| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Daniela Veber, Giuseppe Scalabrin. Are PrP(C)s involved in some human myelin diseases? Relating experimental studies to human pathology. Journal of the neurological sciences. vol 359. issue 1-2. 2016-09-29. PMID:26478128. |
we have experimentally demonstrated that cobalamin (cbl) deficiency increases normal cellular prion (prp(c)) levels in rat spinal cord (sc) and cerebrospinal fluid (csf), and decreases prp(c)-mrna levels in rat sc. |
2016-09-29 |
2023-08-13 |
human |
| Daniela Veber, Giuseppe Scalabrin. Are PrP(C)s involved in some human myelin diseases? Relating experimental studies to human pathology. Journal of the neurological sciences. vol 359. issue 1-2. 2016-09-29. PMID:26478128. |
repeated intracerebroventricular administrations of anti-octapeptide repeat-prp(c)-region antibodies to cbl-deficient (cbl-d) rats prevent sc myelin lesions, and the administrations of prp(c)s to otherwise normal rats cause sc white matter lesions similar to those induced by cbl deficiency. |
2016-09-29 |
2023-08-13 |
human |
| Daniela Veber, Giuseppe Scalabrin. Are PrP(C)s involved in some human myelin diseases? Relating experimental studies to human pathology. Journal of the neurological sciences. vol 359. issue 1-2. 2016-09-29. PMID:26478128. |
cbl positively regulates sc prp(c) synthesis in rat by stimulating the local synthesis of epidermal growth factor (egf), which also induces the local synthesis of prp(c)-mrnas, and downregulating the local synthesis of tumor necrosis factor(tnf)-α, thus preventing local prp(c) overproduction. |
2016-09-29 |
2023-08-13 |
human |
| Daniela Veber, Giuseppe Scalabrin. Are PrP(C)s involved in some human myelin diseases? Relating experimental studies to human pathology. Journal of the neurological sciences. vol 359. issue 1-2. 2016-09-29. PMID:26478128. |
we have clinically demonstrated that prp(c) levels are increased in the csf of patients with subacute combined degeneration (scd), unchanged in the csf of patients with alzheimer's disease and amyotrophic lateral sclerosis, and decreased in the csf and sc of patients with multiple sclerosis (ms), regardless of its clinical course. |
2016-09-29 |
2023-08-13 |
human |
| Ana Paula Lappas Gimenez, Larissa Morato Luciani Richter, Mariana Campos Atherino, Breno Castello Branco Beirão, Celso Fávaro, Michele Dietrich Moura Costa, Silvio Marques Zanata, Bettina Malnic, Adriana Frohlich Mercadant. Identification of novel putative-binding proteins for cellular prion protein and a specific interaction with the STIP1 homology and U-Box-containing protein 1. Prion. vol 9. issue 5. 2016-09-26. PMID:26237451. |
prion diseases involve the conversion of the endogenous cellular prion protein, prp(c), into a misfolded infectious isoform, prp(sc). |
2016-09-26 |
2023-08-13 |
mouse |
| Maria Laura Bolognesi, Salvatore Bongarzone, Suzana Aulic, Hoang Ngoc Ai Tran, Federica Prati, Paolo Carloni, Giuseppe Legnam. Rational approach to an antiprion compound with a multiple mechanism of action. Future medicinal chemistry. vol 7. issue 16. 2016-09-26. PMID:26511069. |
the main pathogenic event of prion disorders has been identified in the deposition of the disease-associated prion protein (prp(sc)), which is accompanied by metal dyshomeostasis. |
2016-09-26 |
2023-08-13 |
Not clear |
| Kohtaro Miyazawa, Hiroyuki Okada, Kentaro Masujin, Yoshifumi Iwamaru, Takashi Yokoyam. Infectivity-associated PrP(Sc) and disease duration-associated PrP(Sc) of mouse BSE prions. Prion. vol 9. issue 5. 2016-09-26. PMID:26555211. |
infectivity-associated prp(sc) and disease duration-associated prp(sc) of mouse bse prions. |
2016-09-26 |
2023-08-13 |
mouse |
| Kohtaro Miyazawa, Hiroyuki Okada, Kentaro Masujin, Yoshifumi Iwamaru, Takashi Yokoyam. Infectivity-associated PrP(Sc) and disease duration-associated PrP(Sc) of mouse BSE prions. Prion. vol 9. issue 5. 2016-09-26. PMID:26555211. |
disease-related prion protein (prp(sc)), which is a structural isoform of the host-encoded cellular prion protein, is thought to be a causative agent of transmissible spongiform encephalopathies. |
2016-09-26 |
2023-08-13 |
mouse |
| Kohtaro Miyazawa, Hiroyuki Okada, Kentaro Masujin, Yoshifumi Iwamaru, Takashi Yokoyam. Infectivity-associated PrP(Sc) and disease duration-associated PrP(Sc) of mouse BSE prions. Prion. vol 9. issue 5. 2016-09-26. PMID:26555211. |
however, the specific role of prp(sc) in prion pathogenesis and its relationship to infectivity remain controversial. |
2016-09-26 |
2023-08-13 |
mouse |
| Kohtaro Miyazawa, Hiroyuki Okada, Kentaro Masujin, Yoshifumi Iwamaru, Takashi Yokoyam. Infectivity-associated PrP(Sc) and disease duration-associated PrP(Sc) of mouse BSE prions. Prion. vol 9. issue 5. 2016-09-26. PMID:26555211. |
a time-course study of prion-affected mice was conducted, which showed that the prion infectivity was not simply proportional to the amount of prp(sc) in the brain. |
2016-09-26 |
2023-08-13 |
mouse |
| Kohtaro Miyazawa, Hiroyuki Okada, Kentaro Masujin, Yoshifumi Iwamaru, Takashi Yokoyam. Infectivity-associated PrP(Sc) and disease duration-associated PrP(Sc) of mouse BSE prions. Prion. vol 9. issue 5. 2016-09-26. PMID:26555211. |
centrifugation (20,000 ×g) of the brain homogenate showed that most of the prp(sc) was precipitated into the pellet, and the supernatant contained only a slight amount of prp(sc). |
2016-09-26 |
2023-08-13 |
mouse |
| Kohtaro Miyazawa, Hiroyuki Okada, Kentaro Masujin, Yoshifumi Iwamaru, Takashi Yokoyam. Infectivity-associated PrP(Sc) and disease duration-associated PrP(Sc) of mouse BSE prions. Prion. vol 9. issue 5. 2016-09-26. PMID:26555211. |
our results suggest that a small population of fine prp(sc) may be responsible for prion infectivity and that large, aggregated prp(sc) may contribute to determining prion disease duration. |
2016-09-26 |
2023-08-13 |
mouse |
| Danzhi Huang, Amedeo Caflisc. The roles of the conserved tyrosine in the β2-α2 loop of the prion protein. Prion. vol 9. issue 6. 2016-09-26. PMID:26689486. |
the latter state includes the toxic species (scrapie prp, prp(sc)) knowledge of which would facilitate the development of drugs against prion diseases. |
2016-09-26 |
2023-08-13 |
human |
| Neena Singh, Abhishek Asthana, Shounak Baksi, Vilok Desai, Swati Haldar, Sahi Hari, Ajai K Tripath. The prion-ZIP connection: From cousins to partners in iron uptake. Prion. vol 9. issue 6. 2016-09-26. PMID:26689487. |
converging observations from disparate lines of inquiry are beginning to clarify the cause of brain iron dyshomeostasis in sporadic creutzfeldt-jakob disease (scjd), a neurodegenerative condition associated with the conversion of prion protein (prp(c)), a plasma membrane glycoprotein, from α-helical to a β-sheet rich prp-scrapie (prp(sc)) isoform. |
2016-09-26 |
2023-08-13 |
Not clear |
| Sandor Dudas, Jace James, Renee Anderson, Stefanie Czu. Exploring the cause of initially reactive bovine brains on rapid tests for BSE. Prion. vol 9. issue 6. 2016-09-26. PMID:26689488. |
the current tests used for bse screening in canada utilize the relative protease resistance of the prion protein gained when it misfolds from prp(c) to prp(sc) as part of the disease process. |
2016-09-26 |
2023-08-13 |
cattle |
| Sandor Dudas, Jace James, Renee Anderson, Stefanie Czu. Exploring the cause of initially reactive bovine brains on rapid tests for BSE. Prion. vol 9. issue 6. 2016-09-26. PMID:26689488. |
proteinase k completely digests prp(c) in normal brains, but leaves most of the prp(sc) in bse positive brains intact which is detected using anti-prion antibodies. |
2016-09-26 |
2023-08-13 |
cattle |
| Ayodeji A Asuni, Maitea Guridi, Sandrine Sanchez, Martin J Sadowsk. Antioxidant peroxiredoxin 6 protein rescues toxicity due to oxidative stress and cellular hypoxia in vitro, and attenuates prion-related pathology in vivo. Neurochemistry international. vol 90. 2016-09-20. PMID:26265052. |
in prion disease, central to these processes is the post-translational transformation of cellular prion protein (prp(c)) to the aberrant conformationally altered isoform; prp(sc). |
2016-09-20 |
2023-08-13 |
mouse |
| Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio. Scientific reports. vol 5. 2016-09-15. PMID:26576925. |
prion or prp(sc) is a proteinaceous infectious agent that consists of a misfolded and aggregated form of a sialoglycoprotein called prion protein or prp(c). |
2016-09-15 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio. Scientific reports. vol 5. 2016-09-15. PMID:26576925. |
in prp(sc), the glycans are directed outward, with the terminal sialic acid residues creating a negative charge on the surface of prion particles. |
2016-09-15 |
2023-08-13 |
Not clear |
| Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Ilia V Baskako. Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio. Scientific reports. vol 5. 2016-09-15. PMID:26576925. |
the current study proposes a new hypothesis that electrostatic repulsion between sialic residues creates structural constraints that control prion replication and prp(sc) glycoform ratio. |
2016-09-15 |
2023-08-13 |
Not clear |