and off-Label Prescribing for Weight Loss, 2024, Clinical Epidemiology
  • Increased 3- O -sulfated heparan sulfate in Alzheimer's disease brain is associated with genetic risk gene HS3ST1, 2023, Science Advances
  • Neutralizing IgG4 antibodies are a biomarker of sustained efficacy after peanut oral immunotherapy, 2024, Journal of Allergy and Clinical Immunology

Best Publications

  • Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.

    Vivien C. Yee;Lars C. Pedersen;Isolde Le Trong;Paul D. Bishop

  • Structure and function of sulfotransferases.

    Masahiko Negishi;Lee G. Pedersen;Lee G. Pedersen;Evgeniy Petrotchenko;Sergei Shevtsov

  • Crystal structure of estrogen sulphotransferase

    Yoshimitsu Kakuta;Lee G. Pedersen;Charles W. Carter;Masahiko Negishi

  • Magnesium-induced assembly of a complete DNA polymerase catalytic complex.

    Vinod K. Batra;William A. Beard;David D. Shock;Joseph M. Krahn

  • Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I.

    Lars C. Pedersen;Kazunori Tsuchida;Hiroshi Kitagawa;Kazuyuki Sugahara

  • 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

  • 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

  • Replication infidelity via a mismatch with Watson-Crick geometry.

    Katarzyna Bebenek;Lars C. Pedersen;Thomas A. Kunkel

  • Conserved structural motifs in the sulfotransferase family

    Yoshimitsu Kakuta;Lee G Pedersen;Lars C Pedersen;Masahiko Negishi

  • Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules.

    L. C. Pedersen;Vivien Yee;P. D. Bishop;I. Le Trong

  • The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis

    Yoshimitsu Kakuta;Evgeny V. Petrotchenko;Lars C. Pedersen;Masahiko Negishi

  • A closed conformation for the Pol lambda catalytic cycle.

    Miguel Garcia-Diaz;Katarzyna Bebenek;Joseph M Krahn;Thomas A Kunkel

  • Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/ N-sulfotransferase 1.

    Yoshimitsu Kakuta;Tatsuya Sueyoshi;Masahiko Negishi;Lars C. Pedersen

  • Anticoagulant heparan sulfate: structural specificity and biosynthesis

    Jian Liu;Lars C. Pedersen

  • Structures of DNA Polymerase β with Active-Site Mismatches Suggest a Transient Abasic Site Intermediate during Misincorporation

    Vinod K. Batra;William A. Beard;David D. Shock;Lars C. Pedersen

  • A Structural Solution for the DNA Polymerase λ-Dependent Repair of DNA Gaps with Minimal Homology

    Miguel Garcia-Diaz;Katarzyna Bebenek;Joseph M Krahn;Luis Blanco

  • The dimerization motif of cytosolic sulfotransferases.

    Evgeniy V. Petrotchenko;Lars C. Pedersen;Christoph H. Borchers;Kenneth B. Tomer

  • Structure of a signal transduction regulator, RACK1, from Arabidopsis thaliana.

    Hemayet Ullah;Erica Louise Scappini;Andrea Florence Moon;Latanya Veronica Williams

  • Crystal Structure of the Human Estrogen Sulfotransferase-PAPS Complex EVIDENCE FOR CATALYTIC ROLE OF Ser137 IN THE SULFURYL TRANSFER REACTION

    Lars C. Pedersen;Evgeniy Petrotchenko;Sergei Shevtsov;Masahiko Negishi

  • CRYSTAL STRUCTURE OF HUMAN CATECHOLAMINE SULFOTRANSFERASE

    Lisa M Bidwell;Michael E McManus;Andrea Gaedigk;Yoshimitsu Kakuta

Frequent Co-Authors

Thomas A. Kunkel
Thomas A. Kunkel National Institutes of Health
Masahiko Negishi
Masahiko Negishi National Institutes of Health
Robert E. London
Robert E. London National Institutes of Health
Katarzyna Bebenek
Katarzyna Bebenek National Institutes of Health
Lee G. Pedersen
Lee G. Pedersen University of North Carolina at Chapel Hill
William A. Beard
William A. Beard National Institutes of Health
Samuel H. Wilson
Samuel H. Wilson National Institutes of Health
Lalith Perera
Lalith Perera National Institutes of Health
Martin D. Chapman
Martin D. Chapman University of Virginia

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