| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Séverine Martin-Lannerée, Théo Z Hirsch, Julia Hernandez-Rapp, Sophie Halliez, Jean-Luc Vilotte, Jean-Marie Launay, Sophie Mouillet-Richar. PrP(C) from stem cells to cancer. Frontiers in cell and developmental biology. vol 2. 2014-11-03. PMID:25364760. |
the cellular prion protein prp(c) was initially discovered as the normal counterpart of the pathological scrapie prion protein prp(sc), the main component of the infectious agent of transmissible spongiform encephalopathies. |
2014-11-03 |
2023-08-13 |
mouse |
| Alana M Thackray, Ying Di, Chang Zhang, Hanna Wolf, Lydia Pradl, Ina Vorberg, Olivier Andréoletti, Raymond Bujdos. Prion-induced and spontaneous formation of transmissible toxicity in PrP transgenic Drosophila. The Biochemical journal. vol 463. issue 1. 2014-10-31. PMID:25000212. |
central to these conditions is the conversion of the normal host prion protein prp(c) into the abnormal prion conformer prp(sc). |
2014-10-31 |
2023-08-13 |
drosophila_melanogaster |
| Alana M Thackray, Ying Di, Chang Zhang, Hanna Wolf, Lydia Pradl, Ina Vorberg, Olivier Andréoletti, Raymond Bujdos. Prion-induced and spontaneous formation of transmissible toxicity in PrP transgenic Drosophila. The Biochemical journal. vol 463. issue 1. 2014-10-31. PMID:25000212. |
proteinase k-resistant prp(sc) was detected by protein misfolding cyclic amplification in prion-exposed drosophila transgenic for membrane-targeted prp. |
2014-10-31 |
2023-08-13 |
drosophila_melanogaster |
| Pravas Kumar Baral, Mridula Swayampakula, Manoj Kumar Rout, Nat N V Kav, Leo Spyracopoulos, Adriano Aguzzi, Michael N G Jame. Structural basis of prion inhibition by phenothiazine compounds. Structure (London, England : 1993). vol 22. issue 2. 2014-10-22. PMID:24373770. |
conformational transitions of the cellular form of the prion protein, prp(c), into an infectious isoform, prp(sc), are considered to be central events in the progression of fatal neurodegenerative diseases known as transmissible spongiform encephalopathies. |
2014-10-22 |
2023-08-12 |
mouse |
| Pravas Kumar Baral, Mridula Swayampakula, Manoj Kumar Rout, Nat N V Kav, Leo Spyracopoulos, Adriano Aguzzi, Michael N G Jame. Structural basis of prion inhibition by phenothiazine compounds. Structure (London, England : 1993). vol 22. issue 2. 2014-10-22. PMID:24373770. |
tricyclic phenothiazine compounds exhibit antiprion activity; however, the underlying molecular mechanism of prp(sc) inhibition remains elusive. |
2014-10-22 |
2023-08-12 |
mouse |
| Morikazu Imamura, Nobuko Kato, Hiroyuki Okada, Miyako Yoshioka, Yoshifumi Iwamaru, Yoshihisa Shimizu, Shirou Mohri, Takashi Yokoyama, Yuichi Murayam. Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins. PloS one. vol 8. issue 12. 2014-10-08. PMID:24367521. |
the central event in prion infection is the conformational conversion of host-encoded cellular prion protein (prp(c)) into the pathogenic isoform (prp(sc)). |
2014-10-08 |
2023-08-12 |
mouse |
| Morikazu Imamura, Nobuko Kato, Hiroyuki Okada, Miyako Yoshioka, Yoshifumi Iwamaru, Yoshihisa Shimizu, Shirou Mohri, Takashi Yokoyama, Yuichi Murayam. Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins. PloS one. vol 8. issue 12. 2014-10-08. PMID:24367521. |
diverse mammalian species possess the cofactors required for in vitro replication of prp(sc) by protein-misfolding cyclic amplification (pmca), but lower organisms, such as bacteria, yeasts, and insects, reportedly lack the essential cofactors. |
2014-10-08 |
2023-08-12 |
mouse |
| Morikazu Imamura, Nobuko Kato, Hiroyuki Okada, Miyako Yoshioka, Yoshifumi Iwamaru, Yoshihisa Shimizu, Shirou Mohri, Takashi Yokoyama, Yuichi Murayam. Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins. PloS one. vol 8. issue 12. 2014-10-08. PMID:24367521. |
mammalian prp(sc) seeds and bac-prp(sc) generated by pmca using bac-prp and insect cell-derived cofactors showed similar pathogenicity and produced very similar lesions in the brains of inoculated mice. |
2014-10-08 |
2023-08-12 |
mouse |
| Morikazu Imamura, Nobuko Kato, Hiroyuki Okada, Miyako Yoshioka, Yoshifumi Iwamaru, Yoshihisa Shimizu, Shirou Mohri, Takashi Yokoyama, Yuichi Murayam. Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins. PloS one. vol 8. issue 12. 2014-10-08. PMID:24367521. |
these results suggested that the essential cofactors required for the high-fidelity replication of mammalian prp(sc) were present in the insect cells but that the cofactor activity was masked or inhibited in the native state. |
2014-10-08 |
2023-08-12 |
mouse |
| Morikazu Imamura, Nobuko Kato, Hiroyuki Okada, Miyako Yoshioka, Yoshifumi Iwamaru, Yoshihisa Shimizu, Shirou Mohri, Takashi Yokoyama, Yuichi Murayam. Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins. PloS one. vol 8. issue 12. 2014-10-08. PMID:24367521. |
pmca using only insect cell-derived substances (ipmca) was highly useful for the ultrasensitive detection of prp(sc) of some prion strains. |
2014-10-08 |
2023-08-12 |
mouse |
| Matthias Schmitz, Katharina Lüllmann, Saima Zafar, Elisabeth Ebert, Marie Wohlhage, Panteleimon Oikonomou, Markus Schlomm, Eva Mitrova, Michael Beekes, Inga Zer. Association of prion protein genotype and scrapie prion protein type with cellular prion protein charge isoform profiles in cerebrospinal fluid of humans with sporadic or familial prion diseases. Neurobiology of aging. vol 35. issue 5. 2014-10-06. PMID:24360565. |
the present study investigates whether posttranslational modifications of cellular prion protein (prp(c)) in the cerebrospinal fluid (csf) of humans with prion diseases are associated with methionine (m) and/or valine (v) polymorphism at codon 129 of the prion protein gene (prnp), scrapie prion protein (prp(sc)) type in sporadic creutzfeldt-jakob disease (scjd), or prnp mutations in familial creutzfeldt-jakob disease (fcjd/e200k), and fatal familial insomnia (ffi). |
2014-10-06 |
2023-08-12 |
Not clear |
| Matthias Schmitz, Katharina Lüllmann, Saima Zafar, Elisabeth Ebert, Marie Wohlhage, Panteleimon Oikonomou, Markus Schlomm, Eva Mitrova, Michael Beekes, Inga Zer. Association of prion protein genotype and scrapie prion protein type with cellular prion protein charge isoform profiles in cerebrospinal fluid of humans with sporadic or familial prion diseases. Neurobiology of aging. vol 35. issue 5. 2014-10-06. PMID:24360565. |
of the 12 most abundant prp(c) isoforms in the examined csf, one (if12) was relatively decreased in (1) scjd with vv (vs. mm or mv) at prnp codon 129; (2) in scjd with prp(sc) type 2 (vs. prp(sc) type 1); and (3) in ffi versus scjd or fcjd. |
2014-10-06 |
2023-08-12 |
Not clear |
| Tuane C R G Vieira, Yraima Cordeiro, Byron Caughey, Jerson L Silv. Heparin binding confers prion stability and impairs its aggregation. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. vol 28. issue 6. 2014-10-06. PMID:24648544. |
the conversion of the prion protein (prp) into scrapie prp (prp(sc)) is a central event in prion diseases. |
2014-10-06 |
2023-08-12 |
mouse |
| Yuichi Koga, Shun-ichi Tanaka, Akikazu Sakudo, Minoru Tobiume, Mutsuo Aranishi, Azumi Hirata, Kazufumi Takano, Kazuyoshi Ikuta, Shigenori Kanay. Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1. Applied microbiology and biotechnology. vol 98. issue 5. 2014-10-03. PMID:23880875. |
the abnormal prion protein (scrapie-associated prion protein, prp(sc)) is considered to be included in the group of infectious agents of transmissible spongiform encephalopathies. |
2014-10-03 |
2023-08-12 |
Not clear |
| Yuichi Koga, Shun-ichi Tanaka, Akikazu Sakudo, Minoru Tobiume, Mutsuo Aranishi, Azumi Hirata, Kazufumi Takano, Kazuyoshi Ikuta, Shigenori Kanay. Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1. Applied microbiology and biotechnology. vol 98. issue 5. 2014-10-03. PMID:23880875. |
since prp(sc) is highly resistant to normal sterilization procedures, the decontamination of prp(sc) is a significant public health issue. |
2014-10-03 |
2023-08-12 |
Not clear |
| Yuichi Koga, Shun-ichi Tanaka, Akikazu Sakudo, Minoru Tobiume, Mutsuo Aranishi, Azumi Hirata, Kazufumi Takano, Kazuyoshi Ikuta, Shigenori Kanay. Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1. Applied microbiology and biotechnology. vol 98. issue 5. 2014-10-03. PMID:23880875. |
in the present study, a hyperthermostable protease, tk-subtilisin, was used to degrade prp(sc). |
2014-10-03 |
2023-08-12 |
Not clear |
| Yuichi Koga, Shun-ichi Tanaka, Akikazu Sakudo, Minoru Tobiume, Mutsuo Aranishi, Azumi Hirata, Kazufumi Takano, Kazuyoshi Ikuta, Shigenori Kanay. Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1. Applied microbiology and biotechnology. vol 98. issue 5. 2014-10-03. PMID:23880875. |
although prp(sc) is known to be resistant toward proteolytic enzymes, tk-subtilisin was able to degrade prp(sc) under extreme conditions. |
2014-10-03 |
2023-08-12 |
Not clear |
| Yuichi Koga, Shun-ichi Tanaka, Akikazu Sakudo, Minoru Tobiume, Mutsuo Aranishi, Azumi Hirata, Kazufumi Takano, Kazuyoshi Ikuta, Shigenori Kanay. Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1. Applied microbiology and biotechnology. vol 98. issue 5. 2014-10-03. PMID:23880875. |
the level of prp(sc) in brain homogenates was found to decrease significantly in vitro following tk-subtilisin treatment at 100 °c, whereas some protease-resistant fractions remain after proteinase k treatment. |
2014-10-03 |
2023-08-12 |
Not clear |
| Yuichi Koga, Shun-ichi Tanaka, Akikazu Sakudo, Minoru Tobiume, Mutsuo Aranishi, Azumi Hirata, Kazufumi Takano, Kazuyoshi Ikuta, Shigenori Kanay. Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1. Applied microbiology and biotechnology. vol 98. issue 5. 2014-10-03. PMID:23880875. |
rather small amounts of tk-subtilisin (0.3 u) were required to degrade prp(sc) at 100 °c and ph 8.0. |
2014-10-03 |
2023-08-12 |
Not clear |
| Yuichi Koga, Shun-ichi Tanaka, Akikazu Sakudo, Minoru Tobiume, Mutsuo Aranishi, Azumi Hirata, Kazufumi Takano, Kazuyoshi Ikuta, Shigenori Kanay. Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1. Applied microbiology and biotechnology. vol 98. issue 5. 2014-10-03. PMID:23880875. |
in addition, tk-subtilisin was observed to degrade prp(sc) in the presence of sodium dodecyl sulfate or other industrial surfactants. |
2014-10-03 |
2023-08-12 |
Not clear |