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Biology and Biochemistry

D-Index
58
Citations
23784
World Ranking
12897
National Ranking
5491

Overview

Darlene Groth is affiliated with the University of California, San Francisco in the United States. Their research interests lie primarily within the fields of Biochemistry, Genetics, and Molecular Biology, with significant focus on subfields such as Molecular Biology and Genetics.

The main topics addressed in their work include Prion Diseases and Protein Misfolding as well as Animal Genetics and Reproduction. These areas reflect a concentration on understanding molecular mechanisms underlying disease processes and genetic factors influencing animal biology.

Groth has contributed to academic literature with publications in recognized venues. Notably, their recent paper titled Genes contributing to prion pathogenesis, published in 2020 in UNC Libraries, examines genetic components involved in prion-related disorders.

Their collaborative efforts include frequent co-authorship with several researchers:

  • Gültekin Tamgüney
  • Kurt Giles
  • David V. Glidden
  • Pierre Lessard
  • Holger Wille

Groth's work has appeared predominantly in UNC Libraries, the publication venue associated with their known research output.

Best Publications

  • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.

    K M Pan;M Baldwin;J Nguyen;M Gasset

  • Eight prion strains have PrP Sc molecules with different conformations

    Jiri Safar;Holger Wille;Vincenza Itri;Darlene Groth

  • Scrapie prions aggregate to form amyloid-like birefringent rods

    Stanley B. Prusiner;Michael P. McKinley;Karen A. Bowman;David C. Bolton

  • Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene

    K. Basler;B. Oesch;M. Scott;D. Westaway

  • Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication.

    Stanley B. Prusiner;Michael Scott;Dallas Foster;Keh-Ming Pan

  • Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques

    Michael Scott;Dallas Foster;Carol Mirenda;Dan Serban

  • Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible.

    Donne Dg;Viles Jh;Groth D;Mehlhorn I

  • Spontaneous neurodegeneration in transgenic mice with mutant prion protein.

    Karen K. Hsiao;Michael Scott;Dallas Foster;Darlene F. Groth

  • Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies

    Stanley B. Prusiner;Darlene Groth;Ana Serban;Ruth Koehler

  • Purification and structural studies of a major scrapie prion protein

    Stanley B. Prusiner;Darlene F. Groth;David C. Bolton;Stephen B. Kent

  • Further purification and characterization of scrapie prions

    S B Prusiner;D C Bolton;D F Groth;K A Bowman

  • Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.

    Thomas L. James;He Liu;Nikolai B. Ulyanov;Shauna Farr-Jones

  • Measurement of the scrapie agent using an incubation time interval assay

    Stanley B. Prusiner;S. Patricia Cochran;Darlene F. Groth;Deborah E. Downey

  • Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes.

    Michael Scott;Darlene Groth;Dallas Foster;Marilyn Torchia

  • Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein.

    Tamao Endo;Darlene Groth;Stanley B. Prusiner;Akira Kobata

  • Transmissible and genetic prion diseases share a common pathway of neurodegeneration

    Ramanujan S. Hegde;Patrick Tremblay;Darlene Groth;Stephen J. DeArmond

  • Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins.

    David Westaway;Stephen J. DeArmond;Juliana Cayetano-Canlas;Darlene Groth

  • Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein

    Karen K. Hsiao;Darlene Groth;Michael Scott;Shu Lian Yang

  • Glycosylation differences between the normal and pathogenic prion protein isoforms.

    Pauline M. Rudd;Tama Endo;Cristina Colominas;Darlene Groth

  • Asparagine-linked glycosylation of the scrapie and cellular prion proteins.

    Tokuko Haraguchi;Susan Fisher;Sigvard Olofsson;Tamao Endo

Frequent Co-Authors

Stanley B. Prusiner
Stanley B. Prusiner University of California, San Francisco
Stephen J. DeArmond
Stephen J. DeArmond University of California, San Francisco
Fred E. Cohen
Fred E. Cohen University of California, San Francisco
George A. Carlson
George A. Carlson University of California, San Francisco
Michael A. Baldwin
Michael A. Baldwin University of California, San Francisco
Holger Wille
Holger Wille University of Alberta
Detlev Riesner
Detlev Riesner Heinrich Heine University Düsseldorf
Ramanujan S. Hegde
Ramanujan S. Hegde MRC Laboratory of Molecular Biology
Jörg Tatzelt
Jörg Tatzelt Ruhr University Bochum
Tomas Hökfelt
Tomas Hökfelt Karolinska Institute

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