RT-QuIC detection of tauopathies using full-length tau substrates.

abstract：:We propose models for in vitro grown mammalian prion protein fibrils based upon left handed beta helices formed both from the N-terminal and C-terminal regions of the proteinase resistant infectious prion core. The C-terminal threading onto a beta-helical structure is almost uniquely determined by fixing the cysteine ...

journal_title：Prion

authors： Kunes KC,Clark SC,Cox DL,Singh RR

更新日期：2008-04-01 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：:M2B cells with persistent classical bovine spongiform encephalopathy (C-BSE) have been established previously. In this study, we performed strain characterization of the M2B cell line in bovine PrPC overexpressing mice (Tg 1896). Mice intracranially inoculated with M2B cells and C-BSE survived for 451 ± 7 and 465 ± 31...

journal_title：Prion

authors： Suh TY,Roh IS,Kim HJ,Griffiths PC,Park KJ,Park HC,Hope J,Kang HE,Kim DY,Sohn HJ

更新日期：2017-11-02 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：:Perturbations of calcium homeostasis have been associated with several neurodegenerative disorders. A common polymorphism (rs2986017) in the CALHM1 gene, coding for a regulator of calcium homeostasis, is a genetic risk factor for the development of Alzheimer disease (AD). Although some authors failed to confirm these ...

journal_title：Prion

authors： Calero O,Bullido MJ,Clarimón J,Hortigüela R,Frank-García A,Martínez-Martín P,Lleó A,Rey MJ,Sastre I,Rábano A,de Pedro-Cuesta J,Ferrer I,Calero M

更新日期：2012-09-01 00:00:00

abstract：:The pathogenic mechanism of prion diseases remains unknown. We recently reported that prion infection disturbs post-Golgi trafficking of certain types of membrane proteins to the cell surface, resulting in reduced surface expression of membrane proteins and abrogating the signal from the proteins. The surface expressi...

journal_title：Prion

authors： Uchiyama K,Miyata H,Sakaguchi S

更新日期：2013-11-01 00:00:00

abstract：:Studies of the ovine prion-related protein (testis-specific) gene (PRNT), including studies of genetic diversity, have highlighted its potential relationship to scrapie infection and economically important ovine traits. PRNT was previously reported to be highly polymorphic in Portuguese sheep. To characterize genetic ...

journal_title：Prion

authors： Li J,Zhang S,Erdenee S,Sun X,Dang R,Huang Y,Lei C,Chen H,Xu H,Cai Y,Lan X

更新日期：2018-01-01 00:00:00

abstract：:Many neurodegenerative disorders share common features including the accumulation of aggregated misfolded proteins, neuroinflammation and the induction of apoptosis. While the contributions of each of these individual elements to neuronal death remain unclear, a commonly used antibiotic, minocycline, has been shown to...

journal_title：Prion

authors： Noble W,Garwood CJ,Hanger DP

更新日期：2009-04-01 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：: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：: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：: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：: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：: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：:Shadoo (Sho) is a brain glycoprotein with similarities to the unstructured region of PrP (C) . Frameshift alleles of the Sho gene, Sprn, are reported in variant Creutzfeldt-Jakob disease (vCJD) patients while Sprn mRNA knockdown in PrP-null (Prnp(0/0) ) embryos produces lethality, advancing Sho as the hypothetical PrP...

journal_title：Prion

authors： Daude N,Westaway D

更新日期：2012-11-01 00:00:00

abstract：:Growing evidence indicates that astrocytes cannot be just considered as passive supportive cells deputed to preserve neuronal activity and survival, but rather they are involved in a striking number of active functions that are critical to the performance of the central nervous system (CNS). As a consequence, it is be...

journal_title：Prion

authors： Brambilla L,Martorana F,Rossi D

更新日期：2013-01-01 00:00:00

abstract：OBJECTIVE:To evaluate whether EPC-MVs could promote bone regeneration by directly regulating osteoblast through miR-126. The underlying mechanisms were also explored. METHODS:EPCs were isolated from bone marrow mononuclear cells. EPC-MVs were collected from EPCs cultured medium. The lentivirus was used to induce miR-1...

journal_title：Prion

authors： Chen G,Li P,Liu Z,Zeng R,Ma X,Chen Y,Xu H,Li Z,Lin H

更新日期：2019-01-01 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：:Prions are infectious, self-propagating protein conformations. [PSI+], [RNQ+] and [URE3] are well characterized prions in Saccharomyces cerevisiae and represent the aggregated states of the translation termination factor Sup35, a functionally unknown protein Rnq1, and a regulator of nitrogen metabolism Ure2, respectiv...

journal_title：Prion

authors： Kurahashi H,Oishi K,Nakamura Y

更新日期：2011-10-01 00:00:00

abstract：:Yeast have been extensively used to model aspects of protein folding diseases, yielding novel mechanistic insights and identifying promising candidate therapeutic targets. In particular, the neurodegenerative disorder Huntington disease (HD), which is caused by the abnormal expansion of a polyglutamine tract in the hu...

journal_title：Prion

authors： Mason RP,Giorgini F

更新日期：2011-10-01 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：:Prions are responsible for a heterogeneous group of fatal neurodegenerative diseases. They can be sporadic, genetic, or infectious disorders involving post-translational modifications of the cellular prion protein (PrP(C)). Prions (PrP(Sc)) are characterized by their infectious property and intrinsic ability to conver...

journal_title：Prion

authors： Benetti F,Legname G

更新日期：2009-10-01 00:00:00

abstract：:Mammalian prions are composed of misfolded aggregated prion protein (PrP) with amyloid-like features. Prions are zoonotic disease agents that infect a wide variety of mammalian species including humans. Mammals and by-products thereof which are frequently encountered in daily life are most important for human health. ...

journal_title：Prion

authors： Hammarström P,Nyström S

更新日期：2015-01-01 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：:Prion and Alzheimer diseases are fatal neurodegenerative diseases caused by misfolding and aggregation of the cellular prion protein (PrP(C)) and the β-amyloid peptide, respectively. Soluble oligomeric species rather than large aggregates are now believed to be neurotoxic. PrP(C) undergoes three proteolytic cleavages ...

journal_title：Prion

authors： Béland M,Roucou X

更新日期：2014-01-01 00:00:00

abstract：:Prion diseases are subacute neurodegenerative diseases that affect humans and a range of domestic and free-ranging animal species. These diseases are characterized by the accumulation of PrP (Sc), an abnormally folded isoform of the cellular prion protein (PrP (C)), in affected tissues. The pathology during prion dise...

journal_title：Prion

authors： Mabbott NA

更新日期：2012-09-01 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：:The molecular chaperone network plays a critical role in the formation and propagation of self-replicating yeast prions. Not only do individual prions differ in their requirements for certain chaperones, but structural variants of the same prion can also display distinct dependences on the chaperone machinery, specifi...

journal_title：Prion

authors： Dulle JE,True HL

更新日期：2013-09-01 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：:In Transmissible Spongiform Encephalopathies (TSEs) and Alzheimer disease (AD) both misfolding and aggregation of specific proteins represent key features. Recently, it was observed that PrP (c) is a mediator of a synaptic dysfunction induced by Aβ oligomers. We tested a novel γ secretase modulator (CHF5074) in a mur...

journal_title：Prion

authors： Poli G,Corda E,Lucchini B,Puricelli M,Martino PA,Dall'ara P,Villetti G,Bareggi SR,Corona C,Vallino Costassa E,Gazzuola P,Iulini B,Mazza M,Acutis P,Mantegazza P,Casalone C,Imbimbo BP

更新日期：2012-01-01 00:00:00