| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Fozia Saleem, Trent C Bjorndahl, Carol L Ladner, Rolando Perez-Pineiro, Burim N Ametaj, David S Wishar. Lipopolysaccharide induced conversion of recombinant prion protein. Prion. vol 8. issue 2. 2015-04-15. PMID:24819168. |
in our ongoing efforts to look for endogenous and exogenous chemical mediators that might initiate, influence, or result in the natural conversion of prp(c) to prp(sc), we discovered that lipopolysaccharide (lps), a component of gram-negative bacterial membranes interacts with recombinant prion proteins and induces conversion to an isoform richer in β sheet at near physiological conditions as long as the lps concentration remains above the critical micelle concentration (cmc). |
2015-04-15 |
2023-08-13 |
Not clear |
| Katsuya Sato. [CSF analysis of patients with prion disease by biomarkers and real-time qucking-induced conversion (RT-QUIC) method]. Rinsho shinkeigaku = Clinical neurology. vol 23. issue 11. 2015-04-13. PMID:24291947. |
in other hand we recently developed a new in vitro amplification technology, designated "rt-quic assay", for the detection of prp(sc) in csf of scjd. |
2015-04-13 |
2023-08-12 |
human |
| Silvia M Bacot, Gerald M Feldman, Kenneth M Yamada, Subhash Dhawa. Pathogenic prion protein fragment (PrP106-126) promotes human immunodeficiency virus type-1 infection in peripheral blood monocyte-derived macrophages. Virology. vol 476. 2015-04-13. PMID:25589240. |
transfusion of blood and blood products contaminated with the pathogenic form of prion protein prp(sc), thought to be the causative agent of variant a creutzfeldt-jakob disease (vcjd), may result in serious consequences in recipients with a compromised immune system, for example, as seen in hiv-1 infection. |
2015-04-13 |
2023-08-13 |
human |
| Silvia M Bacot, Gerald M Feldman, Kenneth M Yamada, Subhash Dhawa. Pathogenic prion protein fragment (PrP106-126) promotes human immunodeficiency virus type-1 infection in peripheral blood monocyte-derived macrophages. Virology. vol 476. 2015-04-13. PMID:25589240. |
in the present study, we demonstrate that treatment of peripheral blood monocyte-derived macrophages (mdm) with prp106-126, a synthetic domain of prp(sc) that has intrinsic functional activities related to the full-length protein, markedly increased their susceptibility to hiv-1 infection, induced cytokine secretion, and enhanced their migratory behavior in response to n-formyl-l-methionyl-l-leucyl-l-phenylalanine (fmlp). |
2015-04-13 |
2023-08-13 |
human |
| H Okada, Y Iwamaru, T Yokoyama, S Mohr. Immunohistochemical detection of disease-associated prion protein in the peripheral nervous system in experimental H-type bovine spongiform encephalopathy. Veterinary pathology. vol 50. issue 4. 2015-04-10. PMID:23269348. |
to determine the localization of disease-associated prion protein (prp(sc)) in the peripheral nerve tissues of cattle affected with h-type bse, we employed highly sensitive immunohistochemical and immunofluorescence techniques with the tyramide signal amplification (tsa) system. |
2015-04-10 |
2023-08-12 |
cattle |
| H Okada, Y Iwamaru, T Yokoyama, S Mohr. Immunohistochemical detection of disease-associated prion protein in the peripheral nervous system in experimental H-type bovine spongiform encephalopathy. Veterinary pathology. vol 50. issue 4. 2015-04-10. PMID:23269348. |
prp(sc) deposition was detected in the inferior ganglia, sympathetic nerve trunk, vagus nerve, spinal nerves, cauda equina, and adrenal medulla, using this system. |
2015-04-10 |
2023-08-12 |
cattle |
| H Okada, Y Iwamaru, T Yokoyama, S Mohr. Immunohistochemical detection of disease-associated prion protein in the peripheral nervous system in experimental H-type bovine spongiform encephalopathy. Veterinary pathology. vol 50. issue 4. 2015-04-10. PMID:23269348. |
notably, granular prp(sc) deposits were present mainly in the schwann cells and fibroblast-like cells and occasionally along certain nerve fibers at the surface of the axons. |
2015-04-10 |
2023-08-12 |
cattle |
| H Okada, Y Iwamaru, T Yokoyama, S Mohr. Immunohistochemical detection of disease-associated prion protein in the peripheral nervous system in experimental H-type bovine spongiform encephalopathy. Veterinary pathology. vol 50. issue 4. 2015-04-10. PMID:23269348. |
in the adrenal gland, prp(sc) immunolabeling was observed within the sympathetic nerve fibers and nerve endings in the adrenal medulla. |
2015-04-10 |
2023-08-12 |
cattle |
| Carlos Hedman, Jaber Lyahyai, Hicham Filali, Belén Marín, Carmen Serrano, Eva Monleón, Bernardino Moreno, Pilar Zaragoza, Juan José Badiola, Inmaculada Martín-Burriel, Rosa Bole. Differential gene expression and apoptosis markers in presymptomatic scrapie affected sheep. Veterinary microbiology. vol 159. issue 1-2. 2015-04-07. PMID:22482719. |
the histopathology, immunolabelling of prp(sc), bax and activated caspase-3, and the analysis of the expression of 7 genes involved in the regulation of the mitochondrial pathway of apoptosis were investigated in the following 4 central nervous system areas: medulla oblongata, diencephalon, frontal cortex and cerebellum. |
2015-04-07 |
2023-08-12 |
Not clear |
| Carlos Hedman, Jaber Lyahyai, Hicham Filali, Belén Marín, Carmen Serrano, Eva Monleón, Bernardino Moreno, Pilar Zaragoza, Juan José Badiola, Inmaculada Martín-Burriel, Rosa Bole. Differential gene expression and apoptosis markers in presymptomatic scrapie affected sheep. Veterinary microbiology. vol 159. issue 1-2. 2015-04-07. PMID:22482719. |
the prp(sc) immunolabelling in the four areas, as well as a neuropil spongiform change, were more evident in the terminal stage than in presymptomatic animals. |
2015-04-07 |
2023-08-12 |
Not clear |
| Marcela Cristina de Moraes, Juliana Bosco Santos, Daniel Meira Dos Anjos, Luciana Pereira Rangel, Tuane Cristine Ramos Gonçalves Vieira, Ruin Moaddel, Jerson Lima da Silv. Prion protein-coated magnetic beads: synthesis, characterization and development of a new ligands screening method. Journal of chromatography. A. vol 1379. 2015-04-01. PMID:25576041. |
conversion of the native prion protein (prp(c)) into the abnormal scrapie prp isoform (prp(sc)), which undergoes aggregation and can eventually form amyloid fibrils, is a critical step leading to the characteristic path morphological hallmark of these diseases. |
2015-04-01 |
2023-08-13 |
Not clear |
| Marcela Cristina de Moraes, Juliana Bosco Santos, Daniel Meira Dos Anjos, Luciana Pereira Rangel, Tuane Cristine Ramos Gonçalves Vieira, Ruin Moaddel, Jerson Lima da Silv. Prion protein-coated magnetic beads: synthesis, characterization and development of a new ligands screening method. Journal of chromatography. A. vol 1379. 2015-04-01. PMID:25576041. |
it is known that ligands can act as cofactors or inhibitors in the conversion mechanism of prp(c) into prp(sc). |
2015-04-01 |
2023-08-13 |
Not clear |
| Aleksandr A Rubel, Tatyana A Ryzhova, Kirill S Antonets, Yury O Chernoff, Alexey Galki. Identification of PrP sequences essential for the interaction between the PrP polymers and Aβ peptide in a yeast-based assay. Prion. vol 7. issue 6. 2015-03-30. PMID:24152606. |
polymeric form of prion protein (prp), prp(sc), is implicated in transmissible spongiform encephalopathies (tses). |
2015-03-30 |
2023-08-12 |
Not clear |
| Aleksandr A Rubel, Tatyana A Ryzhova, Kirill S Antonets, Yury O Chernoff, Alexey Galki. Identification of PrP sequences essential for the interaction between the PrP polymers and Aβ peptide in a yeast-based assay. Prion. vol 7. issue 6. 2015-03-30. PMID:24152606. |
on the other hand, prp(sc) polymers efficiently bind to aβ monomers and accelerate their oligomerization. |
2015-03-30 |
2023-08-12 |
Not clear |
| Chrysanthi Berberidou, Konstantinos Xanthopoulos, Ioannis Paspaltsis, Athanasios Lourbopoulos, Eleni Polyzoidou, Theodoros Sklaviadis, Ioannis Poulio. Homogenous photocatalytic decontamination of prion infected stainless steel and titanium surfaces. Prion. vol 7. issue 6. 2015-03-30. PMID:24247293. |
interestingly, photocatalytic treatment of 263k infected titanium wires, under the same experimental conditions, prolonged the survival interval significantly, but failed to eliminate infectivity, a result that we correlate with the increased adsorption of prp(sc) on titanium, in comparison to stainless steel. |
2015-03-30 |
2023-08-12 |
Not clear |
| Heinz Amenitsch, Federico Benetti, Adriana Ramos, Giuseppe Legname, Jesús R Requen. SAXS structural study of PrP(Sc) reveals ~11 nm diameter of basic double intertwined fibers. Prion. vol 7. issue 6. 2015-03-30. PMID:24247356. |
saxs structural study of prp(sc) reveals ~11 nm diameter of basic double intertwined fibers. |
2015-03-30 |
2023-08-12 |
Not clear |
| Heinz Amenitsch, Federico Benetti, Adriana Ramos, Giuseppe Legname, Jesús R Requen. SAXS structural study of PrP(Sc) reveals ~11 nm diameter of basic double intertwined fibers. Prion. vol 7. issue 6. 2015-03-30. PMID:24247356. |
this measurement offers an estimation of the diameter of prp(sc) fibers in suspension, i.e., free of errors derived from estimations based on 2d projections in transmission electron microscopy images, subjected to further possible distortions from the negative stain. |
2015-03-30 |
2023-08-12 |
Not clear |
| Heinz Amenitsch, Federico Benetti, Adriana Ramos, Giuseppe Legname, Jesús R Requen. SAXS structural study of PrP(Sc) reveals ~11 nm diameter of basic double intertwined fibers. Prion. vol 7. issue 6. 2015-03-30. PMID:24247356. |
this diameter, which corresponds to a maximum diameter of approximately 5.5 nm for each of the two intertwined protofilaments making up the fibers, rules out the possibility that prp(sc) conforms to a stack of in-register, single-rung flat prp(sc) monomers; rather, prp(sc) subunits must necessarily coil, most likely several times, into themselves. |
2015-03-30 |
2023-08-12 |
Not clear |
| Yuzuru Taguchi, Hermann M Schätz. Identifying critical sites of PrP(c)-PrP(Sc) interaction in prion-infected cells by dominant-negative inhibition. Prion. vol 7. issue 6. 2015-03-30. PMID:24401595. |
identifying critical sites of prp(c)-prp(sc) interaction in prion-infected cells by dominant-negative inhibition. |
2015-03-30 |
2023-08-12 |
Not clear |
| Yuzuru Taguchi, Hermann M Schätz. Identifying critical sites of PrP(c)-PrP(Sc) interaction in prion-infected cells by dominant-negative inhibition. Prion. vol 7. issue 6. 2015-03-30. PMID:24401595. |
we hypothesized that structural changes induced by prp(sc) interaction occur in more than one interface and subsequently propagate within the prp(c) substrate, like epicenters of structural changes. |
2015-03-30 |
2023-08-12 |
Not clear |