Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Sumudhu S Perera"'
Autor:
Dominik Sakry, Angela Neitz, Jeet Singh, Renato Frischknecht, Daniele Marongiu, Fabien Binamé, Sumudhu S Perera, Kristina Endres, Beat Lutz, Konstantin Radyushkin, Jacqueline Trotter, Thomas Mittmann
Publikováno v:
PLoS Biology, Vol 12, Iss 11, p e1001993 (2014)
The role of glia in modulating neuronal network activity is an important question. Oligodendrocyte precursor cells (OPC) characteristically express the transmembrane proteoglycan nerve-glia antigen 2 (NG2) and are unique glial cells receiving synapti
Externí odkaz:
https://doaj.org/article/d70a5bd4aee94c9396a0636c718d1f1b
Publikováno v:
Molecular and Cellular Neuroscience. 40:242-248
Endoproteolysis of the cellular prion protein (PrP(C)) modulates both the normal function of the protein and the pathogenesis of the neurodegenerative prion diseases. PrP(C) undergoes alpha-cleavage to generate the N-terminally truncated fragment C1.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af223e15ed4d83fb57a565aebb40d6a3
https://doi.org/10.1016/j.mcn.2008.10.012
https://doi.org/10.1016/j.mcn.2008.10.012
Publikováno v:
Journal of cell science. 118(Pt 21)
The cellular prion protein (PrPC) is essential for the pathogenesis and transmission of prion diseases. Although PrPC is known to be located in detergent-insoluble lipid rafts at the surface of neuronal cells, the mechanism of its internalisation is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a02920514b03a44a8291a6adce3e1fb
https://pubmed.ncbi.nlm.nih.gov/16254249
https://pubmed.ncbi.nlm.nih.gov/16254249
Autor:
Nicole T. Watt, W. Sumudhu S. Perera, Nigel M. Hooper, David R. Taylor, Daniel Thomas, Andrew Gillott
Publikováno v:
The Journal of biological chemistry. 280(43)
The cellular prion protein (PrP(C)) is critical for the development of prion diseases. However, the physiological role of PrP(C) is less clear, although a role in the cellular resistance to oxidative stress has been proposed. PrP(C) is cleaved at the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89023b74d005e14f9dabb3e65f8cb376
https://pubmed.ncbi.nlm.nih.gov/16120605
https://pubmed.ncbi.nlm.nih.gov/16120605
Autor:
Nigel M. Hooper, W. Sumudhu S. Perera
Publikováno v:
FEBS letters. 463(3)
The prion protein (PrP) has been proposed to display sequence and structural similarities to membrane-anchored signal peptidases [Glockshuber et al. (1998) FEBS Lett. 426, 291–296]. We have investigated the role of Tyr-128 and His-177 in the proteo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::770d22d9fcbfa08bdb76c0865f459626
https://pubmed.ncbi.nlm.nih.gov/10606736
https://pubmed.ncbi.nlm.nih.gov/10606736
Autor:
Nigel M. Hooper, W. Sumudhu S. Perera
Publikováno v:
Biochemical Society Transactions. 28:A80-A80
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cac2412aec70a84e028477735b21d03b
https://doi.org/10.1042/bst028a080c
https://doi.org/10.1042/bst028a080c
Autor:
Nigel M. Hooper, W. Sumudhu S. Perera
Publikováno v:
Current Biology. (7):519-523
The neurodegenerative spongiform encephalopathies, or prion diseases, are characterized by the conversion of the normal cellular form of the prion protein PrP C to a pathogenic form, PrP Sc [1]. There are four copies of an octarepeat PHGG(G/S)WGQ tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aab090ff46016104ddec38bcd8473a1a