Poly-L-histidine inhibits prion propagation in a prion-infected cell line.

abstract：:We recently developed a new in vitro amplification technology, designated "real-time quaking-induced conversion (RT-QUIC)", for detection of the abnormal form of prion protein (PrPSc) in easily accessible specimens such as cerebrospinal fluid (CSF). After assessment of more than 200 CSF specimens from Japanese and Aus...

journal_title：Prion

authors： Atarashi R,Sano K,Satoh K,Nishida N

更新日期：2011-07-01 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：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：:Heat shock proteins HSP27, HSP70 and HSP90 are molecular chaperones whose expression is increased after many different types of stress. They have a protective function helping the cell to cope with lethal conditions. The cytoprotective function of HSPs is largely explained by their anti-apoptotic function. HSPs have b...

journal_title：Prion

authors： Lanneau D,de Thonel A,Maurel S,Didelot C,Garrido C

更新日期：2007-01-01 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：:Prions, the causative agent of chronic wasting disease (CWD) enter the environment through shedding of bodily fluids and carcass decay, posing a disease risk as a result of their environmental persistence. Plants have the ability to take up large organic particles, including whole proteins, and microbes. This study us...

journal_title：Prion

authors： Rasmussen J,Gilroyed BH,Reuter T,Dudas S,Neumann NF,Balachandran A,Kav NN,Graham C,Czub S,McAllister TA

更新日期：2014-01-01 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：:The objectives of this study were to test whether recombinant mouse (mo)PrP alone or in combination with LPS or under simulated endotoxemia would affect expression of genes related to host inflammatory and antimicrobial responses. To test our hypotheses colon tissues were collected from 16 male mice (FVB/N strain) and...

journal_title：Prion

authors： Dervishi E,Lam TH,Dunn SM,Zwierzchowski G,Saleem F,Wishart DS,Ametaj BN

更新日期：2015-01-01 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：:The yeast, fungal and mammalian prions determine heritable and infectious traits that are encoded in alternative conformations of proteins. They cause lethal sporadic, familial and infectious neurodegenerative conditions in man, including Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), ...

journal_title：Prion

authors： Safar JG

更新日期：2012-04-01 00:00:00

abstract：:Prion diseases are infectious conformational diseases. Despite the determination of many native prion protein (PrP) structures and in vitro production of infectious prions from recombinant PrP the structural background of PrP conversion remains the largest unsolved problem. The aggregated state of PrP (Sc) makes it in...

journal_title：Prion

authors： Hafner-Bratkovič I,Jerala R

更新日期：2011-04-01 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：:The aggregation of a soluble protein into insoluble, beta-sheet rich amyloid fibrils is a defining characteristic of many neurodegenerative diseases, including prion disorders. The prion protein has so far been considered unique because of its infectious nature. Recent investigations, however, suggest that other amylo...

journal_title：Prion

authors： Frost B,Diamond MI

更新日期：2009-04-01 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：: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：: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：: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：: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：:Tauopathies are a family of neurodegenerative diseases in which fibrils of human hyperphosphorylated tau (P-tau) are believed to cause neuropathology. In Alzheimer disease, P-tau associates with A-beta amyloid and contributes to disease pathogenesis. In familial human prion diseases and variant CJD, P-tau often co-ass...

journal_title：Prion

authors： Race B,Phillips K,Kraus A,Chesebro B

更新日期：2016-07-03 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

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：: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：: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：: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：: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 self-propagating infectious protein aggregates of mammals and fungi. The exact mechanism of prion formation is poorly understood. In a recent study, a comparative analysis of the aggregation propensities of chimeric proteins derived from the yeast Sup35p and mouse PrP prion proteins was performed in neurobl...

journal_title：Prion

authors： Krammer C,Kremmer E,Schätzl HM,Vorberg I

更新日期：2008-07-01 00:00:00

abstract：:Synaptic dysfunction is a key process in the evolution of many neurodegenerative diseases, with synaptic loss preceding that of neuronal cell bodies. In Alzheimer, Huntington, and prion diseases early synaptic changes correlate with cognitive and motor decline, and altered synaptic function may also underlie deficits ...

journal_title：Prion

authors： Mallucci GR

更新日期：2009-10-01 00:00:00

abstract：:Each known abnormal prion protein (PrP (Sc) ) is considered to have a specific range and therefore the ability to infect some species and not others. Consequently, some species have been assumed to be prion disease resistant as no successful natural or experimental challenge infections have been reported. This assumpt...

journal_title：Prion

authors： Fernández-Borges N,Chianini F,Eraña H,Vidal E,Eaton SL,Pintado B,Finlayson J,Dagleish MP,Castilla J

更新日期：2012-11-01 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：:A case of L-type-like atypical bovine spongiform encephalopathy was detected in 14-year-old Japanese black beef cattle (BSE/JP24). To clarify the biological and biochemical properties of the prion in BSE/JP24, we performed a transmission study with wild-type mice and bovinized transgenic mice (TgBoPrP). The BSE/JP24 p...

journal_title：Prion

authors： Masujin K,Shu Y,Yamakawa Y,Hagiwara K,Sata T,Matsuura Y,Iwamaru Y,Imamura M,Okada H,Mohri S,Yokoyama T

更新日期：2008-07-01 00:00:00