On the reactive states of astrocytes in prion diseases.

abstract：:The prion infection is a conversion of host encoded prion protein (PrP) from its cellular isoform PrP(C) into the pathological and infectious isoform PrP(Sc); the conversion process was investigated by in vitro studies using recombinant and cellular PrP and natural PrP(Sc). We present a brief summary of the results de...

journal_title：Prion

authors： Birkmann E,Riesner D

更新日期：2008-04-01 00:00:00

abstract：:Prion protein (PrP)-like molecule, doppel (Dpl), is neurotoxic in mice, causing Purkinje cell degeneration. In contrast, PrP antagonizes Dpl in trans, rescuing mice from Purkinje cell death. We have previously shown that PrP with deletion of the N-terminal residues 23-88 failed to neutralize Dpl in mice, indicating th...

journal_title：Prion

authors： Sakaguchi S

更新日期：2008-07-01 00:00:00

abstract：:A simple diagnostic test is described for the detection of TSE in bovine, ovine and human brain and lymphoid tissue that obviates the use of proteinase K as a discriminating reagent. The immunoassay utilises high affinity anti-peptide antibodies that appear blind to the normal isoform of prion protein (PrP(C)). These ...

journal_title：Prion

authors： Barnard G,Hopkins L,Moorthie S,Seilly D,Tonks P,Dabaghian R,Clewley J,Coward J,McConnell I

更新日期：2007-04-01 00:00:00

abstract：:In yeast Saccharomyces cerevisiae translation termination factors eRF1 (Sup45) and eRF3 (Sup35) are encoded by the essential genes SUP45 and SUP35 respectively. Heritable aggregation of Sup35 results in formation of the yeast prion [PSI(+)]. It is known that combination of [PSI(+)] with some mutant alleles of the SUP3...

journal_title：Prion

authors： Kiktev D,Vechtomov SI,Zhouravleva G

更新日期：2007-04-01 00:00:00

abstract：:Prions are infectious proteins. In fungi, prions correspond to non-Mendelian genetic elements whose mode of inheritance has long eluded explanation. The [Het-s] cytoplasmic genetic element of the filamentous fungus Podospora anserina, was originally identified in 1952 and recognized as a prion nearly half a century la...

journal_title：Prion

authors： Saupe SJ

更新日期：2007-04-01 00:00:00

abstract：:The common feature of many neurodegenerative diseases is emergence of protein aggregates. Identifying their composition can provide valuable insights into the cellular mechanisms of protein aggregation and neuronal death. No reliable method for identification of the aggregate-associated proteins has been available. He...

journal_title：Prion

authors： Wang Y,Meriin AB,Costello CE,Sherman MY

更新日期：2007-04-01 00:00:00

abstract：:Amyloid deposition is one of the central neuropathological abnormalities in Alzheimer's disease (AD) but it also takes places in many neurodegenerative diseases such as prionic disorders, Huntington's disease (HD) and others. Up to very recently amyloid formation was considered a very slow process of deposition of an ...

journal_title：Prion

authors： Mena MA,Rodríguez-Navarro JA,de Yébenes JG

更新日期：2009-01-01 00:00:00

abstract：:The structural organization of the amyloidogenic beta-protein containing 40 amino acid residues (Abeta40) was studied by the high temperature molecular dynamics simulations in the acidic (pH approximately 3) and basic (pH approximately 8) pH regions. The obtained data suggest that the central Ala21-Gly29 segment of Ab...

journal_title：Prion

authors： Rubinstein A,Lyubchenko YL,Sherman S

更新日期：2009-01-01 00:00:00

abstract：:The self-association of misfolded or damaged proteins into ordered amyloid-like aggregates characterizes numerous neurodegenerative disorders. Insoluble amyloid plaques are diagnostic of many disease states. Yet soluble, oligomeric intermediates in the aggregation pathway appear to represent the toxic culprit. Molecul...

journal_title：Prion

authors： Douglas PM,Summers DW,Cyr DM

更新日期：2009-04-01 00:00:00

abstract：:The discovery of tunnelling nanotubes (TNTs) and their proposed role in long intercellular transport of organelles, bacteria and viruses have led us to examine their potential role during prion spreading. We have recently shown that these membrane bridges can form between neuronal cells, as well as between dendritic c...

journal_title：Prion

authors： Gousset K,Zurzolo C

更新日期：2009-04-01 00:00:00

abstract：:The host encoded cellular prion protein (PrP(C)) is an N-linked glycoprotein tethered to the cell membrane by a glycophosphatidylinositol (GPI) anchor. Under certain conditions, PrP(C) can undergo conversion into a conformationally-altered isoform (PrP(Sc)) widely believed to be the pathogenic agent of transmissible s...

journal_title：Prion

authors： Peralta OA,Eyestone WH

更新日期：2009-07-01 00:00:00

abstract：:The prion hypothesis states that the prion and non-prion form of a protein differ only in their 3D conformation and that different strains of a prion differ by their 3D structure. Recent technical developments have enabled solid-state NMR to address the atomic-resolution structures of full-length prions, and a first c...

journal_title：Prion

authors： Böckmann A,Meier BH

更新日期：2010-04-01 00:00:00

abstract：:Neurodegenerative diseases are caused by proteinaceous aggregates, usually consisting of misfolded proteins which are often typified by a high proportion of β-sheets, which accumulate in the Central Nervous System. These diseases, including Morbus Alzheimer, Parkinson disease and Transmissible Spongiform Encephalopath...

journal_title：Prion

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

更新日期：2011-01-01 00:00:00

abstract：:Amyloid fibrils share a structural motif consisting of highly ordered β-sheets aligned perpendicular to the fibril axis ( 1, 2) . At each fibril end, β-sheets provide a template for recruiting and converting monomers ( 3) . Various amyloid fibrils often occur in the same individual, yet whether distinct protein aggreg...

journal_title：Prion

authors： Sigurdson CJ,Bartz JC,Nilsson KP

更新日期：2011-04-01 00:00:00

abstract：:Over the last decade remarkable advances in genotyping and sequencing technology have resulted in hundreds of novel gene associations with disease. These have typically involved high frequency alleles in common diseases and with the advent of next generation sequencing, disease causing recessive mutations in rare inhe...

journal_title：Prion

authors： Lukic A,Mead S

更新日期：2011-07-01 00:00:00

abstract：:The [PSI+] determinant in Saccharomyces cerevisiae is the prion protein corresponding to the eRF3 translation termination factor. Numerous infectious proteins have been described in yeast, in comparison of the unique PrP protein in higher eukaryotes. The presence of the PrP prion is associated with mammalian diseases....

journal_title：Prion

authors： Baudin-Baillieu A,Fabret C,Namy O

更新日期：2011-10-01 00:00:00

abstract：:The ability of abnormal TSE-associated forms of PrP to seed the formation of amyloid fibrils from recombinant PrP(Sen) has served as the basis for several relatively rapid and highly sensitive tests for prion diseases. These tests include rPrP-PMCA (rPMCA), standard quaking-induced conversion (S-QuIC), amyloid seeding...

journal_title：Prion

authors： Orrù CD,Wilham JM,Vascellari S,Hughson AG,Caughey B

更新日期：2012-04-01 00:00:00

abstract：:The oral route is considered to be the main entry site of several transmissible spongiform encephalopathies or prion diseases of animals and man. Following natural and experimental oral exposure to scrapie, sheep first accumulate disease associated prion protein (PrP (d) ) in Peyer's patch (PP) lymphoid follicles. In ...

journal_title：Prion

authors： Piercey Åkesson C,Press CM,Tranulis MA,Jeffrey M,Aleksandersen M,Landsverk T,Espenes A

更新日期：2012-07-01 00:00:00

abstract：:The conversion to a disease-associated conformer (PrP(Sc)) of the cellular prion protein (PrP(C)) is the central event in prion diseases. Wild-type PrPC converts to PrP(Sc) in the sporadic forms of the disorders through an unknown mechanism. These forms account for up to 85% of all human (Hu) occurrences; the infectio...

journal_title：Prion

authors： Legname G

更新日期：2012-01-01 00:00:00

abstract：:Most prions in yeast form amyloid fibrils that must be severed by the protein disaggregase Hsp104 to be propagated and transmitted efficiently to newly formed buds. Only one yeast prion, [PSI (+) ], is cured by Hsp104 overexpression. We investigated the interaction between Hsp104 and Sup35, the priongenic protein in y...

journal_title：Prion

authors： Helsen CW,Glover JR

更新日期：2012-07-01 00:00:00

abstract：:The Creutzfeldt-Jakob Disease (CJD) Foundation was formed in 1993 in Miami, Florida by two women who each lost a loved one to this terrible disease. They were instrumental in designing the Foundation's mission, which stresses a strong dedication to providing support and information to all affected families who turn to...

journal_title：Prion

authors： Kranitz F

更新日期：2012-04-01 00:00:00

abstract：:The concept of "prion-like" has been proposed to explain the pathogenic mechanism of the principal neurodegenerative disorders associated with protein misfolding, including Alzheimer disease (AD). Other evidence relates prion protein with AD: the cellular prion protein (PrP(C)) binds β amyloid oligomers, allegedly res...

journal_title：Prion

authors： Forloni G,Sclip A,Borsello T,Balducci C

更新日期：2013-01-01 00:00:00

abstract：:PrP (C) is associated with a variety of functions, and its ability to interact with a multitude of partners, including itself, may largely explain PrP multifunctionality and the lack of consensus on the genuine physiological function of the protein in vivo. In contrast, there is a consensus in the literature that alte...

journal_title：Prion

authors： Béland M,Roucou X

更新日期：2013-03-01 00:00:00

abstract：:Yeast prions are infectious proteins that spread exclusively by mating. The frequency of prions in the wild therefore largely reflects the rate of spread by mating counterbalanced by prion growth slowing effects in the host. We recently showed that the frequency of outcross mating is about 1% of mitotic doublings with...

journal_title：Prion

authors： Kelly AC,Wickner RB

更新日期：2013-05-01 00:00:00

abstract：:Central to understanding the nature TSE agents (or prions) is how their genetic information is distinguished from the host. Are TSEs truly infectious diseases with host-independent genomes, or are they aberrations of a host component derived from the host genome? Recent experiments tested whether glycosylation of host...

journal_title：Prion

authors： Somerville RA

更新日期：2013-07-01 00:00:00

abstract：:Alzheimer disease is associated with the accumulation of oligomeric amyloid β peptide (Aβ), accompanied by synaptic dysfunction and neuronal death. Polymeric form of prion protein (PrP), PrP(Sc), is implicated in transmissible spongiform encephalopathies (TSEs). Recently, it was shown that the monomeric cellular form ...

journal_title：Prion

authors： Rubel AA,Ryzhova TA,Antonets KS,Chernoff YO,Galkin A

更新日期：2013-11-01 00:00:00

abstract：:A sample of purified Syrian hamster PrP27-30 prion fibers was analyzed by synchrotron small-angle X-ray scattering (SAXS). The SAXS pattern obtained was fitted to a model based on infinitely long cylinders with a log-normal intensity distribution, a hard-sphere structure factor and a general Porod term for larger aggr...

journal_title：Prion

authors： Amenitsch H,Benetti F,Ramos A,Legname G,Requena JR

更新日期：2013-11-01 00:00:00

abstract：:The co-existence of certain peptides influenced the kinetic rate of aggregation and the lag-time of fibril formation of rbPrP. Using recently developed structural conversion assay system, peptides have been screened from bovine brain peptide library. Peptide sequences of positive components have been elucidated by mas...

journal_title：Prion

authors： Nokihara K,Yajima S,Hirata A

更新日期：2014-01-01 00:00:00

abstract：:One fundamental property of prions is the formation of strains-prions that have distinct biological effects, despite a common amino acid sequence. The strain phenomenon is thought to be caused by the formation of different molecular structures, each encoding for a particular biological activity. While the precise mech...

journal_title：Prion

authors： Wan W,Stubbs G

更新日期：2014-03-01 00:00:00

abstract：:Prion diseases are infectious and inevitably fatal neurodegenerative diseases characterized by prion replication, widespread protein aggregation and spongiform degeneration of major brain regions controlling motor function. Oxidative stress has been implicated in prion-related neuronal degeneration, but the molecular ...

journal_title：Prion

authors： Harischandra DS,Kondru N,Martin DP,Kanthasamy A,Jin H,Anantharam V,Kanthasamy AG

更新日期：2014-01-01 00:00:00