Heligmosomoides polygyrus antigens inhibit the intrinsic pathway of apoptosis by overexpression of survivin and Bcl-2 protein in CD4 T cells.

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：: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：:Recent studies on iatrogenic Creutzfeldt-Jakob disease (CJD) raised concerns that one of the hallmark lesions of Alzheimer disease (AD), amyloid-β (Aβ), may be transmitted from human-to-human. The neuropathology of AD-related lesions is complex. Therefore, many aspects need to be considered in deciding on this issue. ...

journal_title：Prion

authors： Kovacs GG

更新日期：2016-09-02 00:00:00

abstract：:Prions are responsible for a heterogeneous group of fatal neurodegenerative diseases. They can be sporadic, genetic, or infectious disorders involving post-translational modifications of the cellular prion protein (PrP(C)). Prions (PrP(Sc)) are characterized by their infectious property and intrinsic ability to conver...

journal_title：Prion

authors： Benetti F,Legname G

更新日期：2009-10-01 00:00:00

abstract：:The pathogenic mechanism of prion diseases remains unknown. We recently reported that prion infection disturbs post-Golgi trafficking of certain types of membrane proteins to the cell surface, resulting in reduced surface expression of membrane proteins and abrogating the signal from the proteins. The surface expressi...

journal_title：Prion

authors： Uchiyama K,Miyata H,Sakaguchi S

更新日期：2013-11-01 00:00:00

abstract：:Many neurodegenerative disorders share common features including the accumulation of aggregated misfolded proteins, neuroinflammation and the induction of apoptosis. While the contributions of each of these individual elements to neuronal death remain unclear, a commonly used antibiotic, minocycline, has been shown to...

journal_title：Prion

authors： Noble W,Garwood CJ,Hanger DP

更新日期：2009-04-01 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：: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：: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：: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：: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 normal function of PrPC, the cellular prion protein, has remained mysterious since its first description over 30 years ago. Amazingly, although complete deletion of the gene encoding PrPC has little phenotypic consequence, expression in transgenic mice of PrP molecules carrying certain internal deletions produces ...

journal_title：Prion

authors： McDonald AJ,Wu B,Harris DA

更新日期：2017-11-02 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：: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：: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：: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：: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：: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：: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：: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

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：: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：:The degeneration of pre-synaptic boutons in the stratum radiatum of the dorsal hippocampus is one of earliest components of neurodegeneration in several models of murine prion disease. We recently showed that blockade of synaptic transmission by infusion of botulinum neurotoxin A (BoNT/A) into the hippocampus several ...

journal_title：Prion

authors： Caleo M,Restani L,Perry VH

更新日期：2013-03-01 00:00:00

abstract：:The conformational diseases, linked to protein aggregation into amyloid conformations, range from non-infectious neurodegenerative disorders, such as Alzheimer disease (AD), to highly infectious ones, such as human transmissible spongiform encephalopathies (TSEs). They are commonly known as prion diseases. However, si...

journal_title：Prion

authors： Sabate R

更新日期：2014-01-01 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：:Conversion of native cellular prion protein (PrPc) from an α-helical structure to a toxic and infectious β-sheet structure (PrPSc) is a critical step in the development of prion disease. There are some indications that the formation of PrPSc is preceded by a β-sheet rich PrP (PrPβ) form which is non-infectious, but is...

journal_title：Prion

authors： Ladner-Keay CL,LeVatte M,Wishart DS

更新日期：2016-11-01 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：: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：: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