Interplays between covalent modifications in the endoplasmic reticulum increase conformational diversity in nascent prion protein.

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：: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：:Mechanisms for the spread of transmissible spongiform encephalopathy diseases, including chronic wasting disease (CWD) in North American cervids, are incompletely understood, but primary routes include horizontal and environmental transmission. Birds have been identified as potential vectors for a number of diseases, ...

journal_title：Prion

authors： Fischer JW,Phillips GE,Nichols TA,Vercauteren KC

更新日期：2013-07-01 00:00:00

abstract：:Scrapie and CWD are horizontally transmissible, and the environment likely serves as a stable reservoir of infectious prions, facilitating a sustained incidence of CWD in free-ranging cervid populations and complicating efforts to eliminate disease in captive herds. Prions will enter the environment through mortalitie...

journal_title：Prion

authors： Saunders SE,Bartelt-Hunt SL,Bartz JC

更新日期：2008-10-01 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：:Prion diseases are subacute neurodegenerative diseases that affect humans and a range of domestic and free-ranging animal species. These diseases are characterized by the accumulation of PrP (Sc), an abnormally folded isoform of the cellular prion protein (PrP (C)), in affected tissues. The pathology during prion dise...

journal_title：Prion

authors： Mabbott NA

更新日期：2012-09-01 00:00:00

abstract：:Among different types of protein aggregation, amyloids are a biochemically well characterized state of protein aggregation that are associated with a large number of neurodegenerative diseases including Parkinson's disease, Alzheimer and Creutzfeldt-Jakob disease. Yeast, Saccharomyces cerevisiae is an insightful model...

journal_title：Prion

authors： Aslam K,Hazbun TR

更新日期：2016-03-03 00:00:00

abstract：:TDP-43 and FUS are DNA/RNA binding proteins associated with neuronal inclusions in amyotrophic lateral sclerosis (ALS) patients. Other neurodegenerative diseases are also characterized by neuronal protein aggregates, e.g. Huntington's disease, associated with polyglutamine (polyQ) expansions in the protein huntingtin....

journal_title：Prion

authors： Park SK,Arslan F,Kanneganti V,Barmada SJ,Purushothaman P,Verma SC,Liebman SW

更新日期：2018-01-02 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：:Many laboratory studies and epidemiological observations confirm that nematodes prevent some immune-mediated diseases. The development of immunologically well-defined laboratory models of intestinal nematode infection has allowed significant advances to be made in understanding the immunological basis of effector mech...

journal_title：Prion

authors： Donskow-Łysoniewska K,Brodaczewska K,Doligalska M

更新日期：2013-07-01 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：:The prion paradigm is increasingly invoked to explain the molecular pathogenesis of neurodegenerative diseases involving the misfolding and aggregation of proteins other than the prion protein (PrP). Extensive evidence from in vitro and in vivo studies indicates that misfolded and aggregated Aβ peptide, which is the p...

journal_title：Prion

authors： Rasmussen J,Jucker M,Walker LC

更新日期：2017-07-04 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：: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：:Prion diseases are consistently associated with prion protein (PrP(C)) misfolding rendering a cascade of auto-catalytic self-perpetuation of misfolded PrP in an afflicted individual. The molecular process is intriguingly similar to all known amyloid diseases both local and systemic. The prion disease is also infectiou...

journal_title：Prion

authors： Nyström S,Hammarström P

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：:M2B cells with persistent classical bovine spongiform encephalopathy (C-BSE) have been established previously. In this study, we performed strain characterization of the M2B cell line in bovine PrPC overexpressing mice (Tg 1896). Mice intracranially inoculated with M2B cells and C-BSE survived for 451 ± 7 and 465 ± 31...

journal_title：Prion

authors： Suh TY,Roh IS,Kim HJ,Griffiths PC,Park KJ,Park HC,Hope J,Kang HE,Kim DY,Sohn HJ

更新日期：2017-11-02 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：:Transmissible spongiform encephalopathies (TSEs) are a group of lethal neurodegenerative diseases involving the structural conversion of cellular prion protein (PrPC) into the pathogenic isoform (PrPSc) for which no effective treatment is currently available. Previous studies have implicated that a polymeric molecule ...

journal_title：Prion

authors： Honda R,Yamaguchi KI,Elhelaly AE,Fuji M,Kuwata K

更新日期：2018-01-01 00:00:00

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：:Proteins with expanded polyglutamine (polyQ) regions are prone to form amyloids, which can cause diseases in humans and toxicity in yeast. Recently, we showed that in yeast non-toxic amyloids of Q-rich proteins can induce aggregation and toxicity of wild type huntingtin (Htt) with a short non-pathogenic polyglutamine ...

journal_title：Prion

authors： Alexandrov AI,Serpionov GV,Kushnirov VV,Ter-Avanesyan MD

更新日期：2016-05-03 00:00:00

abstract：:Genetic prion diseases are degenerative brain disorders caused by mutations in the gene encoding the prion protein (PrP). Different PrP mutations cause different diseases, including Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker (GSS) syndrome and fatal familial insomnia (FFI). The reason for this var...

journal_title：Prion

authors： Chiesa R,Restelli E,Comerio L,Del Gallo F,Imeri L

更新日期：2016-03-03 00:00:00

abstract：:Early detection and diagnosis of neurodegenerative diseases has been hampered by the lack of sensitive testing. Real-time quaking induced conversion (RT-QuIC) has been used for the early and sensitive detection of prion-induced neurologic disease, and has more recently been adapted to detect misfolded alpha-synuclein ...

journal_title：Prion

authors： Tennant JM,Henderson DM,Wisniewski TM,Hoover EA

更新日期：2020-12-01 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：: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：:Prion protein, PrP(C), is a glycoprotein that is expressed on the cell surface beginning with the early stages of embryonic stem cell differentiation. Previously, we showed that ectopic expression of PrP(C) in human embryonic stem cells (hESCs) triggered differentiation toward endodermal, mesodermal, and ectodermal li...

journal_title：Prion

authors： Lee YJ,Baskakov IV

更新日期：2014-01-01 00:00:00

abstract：:It has been described that the breakdown of β-sheets in PrP (Sc) by denaturation results in loss of infectivity and PK-sensitivity, suggesting a relationship between the structure and PK-resistance. It is also known that an important fraction of total PrP (Sc) is PK-sensitive and can be isolated by the method we alr...

journal_title：Prion

authors： Sajnani G,Requena JR

更新日期：2012-11-01 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：: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：:Perturbations of calcium homeostasis have been associated with several neurodegenerative disorders. A common polymorphism (rs2986017) in the CALHM1 gene, coding for a regulator of calcium homeostasis, is a genetic risk factor for the development of Alzheimer disease (AD). Although some authors failed to confirm these ...

journal_title：Prion

authors： Calero O,Bullido MJ,Clarimón J,Hortigüela R,Frank-García A,Martínez-Martín P,Lleó A,Rey MJ,Sastre I,Rábano A,de Pedro-Cuesta J,Ferrer I,Calero M

更新日期：2012-09-01 00:00:00