All Relations between sc and nucleus prepositus

Publication Sentence Publish Date Extraction Date Species
Zhuming Zhang, Renli Wang, Lihua Xu, Fangzhong Yuan, Xiangmei Zhou, Lifeng Yang, Xiaomin Yin, Binrui Xu, Deming Zha. Molecular cloning and sequence analysis of prion protein gene in Xiji donkey in China. Gene. vol 529. issue 2. 2013-11-12. PMID:23954254. prion diseases are a group of human and animal neurodegenerative disorders caused by the deposition of an abnormal isoform prion protein (prp(sc)) encoded by a single copy prion protein gene (prnp). 2013-11-12 2023-08-12 human
Hans Kretzschmar, Jörg Tatzel. Prion disease: a tale of folds and strains. Brain pathology (Zurich, Switzerland). vol 23. issue 3. 2013-10-28. PMID:23587138. it has now become firmly established that particular prp(sc) isoforms are closely related to specific human prion strains. 2013-10-28 2023-08-12 human
Hermann C Altmeppen, Johannes Prox, Berta Puig, Frank Dohler, Clemens Falker, Susanne Krasemann, Markus Glatze. Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration. The FEBS journal. vol 280. issue 18. 2013-10-25. PMID:23413979. first, it is the well-established substrate for the conformational conversion into its pathogenic isoform (prp(sc)) giving rise to progressive and fatal prion diseases. 2013-10-25 2023-08-12 human
Cristina Acín, Inmaculada Martín-Burriel, Eva Monleón, Jaber Lyahyai, José Luis Pitarch, Carmen Serrano, Marta Monzón, Pilar Zaragoza, Juan José Badiol. Prion protein gene variability in Spanish goats. Inference through susceptibility to classical scrapie strains and pathogenic distribution of peripheral PrP(sc.). PloS one. vol 8. issue 4. 2013-10-22. PMID:23580248. inference through susceptibility to classical scrapie strains and pathogenic distribution of peripheral prp(sc.). 2013-10-22 2023-08-12 cattle
Cristina Acín, Inmaculada Martín-Burriel, Eva Monleón, Jaber Lyahyai, José Luis Pitarch, Carmen Serrano, Marta Monzón, Pilar Zaragoza, Juan José Badiol. Prion protein gene variability in Spanish goats. Inference through susceptibility to classical scrapie strains and pathogenic distribution of peripheral PrP(sc.). PloS one. vol 8. issue 4. 2013-10-22. PMID:23580248. classical scrapie is a neurological disorder of the central nervous system (cns) characterized by the accumulation of an abnormal, partially protease resistant prion protein (prp(sc)) in the cns and in some peripheral tissues in domestic small ruminants. 2013-10-22 2023-08-12 cattle
Cristina Acín, Inmaculada Martín-Burriel, Eva Monleón, Jaber Lyahyai, José Luis Pitarch, Carmen Serrano, Marta Monzón, Pilar Zaragoza, Juan José Badiol. Prion protein gene variability in Spanish goats. Inference through susceptibility to classical scrapie strains and pathogenic distribution of peripheral PrP(sc.). PloS one. vol 8. issue 4. 2013-10-22. PMID:23580248. all the animals displayed prp(sc) distribution patterns and western blot characteristics compatible with classical scrapie. 2013-10-22 2023-08-12 cattle
Natsuo Ohsawa, Chang-Hyun Song, Akio Suzuki, Hidefumi Furuoka, Rie Hasebe, Motohiro Horiuch. Therapeutic effect of peripheral administration of an anti-prion protein antibody on mice infected with prions. Microbiology and immunology. vol 57. issue 4. 2013-10-22. PMID:23586633. the level of prp(sc) in the mab 31c6-treated mice was lower than that in mice treated with the negative control mab and progression of neuropathological lesions in the cerebellum, where the mab 31c6 was well distributed, appeared to be mitigated. 2013-10-22 2023-08-12 mouse
Ning Ding, Norman F Neumann, Luke M Price, Shannon L Braithwaite, Aru Balachandran, Gordon Mitchell, Miodrag Belosevic, Mohamed Gamal El-Di. Kinetics of ozone inactivation of infectious prion protein. Applied and environmental microbiology. vol 79. issue 8. 2013-10-21. PMID:23416994. the kinetics of ozone inactivation of infectious prion protein (prp(sc), scrapie 263k) was investigated in ozone-demand-free phosphate-buffered saline (pbs). 2013-10-21 2023-08-12 Not clear
Ning Ding, Norman F Neumann, Luke M Price, Shannon L Braithwaite, Aru Balachandran, Gordon Mitchell, Miodrag Belosevic, Mohamed Gamal El-Di. Kinetics of ozone inactivation of infectious prion protein. Applied and environmental microbiology. vol 79. issue 8. 2013-10-21. PMID:23416994. the inactivation of prp(sc) was quantified by determining the in vitro destruction of prp(sc) templating properties using the protein misfolding cyclic amplification (pmca) assay and bioassay, which were shown to correlate well. 2013-10-21 2023-08-12 Not clear
Ning Ding, Norman F Neumann, Luke M Price, Shannon L Braithwaite, Aru Balachandran, Gordon Mitchell, Miodrag Belosevic, Mohamed Gamal El-Di. Kinetics of ozone inactivation of infectious prion protein. Applied and environmental microbiology. vol 79. issue 8. 2013-10-21. PMID:23416994. the efficacy of ozone inactivation of prp(sc) was both ph and temperature dependent. 2013-10-21 2023-08-12 Not clear
James M McCarthy, Beatriz Rasines Moreno, Damien Filippini, Hartmut Komber, Marek Maly, Michaela Cernescu, Bernhard Brutschy, Dietmar Appelhans, Mark S Roger. Influence of surface groups on poly(propylene imine) dendrimers antiprion activity. Biomacromolecules. vol 14. issue 1. 2013-10-17. PMID:23234313. prion diseases are characterized by the accumulation of prp(sc), an aberrantly folded isoform of the host protein prp(c). 2013-10-17 2023-08-12 Not clear
James M McCarthy, Beatriz Rasines Moreno, Damien Filippini, Hartmut Komber, Marek Maly, Michaela Cernescu, Bernhard Brutschy, Dietmar Appelhans, Mark S Roger. Influence of surface groups on poly(propylene imine) dendrimers antiprion activity. Biomacromolecules. vol 14. issue 1. 2013-10-17. PMID:23234313. specific forms of synthetic molecules known as dendrimers are able to eliminate protease-resistant prp(sc) in both an intracellular and in vitro setting. 2013-10-17 2023-08-12 Not clear
James M McCarthy, Beatriz Rasines Moreno, Damien Filippini, Hartmut Komber, Marek Maly, Michaela Cernescu, Bernhard Brutschy, Dietmar Appelhans, Mark S Roger. Influence of surface groups on poly(propylene imine) dendrimers antiprion activity. Biomacromolecules. vol 14. issue 1. 2013-10-17. PMID:23234313. several of the modified dendrimers, including an anionic glycodendrimer, reduced the level of protease resistant prp(sc) in a prion strain-dependent manner. 2013-10-17 2023-08-12 Not clear
James M McCarthy, Beatriz Rasines Moreno, Damien Filippini, Hartmut Komber, Marek Maly, Michaela Cernescu, Bernhard Brutschy, Dietmar Appelhans, Mark S Roger. Influence of surface groups on poly(propylene imine) dendrimers antiprion activity. Biomacromolecules. vol 14. issue 1. 2013-10-17. PMID:23234313. this led to the formulation of a new working model for dendrimer/prion interactions which proposes dendrimers eliminate prp(sc) by destabilizing the protein and rendering it susceptible to proteolysis. 2013-10-17 2023-08-12 Not clear
Abdul-Hamid M Emwas, Zeyad A Al-Talla, Xianrong Guo, Suliman Al-Ghamdi, Harbi T Al-Masr. Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases. Magnetic resonance in chemistry : MRC. vol 51. issue 5. 2013-10-17. PMID:23436479. prion protein (prp) is a copper-binding, cell-surface glycoprotein that exists in two alternatively folded conformations: a normal isoform (prp(c)) and a disease-associated isoform (prp(sc)). 2013-10-17 2023-08-12 Not clear
Abdul-Hamid M Emwas, Zeyad A Al-Talla, Xianrong Guo, Suliman Al-Ghamdi, Harbi T Al-Masr. Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases. Magnetic resonance in chemistry : MRC. vol 51. issue 5. 2013-10-17. PMID:23436479. prion diseases are a group of lethal neurodegenerative disorders that develop as a result of conformational conversion of prp(c) into prp(sc). 2013-10-17 2023-08-12 Not clear
Maya Higuma, Nobuo Sanjo, Katsuya Satoh, Yusei Shiga, Kenji Sakai, Ichiro Nozaki, Tsuyoshi Hamaguchi, Yosikazu Nakamura, Tetsuyuki Kitamoto, Susumu Shirabe, Shigeo Murayama, Masahito Yamada, Jun Tateishi, Hidehiro Mizusaw. Relationships between clinicopathological features and cerebrospinal fluid biomarkers in Japanese patients with genetic prion diseases. PloS one. vol 8. issue 3. 2013-09-30. PMID:23555862. we retrospectively analyzed age at onset and disease duration; the concentrations and incidences of 14-3-3 protein, tau protein, and abnormal prion protein (prp(sc)) in the csf of 309 gprd patients with p102l, p105l, e200k, v180i, or m232r mutations; and brain pathology in 32 autopsied patients. 2013-09-30 2023-08-12 Not clear
Maya Higuma, Nobuo Sanjo, Katsuya Satoh, Yusei Shiga, Kenji Sakai, Ichiro Nozaki, Tsuyoshi Hamaguchi, Yosikazu Nakamura, Tetsuyuki Kitamoto, Susumu Shirabe, Shigeo Murayama, Masahito Yamada, Jun Tateishi, Hidehiro Mizusaw. Relationships between clinicopathological features and cerebrospinal fluid biomarkers in Japanese patients with genetic prion diseases. PloS one. vol 8. issue 3. 2013-09-30. PMID:23555862. prp(sc) was detected in the csf of more than 80% of patients with e200k, m232r, or p102l mutations but in only 39% of patients with v180i. 2013-09-30 2023-08-12 Not clear
Maya Higuma, Nobuo Sanjo, Katsuya Satoh, Yusei Shiga, Kenji Sakai, Ichiro Nozaki, Tsuyoshi Hamaguchi, Yosikazu Nakamura, Tetsuyuki Kitamoto, Susumu Shirabe, Shigeo Murayama, Masahito Yamada, Jun Tateishi, Hidehiro Mizusaw. Relationships between clinicopathological features and cerebrospinal fluid biomarkers in Japanese patients with genetic prion diseases. PloS one. vol 8. issue 3. 2013-09-30. PMID:23555862. patients negative for prp(sc) in the csf were older at disease onset than positive patients. 2013-09-30 2023-08-12 Not clear
Maya Higuma, Nobuo Sanjo, Katsuya Satoh, Yusei Shiga, Kenji Sakai, Ichiro Nozaki, Tsuyoshi Hamaguchi, Yosikazu Nakamura, Tetsuyuki Kitamoto, Susumu Shirabe, Shigeo Murayama, Masahito Yamada, Jun Tateishi, Hidehiro Mizusaw. Relationships between clinicopathological features and cerebrospinal fluid biomarkers in Japanese patients with genetic prion diseases. PloS one. vol 8. issue 3. 2013-09-30. PMID:23555862. positivity for prp(sc) in the csf may reflect the pathological process before or at disease onset, or abnormality in the secretion or metabolism of prp(sc). 2013-09-30 2023-08-12 Not clear