Results 21 to 30 of about 1,553,593 (211)

The Functional Role of Prion Protein (PrPC) on Autophagy [PDF]

Pathogens, 2013
Cellular prion protein (PrPC) plays an important role in the cellular defense against oxidative stress. However, the exact protective mechanism of PrPC is unclear. Autophagy is essential for survival, differentiation, development, and homeostasis in several organisms.
Hae-Young Shin, Yong-Sun Kim, Jae-Min Oh
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Short-term memory formation and long-term memory consolidation are enhanced by cellular prion association to stress-inducible protein 1

Neurobiology of Disease, 2007
Cellular prion protein (PrPC) is a cell surface glycoprotein that interacts with several ligands such as laminin, NCAM (Neural-Cell Adhesion Molecule) and the stress-inducible protein 1 (STI1).
Adriana S. Coitinho, Marilene H. Lopes, Glaucia N.M. Hajj, Janine I. Rossato, Adriana R. Freitas, Cibele C. Castro, Martin Cammarota, Ricardo R. Brentani, Ivan Izquierdo, Vilma R. Martins   +9 more
doaj   +1 more source

HTLV-1 p12 modulates the levels of prion protein (PrPC) in CD4+ T cells

Frontiers in Microbiology, 2023
IntroductionInfection with human T cell lymphotropic virus type 1 (HTLV-1) is endemic in Brazil and is linked with pro-inflammatory conditions including HTLV-1-associated myelopathy/tropical spastic paraparesis (HAM/TSP), a chronic neuroinflammatory ...
Isabela Silva De Castro, Isabela Silva De Castro, Alessandra Granato, Rafael Meyer Mariante, Rafael Meyer Mariante, Marco Antonio Lima, Ana Claudia Celestino Leite, Otávio de Melo Espindola, Cynthia A. Pise-Masison, Genoveffa Franchini, Rafael Linden, Juliana Echevarria-Lima   +11 more
doaj   +1 more source

Immunohistochemical Expression of Prion Protein (PrPC) in the Human Forebrain During Development [PDF]

Journal of Neuropathology and Experimental Neurology, 2006
The cellular prion protein (PrPC) is a ubiquitous protein whose expression in the adult brain occurs mainly in synapses. We used monoclonal antibodies to study fetal and perinatal PrPC expression in the human forebrain. Double immunofluorescence and confocal microscopy with GFAP, Iba1, MAP2, doublecortin, synaptophysin, and GAP-43 were used to localize
Adle-Biassette, Homa, Verney, Catherine, Peoc'h, Katell, Dauge, Marie-Christine, Razavi, Férechté, Choudat, Laurence, Gressens, Pierre, Budka, Herbert, Henin, Dominique   +8 more
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New insights into cellular prion protein (PrPc) functions: The “ying and yang” of a relevant protein [PDF]

Brain Research Reviews, 2009
The conversion of cellular prion protein (PrP(c)), a GPI-anchored protein, into a protease-K-resistant and infective form (generally termed PrP(sc)) is mainly responsible for Transmissible Spongiform Encephalopathies (TSEs), characterized by neuronal degeneration and progressive loss of basic brain functions.
Nicolás i Pallejà, Josep Oriol, Gavín Marín, Rosalina, Río Fernández, José Antonio del   +2 more
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Role of lipid rafts and GM1 in the segregation and processing of prion protein.

PLoS ONE, 2014
The prion protein (PrPC) is highly expressed within the nervous system. Similar to other GPI-anchored proteins, PrPC is found in lipid rafts, membrane domains enriched in cholesterol and sphingolipids.
Laura Botto, Diana Cunati, Silvia Coco, Silvia Sesana, Alessandra Bulbarelli, Emiliano Biasini, Laura Colombo, Alessandro Negro, Roberto Chiesa, Massimo Masserini, Paola Palestini   +10 more
doaj   +1 more source

Prion protein self-peptides modulate prion interactions and conversion [PDF]

, 2009
Background: Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood.
Bossers, A., Fred G van Zijderveld, Priem, J., Drophatie Timmers-Parohi, Rigter, A., Alex Bossers, Alan Rigter, Timmers-Parohi, D., Jan PM Langeveld, van Zijderveld, F.G., Zijderveld, F.G., van, Jan Priem, Langeveld, J.P.M.   +12 more
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Cellular prion protein and NMDA receptor modulation: protecting against excitotoxicity

Frontiers in Cell and Developmental Biology, 2014
Although it is well established that misfolding of the cellular prion protein (PrPC) into the beta-sheet-rich, aggregated scrapie conformation (PrPSc) causes a variety of transmissible spongiform encephalopathies (TSEs), the physiological roles of PrPC ...
Stefanie A.G. Black, Stefanie A.G. Black, Peter K. Stys, Peter K. Stys, Gerald W. Zamponi, Gerald W. Zamponi, Shigeki eTsutsui, Shigeki eTsutsui   +7 more
doaj   +1 more source

The crystal structure of the globular domain of sheep prion protein [PDF]

, 2004
The prion protein PrP is a naturally occurring polypeptide that becomes transformed from a normal conformation to that of an aggregated form, characteristic of pathological states in fatal transmissible spongiform conditions such as Creutzfeld–Jacob ...
Vasisht N, Whyte, SM, Dodson EJ, Vasisht, N, Gill, A.C., Whyte, S.M., Dodson, G.G., Whyte, S M, Vasisht, N., Bayley, P M, Verma, C., Verma C, Gill, A C, Bayley, PM, Bayley, P.M., Whyte SM, Haire LF, Gill AC, Gill, AC, Bayley PM, Dodson, EJ, Haire, L.F., Dodson, GG, Dodson, E.J., Haire, L F, Verma, C, Haire, LF, Dodson, E J, Dodson, G G   +28 more
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Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]

, 2006
During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Hicks, M R, David H. Crout, Crout, D H, Teresa J. T. Pinheiro, Ian D. Sylvester, Andrew C. Gill, Imanpreet K. Bath, Atvinder K. Rullay, Gill, A C, Bath, I K, Pinheiro, T J T, Matthew R. Hicks, Sylvester, I D, Rullay, A K   +13 more
core   +1 more source