Shadoo/PrP (Sprn(0/0) /Prnp(0/0) ) double knockout mice: more than zeroes.

abstract：:Genetic prion diseases are degenerative brain disorders caused by mutations in the gene encoding the prion protein (PrP). Different PrP mutations cause different diseases, including Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker (GSS) syndrome and fatal familial insomnia (FFI). The reason for this var...

journal_title：Prion

authors： Chiesa R,Restelli E,Comerio L,Del Gallo F,Imeri L

更新日期：2016-03-03 00:00:00

abstract：:Prion protein (PrP), the causative agent of transmissible spongiform encephalopathies, is synthesized in the endoplasmic reticulum (ER) where it undergoes numerous covalent modifications. Here we investigate the interdependence and regulation of PrP oxidative folding, N-glycosylation and GPI addition in diverse ER con...

journal_title：Prion

authors： Orsi A,Sitia R

更新日期：2007-10-01 00:00:00

abstract：:The yeast, fungal and mammalian prions determine heritable and infectious traits that are encoded in alternative conformations of proteins. They cause lethal sporadic, familial and infectious neurodegenerative conditions in man, including Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), ...

journal_title：Prion

authors： Safar JG

更新日期：2012-04-01 00:00:00

abstract：:Prion diseases are consistently associated with prion protein (PrP(C)) misfolding rendering a cascade of auto-catalytic self-perpetuation of misfolded PrP in an afflicted individual. The molecular process is intriguingly similar to all known amyloid diseases both local and systemic. The prion disease is also infectiou...

journal_title：Prion

authors： Nyström S,Hammarström P

更新日期：2014-01-01 00:00:00

abstract：:A case of L-type-like atypical bovine spongiform encephalopathy was detected in 14-year-old Japanese black beef cattle (BSE/JP24). To clarify the biological and biochemical properties of the prion in BSE/JP24, we performed a transmission study with wild-type mice and bovinized transgenic mice (TgBoPrP). The BSE/JP24 p...

journal_title：Prion

authors： Masujin K,Shu Y,Yamakawa Y,Hagiwara K,Sata T,Matsuura Y,Iwamaru Y,Imamura M,Okada H,Mohri S,Yokoyama T

更新日期：2008-07-01 00:00:00

abstract：:Early detection and diagnosis of neurodegenerative diseases has been hampered by the lack of sensitive testing. Real-time quaking induced conversion (RT-QuIC) has been used for the early and sensitive detection of prion-induced neurologic disease, and has more recently been adapted to detect misfolded alpha-synuclein ...

journal_title：Prion

authors： Tennant JM,Henderson DM,Wisniewski TM,Hoover EA

更新日期：2020-12-01 00:00:00

abstract：:The normal function of PrPC, the cellular prion protein, has remained mysterious since its first description over 30 years ago. Amazingly, although complete deletion of the gene encoding PrPC has little phenotypic consequence, expression in transgenic mice of PrP molecules carrying certain internal deletions produces ...

journal_title：Prion

authors： McDonald AJ,Wu B,Harris DA

更新日期：2017-11-02 00:00:00

abstract：:We report here on the proceedings of the Global Alzheimer Summit that took place September 22-23, 2011 in Madrid, Spain. As Alzheimer disease (AD) is the leading cause of neurodegeneration in elderly individuals and as yet has no effective therapeutic option, it continues to stimulate global research interests. At the...

journal_title：Prion

authors： Gonsalves D,Jovanovic K,Da Costa Dias B,Weiss SF

更新日期：2012-01-01 00:00:00

abstract：:The evolutionary origins of vertebrate prion genes had remained elusive until recently when multiple lines of evidence converged to the proposition that members of the prion gene family represent an ancient branch of a larger family of ZIP metal ion transporters. (1) A follow-up investigation which explored the mechan...

journal_title：Prion

authors： Ehsani S,Mehrabian M,Pocanschi CL,Schmitt-Ulms G

更新日期：2012-09-01 00:00:00

abstract：:Here, we report a Chinese case of Creutzfeldt-Jakob disease (CJD) with a rare mutation in the prion protein gene (PRNP) leading to an exchange of amino acid from valine (Val) to isoleucine (I) at codon 203 (V203I). The 80-y-old male presented with sudden memory loss, rapid loss of vocabulary, inattention and slow resp...

journal_title：Prion

authors： Shi Q,Chen C,Wang XJ,Zhou W,Wang JC,Zhang BY,Gao C,Gao C,Han J,Dong XP

更新日期：2013-05-01 00:00:00

abstract：:The aggregation of a soluble protein into insoluble, beta-sheet rich amyloid fibrils is a defining characteristic of many neurodegenerative diseases, including prion disorders. The prion protein has so far been considered unique because of its infectious nature. Recent investigations, however, suggest that other amylo...

journal_title：Prion

authors： Frost B,Diamond MI

更新日期：2009-04-01 00:00:00

abstract：:The description of prions as causal agents of Transmissible Spongiform Encephalopathies (TSE), is nowadays accepted as an important breakthrough in biology as revealed the existence of a completely new group of pathogens and a new way of transmission for biological information. A common feature of many neurodegenerati...

journal_title：Prion

authors： Eraña H

更新日期：2019-01-01 00:00:00

abstract：:The prion paradigm is increasingly invoked to explain the molecular pathogenesis of neurodegenerative diseases involving the misfolding and aggregation of proteins other than the prion protein (PrP). Extensive evidence from in vitro and in vivo studies indicates that misfolded and aggregated Aβ peptide, which is the p...

journal_title：Prion

authors： Rasmussen J,Jucker M,Walker LC

更新日期：2017-07-04 00:00:00

abstract：:Bovine spongiform encephalopathy (BSE) created a global European crisis in the 1980s and 90s, with very serious health and economic implications. Classical BSE now appears to be under control, to a great extent as a result of a global research effort that identified the sources of prions in meat and bone meal (MBM) an...

journal_title：Prion

authors： Requena JR,Kristensson K,Korth C,Zurzolo C,Simmons M,Aguilar-Calvo P,Aguzzi A,Andreoletti O,Benestad SL,Böhm R,Brown K,Calgua B,Del Río JA,Espinosa JC,Girones R,Godsave S,Hoelzle LE,Knittler MR,Kuhn F,Legname G,La

更新日期：2016-05-03 00:00:00

abstract：:Transmissible spongiform encephalopathies (TSEs) are a group of lethal neurodegenerative diseases involving the structural conversion of cellular prion protein (PrPC) into the pathogenic isoform (PrPSc) for which no effective treatment is currently available. Previous studies have implicated that a polymeric molecule ...

journal_title：Prion

authors： Honda R,Yamaguchi KI,Elhelaly AE,Fuji M,Kuwata K

更新日期：2018-01-01 00:00:00

abstract：:Each known abnormal prion protein (PrP (Sc) ) is considered to have a specific range and therefore the ability to infect some species and not others. Consequently, some species have been assumed to be prion disease resistant as no successful natural or experimental challenge infections have been reported. This assumpt...

journal_title：Prion

authors： Fernández-Borges N,Chianini F,Eraña H,Vidal E,Eaton SL,Pintado B,Finlayson J,Dagleish MP,Castilla J

更新日期：2012-11-01 00:00:00

abstract：:A variety of signaling pathways, in particular with roles in cell fate and host defense, operate by a prion-like mechanism consisting in the formation of open-ended oligomeric signaling complexes termed signalosomes. This mechanism emerges as a novel paradigm in signal transduction. Among the proteins forming such sig...

journal_title：Prion

authors： Daskalov A,Saupe SJ

更新日期：2015-01-01 00:00:00

abstract：:Amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) are clinically overlapping neurodegenerative disorders whose pathophysiology remains incompletely understood. ALS initiates in a discrete location, and typically progresses in a pattern consistent with spread of the degenerative process t...

journal_title：Prion

authors： Udan M,Baloh RH

更新日期：2011-01-01 00:00:00

abstract：:Many laboratory studies and epidemiological observations confirm that nematodes prevent some immune-mediated diseases. The development of immunologically well-defined laboratory models of intestinal nematode infection has allowed significant advances to be made in understanding the immunological basis of effector mech...

journal_title：Prion

authors： Donskow-Łysoniewska K,Brodaczewska K,Doligalska M

更新日期：2013-07-01 00:00:00

abstract：:Prion diseases are infectious conformational diseases. Despite the determination of many native prion protein (PrP) structures and in vitro production of infectious prions from recombinant PrP the structural background of PrP conversion remains the largest unsolved problem. The aggregated state of PrP (Sc) makes it in...

journal_title：Prion

authors： Hafner-Bratkovič I,Jerala R

更新日期：2011-04-01 00:00:00

abstract：:Conversion of native cellular prion protein (PrPc) from an α-helical structure to a toxic and infectious β-sheet structure (PrPSc) is a critical step in the development of prion disease. There are some indications that the formation of PrPSc is preceded by a β-sheet rich PrP (PrPβ) form which is non-infectious, but is...

journal_title：Prion

authors： Ladner-Keay CL,LeVatte M,Wishart DS

更新日期：2016-11-01 00:00:00

abstract：:Modified nucleosides in tRNA anticodon loops such as 5-methoxy-carbonyl-methyl-2-thiouridine (mcm5s2U) and pseuduridine (Ψ) are thought to be required for an efficient decoding process. In Saccharomyces cerevisiae, the simultaneous presence of mcm5s2U and Ψ38 in tRNAGlnUUG was shown to mediate efficient synthesis of t...

journal_title：Prion

authors： Schaffrath R,Klassen R

更新日期：2017-01-02 00:00:00

abstract：:Proteins with expanded polyglutamine (polyQ) regions are prone to form amyloids, which can cause diseases in humans and toxicity in yeast. Recently, we showed that in yeast non-toxic amyloids of Q-rich proteins can induce aggregation and toxicity of wild type huntingtin (Htt) with a short non-pathogenic polyglutamine ...

journal_title：Prion

authors： Alexandrov AI,Serpionov GV,Kushnirov VV,Ter-Avanesyan MD

更新日期：2016-05-03 00:00:00

abstract：:The objectives of this study were to test whether recombinant mouse (mo)PrP alone or in combination with LPS or under simulated endotoxemia would affect expression of genes related to host inflammatory and antimicrobial responses. To test our hypotheses colon tissues were collected from 16 male mice (FVB/N strain) and...

journal_title：Prion

authors： Dervishi E,Lam TH,Dunn SM,Zwierzchowski G,Saleem F,Wishart DS,Ametaj BN

更新日期：2015-01-01 00:00:00

abstract：:Prions are self-propagating infectious protein aggregates of mammals and fungi. The exact mechanism of prion formation is poorly understood. In a recent study, a comparative analysis of the aggregation propensities of chimeric proteins derived from the yeast Sup35p and mouse PrP prion proteins was performed in neurobl...

journal_title：Prion

authors： Krammer C,Kremmer E,Schätzl HM,Vorberg I

更新日期：2008-07-01 00:00:00

abstract：:Among different types of protein aggregation, amyloids are a biochemically well characterized state of protein aggregation that are associated with a large number of neurodegenerative diseases including Parkinson's disease, Alzheimer and Creutzfeldt-Jakob disease. Yeast, Saccharomyces cerevisiae is an insightful model...

journal_title：Prion

authors： Aslam K,Hazbun TR

更新日期：2016-03-03 00:00:00

abstract：:Transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative diseases caused by the misfolding of the cellular prion protein to an infectious form PrP(Sc). The intercellular transfer of PrP(Sc) is a question of immediate interest as the cell-to-cell movement of the infectious particle causes the i...

journal_title：Prion

authors： Zhu S,Victoria GS,Marzo L,Ghosh R,Zurzolo C

更新日期：2015-01-01 00:00:00

abstract：:The yeast prion [PSI(+)] represents an aggregated state of the translational release factor Sup35 (eRF3) and deprives termination complexes of functional Sup35, resulting in nonsense codon suppression. Protein-remodeling factor Hsp104 is involved in thermotolerance and [PSI(+)] propagation, however the structure-and-f...

journal_title：Prion

authors： Takahashi A,Hara H,Kurahashi H,Nakamura Y

更新日期：2007-01-01 00:00:00

abstract：:In most human and animal prion diseases the abnormal disease-associated prion protein (PrPSc) is deposited as non-amyloid aggregates in CNS, spleen and lymphoid organs. In contrast, in humans and transgenic mice with PrP mutations which cause expression of PrP lacking a glycosylphosphatidylinositol (GPI)-anchor, most ...

journal_title：Prion

authors： Race B,Jeffrey M,McGovern G,Dorward D,Chesebro B

更新日期：2017-07-04 00:00:00

abstract：:TDP-43 and FUS are DNA/RNA binding proteins associated with neuronal inclusions in amyotrophic lateral sclerosis (ALS) patients. Other neurodegenerative diseases are also characterized by neuronal protein aggregates, e.g. Huntington's disease, associated with polyglutamine (polyQ) expansions in the protein huntingtin....

journal_title：Prion

authors： Park SK,Arslan F,Kanneganti V,Barmada SJ,Purushothaman P,Verma SC,Liebman SW

更新日期：2018-01-02 00:00:00