| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Rob Goold, Chris McKinnon, Samira Rabbanian, John Collinge, Giampietro Schiavo, Sarah J Tabriz. Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane. Journal of cell science. vol 126. issue Pt 16. 2014-06-15. PMID:23813960. |
we have recently generated a unique cell system in which epitope-tagged prp(c) competent to produce bona fide prp(sc) is expressed in neuroblastoma cells. |
2014-06-15 |
2023-08-12 |
human |
| Rob Goold, Chris McKinnon, Samira Rabbanian, John Collinge, Giampietro Schiavo, Sarah J Tabriz. Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane. Journal of cell science. vol 126. issue Pt 16. 2014-06-15. PMID:23813960. |
using this system we demonstrated that prp(sc) forms on the cell surface within minutes of prion exposure. |
2014-06-15 |
2023-08-12 |
human |
| Rob Goold, Chris McKinnon, Samira Rabbanian, John Collinge, Giampietro Schiavo, Sarah J Tabriz. Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane. Journal of cell science. vol 126. issue Pt 16. 2014-06-15. PMID:23813960. |
here, we describe the intracellular trafficking of newly formed prp(sc). |
2014-06-15 |
2023-08-12 |
human |
| Rob Goold, Chris McKinnon, Samira Rabbanian, John Collinge, Giampietro Schiavo, Sarah J Tabriz. Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane. Journal of cell science. vol 126. issue Pt 16. 2014-06-15. PMID:23813960. |
after formation in gm1-enriched lipid microdomains at the plasma membrane, prp(sc) is rapidly internalised to early endosomes containing transferrin and cholera toxin b subunit. |
2014-06-15 |
2023-08-12 |
human |
| Rob Goold, Chris McKinnon, Samira Rabbanian, John Collinge, Giampietro Schiavo, Sarah J Tabriz. Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane. Journal of cell science. vol 126. issue Pt 16. 2014-06-15. PMID:23813960. |
following endocytosis, prp(sc) intracellular trafficking diverges: some is recycled to the plasma membrane via rab11-labelled recycling endosomes; the remaining prp(sc) is subject to retromer-mediated retrograde transport to the golgi. |
2014-06-15 |
2023-08-12 |
human |
| Rob Goold, Chris McKinnon, Samira Rabbanian, John Collinge, Giampietro Schiavo, Sarah J Tabriz. Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane. Journal of cell science. vol 126. issue Pt 16. 2014-06-15. PMID:23813960. |
this pathway leads to lysosomal degradation, and we show that this is the dominant prp(sc) degradative mechanism in the early stages of prion infection. |
2014-06-15 |
2023-08-12 |
human |
| Yuko Ushiki-Kaku, Yoshifumi Iwamaru, Kentaro Masujin, Morikazu Imamura, Shigeyoshi Itohara, Kiyoko Ogawa-Goto, Shunji Hattori, Takashi Yokoyam. Different antigenicities of the N-terminal region of cellular and scrapie prion proteins. Microbiology and immunology. vol 57. issue 11. 2014-06-12. PMID:24117858. |
limited information is available about conformational differences between the abnormal isoform of prion protein (prp(sc) ) and cellular prion protein (prp(c) ) under native conditions. |
2014-06-12 |
2023-08-12 |
mouse |
| Yuko Ushiki-Kaku, Yoshifumi Iwamaru, Kentaro Masujin, Morikazu Imamura, Shigeyoshi Itohara, Kiyoko Ogawa-Goto, Shunji Hattori, Takashi Yokoyam. Different antigenicities of the N-terminal region of cellular and scrapie prion proteins. Microbiology and immunology. vol 57. issue 11. 2014-06-12. PMID:24117858. |
peptide array analysis of these serum samples revealed a distinctive epitope of prp(sc) consisting of qgspggn (prp41-47) at the n-terminus. |
2014-06-12 |
2023-08-12 |
mouse |
| Yuko Ushiki-Kaku, Yoshifumi Iwamaru, Kentaro Masujin, Morikazu Imamura, Shigeyoshi Itohara, Kiyoko Ogawa-Goto, Shunji Hattori, Takashi Yokoyam. Different antigenicities of the N-terminal region of cellular and scrapie prion proteins. Microbiology and immunology. vol 57. issue 11. 2014-06-12. PMID:24117858. |
this study demonstrated a conformational dissimilarity at the n-terminus between prp(sc) and prp(c) , a finding that may provide novel information about conformational features of prp(sc) . |
2014-06-12 |
2023-08-12 |
mouse |
| Gabor G Kovacs, Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles. The American journal of pathology. vol 183. issue 5. 2014-06-10. PMID:24012784. |
the relationship between atypical prpres and prp(sc), and their role in etiology of prion diseases, remains unknown. |
2014-06-10 |
2023-08-12 |
Not clear |
| Gabor G Kovacs, Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles. The American journal of pathology. vol 183. issue 5. 2014-06-10. PMID:24012784. |
we examined the relationship between prp(sc) and atypical prpres, a form characterized by short c-terminal proteinase k-resistant fragments, in a prion strain of synthetic origin. |
2014-06-10 |
2023-08-12 |
Not clear |
| Gabor G Kovacs, Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles. The American journal of pathology. vol 183. issue 5. 2014-06-10. PMID:24012784. |
unlike prp(sc), atypical prpres did not show significant perineuronal, vascular, or perivascular immunoreactivity. |
2014-06-10 |
2023-08-12 |
Not clear |
| Claudia A Madampage, Pekka Määttänen, Kristen Marciniuk, Robert Brownlie, Olga Andrievskaia, Andrew Potter, Neil R Cashman, Jeremy S Lee, Scott Nappe. Binding of bovine T194A PrP(C) by PrP(Sc)-specific antibodies: potential implications for immunotherapy of familial prion diseases. Prion. vol 7. issue 4. 2014-06-09. PMID:23787697. |
binding of bovine t194a prp(c) by prp(sc)-specific antibodies: potential implications for immunotherapy of familial prion diseases. |
2014-06-09 |
2023-08-12 |
human |
| Claudia A Madampage, Pekka Määttänen, Kristen Marciniuk, Robert Brownlie, Olga Andrievskaia, Andrew Potter, Neil R Cashman, Jeremy S Lee, Scott Nappe. Binding of bovine T194A PrP(C) by PrP(Sc)-specific antibodies: potential implications for immunotherapy of familial prion diseases. Prion. vol 7. issue 4. 2014-06-09. PMID:23787697. |
transmissible spongiform encephalopathies (tses) are fatal neurodegenerative diseases that are based on the misfolding of a cellular prion protein (prp(c)) into an infectious, pathological conformation (prp(sc)). |
2014-06-09 |
2023-08-12 |
human |
| Claudia A Madampage, Pekka Määttänen, Kristen Marciniuk, Robert Brownlie, Olga Andrievskaia, Andrew Potter, Neil R Cashman, Jeremy S Lee, Scott Nappe. Binding of bovine T194A PrP(C) by PrP(Sc)-specific antibodies: potential implications for immunotherapy of familial prion diseases. Prion. vol 7. issue 4. 2014-06-09. PMID:23787697. |
by targeting epitopes that are specifically exposed upon protein misfolding, our group developed a vaccine that induces prp(sc)-specific antibody responses. |
2014-06-09 |
2023-08-12 |
human |
| Midori Suenaga, Yusuke Hiramoto, Yoichi Matsunag. Vitamin D 2 interacts with Human PrP(c) (90-231) and breaks PrP(c) oligomerization in vitro. Prion. vol 7. issue 4. 2014-06-09. PMID:23857314. |
prp(sc), the pathogenic isoform of prp(c), can convert prp(c) into prp(sc) through direct interactions. |
2014-06-09 |
2023-08-12 |
human |
| Midori Suenaga, Yusuke Hiramoto, Yoichi Matsunag. Vitamin D 2 interacts with Human PrP(c) (90-231) and breaks PrP(c) oligomerization in vitro. Prion. vol 7. issue 4. 2014-06-09. PMID:23857314. |
prp(c) oligomerization is a required processing step before prp(sc) formation, and soluble oligomers appear to be the toxic species in amyloid-related disorders. |
2014-06-09 |
2023-08-12 |
human |
| Thorsten Kuczius, Martin H Groschu. Cellular prion proteins in humans and cattle but not sheep are characterized by a low-solubility phenotype. Comparative immunology, microbiology and infectious diseases. vol 36. issue 6. 2014-06-09. PMID:23948376. |
a feature of transmissible spongiform encephalopathies is the accumulation of infectious prion proteins (prp(sc)), which are formed by the conversion of physiological prion proteins (prp(c)). |
2014-06-09 |
2023-08-12 |
human |
| Thorsten Kuczius, Martin H Groschu. Cellular prion proteins in humans and cattle but not sheep are characterized by a low-solubility phenotype. Comparative immunology, microbiology and infectious diseases. vol 36. issue 6. 2014-06-09. PMID:23948376. |
as prp(c), which is modified posttranslationally with various types of glycoproteins, serves as the substrates for prp(sc) conversion, various prp(c) subtypes may play a role in the formation of prp(sc) and species-specific transmission; the cattle disease bse is transmissible naturally to humans, but the sheep disease scrapie is not. |
2014-06-09 |
2023-08-12 |
human |
| Xuesong Wang, Bingbing Zhang, Cong Zhao, Yanli Wang, Lei He, Menghan Cui, Xiaotong Zhu, Weihong D. Inhibition of human prion neuropeptide PrP106-126 aggregation by hexacoordinated ruthenium complexes. Journal of inorganic biochemistry. vol 128. 2014-06-07. PMID:23911565. |
the aberrant isoform of prion protein prp(sc) has been identified as the infectious agent. |
2014-06-07 |
2023-08-12 |
human |