| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Xiangzhu Xiao, Jue Yuan, Stéphane Haïk, Ignazio Cali, Yian Zhan, Mohammed Moudjou, Baiya Li, Jean-Louis Laplanche, Hubert Laude, Jan Langeveld, Pierluigi Gambetti, Tetsuyuki Kitamoto, Qingzhong Kong, Jean-Philippe Brandel, Brian A Cobb, Robert B Petersen, Wen-Quan Zo. Glycoform-selective prion formation in sporadic and familial forms of prion disease. PloS one. vol 8. issue 3. 2013-09-27. PMID:23527023. |
the four glycoforms of the cellular prion protein (prp(c)) variably glycosylated at the two n-linked glycosylation sites are converted into their pathological forms (prp(sc)) in most cases of sporadic prion diseases. |
2013-09-27 |
2023-08-12 |
Not clear |
| Xiangzhu Xiao, Jue Yuan, Stéphane Haïk, Ignazio Cali, Yian Zhan, Mohammed Moudjou, Baiya Li, Jean-Louis Laplanche, Hubert Laude, Jan Langeveld, Pierluigi Gambetti, Tetsuyuki Kitamoto, Qingzhong Kong, Jean-Philippe Brandel, Brian A Cobb, Robert B Petersen, Wen-Quan Zo. Glycoform-selective prion formation in sporadic and familial forms of prion disease. PloS one. vol 8. issue 3. 2013-09-27. PMID:23527023. |
however, a prominent molecular characteristic of prp(sc) in the recently identified variably protease-sensitive prionopathy (vpspr) is the absence of a diglycosylated form, also notable in familial creutzfeldt-jakob disease (fcjd), which is linked to mutations in prp either from val to ile at residue 180 (fcjd(v180i)) or from thr to ala at residue 183 (fcjd(t183a)). |
2013-09-27 |
2023-08-12 |
Not clear |
| Xiangzhu Xiao, Jue Yuan, Stéphane Haïk, Ignazio Cali, Yian Zhan, Mohammed Moudjou, Baiya Li, Jean-Louis Laplanche, Hubert Laude, Jan Langeveld, Pierluigi Gambetti, Tetsuyuki Kitamoto, Qingzhong Kong, Jean-Philippe Brandel, Brian A Cobb, Robert B Petersen, Wen-Quan Zo. Glycoform-selective prion formation in sporadic and familial forms of prion disease. PloS one. vol 8. issue 3. 2013-09-27. PMID:23527023. |
taken together, our current in vivo and in vitro studies indicate that sporadic vpspr and familial cjd(v180i) share a unique glycoform-selective prion formation pathway in which the conversion of diglycosylated and mono181 prp(c) to prp(sc) is inhibited, probably by a dominant-negative effect, or by other co-factors. |
2013-09-27 |
2023-08-12 |
Not clear |
| Michele Angelo Di Bari, Romolo Nonno, Joaquín Castilla, Claudia D'Agostino, Laura Pirisinu, Geraldina Riccardi, Michela Conte, Juergen Richt, Robert Kunkle, Jan Langeveld, Gabriele Vaccari, Umberto Agrim. Chronic wasting disease in bank voles: characterisation of the shortest incubation time model for prion diseases. PLoS pathogens. vol 9. issue 3. 2013-09-05. PMID:23505374. |
bv(109i)cwd was characterised by a mild and discrete distribution of spongiosis and relatively low levels of protease-resistant prp(sc) (prp(res)) in the same brain regions. |
2013-09-05 |
2023-08-12 |
Not clear |
| Michele Angelo Di Bari, Romolo Nonno, Joaquín Castilla, Claudia D'Agostino, Laura Pirisinu, Geraldina Riccardi, Michela Conte, Juergen Richt, Robert Kunkle, Jan Langeveld, Gabriele Vaccari, Umberto Agrim. Chronic wasting disease in bank voles: characterisation of the shortest incubation time model for prion diseases. PLoS pathogens. vol 9. issue 3. 2013-09-05. PMID:23505374. |
bv(109i)cwd showed unique characteristics of "virulence", low prp(res) accumulation and high infectivity, thus providing exceptional opportunities to improve basic knowledge of the relationship between prp(sc), neurodegeneration and infectivity. |
2013-09-05 |
2023-08-12 |
Not clear |
| Fani Koukouli, Ioannis Paspaltsis, Evgenia Salta, Konstantinos Xanthopoulos, Eftychia N Koini, Theodora Calogeropoulou, Theodoros Sklaviadi. Inhibition of PrP(Sc) formation in scrapie infected N2a cells by 5,7,8-trimethyl-3,4-dihydro-2H-1,4-benzoxazine derivatives. Prion. vol 6. issue 5. 2013-08-30. PMID:22918434. |
inhibition of prp(sc) formation in scrapie infected n2a cells by 5,7,8-trimethyl-3,4-dihydro-2h-1,4-benzoxazine derivatives. |
2013-08-30 |
2023-08-12 |
Not clear |
| Fani Koukouli, Ioannis Paspaltsis, Evgenia Salta, Konstantinos Xanthopoulos, Eftychia N Koini, Theodora Calogeropoulou, Theodoros Sklaviadi. Inhibition of PrP(Sc) formation in scrapie infected N2a cells by 5,7,8-trimethyl-3,4-dihydro-2H-1,4-benzoxazine derivatives. Prion. vol 6. issue 5. 2013-08-30. PMID:22918434. |
prion diseases are fatal, neurodegenerative diseases characterized by the structural conversion of the normal, cellular prion protein, prp (c) into an abnormally structured, aggregated and partially protease-resistant isoform, termed prp (sc) . |
2013-08-30 |
2023-08-12 |
Not clear |
| Fani Koukouli, Ioannis Paspaltsis, Evgenia Salta, Konstantinos Xanthopoulos, Eftychia N Koini, Theodora Calogeropoulou, Theodoros Sklaviadi. Inhibition of PrP(Sc) formation in scrapie infected N2a cells by 5,7,8-trimethyl-3,4-dihydro-2H-1,4-benzoxazine derivatives. Prion. vol 6. issue 5. 2013-08-30. PMID:22918434. |
in an effort to identify novel inhibitors of prion formation, several 5,7,8-trimethyl-1,4-benzoxazine derivatives were evaluated in vitro for their effectiveness on the expression levels of normal prp (c) and its conversion to the abnormal isoforms of prp (sc) in a scrapie-infected cell culture model. |
2013-08-30 |
2023-08-12 |
Not clear |
| Fani Koukouli, Ioannis Paspaltsis, Evgenia Salta, Konstantinos Xanthopoulos, Eftychia N Koini, Theodora Calogeropoulou, Theodoros Sklaviadi. Inhibition of PrP(Sc) formation in scrapie infected N2a cells by 5,7,8-trimethyl-3,4-dihydro-2H-1,4-benzoxazine derivatives. Prion. vol 6. issue 5. 2013-08-30. PMID:22918434. |
the most potent compound was 2-(4-methoxyphenyl)-5,7,8-trimethyl-3,4-dihydro-2h-1,4-benzoxazine, with a diminishing effect on the formation of prp (sc) , thus establishing a class of compounds with a promising therapeutic use against prion diseases. |
2013-08-30 |
2023-08-12 |
Not clear |
| Ryan J Arsenault, Yue Li, Andrew Potter, Philip J Griebel, Anthony Kusalik, Scott Nappe. Induction of ligand-specific PrP (C) signaling in human neuronal cells. Prion. vol 6. issue 5. 2013-08-30. PMID:22918447. |
in spite of being a point of intense research effort critical questions still remain regarding the physiological function of prp (c) and how these functions may change with the conversion of the protein into the infectious and pathological conformation (prp (sc) ). |
2013-08-30 |
2023-08-12 |
human |
| Natalia Fernández-Borges, Francesca Chianini, Hasier Eraña, Enric Vidal, Samantha L Eaton, Belén Pintado, Jeanie Finlayson, Mark P Dagleish, Joaquín Castill. Naturally prion resistant mammals: a utopia? Prion. vol 6. issue 5. 2013-08-30. PMID:22954650. |
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. |
2013-08-30 |
2023-08-12 |
rabbit |
| Natalia Fernández-Borges, Francesca Chianini, Hasier Eraña, Enric Vidal, Samantha L Eaton, Belén Pintado, Jeanie Finlayson, Mark P Dagleish, Joaquín Castill. Naturally prion resistant mammals: a utopia? Prion. vol 6. issue 5. 2013-08-30. PMID:22954650. |
this assumption suggested that, independent of the virulence of the prp (sc) strain, normal prion protein (prp (c) ) from these 'resistant' species could not be induced to misfold. |
2013-08-30 |
2023-08-12 |
rabbit |
| Natalia Fernández-Borges, Francesca Chianini, Hasier Eraña, Enric Vidal, Samantha L Eaton, Belén Pintado, Jeanie Finlayson, Mark P Dagleish, Joaquín Castill. Naturally prion resistant mammals: a utopia? Prion. vol 6. issue 5. 2013-08-30. PMID:22954650. |
numerous in vitro and in vivo studies trying to corroborate the unique properties of prp (sc) have been undertaken. |
2013-08-30 |
2023-08-12 |
rabbit |
| Natalia Fernández-Borges, Francesca Chianini, Hasier Eraña, Enric Vidal, Samantha L Eaton, Belén Pintado, Jeanie Finlayson, Mark P Dagleish, Joaquín Castill. Naturally prion resistant mammals: a utopia? Prion. vol 6. issue 5. 2013-08-30. PMID:22954650. |
the results presented in the article "rabbits are not resistant to prion infection" demonstrated that normal rabbit prp (c) , which was considered to be resistant to prion disease, can be misfolded to prp (sc) and subsequently used to infect and transmit a standard prion disease to leporids. |
2013-08-30 |
2023-08-12 |
rabbit |
| Gustavo Sajnani, Jesús R Requen. Prions, proteinase K and infectivity. Prion. vol 6. issue 5. 2013-08-30. PMID:23044510. |
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. |
2013-08-30 |
2023-08-12 |
Not clear |
| Gustavo Sajnani, Jesús R Requen. Prions, proteinase K and infectivity. Prion. vol 6. issue 5. 2013-08-30. PMID:23044510. |
it is also known that an important fraction of total prp (sc) is pk-sensitive and can be isolated by the method we already described. |
2013-08-30 |
2023-08-12 |
Not clear |
| Gustavo Sajnani, Jesús R Requen. Prions, proteinase K and infectivity. Prion. vol 6. issue 5. 2013-08-30. PMID:23044510. |
consequently, we decided to employ the pk-sensitive fraction of prp (sc) as a potential and useful tool for structural studies. |
2013-08-30 |
2023-08-12 |
Not clear |
| Gustavo Sajnani, Jesús R Requen. Prions, proteinase K and infectivity. Prion. vol 6. issue 5. 2013-08-30. PMID:23044510. |
first, the difference in the infectivity between the sensitive and resistant fractions and second, whether sensitive and resistant prp (sc) shared the same conformation or were only different size multimers with the same basic conformation. |
2013-08-30 |
2023-08-12 |
Not clear |
| Jingjing Liang, Qingzhong Kon. α-Cleavage of cellular prion protein. Prion. vol 6. issue 5. 2013-08-30. PMID:23052041. |
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 is neuroprotective and the c1 fragment that enhances the pro-apoptotic effect of staurosporine in one report and inhibits prion in another. |
2013-08-30 |
2023-08-12 |
Not clear |
| Daisuke Ishibashi, Ryuichiro Atarashi, Noriyuki Nishid. Protective role of MyD88-independent innate immune responses against prion infection. Prion. vol 6. issue 5. 2013-08-30. PMID:23093799. |
in addition, irf3 stimulation inhibited prp (sc) replication in prion persistently-infected cells, and a de novo prion infection assay revealed that irf3-overexpression could make host cells resistant to prion infection. |
2013-08-30 |
2023-08-12 |
mouse |