نتایج جستجو برای: prions

تعداد نتایج: 4608  

Journal: :Microbiology spectrum 2016
Sven J Saupe Daniel F Jarosz Heather L True

Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements. Fungal prions correspond in most cases to fibrillary β-sheet-rich protein aggregates termed amyloids. Fungal prion models and, in particular, yeast prions were ins...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2015
Amanda L Woerman Jan Stöhr Atsushi Aoyagi Ryan Rampersaud Zuzana Krejciova Joel C Watts Takao Ohyama Smita Patel Kartika Widjaja Abby Oehler David W Sanders Marc I Diamond William W Seeley Lefkos T Middleton Steve M Gentleman Daniel A Mordes Thomas C Südhof Kurt Giles Stanley B Prusiner

Increasingly, evidence argues that many neurodegenerative diseases, including progressive supranuclear palsy (PSP), are caused by prions, which are alternatively folded proteins undergoing self-propagation. In earlier studies, PSP prions were detected by infecting human embryonic kidney (HEK) cells expressing a tau fragment [TauRD(LM)] fused to yellow fluorescent protein (YFP). Here, we report ...

2013
Sybille Krauss Ina Vorberg

Prions are unconventional infectious agents that are composed of misfolded aggregated prion protein. Prions replicate their conformation by template-assisted conversion of the endogenous prion protein PrP. Templated conversion of soluble proteins into protein aggregates is also a hallmark of other neurodegenerative diseases. Alzheimer's disease or Parkinson's disease are not considered infectio...

Journal: :Molecular cell 2007
Vibha Taneja Marie-Lise Maddelein Nicolas Talarek Sven J Saupe Susan W Liebman

Prions are self-propagating, infectious aggregates of misfolded proteins. The mammalian prion, PrP(Sc), causes fatal neurodegenerative disorders. Fungi also have prions. While yeast prions depend upon glutamine/asparagine (Q/N)-rich regions, the Podospora anserina HET-s and PrP prion proteins lack such sequences. Nonetheless, we show that the HET-s prion domain fused to GFP propagates as a prio...

Journal: :Developmental Immunology 2001
Alex J. Raeber Fabio Montrasio Ivan Hegyi Rico Frigg Michael A. Klein Adriano Aguzzi Charles Weissmann

Some of the early events following scrapie infection take place in the lymphoreticular system (LRS) and result in significant replication of prions in lymphoid organs. The identity of the cells in the LRS that produce prions and their role in neuroinvasion are still unknown. We find that in the spleen of scrapie-infected mice, prions are associated with T and B cells and to a somewhat lesser de...

Journal: :Journal of virology 2011
Timothy D Kurt Davis M Seelig Jay R Schneider Christopher J Johnson Glenn C Telling Dennis M Heisey Edward A Hoover

Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy (TSE) of cervids now detected in 19 states of the United States, three Canadian provinces, and South Korea. Whether noncervid species can be infected by CWD and thereby serve as reservoirs for the infection is not known. To investigate this issue, we previously used serial protein misfolding cyclic amplification (sPMCA) ...

Journal: :Cell 1999
Surachai Supattapone Patrick Bosque Tamaki Muramoto Holger Wille Claus Aagaard David Peretz Hoang-Oanh B Nguyen Cornelia Heinrich Marilyn Torchia Jiri Safar Fred E Cohen Stephen J DeArmond Stanley B Prusiner Michael Scott

A redacted prion protein (PrP) of 106 amino acids with two large deletions was expressed in transgenic (Tg) mice deficient for wild-type (wt) PrP (Prnp0/0) and supported prion propagation. RML prions containing full-length PrP(Sc)produced disease in Tg(PrP106)Prnp0/0 mice after approximately 300 days, while transmission of RML106 prions containing PrP(Sc)106 created disease in Tg(PrP106) Prnp0/...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2013
David B Berry Duo Lu Michal Geva Joel C Watts Sumita Bhardwaj Abby Oehler Adam R Renslo Stephen J DeArmond Stanley B Prusiner Kurt Giles

There is not a single pharmaceutical that halts or even slows any neurodegenerative disease. Mounting evidence shows that prions cause many neurodegenerative diseases, and arguably, scrapie and Creutzfeldt-Jakob disease prions represent the best therapeutic targets. We report here that the previously identified 2-aminothiazoles IND24 and IND81 doubled the survival times of scrapie-infected, wil...

Journal: :Current Biology 1999
Jim Hope

plants are cloaked in hundreds of tiny projections, known as trichomes. These structures vary in function, shape, size and spacing from species to species, and it’s not known whether similar cellular differentiation programs are responsible for making trichomes in different plants. Trichomes are clearly visible in the scanning electron micrograph of a wild-type Nicotiana tabacum seedling above ...

2017
Barry M Bradford Boris Reizis Neil A Mabbott

After oral exposure, the early replication of certain prion strains upon stromal cell-derived follicular dendritic cells (FDC) in the Peyer's patches in the small intestine is essential for the efficient spread of disease to the brain. However, little is known of how prions are initially conveyed from the gut lumen to establish infection on FDC. Our previous data suggest that mononuclear phagoc...

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