The expanding scope of amyloid signalling.

abstract：:In order to obtain RNA aptamers against bovine prion protein (bPrP), we carried out in vitro selection from RNA pools containing a 55-nucleotide randomized region to target recombinant bPrP. Most of obtained aptamers contained conserved GGA tandem repeats (GGA)(4) and aptamer #1 (apt #1) showed a high affinity for bot...

journal_title：Prion

authors： Murakami K,Nishikawa F,Noda K,Yokoyama T,Nishikawa S

更新日期：2008-04-01 00:00:00

abstract：:Concerns over the potential for infectious prion proteins to contaminate human biologics and biotherapeutics have been raised from time to time. Transmission of the pathogenic form of prion protein (PrP(Sc)) through veterinary vaccines has been observed, yet no human case through the use of vaccine products has been r...

journal_title：Prion

authors： LeBrun M,Huang H,Li X

更新日期：2008-01-01 00:00:00

abstract：:Among the diseases caused by protein misfolding is the family associated with the prion protein (PrP). This is a small extracellular membrane-anchored molecule of yet unknown function. Understanding how PrP folds both into its cellular and pathological forms is thought to be crucial for explaining protein misfolding i...

journal_title：Prion

authors： Pastore A,Zagari A

更新日期：2007-07-01 00:00:00

abstract：:We identified the 37kDa/67kDa laminin receptor (LRP/LR) as a cell surface receptor for the cellular prion protein (PrP(c)) and the infectious prion protein (PrP(Sc)). Recently, we showed that anti-LRP/LR antibody W3 cured scrapie infected N2a cells. Here, we demonstrate that W3 delivered by passive immunotransfer into...

journal_title：Prion

authors： Zuber C,Mitteregger G,Pace C,Zerr I,Kretzschmar HA,Weiss S

更新日期：2007-07-01 00:00:00

abstract：:Asymmetric stem cell division is a mechanism widely employed by the cell to maintain tissue homeostasis, resulting in the production of one stem cell and one differentiating cell. However, asymmetric cell division is not limited to stem cells and is widely observed even in unicellular organisms as well as in cells tha...

journal_title：Prion

authors： Yamashita YM

更新日期：2009-04-01 00:00:00

abstract：:The complete molecular characterization of human genetic prion diseases from different backgrounds is important for clinical diagnosis and epidemiological classification. The characterization of the PRNP gene should always include the description of the pathogenic mutation, as well as the status at each allele of the ...

journal_title：Prion

authors： Calero O,Hortigüela R,Albo C,de Pedro-Cuesta J,Calero M

更新日期：2009-07-01 00:00:00

abstract：:Propagation and infectivity of prions in human prionopathies are likely associated with conversion of the mainly alpha-helical human prion protein, HuPrP, into an aggregated form with amyloid-like properties. Previous reports on efficient conversion of recombinant HuPrP have used mild to harsh denaturing conditions to...

journal_title：Prion

authors： Almstedt K,Nyström S,Nilsson KP,Hammarström P

更新日期：2009-10-01 00:00:00

abstract：:Alu DNA elements were long considered to be of no biological significance and thus have been only poorly defined. However, in the past Alu DNA elements with well-defined nucleotide sequences have been suspected to contribute to disease, but the role of Alu DNA element transcripts has rarely been investigated. For the ...

journal_title：Prion

authors： Kiesel P,Gibson TJ,Ciesielczyk B,Bodemer M,Kaup FJ,Bodemer W,Zischler H,Zerr I

更新日期：2010-04-01 00:00:00

abstract：:Understanding the mechanism by which prion infectivity is encoded by the misfolded protein PrP (Sc ) remains a high priority within the prion field. Work from several groups has indicated cellular cofactors may be necessary to form infectious prions in vitro. The identity of endogenous prion conversion cofactors is cu...

journal_title：Prion

authors： Piro JR,Supattapone S

更新日期：2011-04-01 00:00:00

abstract：:The prion protein is a glycoprotein characterized by a folded α-helical structure that, under pathological conditions, misfolds and aggregates into its infectious isoform as β-sheet rich amyloidic deposits. The accumulation of the abnormal protein is responsible for a group of progressive and fatal disorders character...

journal_title：Prion

authors： Natale G,Ferrucci M,Lazzeri G,Paparelli A,Fornai F

更新日期：2011-07-01 00:00:00

abstract：:Amyloid β (Aβ) is a major causative agent of Alzheime disease. This neurotoxic peptide is generated as a result of the cleavage of the Amyloid-Precursor-Protein (APP) by the action of beta secretase and gamma secretase. The neurotoxicity was previously thought to be the result of aggregation. However, recent studies s...

journal_title：Prion

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

更新日期：2011-07-01 00:00:00

abstract：:Prion proteins misfold and aggregate into multiple infectious strain variants that possess unique abilities to overcome prion species barriers, yet the structural basis for the species-specific infectivities of prion strains is poorly understood. Therefore, we have investigated the site-specific structural properties ...

journal_title：Prion

authors： Marcelino-Cruz AM,Bhattacharya M,Anselmo AC,Tessier PM

更新日期：2011-07-01 00:00:00

abstract：:The unexpected discovery of two prions, [URE3] and [PSI+], in Saccharomyces cerevisiae led to questions about how many other proteins could undergo similar prion-based structural conversions. However, [URE3] and [PSI+] were discovered by serendipity in genetic screens. Cataloging the full range of prions in yeast or i...

journal_title：Prion

authors： MacLea KS,Ross ED

更新日期：2011-10-01 00:00:00

abstract：:Prions are infectious proteins with altered conformations converted from otherwise normal host proteins. While there is only one known mammalian prion protein, PrP, a handful of prion proteins have been identified in the yeast Saccharomyces cerevisiae. Yeast prion proteins usually have a defined region called prion do...

journal_title：Prion

authors： Du Z

更新日期：2011-10-01 00:00:00

abstract：:Nanopore analysis is an emerging technique that enables the investigation of the conformation of a single peptide or protein molecule. Briefly, a pore is inserted into a membrane under voltage clamp conditions. When a molecule interacts with the pore there is a change in the current, I, for a time, T. Small unfolded m...

journal_title：Prion

authors： Madampage C,Tavassoly O,Christensen C,Kumari M,Lee JS

更新日期：2012-04-01 00:00:00

abstract：:The prion protein (PrP) sequence of European moose, reindeer, roe deer and fallow deer in Scandinavia has high homology to the PrP sequence of North American cervids. Variants in the European moose PrP sequence were found at amino acid position 109 as K or Q. The 109Q variant is unique in the PrP sequence of vertebrat...

journal_title：Prion

authors： Wik L,Mikko S,Klingeborn M,Stéen M,Simonsson M,Linné T

更新日期：2012-07-01 00:00:00

abstract：:The yeast prion phenomenon is very widespread and mounting evidence suggests that it has an impact on cellular regulatory mechanisms related to phenotypic responses to changing environments. Studying the aggregation patterns of prion amyloids during different stages of the prion life cycle is a first key step to under...

journal_title：Prion

authors： Tyedmers J

更新日期：2012-07-01 00:00:00

abstract：:The prion diseases sheep scrapie and cervid chronic wasting disease are transmitted, in part, via an environmental reservoir of infectivity; prions released from infected animals persist in the environment and can cause disease years later. Central to controlling disease transmission is the identification of methods c...

journal_title：Prion

authors： Rodriguez CM,Bennett JP,Johnson CJ

更新日期：2012-01-01 00:00:00

abstract：:The etiology of behavioral and psychological symptoms of dementia (BPSD) is complex, including putative biological, psychological, social and environmental factors. Recent years have witnessed accumulation of data on the association between genetic factors and behavioral abnormalities in Alzheimer disease (AD). In thi...

journal_title：Prion

authors： Flirski M,Sieruta M,Golańska E,Kłoszewska I,Liberski PP,Sobów T

更新日期：2012-01-01 00:00:00

abstract：:Doppel (Dpl) protein is a paralog of the prion protein (PrP) that shares 25% sequence similarity with the C-terminus of PrP, a common N-glycosylation site and a C-terminal signal peptide for attachment of a glycosylphophatidyl inositol anchor. Whereas PrP (C) is highly expressed in the central nervous system (CNS), D...

journal_title：Prion

authors： Didonna A,Sussman J,Benetti F,Legname G

更新日期：2012-07-01 00:00:00

abstract：:The self-assembly of proteins into higher order structures is both central to normal biology and a dominant force in disease. Certain glutamine/asparagine (Q/N)-rich proteins in the budding yeast Saccharomyces cerevisiae assemble into self-replicating amyloid-like protein polymers, or prions, that act as genetic eleme...

journal_title：Prion

authors： Halfmann R,Wright JR,Alberti S,Lindquist S,Rexach M

更新日期：2012-09-01 00:00:00

abstract：:Amyloids are fibrillar protein aggregates resulting from non-covalent autocatalytic polymerization of various structurally and functionally unrelated proteins. Previously we have selected DNA aptamers, which bind specifically to the in vitro assembled amyloid fibrils of the yeast prionogenic protein Sup35. Here we sho...

journal_title：Prion

authors： Mitkevich OV,Kochneva-Pervukhova NV,Surina ER,Benevolensky SV,Kushnirov VV,Ter-Avanesyan MD

更新日期：2012-09-01 00:00:00

abstract：:Mammalian prions with significant levels of specific infectivity can be formed in vitro from mixtures of prion protein (PrP) and cofactor molecules, but not from PrP alone. We recently isolated and identified the essential membrane phospholipid phosphatidylethanolamine (PE) as an endogenous cofactor for prion propagat...

journal_title：Prion

authors： Supattapone S

更新日期：2012-11-01 00:00:00

abstract：:The cellular prion protein (PrP (C) ) is subjected to various processing under physiological and pathological conditions, of which the α-cleavage within the central hydrophobic domain not only disrupts a region critical for both PrP toxicity and PrP (C) to PrP (Sc) conversion but also produces the N1 fragment that i...

journal_title：Prion

authors： Liang J,Kong Q

更新日期：2012-11-01 00:00:00

abstract：:Although multiple sclerosis (MS) is a chronic inflammatory-demyelinating disease of the white matter (WM) of the central nervous system, several pathological and magnetic resonance imaging (MRI) studies have shown that a large amount of lesions are located in the cortical and deep gray matter. The histopathological an...

journal_title：Prion

authors： Calabrese M,Favaretto A,Martini V,Gallo P

更新日期：2013-01-01 00:00:00

abstract：:Like patients with prion disease, Alzheimer patients suffer from a fatal, progressive form of dementia. There is growing evidence that amyloid-β (Aβ) aggregates may be transmissible similar to prions, at least under extreme experimental conditions. However, unlike mice infected with prion protein (PrP) prions, those i...

journal_title：Prion

authors： Ashe KH,Aguzzi A

更新日期：2013-01-01 00:00:00

abstract：:The pH-dependence of the ability of Bgl2p to form fibrils was studied using synthetic peptides with potential amyloidogenic determinants (PADs) predicted in the Bgl2p sequence. Three PADs, FTIFVGV, SWNVLVA and NAFS, were selected on the basis of combination of computational algorithms. Peptides AEGFTIFVGV, VDSWNVLVAG ...

journal_title：Prion

authors： Bezsonov EE,Groenning M,Galzitskaya OV,Gorkovskii AA,Semisotnov GV,Selyakh IO,Ziganshin RH,Rekstina VV,Kudryashova IB,Kuznetsov SA,Kulaev IS,Kalebina TS

更新日期：2013-03-01 00:00:00

abstract：:The structural conversion of the prion protein PrP into a transmissible, misfolded form is the central element of prion disease, yet there is little consensus as to how it occurs. Key aspects of conversion into the diseased state remain unsettled, from details about the earliest stages of misfolding such as the involv...

journal_title：Prion

authors： Yu H,Dee DR,Woodside MT

更新日期：2013-03-01 00:00:00

abstract：:Single nucleotide polymorphisms in the ubiquilin-1 gene may confer risk for late-onset Alzheimer disease (AD). We have shown previously that ubiquilin-1 functions as a molecular chaperone for the amyloid precursor protein (APP) and that protein levels of ubiquilin-1 are decreased in the brains of AD patients. We have ...

journal_title：Prion

authors： El Ayadi A,Stieren ES,Barral JM,Boehning D

更新日期：2013-03-01 00:00:00

abstract：:Structure is a key determinant of function, with the nervous system being no exception. For example, in the nervous system the physiological properties of different synapses may be understood by comparing their structures. However, it is not clear whether specific structural properties of some neurons might play a rol...

journal_title：Prion

authors： Sišková Z

更新日期：2013-07-01 00:00:00