Long-term preservation of pharyngeal swallowing function in MM2-cortical-type sporadic Creutzfeldt-Jakob disease.

abstract：:In the past decade, the interaction between prions and nucleic acids has garnered significant attention from the scientific community. for many years, the participation of RNA and/or DNA in prion pathology has been largely ruled out by the "protein-only" hypothesis, but this is now being reconsidered. Experimental dat...

journal_title：Prion

authors： Gomes MP,Cordeiro Y,Silva JL

更新日期：2008-04-01 00:00:00

abstract：:The structure and the dissociation reaction of oligomers Pr(Poligo) from reduced human prion huPrP(C)(23-231) have been studied by (1)H-NMR and tryptophan fluorescence spectroscopy at varying pressure, along with circular dichroism and atomic force microscopy. The 1H-NMR and fluorescence spectral feature of the oligom...

journal_title：Prion

authors： Sasaki K,Gaikwad J,Hashiguchi S,Kubota T,Sugimura K,Kremer W,Kalbitzer HR,Akasaka K

更新日期：2008-07-01 00:00:00

abstract：:This review will first recall the phenomena of "cortical inheritance" observed and genetically demonstrated in Paramecium 40 years ago, and later in other ciliates (Tetrahymena, Oxytricha, Paraurostyla), and will analyze the deduced concept of "cytotaxis" or "structural memory." The significance of these phenomena, al...

journal_title：Prion

authors： Beisson J

更新日期：2008-01-01 00:00:00

abstract：:The rate of spontaneous change from psi(-) to the psi(+) condition, determined in yeast by states of the Sup35p protein, is briefly discussed together with the conditions necessary for such change to occur. Conditions that promote and which affect the rate of induction of psi(+) in Sup35p and of other prion-forming pr...

journal_title：Prion

authors： Cox BS,Byrne LJ,Tuite MF

更新日期：2007-07-01 00:00:00

abstract：:A dysfunction in copper homeostasis seems to occur in Alzheimer's disease (AD). We recently demonstrated that an excess of non-ceruloplasmin-copper (i.e., 'free' copper) correlates with the main functional and anatomical deficits as well as the cerebrospinal markers of the disease, thus suggesting that copper contribu...

journal_title：Prion

authors： Squitti R,Quattrocchi CC,Salustri C,Rossini PM

更新日期：2008-01-01 00:00:00

abstract：:There is strong evidence that the oligomers of key proteins, formed during the early steps of aggregation, could be the primary toxic species associated with human neuro-degenerative diseases, such as Alzheimer's and prion diseases. Here, we review recent progress in the development of computational approaches in orde...

journal_title：Prion

authors： Wei G,Mousseau N,Derreumaux P

更新日期：2007-01-01 00:00:00

abstract：:Our laboratory recently reported a novel prion [SWI+], in the budding yeast Saccharomyces cerevisiae. [SWI+] is the prion form of Swi1, a component of the SWI/SNF chromatin-remodeling complex. Cells harboring [SWI+] exhibit a partial loss-of-function phenotype for SWI/SNF, which can be easily assayed by poor growth on...

journal_title：Prion

authors： Crow E,Du Z,Li L

更新日期：2008-10-01 00:00:00

abstract：:The formation and maintenance of prions in the yeast Saccharomyces cerevisiae is highly regulated by the cellular chaperone machinery. The most important player in this regulation is Hsp104p, which is required for the maintenance of all known prions. The requirements for other chaperones, such as members of the Hsp40 ...

journal_title：Prion

authors： Bardill JP,Dulle JE,Fisher JR,True HL

更新日期：2009-07-01 00:00:00

abstract：:Our laboratory recently reported the identification of a peptide region, QVNI, within the prion domain of the yeast protein Ure2 that may act as an initiation point for fibril formation.(1) This potential amyloid-forming region, which corresponds to residues 18-21 of Ure2, was initially identified by systematic cystei...

journal_title：Prion

authors： Fei L,Perrett S

更新日期：2010-01-01 00:00:00

abstract：:It has been estimated that cerebrospinal fluid (CSF) contains approximately 80 proteins that significantly increase or decrease in response to various clinical conditions. Here we have evaluated the CSF protein PrP(C) (cellular prion protein) for possible increases or decreases following spinal cord injury. The physio...

journal_title：Prion

authors： Carnini A,Casha S,Yong VW,Hurlbert RJ,Braun JE

更新日期：2010-04-01 00:00:00

abstract：:Prion diseases are neurodegenerative conditions caused by the transconformation of a normal host glycoprotein, the cellular prion protein (PrPc) into a neurotoxic, self-aggregating conformer (PrPSc). TSEs are ineluctably fatal and no treatment is yet available. In principle, prion diseases could be attacked from diffe...

journal_title：Prion

authors： Carnaud C,Bachy V

更新日期：2010-04-01 00:00:00

abstract：:Misfolding and aggregation of prion proteins is linked to a number of neurodegenerative disorders such as Creutzfeldt-Jacob disease (CJD) and its variants: Kuru, Gerstmann-Straussler-Scheinker syndrome and fatal familial insomnia. In prion diseases, infectious particles are proteins that propagate by transmitting a mi...

journal_title：Prion

authors： Krasnoslobodtsev AV,Portillo AM,Deckert-Gaudig T,Deckert V,Lyubchenko YL

更新日期：2010-10-01 00:00:00

abstract：:To understand why cross-species infection of prion disease often results in inefficient transmission and reduced protein conversion, most research has focused on defining the effect of variations in PrP primary structures, including sequence compatibility of substrate and seed. By contrast, little research has been ai...

journal_title：Prion

authors： Gill AC,Agarwal S,Pinheiro TJ,Graham JF

更新日期：2010-10-01 00:00:00

abstract：:Several fatal, progressive neurodegenerative diseases, including various prion and prion-like disorders, are connected with the misfolding of specific proteins. These proteins misfold into toxic oligomeric species and a spectrum of distinct self-templating amyloid structures, termed strains. Hence, small molecules tha...

journal_title：Prion

authors： Duennwald ML,Shorter J

更新日期：2010-10-01 00:00:00

abstract：:Evidence is growing at an increasing -pace that amyloid fibers are not just the result of aberrant protein folding associated with neurodegenerative diseases, but are widespread in nature for beneficial reasons. Amyloid is an attractive building material because its robust design and simple repetitive structure make f...

journal_title：Prion

authors： Otzen D

更新日期：2010-10-01 00:00:00

abstract：:The infectious agent of prion diseases is believed to be nucleic acid-free particles composed of misfolded conformational isomers of a host protein known as prion protein (PrP). Although this "protein-only" concept is generally accepted, decades of extensive research have not been able to elucidate the mechanisms by w...

journal_title：Prion

authors： Park KW,Li L

更新日期：2011-01-01 00:00:00

abstract：:Behavioral and neuropathological changes have been widely investigated in murine prion disease but stereological based unbiased estimates of key neuropathological features have not been carried out. After injections of ME7 infected (ME7) or normal brain homogenates (NBH) into dorsal CA1 of albino Swiss mice and C57BL6...

journal_title：Prion

authors： Borner R,Bento-Torres J,Souza DR,Sadala DB,Trevia N,Farias JA,Lins N,Passos A,Quintairos A,Diniz JA,Perry VH,Vasconcelos PF,Cunningham C,Picanço-Diniz CW

更新日期：2011-07-01 00:00:00

abstract：:The formation of fibrillar amyloid is most often associated with protein conformational disorders such as prion diseases, Alzheimer disease and Huntington disease. Interestingly, however, an increasing number of studies suggest that amyloid structures can sometimes play a functional role in normal biology. Several pro...

journal_title：Prion

authors： Stein KC,True HL

更新日期：2011-10-01 00:00:00

abstract：:Prion diseases exhibit different disease phenotypes in their natural hosts and when transmitted to rodents, and this variability is regarded as indicative of prion strain diversity. Phenotypic characterization of scrapie strains in sheep can be attempted by histological, immunohistochemical and biochemical approaches,...

journal_title：Prion

authors： Sisó S,Chianini F,Eaton SL,Witz J,Hamilton S,Martin S,Finlayson J,Pang Y,Stewart P,Steele P,Dagleish MP,Goldmann W,Reid HW,Jeffrey M,González L

更新日期：2012-04-01 00:00:00

abstract：:For several different proteins an apparent correlation has been observed between the propensity for dimerization by domain-swapping and the ability to aggregate into amyloid-like fibrils. Examples include the disease-related proteins β 2-microglobulin and transthyretin. This has led to proposals that the amyloid-forma...

journal_title：Prion

authors： van der Wel PC

更新日期：2012-07-01 00:00:00

abstract：:Prion diseases comprise a group of rapidly progressive and invariably fatal neurodegenerative disorders for which there are no effective treatments. While conversion of the cellular prion protein (PrP(C)) to a β-sheet rich isoform (PrP(Sc) ) is known to be a critical event in propagation of infectious prions, the iden...

journal_title：Prion

authors： Solomon IH,Biasini E,Harris DA

更新日期：2012-01-01 00:00:00

abstract：:Aggregation-prone proteins associated with neurodegenerative disease, such as α synuclein and β amyloid, now appear to share key prion-like features with mammalian prion protein, such as the ability to recruit normal proteins to aggregates and to translocate between neurons. These features may shed light on the genesi...

journal_title：Prion

authors： Hall GF,Patuto BA

更新日期：2012-07-01 00:00:00

abstract：:Aberrant activation of Cdk5 has been implicated in the process of neurodegenerative diseases such as Alzheimer's disease (AD). We recently reported that S-nitrosylation of Cdk5 (forming SNO-Cdk5) at specific cysteine residues results in excessive activation of Cdk5, contributing to mitochondrial dysfunction, synaptic ...

journal_title：Prion

authors： Qu J,Nakamura T,Holland EA,McKercher SR,Lipton SA

更新日期：2012-09-01 00:00:00

abstract：:Classical bovine spongiform encephalopathy is a transmissible prion disease that is fatal to cattle and is a human health risk due to its association with a strain of Creutzfeldt-Jakob disease (vCJD). Mutations to the coding region of the prion gene (PRNP) have been associated with susceptibility to transmissible spon...

journal_title：Prion

authors： Thomson JM,Bowles V,Choi JW,Basu U,Meng Y,Stothard P,Moore S

更新日期：2012-11-01 00:00:00

abstract：:Cellular prion protein (PrP (C) ) has attracted considerable attention for its role in transmissible spongiform encephalopathies (TSEs). In spite of being a point of intense research effort critical questions still remain regarding the physiological function of PrP (C) and how these functions may change with the conv...

journal_title：Prion

authors： Arsenault RJ,Li Y,Potter A,Griebel PJ,Kusalik A,Napper S

更新日期：2012-11-01 00:00:00

abstract：:Evidence is now accumulating that damaged proteins are not randomly distributed but often concentrated in microscopically visible and functionally distinct inclusion bodies. How misfolded proteins are organized into these compartments, however, is still unknown. We have recently begun to investigate stress-inducible p...

journal_title：Prion

authors： Alberti S

更新日期：2012-11-01 00:00:00

abstract：:Bovine spongiform encephalopathy (BSE), a member of the prion diseases, is a fatal neurodegenerative disorder suspected to be caused by a malfunction of prion protein (PrP). Although BSE prions have been reported to be transmitted to a wide range of animal species, dogs and hamsters are known to be BSE-resistant anima...

journal_title：Prion

authors： Hasegawa K,Mohri S,Yokoyama T

更新日期：2013-03-01 00:00:00

abstract：:Prion colonization of secondary lymphoid organs (SLOs) is a critical step preceding neuroinvasion in prion pathogenesis. Follicular dendritic cells (FDCs), which depend on both tumor necrosis factor receptor 1 (TNFR1) and lymphotoxin β receptor (LTβR) signaling for maintenance, are thought to be the primary sites of p...

journal_title：Prion

authors： O'Connor T,Aguzzi A

更新日期：2013-03-01 00:00:00

abstract：:Murine prion protein deleted for residues 105-125 is intrinsically neurotoxic and mediates a TSE-like phenotype in transgenic mice. Equivalent and overlapping deletions were expressed in E.coli, purified and analyzed. Among mutants spanning the region 95-135, a construct lacking solely residues 105-125 had distinct pr...

journal_title：Prion

authors： Patel A,Vasiljevic S,Jones IM

更新日期：2013-05-01 00:00:00

abstract：:Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases that are based on the misfolding of a cellular prion protein (PrP(C)) into an infectious, pathological conformation (PrP(Sc)). There is proof-of-principle evidence that a prion vaccine is possible but this is tempered with concerns o...

journal_title：Prion

authors： Madampage CA,Määttänen P,Marciniuk K,Brownlie R,Andrievskaia O,Potter A,Cashman NR,Lee JS,Napper S

更新日期：2013-07-01 00:00:00