Hypothesis: AA amyloidosis is a factor causing systemic complications after coronavirus disease.

abstract：:Glucantransferase Bgl2p is a major conserved cell wall constituent described for a wide range of yeast species. In the baker's yeast Saccharomyces cerevisiae it is the only non-covalently bound cell wall protein that cannot be released from cell walls by sequential SDS and trypsin treatment. It contains seven amyloido...

journal_title：Prion

authors： Kalebina TS,Plotnikova TA,Gorkovskii AA,Selyakh IO,Galzitskaya OV,Bezsonov EE,Gellissen G,Kulaev IS

更新日期：2008-04-01 00:00:00

abstract：:The serpins are the largest superfamily of protease inhibitors. They are found in almost all branches of life including viruses, prokaryotes and eukaryotes. They inhibit their target protease by a unique mechanism that involves a large conformational transition and the translocation of the enzyme from the upper to the...

journal_title：Prion

authors： Belorgey D,Hägglöf P,Karlsson-Li S,Lomas DA

更新日期：2007-01-01 00:00:00

abstract：:Yeast prion determinants are related to polymerization of some proteins into amyloid-like fibers. The [PSI(+)] determinant reflects polymerization of the Sup35 protein. Fragmentation of prion polymers by the Hsp104 chaperone represents a key step of the prion replication cycle. The frequency of fragmentation varies de...

journal_title：Prion

authors： Kushnirov VV,Vishnevskaya AB,Alexandrov IM,Ter-Avanesyan MD

更新日期：2007-07-01 00:00:00

abstract：:We previously showed that over production of a fusion protein in which the prion domain of Saccharomyces cerevisiae [PSI(+)] is connected to glutathione S-transferase (GST-Sup35NM) causes a marked decrease in the colony forming ability of Escherichia coli strain BL21 after reaching stationary phase. Evidence indicated...

journal_title：Prion

authors： Ono B,Kawaminami H,Kobayashi H,Kubota M,Murakami Y

更新日期：2008-01-01 00:00:00

abstract：:The pathogenic mechanism(s) underlying neurodegenerative diseases associated with protein misfolding is unclear. Several studies have implicated ER stress pathways in neurodegenerative conditions, including prion disease, amyotrophic lateral sclerosis, Alzheimer's disease and many others. The ER stress response and up...

journal_title：Prion

authors： Steele AD,Hetz C,Yi CH,Jackson WS,Borkowski AW,Yuan J,Wollmann RH,Lindquist S

更新日期：2007-10-01 00:00:00

abstract：:Early cell biologists perceived centrosomes to be permanent cellular structures. Centrosomes were observed to reproduce once each cycle and to orchestrate assembly a transient mitotic apparatus that segregated chromosomes and a centrosome to each daughter at the completion of cell division. Centrosomes are composed of...

journal_title：Prion

authors： Wilson PG

更新日期：2008-01-01 00:00:00

abstract：:HLA-B27 plays a central role in the pathogenesis of many spondyloarthropathies and in particular ankylosing spondylitis. The observation that the HLA-B27 heavy chain has a tendency to misfold has raised the possibility that associated diseases may belong in a rapidly expanding category of protein misfolding disorders....

journal_title：Prion

authors： Colbert RA,DeLay ML,Layh-Schmitt G,Sowders DP

更新日期：2009-01-01 00:00:00

abstract：:Deposits of amyloid fibrils characterize a diverse group of human diseases that includes Alzheimer's disease, Creutzfeldt-Jakob disease and type II diabetes. Amyloid fibrils formed from different polypeptides contain a common cross-beta spine. Nevertheless, amyloid fibrils formed from the same polypeptide can occur in...

journal_title：Prion

authors： Fändrich M,Meinhardt J,Grigorieff N

更新日期：2009-04-01 00:00:00

abstract：:Insights into the molecular basis and the temporal evolution of neurotoxicity in prion disease are increasing, and recent work in mice leads to new avenues for targeting treatment of these disorders. Using lentivirally mediated RNA interference (RNAi) against native prion protein (PrP), White et al. report the first t...

journal_title：Prion

authors： White MD,Mallucci GR

更新日期：2009-07-01 00:00:00

abstract：:Chronic wasting disease (CWD) is the only known transmissible spongiform encephalopathy affecting free-ranging wildlife. Although the exact mode of natural transmission remains unknown, substantial evidence suggests that prions can persist in the environment, implicating components thereof as potential prion reservoir...

journal_title：Prion

authors： Nichols TA,Pulford B,Wyckoff AC,Meyerett C,Michel B,Gertig K,Hoover EA,Jewell JE,Telling GC,Zabel MD

更新日期：2009-07-01 00:00:00

abstract：:Alzheimer and prion diseases are neurodegenerative disorders characterised by the abnormal processing of amyloid-beta (Abeta) peptide and prion protein (PrP(C)), respectively. Recent evidence indicates that PrP(C) may play a critical role in the pathogenesis of Alzheimer disease. PrP(C) interacts with and inhibits the...

journal_title：Prion

authors： Kellett KA,Hooper NM

更新日期：2009-10-01 00:00:00

abstract：:Amyloid formation is a hallmark of several systemic and neurodegenerative diseases. Extracellular amyloid deposits or intracellular inclusions arise from the conformational transition of normally soluble proteins into highly ordered fibrillar aggregates. Amyloid fibrils are formed by nucleated polymerization, a proces...

journal_title：Prion

authors： Krammer C,Schätzl HM,Vorberg I

更新日期：2009-10-01 00:00:00

abstract：:Although it has been known for more than twenty years that an aberrant conformation of the prion protein (PrP) is the causative agent in prion diseases, the role of PrP in normal biology is undetermined. Numerous studies have suggested a protective function for PrP, including protection from ischemic and excitotoxic l...

journal_title：Prion

authors： Steele AD,Zhou Z,Jackson WS,Zhu C,Auluck P,Moskowitz MA,Chesselet MF,Lindquist S

更新日期：2009-10-01 00:00:00

abstract：:Protein Misfolding Cyclic Amplification (PMCA) has proved to be an efficient method mimicking in vitro some of the fundamental steps involved in prion replication in vivo. Thus, it can be used to efficiently replicate a variety of prion strains/species. The in vitro generated prions possess key prion features, i.e., t...

journal_title：Prion

authors： Fernández-Borges N,de Castro J,Castilla J

更新日期：2009-10-01 00:00:00

abstract：:In eukaryotic cells amyloid aggregates may incorporate various functionally unrelated proteins. In mammalian diseases this may cause amyloid toxicity, while in yeast this could contribute to prion phenotypes. Insolubility of amyloids in the presence of strong ionic detergents, such as SDS or sarcosyl, allows discrimin...

journal_title：Prion

authors： Urakov VN,Vishnevskaya AB,Alexandrov IM,Kushnirov VV,Smirnov VN,Ter-Avanesyan MD

更新日期：2010-01-01 00:00:00

abstract：:Yeast prions provide a powerful model system for examining prion formation and propagation in vivo. Yeast prion formation is driven primarily by amino acid composition, not by primary amino acid sequence. However, although yeast prion domains are consistently glutamine/asparagine-rich, they otherwise vary significantl...

journal_title：Prion

authors： Ross ED,Toombs JA

更新日期：2010-04-01 00:00:00

abstract：:Prion diseases are fatal neurodegenerative disorders caused by prion proteins (PrP). Infectious prions accumulate in the brain through a template-mediated conformational conversion of endogenous PrP(C) into alternately folded PrP(Sc). Immunoassays toward pre-clinical detection of infectious PrP(Sc) have been confounde...

journal_title：Prion

authors： Hnasko R,Serban AV,Carlson G,Prusiner SB,Stanker LH

更新日期：2010-04-01 00:00:00

abstract：:Misfolded proteins are at the core of many neurodegenerative diseases, nearly all of them associated with cognitive impairment. For example Creutzfeldt-Jacob disease is associated with aggregation of prion protein, Lewy body dementia and Parkinson disease with α-synuclein and forms of frontotemporal dementia with tau,...

journal_title：Prion

authors： Galvin JE

更新日期：2011-01-01 00:00:00

abstract：:The intricate complexity, at the molecular and cellular levels, of the processes leading to the development of amyloid proteinopathies is somehow counterbalanced by their common, universal structural basis. The later has fueled the quest for suitable model systems to study protein amyloidosis under quasi-physiological...

journal_title：Prion

authors： Giraldo R,Moreno-Díaz de la Espina S,Fernández-Tresguerres ME,Gasset-Rosa F

更新日期：2011-04-01 00:00:00

abstract：:The prion diseases occur following the conversion of the cellular prion protein (PrPC) into a disease-related isoform (PrPSc). In this study a cell painting technique was used to examine the role of the glycosylphosphatidylinositol (GPI) anchor attached to PrPC in prion formation. The introduction of PrPC to infected ...

journal_title：Prion

authors： Bate C,Williams A

更新日期：2011-04-01 00:00:00

abstract：:We and others have recently reported that prions can be transmitted to mice via aerosols. These reports spurred a lively public discussion on the possible public-health threats represented by prion-containing aerosols. Here we offer our view on the context in which these findings should be placed. On the one hand, the...

journal_title：Prion

authors： Stitz L,Aguzzi A

更新日期：2011-07-01 00:00:00

abstract：:Yeast prions are self-perpetuating protein aggregates that are at the origin of heritable and transmissible non-Mendelian phenotypic traits. Among these, [PSI+], [URE3] and [PIN+] are the most well documented prions and arise from the assembly of Sup35p, Ure2p and Rnq1p, respectively, into insoluble fibrillar assembli...

journal_title：Prion

authors： Kabani M,Melki R

更新日期：2011-10-01 00:00:00

abstract：:[ISP+] is a prion form of the global transcriptional regulator Sfp1 in Saccharomyces cerevisiae that manifests phenotypically as an antisuppressor of specific sup35 nonsense suppressor mutations. Although SUP35 is a Sfp1 target, the mechanism of antisuppression is unclear. Here we show that the level of SUP35 transcri...

journal_title：Prion

authors： Radchenko E,Rogoza T,Khokhrina M,Drozdova P,Mironova L

更新日期：2011-10-01 00:00:00

abstract：:Transmissible spongiform encephalopathies (TSEs), or prion diseases, are neurological diseases that can be transmitted through a number of different routes. A wide range of mammalian species are affected by the disease. After peripheral exposure, some TSE agents accumulate in lymphoid tissues at an early stage of dise...

journal_title：Prion

authors： Wathne GJ,Mabbott NA

更新日期：2012-04-01 00:00:00

abstract：:The development of disinfectants with broad-range efficacy against bacteria, viruses, fungi, protozoa and prions constitutes an ongoing challenge. Prions, the causative agents of transmissible spongiform encephalopathies (TSEs) such as Creutzfeldt-Jakob disease (CJD) or its variant (vCJD) rank among the pathogens with...

journal_title：Prion

authors： Wagenführ K,Beekes M

更新日期：2012-01-01 00:00:00

abstract：:Scrapie of sheep and chronic wasting disease (CWD) of cervids are transmissible prion diseases. Milk and placenta have been identified as sources of scrapie prions but do not explain horizontal transmission. In contrast, CWD prions have been reported in saliva, urine and feces, which are thought to be responsible for ...

journal_title：Prion

authors： Tamgüney G,Richt JA,Hamir AN,Greenlee JJ,Miller MW,Wolfe LL,Sirochman TM,Young AJ,Glidden DV,Johnson NL,Giles K,DeArmond SJ,Prusiner SB

更新日期：2012-01-01 00:00:00

abstract：:Fibrillar aggregates of misfolded amyloid proteins are involved in a variety of diseases such as Alzheimer disease (AD), type 2 diabetes, Parkinson, Huntington and prion-related diseases. In the case of AD amyloid β (Aβ) peptides, the toxicity of amyloid oligomers and larger fibrillar aggregates is related to perturbi...

journal_title：Prion

authors： Tofoleanu F,Buchete NV

更新日期：2012-09-01 00:00:00

abstract：:Precisely how the accumulation of PrP (Sc) causes the neuronal degeneration that leads to the clinical symptoms of prion diseases is poorly understood. Our recent paper showed that the clustering of specific glycosylphosphatidylinositol (GPI) anchors attached to PrP proteins triggered synapse damage in cultured neuron...

journal_title：Prion

authors： Bate C,Williams A

更新日期：2012-09-01 00:00:00

abstract：:Mutations in the gene encoding the amyloid precursor protein (APP) or the enzymes that process APP are correlated with familial Alzheimer disease. Alzheimer disease is also associated with insulin resistance (type 2 diabetes). In our recently published study, ( 1) we obtained genetic evidence that the extracellular f...

journal_title：Prion

authors： Ewald CY,Li C

更新日期：2012-11-01 00:00:00

abstract：:Results from recent experiments with rodents imply that Alzheimer disease might be inducible by seeding Aβ peptides into recipient animals. In respect to this new experimental data, public health aspects as well as epidemiological data have to be reevaluated. In this article, the available experimental and epidemiolog...

journal_title：Prion

authors： Schmidt C,Karch A,Korth C,Zerr I

更新日期：2012-11-01 00:00:00