Results 141 to 150 of about 5,869 (184)

Unfold to refold: Tracking the initial steps of PrP^C unfolding in the context of PrP^Sc propagation

Sabzehei S, Rigoli M, Cacheiro R, Díaz-Arias I, Eraña H, Lago RP, Guerra A, Rezaei H, Castilla J, Biasini E, Sánchez-Pedregal VM, Martín-Pastor M, Requena JR.   +12 more
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A noninvasive test for human prion disease using hair roots and scalp. [PDF]

Sci Rep
Dong TT, Honda H, Akagi A, Iwasaki Y, Kishida H, Tsukamoto T, Kasuga K, Takashima H, Terada T, Ikenaka K, Ikeuchi T, Mori T, Mochizuki H, Ono K, Takiyama Y, Hamaguchi T, Murota H, Sanjo N, Fujimoto T, Kitayama M, Fujita K, Yukitake M, Fujioka S, Nishida N, Tsuboi Y, Kitamoto T, Takao M, Yamada M, Mizusawa H, Satoh K.   +29 more
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Prion-Protein-Specific Aptamer Reduces PrPSc Formation

ChemBioChem, 2002
The critical initial event in the pathophysiology of transmissible spongiform encephalopathies (TSEs) appears to be the conversion of the cellular prion protein (PrP(C)) into the abnormal isoform PrP(Sc). This isoform forms high-molecular-weight protease K (PK) resistant aggregates that accumulate in the central nervous system of affected individuals ...
Daniela, Proske, Sabine, Gilch, Franziska, Wopfner, Hermann M, Schätzl, Ernst-L, Winnacker, Michael, Famulok   +5 more
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Reversible Aggregation of Mouse Prion Protein Derivatives with PrPSC-Like Structural Properties

Journal of Protein Chemistry, 2003
Three carbamylated derivatives of reduced mouse prion protein (mPrP) were isolated during the aborted oxidative folding in the presence of urea. These three prion protein derivatives (mPrP-a, mPrP-b, and mPrP-c) exist as monomer in the acidic solution (pH < 2.0) and exhibit prevalent random coil structure.
Bao-Yuan, Lu, Ivo, Atanasov, Z Hong, Zhou, Jui-Yoa, Chang   +3 more
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V180I mutation of the prion protein gene associated with atypical PrPSc glycosylation

Neuroscience Letters, 2006
A valine to isoleucine mutation at residue 180 was identified in a French patient with Creutzfeldt-Jakob disease (CJD). The mutation is located in the close vicinity of one of the two N-glycosylation sites of the cellular prion protein (PrP(C)). Western blot analysis revealed accumulation in the brain of the pathogenic proteinase K-resistant PrP (PrP ...
Stéphanie, Chasseigneaux, Stéphane, Haïk, Isabelle, Laffont-Proust, Olivier, De Marco, Martine, Lenne, Jean-Philippe, Brandel, Jean-Jacques, Hauw, Jean-Louis, Laplanche, Katell, Peoc'h   +8 more
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Methamphetamine increases Prion Protein and induces dopamine-dependent expression of protease resistant PrPsc

Archives Italiennes de Biologie, 2017
The cellular prion protein (PrPc) is physiologically expressed within selective brain areas of mammals. Alterations in the secondary structure of this protein lead to scrapie-like prion protein (PrPsc), which precipitates in the cell. PrPsc has been detected in infectious, inherited or sporadic neurodegenerative disorders.
FERRUCCI, MICHELA, RYSKALIN, LARISA, BIAGIONI, FRANCESCA, Gambardella, S, Busceti, Cl, FALLENI, ALESSANDRA, LAZZERI, GLORIA, FORNAI, FRANCESCO   +7 more
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The effect of Fenton reaction on protease-resistant prion protein (PrPSc) degradation and scrapie infectivity

Brain Research, 2008
In prion diseases, metal imbalances in brain and/or metal substitutions for copper in prion protein suggest that metal-catalyzed oxidation (MCO) and oxidative stress may affect cellular function and accumulation of protease-resistant prion protein (PrP(Sc)).
Seok-Joo, Park, Nam-Ho, Kim, Byung-Hoon, Jeong, Jae-Kwang, Jin, Jin-Kyu, Choi, Young-Jae, Park, Jae-Il, Kim, Richard I, Carp, Yong-Sun, Kim   +8 more
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Use of streptomycin for precipitation and detection of proteinase K resistant prion protein (PrPsc) in biological samples

Chemical Communications, 2006
The ability of streptomycin to form multimolecular aggregates with pathogenic prion proteins and their recovery by precipitation via a low-speed centrifugation step has been demonstrated; these novel properties of streptomycin make it a useful substance that increases the sensitivity of laboratory diagnostic techniques for prion infections in man and ...
Aly, Moussa, Anthony W, Coleman, Anna, Bencsik, Edwige, Leclere, Florent, Perret, Ambroise, Martin, Hervé, Perron   +6 more
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Biochemical evidence for the proteolytic degradation of infectious prion protein PrPsc in hamster brain homogenates by foodborne bacteria

Systematic and Applied Microbiology, 2006
PrP(Sc) is a general term to describe the infectious agent causing transmissible spongiform encephalopathy (TSE), and the protease-resistant form of cellular PrP(C). In this study, we have identified several protease-secreting bacteria able to degrade PrP(Sc) under more or less native conditions (30 degrees C, pH 8), focusing on strains isolated mainly
Simone, Müller-Hellwig, Martin H, Groschup, Rohtraud, Pichner, Manfred, Gareis, Erwin, Märtlbauer, Siegfried, Scherer, Martin J, Loessner   +6 more
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