Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Darlene Groth"'
Autor:
Robert W. Mahley, Carsten Korth, Charles J. Epstein, Patrick Tremblay, Fred E. Cohen, Darlene Groth, Gültekin Tamgüney, Lennart Mucke, Pauline M. Rudd, Karen H. Ashe, Karl H. Weisgraber, Jan Sap, George A. Carlson, Eric Rubinstein, Kurt Giles, Ina Tesseur, Pamela Stanley, Xiaoping Yang, Richard C. Moore, William A. Kuziel, Raymond A. Dwek, Michael P. Lisanti, Fruma Yehiely, Tony Wyss-Coray, Tracey Dawson Cruz, Claude Boucheix, David V. Glidden, Jörg Tatzelt, Jackob Moskovitz, Holger Wille, Stanley B. Prusiner, Pierre Lessard, Nobuyo Maeda
Publikováno v:
Journal of General Virology. 89:1777-1788
Prion diseases are caused by conversion of a normally folded, non-pathogenic isoform of the prion protein (PrPC) to a misfolded, pathogenic isoform (PrPSc). Prion inoculation experiments in mice expressing homologous PrPCmolecules on different geneti
Autor:
Awad A. Osman, Darlene Groth, Heinz Schimmel, Kurt Giles, Reet Toomik, Ingolf Lachmann, Muriel Feyssaguet, Wolfgang J. Philipp, Stanley B. Prusiner, Jean-Noel Arsac, Angus Wear, Pavel Vodrazka, Pascal Schacher
Publikováno v:
Biological Chemistry. 388:349-354
Rapid BSE tests are widely used diagnostics in veterinary medicine and more than 11 million tests are applied worldwide. The evaluation of new rapid BSE tests and the quality assurance of approved BSE tests pose a challenge owing to the natural scarc
Autor:
Jiri G. Safar, Darlene Groth, K. Kellings, Stanley B. Prusiner, Detlev Riesner, James E. Cleaver, Ana Serban
Publikováno v:
Journal of Virology. 79:10796-10806
Diversity of prion strains was attributed to an elusive nucleic acid, yet a search spanning nearly two decades has failed to identify a prion-specific polynucleotide. In our search for a prion-specific nucleic acid, we analyzed nucleic acids in purif
Publikováno v:
Neurobiology of Disease, Vol 8, Iss 4, Pp 692-699 (2001)
The neurochemical alterations associated with neurodegeneration in prion diseases are not well defined. It is therefore of interest to study the influence of prion infection on messenger molecules and their receptors. In the present study we have ana
Autor:
Stanley B. Prusiner, Earl R. Stadtman, Darlene Groth, Jesús R. Requena, Rodney L. Levine, Giuseppe Legname
Publikováno v:
Proceedings of the National Academy of Sciences. 98:7170-7175
Metal-catalyzed oxidation may result in structural damage to proteins and has been implicated in aging and disease, including neurological disorders such as Alzheimer's disease and amyotrophic lateral sclerosis. The selective modification of specific
Autor:
Christine Ebeling, Stanley B. Prusiner, Stephen J. DeArmond, Kami E. Chiotti, Dennis A. Stephenson, George A. Carlson, Darlene Groth
Publikováno v:
Genomics. 69:47-53
Although the gene encoding prion protein (PrP) is the major determinant of susceptibility to prion disease, other genes also affect prion incubation time in mice and may be involved in prion replication. Scrapie incubation time was analyzed as a quan
Autor:
Haydn L. Ball, Patrick Tremblay, Hong Zhang, Stephen J. DeArmond, Darlene Groth, Michael A. Baldwin, Fred E. Cohen, Stanley B. Prusiner, Jiri G. Safar, Holger Wille, Kiyotoshi Kaneko, Marilyn Torchia
Publikováno v:
Journal of Molecular Biology. 295:997-1007
The molecular basis of the infectious, inherited and sporadic forms of prion diseases is best explained by a conformationally dimorphic protein that can exist in distinct normal and disease-causing isoforms. We identified a 55-residue peptide of a mu
Publikováno v:
Journal of Neuropathology & Experimental Neurology. 58:1244-1249
The kinetics of PrP(Sc) and insoluble PrP accumulation in the spleens and brains of CD-1 mice were studied. The mice were inoculated intracerebrally with RML prions and euthanized at various times between inoculation and the onset of illness at appro
Autor:
Pauline M. Rudd, Tama Endo, Cristina Colominas, Raymond A. Dwek, Stanley B. Prusiner, Susan F. Wheeler, Hana Serban, Mark R. Wormald, David Harvey, Darlene Groth, Akira Kobata
Publikováno v:
Proceedings of the National Academy of Sciences. 96:13044-13049
Prion protein consists of an ensemble of glycosylated variants or glycoforms. The enzymes that direct oligosaccharide processing, and hence control the glycan profile for any given glycoprotein, are often exquisitely sensitive to other events taking
Autor:
Ingrid Mehlhorn, David G. Donne, He Liu, Shauna Farr-Jones, Fred E. Cohen, Kiyotoshi Kaneko, Nikolai B. Ulyanov, Hong Zhang, Thomas L. James, Darlene Groth, Stanley B. Prusiner
Publikováno v:
Proceedings of the National Academy of Sciences. 94:10086-10091
The scrapie prion protein (PrP Sc ) is the major, and possibly the only, component of the infectious prion; it is generated from the cellular isoform (PrP C ) by a conformational change. N-terminal truncation of PrP Sc by limited proteolysis produces