Darlene Groth

Department of Neurology, University of California, San Francisco, California 94143, USA

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Human prion strain selection in transgenic mice

Kurt Giles,David V Glidden,Smita Patel,Carsten Korth,Darlene Groth,Azucena Lemus,Stephen J DeArmond,Stanley B Prusiner

ANNALS OF NEUROLOGY, no. 2.0 (2010): 151-161

Cited by40WOSBibtex

Changes in neuropeptide expression in mice infected with prions

Margarita Diez,Darlene Groth,Stephen J DeArmond,Stanley B Prusiner,Tomas Hökfelt

Neurobiology of Aging, no. 5 (2007): 748-765

Cited by9WOSEIBibtex

17 Biosafety Issues in Prion Diseases

Henry Baron,Jiri G Safar,Darlene Groth,Stephen J Dearmond,Stanley B Prusiner

(2004)

Bibtex

Mutant PrPSc conformers induced by a synthetic peptide and several prion strains

Patrick Tremblay,Haydn L Ball,Kiyotoshi Kaneko,Darlene Groth,Ramanujan S Hegde,Fred E Cohen,Stephen J DeArmond,Stanley B Prusiner,Jiri G Safar

Journal of virology, no. 4 (2004): 2088-2099

Cited by122WOSBibtex

Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene

Carsten Korth,Kiyotoshi Kaneko,Darlene Groth,Norbert Heye,Glenn Telling,James Mastrianni,Piero Parchi,Pierluigi Gambetti,Robert Will,James Ironside,Cornelia Heinrich,Patrick Tremblay

Proceedings of the National Academy of Sciences of the United States of America, no. 8 (2003): 4784-4789

Cited by114WOSBibtex

A novel transgenic mouse model for Creutzfeldt-Jakob disease (CJD) with abbreviated incubation times for most human prion strains reveals homogeneity of sporadic CJD

C Korth,K Kaneko,D Groth,S DeArmond,SB Prusiner

ACTA NEUROPATHOLOGICA, no. 5 (2002): 556-556

Bibtex

Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice

Jiri G. Safar,Michael Scott,Jeff Monaghan,Camille Deering,Svetlana Didorenko,Julie Vergara,Haydn Ball,Giuseppe Legname,Estelle Leclerc,Laura Solforosi,Hana Serban,Darlene Groth

Nature Biotechnology, no. 11 (2002): 1147-1150

Cited by247WOSNATUREBibtex

Cryptic epitopes in N-terminally truncated prion protein are exposed in the full-length molecule: dependence of conformation on pH

Y Matsunaga,D Peretz,A Williamson,D Burton,I Mehlhorn,D Groth,F E Cohen,S B Prusiner,M A Baldwin

Proteins, no. 2 (2001): 110-118

Cited by40WOSBibtex

Copper-catalyzed oxidation of the recombinant SHa(29–231) prion protein

Jesús R. Requena,Darlene Groth,Giuseppe Legname,Earl R. Stadtman,Stanley B. Prusiner,Rodney L. Levine

Proceedings of the National Academy of Sciences of the United States of America, no. 13 (2001): 7170-7175

Cited by164WOSBibtex

A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice

K Kaneko,H L Ball,H Wille,H Zhang,D Groth,M Torchia,P Tremblay,J Safar,S B Prusiner,S J DeArmond,M A Baldwin,F E Cohen

Journal of molecular biology, no. 4 (2000): 997-1007

Cited by147WOSBibtex

A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice11Edited by P. E. Wright

Kiyotoshi Kaneko,Haydn L Ball,Holger Wille,Hong Zhang,Darlene Groth,Marilyn Torchia,Patrick Tremblay,Jiri Safar,Stanley B Prusiner,Stephen J DeArmond,Michael A Baldwin,Fred E Cohen

Journal of Molecular Biology, no. 4 (2000): 997-1007

EIBibtex

Quantitative Trait Loci Affecting Prion Incubation Time in Mice

Dennis A. Stephenson,Kami Chiotti,Christine Ebeling,Darlene Groth,Stephen J. DeArmond,Stanley B. Prusiner,George A. Carlson

GENOMICS, no. 1 (2000): 47-53

EIWOSBibtex

A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice 1 1 Edited by P. E. Wright

Kiyotoshi Kaneko,Haydn L Ball,Holger Wille,Hong Zhang,Darlene Groth,Marilyn Torchia,Patrick Tremblay,Jiri G Safar,Stanley B Prusiner,Stephen J Dearmond,Michael A Baldwin,Fred E Cohen

Journal of Molecular Biology, (2000)

Cited by41Bibtex

Self-Assembly of Recombinant Prion Protein of 106 Residues �

Ilia V Baskakov,Claus Aagaard,Ingrid Mehlhorn,Holger Wille,Darlene Groth,Michael A Baldwin,Stanley B Prusiner,Fred E Cohen

Biochemistry, (2000)

Cited by22Bibtex

Glycosylation differences between the normal and pathogenic prion protein isoforms

Pauline M. Rudd,Tama Endo,Cristina Colominas,Darlene Groth,Susan F. Wheeler,David J. Harvey,Mark R. Wormald,Hana Serban,Stanley B. Prusiner,Akira Kobata,Raymond A. Dwek

Proceedings of the National Academy of Sciences of the United States of America, no. 23 (1999): 13044-13049

Cited by40WOSBibtex

Vishwanath R. Lingappa,Ramanujan S. Hegde,Patrick Tremblay,Darlene Groth,Stephen J. DeArmond,Stanley B. Prusiner

Nature, no. 6763 (1999): 822-826

Cited by1Bibtex

Eight prion strains have PrPSc molecules with different conformations

Jiri Safar,Holger Wille,Vincenza Itri,Darlene Groth,Hana Serban,Marilyn Torchia,Fred E. Cohen,Stanley B. Prusiner

Nature Medicine, no. 10 (1998): 1157-1165

Cited by145WOSNATUREBibtex

Eight prion strains have PrPSc molecules with differentconformations

Jiri G Safar,Holger Wille,Vincenza Itri,Darlene Groth,Hana Serban,Marilyn Torchia,Fred E Cohen,Stanley B Prusiner

Nature Medicine, (1998)

Bibtex

Biophysical Studies on Structure Structural Transitions and Infectivity of the Prion Protein

Detlev Riesner, K Kellings,Karin Post,Martin Pitschke,Holger Wille,Hana Serban,Darlene Groth,Michael A Baldwin,Stanley B Prusiner

(1998)

Bibtex

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,Hong Zhang,David G. Donne,Kiyotoshi Kaneko,Darlene Groth,Ingrid Mehlhorn,Stanley B. Prusiner,Fred E. Cohen

Proceedings of the National Academy of Sciences of the United States of America, no. 19 (1997): 10086-10091

WOSBibtex

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