Results 171 to 180 of about 1,549,882 (213)

DMSO inhibits the aggregation of the prion proteins (PRPSC) into amyloid rods

Neuroscience Letters, 1997
G. Shaked, A. Taraboulos, R. Gabizon
exaly   +2 more sources

Spontaneous conversion of PrPC to PrPSc [PDF]

FEBS Letters, 1992
Octa-repeats of prion proteins (PrP) contain histidine and tryptophan residues which are known to function as ligands for transition metals. It is proposed that the spontaneous conversion of the PrPC (cellular) isoform into PrPSc (scrapie) isoform may be
E Sulkowski
exaly   +2 more sources

Recombinant PrPSc shares structural features with brain-derived PrPSc: Insights from limited proteolysis [PDF]

PLoS Pathogens, 2018
Very solid evidence suggests that the core of full length PrPSc is a 4-rung β-solenoid, and that individual PrPSc subunits stack to form amyloid fibers. We recently used limited proteolysis to map the β-strands and connecting loops that make up the PrPSc
Natalia Fernández-Borges, Saioa R Elezgarai, Romolo Nonno   +2 more
exaly   +5 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

[Establishment of a protein misfolding cyclic amplification for PrPSc].

Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology, 2009
To establish a methodology of protein misfolding cyclic amplification (PMCA) and utilize in the detection of PrP(Sc) in brain tissues from prion diseases.Different amounts of Scrapie 263K agent bulk were mixed with brain homogenates of health hamsters and treated with repeated incubation/sonication for 10 to 15 cycles. The proteinase K-resistant PrP(Sc)
Jun, Han, Lu, Han, Qi, Shi, Song, Shi, Xin, Wang, Bao-Yun, Zhang, Xiao-Ping, Dong   +6 more
openaire   +1 more source

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
openaire   +2 more sources