Relevant bibliographies by topics / Cellular prion protein physiological function, Myelin

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Cellular prion protein physiological function, Myelin'

Author: Grafiati
Published: 14 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "Cellular prion protein physiological function, Myelin"

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Nuvolone, Mario, Mario Hermann, Silvia Sorce, et al. "Strictly co-isogenic C57BL/6J-Prnp−/− mice: A rigorous resource for prion science." Journal of Experimental Medicine 213, no. 3 (2016): 313–27. http://dx.doi.org/10.1084/jem.20151610.

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Although its involvement in prion replication and neurotoxicity during transmissible spongiform encephalopathies is undisputed, the physiological role of the cellular prion protein (PrPC) remains enigmatic. A plethora of functions have been ascribed to PrPC based on phenotypes of Prnp−/− mice. However, all currently available Prnp−/− lines were generated in embryonic stem cells from the 129 strain of the laboratory mouse and mostly crossed to non-129 strains. Therefore, Prnp-linked loci polymorphic between 129 and the backcrossing strain resulted in systematic genetic confounders and led to er
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Martins, V. R., A. F. Mercadante, A. L. B. Cabral, A. R. O. Freitas, and R. M. R. P. S. Castro. "Insights into the physiological function of cellular prion protein." Brazilian Journal of Medical and Biological Research 34, no. 5 (2001): 585–95. http://dx.doi.org/10.1590/s0100-879x2001000500005.

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Franzmann, Titus M., Marcus Jahnel, Andrei Pozniakovsky, et al. "Phase separation of a yeast prion protein promotes cellular fitness." Science 359, no. 6371 (2018): eaao5654. http://dx.doi.org/10.1126/science.aao5654.

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Despite the important role of prion domains in neurodegenerative disease, their physiological function has remained enigmatic. Previous work with yeast prions has defined prion domains as sequences that form self-propagating aggregates. Here, we uncovered an unexpected function of the canonical yeast prion protein Sup35. In stressed conditions, Sup35 formed protective gels via pH-regulated liquid-like phase separation followed by gelation. Phase separation was mediated by the N-terminal prion domain and regulated by the adjacent pH sensor domain. Phase separation promoted yeast cell survival b
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Go, Gyeongyun, and Sang Hun Lee. "The Cellular Prion Protein: A Promising Therapeutic Target for Cancer." International Journal of Molecular Sciences 21, no. 23 (2020): 9208. http://dx.doi.org/10.3390/ijms21239208.

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Studies on the cellular prion protein (PrPC) have been actively conducted because misfolded PrPC is known to cause transmissible spongiform encephalopathies or prion disease. PrPC is a glycophosphatidylinositol-anchored cell surface glycoprotein that has been reported to affect several cellular functions such as stress protection, cellular differentiation, mitochondrial homeostasis, circadian rhythm, myelin homeostasis, and immune modulation. Recently, it has also been reported that PrPC mediates tumor progression by enhancing the proliferation, metastasis, and drug resistance of cancer cells.
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Miranzadeh Mahabadi, Hajar, and Changiz Taghibiglou. "Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction." International Journal of Molecular Sciences 21, no. 19 (2020): 7058. http://dx.doi.org/10.3390/ijms21197058.

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Cellular prion protein (PrPc) is a small glycosylphosphatidylinositol (GPI) anchored protein most abundantly found in the outer leaflet of the plasma membrane (PM) in the central nervous system (CNS). PrPc misfolding causes neurodegenerative prion diseases in the CNS. PrPc interacts with a wide range of protein partners because of the intrinsically disordered nature of the protein’s N-terminus. Numerous studies have attempted to decipher the physiological role of the prion protein by searching for proteins which interact with PrPc. Biochemical characteristics and biological functions both appe
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Aguzzi, Adriano, and Anna Maria Calella. "Prions: Protein Aggregation and Infectious Diseases." Physiological Reviews 89, no. 4 (2009): 1105–52. http://dx.doi.org/10.1152/physrev.00006.2009.

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Transmissible spongiform encephalopathies (TSEs) are inevitably lethal neurodegenerative diseases that affect humans and a large variety of animals. The infectious agent responsible for TSEs is the prion, an abnormally folded and aggregated protein that propagates itself by imposing its conformation onto the cellular prion protein (PrPC) of the host. PrPCis necessary for prion replication and for prion-induced neurodegeneration, yet the proximal causes of neuronal injury and death are still poorly understood. Prion toxicity may arise from the interference with the normal function of PrPC, and
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Westergard, Laura, Heather M. Christensen, and David A. Harris. "The cellular prion protein (PrPC): Its physiological function and role in disease." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1772, no. 6 (2007): 629–44. http://dx.doi.org/10.1016/j.bbadis.2007.02.011.

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Henzi, Anna, and Adriano Aguzzi. "The prion protein is not required for peripheral nerve de- and remyelination after crush injury." PLOS ONE 16, no. 1 (2021): e0245944. http://dx.doi.org/10.1371/journal.pone.0245944.

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The cellular prion protein (PrP) is essential to the long-term maintenance of myelin sheaths in peripheral nerves. PrP activates the adhesion G-protein coupled receptor Adgrg6 on Schwann cells and initiates a pro-myelination cascade of molecular signals. Because Adgrg6 is crucial for peripheral myelin development and regeneration after nerve injury, we investigated the role of PrP in peripheral nerve repair. We performed experimental sciatic nerve crush injuries in co-isogenic wild-type and PrP-deficient mice, and examined peripheral nerve repair processes. Generation of repair Schwann cells,
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Kovač, Valerija, and Vladka Čurin Šerbec. "Prion Protein: The Molecule of Many Forms and Faces." International Journal of Molecular Sciences 23, no. 3 (2022): 1232. http://dx.doi.org/10.3390/ijms23031232.

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Cellular prion protein (PrPC) is a glycosylphosphatidylinositol (GPI)-anchored protein most abundantly found in the outer membrane of neurons. Due to structural characteristics (a flexible tail and structured core), PrPC interacts with a wide range of partners. Although PrPC has been proposed to be involved in many physiological functions, only peripheral nerve myelination homeostasis has been confirmed as a bona fide function thus far. PrPC misfolding causes prion diseases and PrPC has been shown to mediate β-rich oligomer-induced neurotoxicity in Alzheimer’s and Parkinson’s disease as well a
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Rolle, Irene Giulia, Anna Burato, Merve Begüm Bacınoğlu, Fabio Moda, and Giuseppe Legname. "The Role of Prion Protein in Reelin/Dab1 Signaling: Implications for Neurodegeneration." Viruses 17, no. 7 (2025): 928. https://doi.org/10.3390/v17070928.

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The cellular prion protein (PrPC) is studied in prion diseases, where its misfolded isoform (PrPSc) leads to neurodegeneration. PrPC has also been implicated in several physiological functions. The protein is abundant in the nervous system, and it is critical for cell signaling in cellular communication, where it acts as a scaffold for various signaling molecules. The Reelin signaling pathway, implicated both in Alzheimer’s and prion diseases, engages Dab1, an adaptor protein influencing APP processing and amyloid beta deposition. Here, we show, using Prnp knockout models (Prnp0/0), that PrPC
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Dissertations / Theses on the topic "Cellular prion protein physiological function, Myelin"

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Meneghetti, Elisa. "Role of cellular prion protein in central nervous system myelination." Doctoral thesis, SISSA, 2016. http://hdl.handle.net/20.500.11767/4899.

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The cellular form of the prion protein (PrPC) has been widely investigated since its alternative folded isoform is the causative agent of prion disorders. PrPC is highly expressed in the nervous system, where it is involved in many physiological processes such as the maintenance of peripheral nervous system (PNS) myelination. A similar role in the central nervous system (CNS) is still controversial, since PrPC absence affects proliferation and maturation of oligodendrocyte precursor cells without affecting myelination. On the other hand, PrPC is involved in metal homeostasis and modulates oxid
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Thurm, Dana Kathrin [Verfasser], and Markus [Akademischer Betreuer] Glatzel. "Novel Physiological Function of the Cellular Prion Protein (PrPC) in Exosomal Trafficking / Dana Kathrin Thurm. Betreuer: Markus Glatzel." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2012. http://d-nb.info/1022684361/34.

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Thurm, Dana Kathrin Verfasser], and Markus [Akademischer Betreuer] [Glatzel. "Novel Physiological Function of the Cellular Prion Protein (PrPC) in Exosomal Trafficking / Dana Kathrin Thurm. Betreuer: Markus Glatzel." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2012. http://nbn-resolving.de/urn:nbn:de:gbv:18-56417.

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Book chapters on the topic "Cellular prion protein physiological function, Myelin"

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Oyindamola, Eyitayo Adeyemi, Maxwell Kwadwo Agyemang, Joseph Owusu-Sarfo, Oduro Kofi Yeboah, and Newman Osafo. "Microglial Mitophagy and Neurodegenerative Disorders." In Quality Control of Cellular Protein in Neurodegenerative Disorders. IGI Global, 2020. http://dx.doi.org/10.4018/978-1-7998-1317-0.ch004.

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Microglia are important in the regulation of the inflammatory response in regulating the release of proinflammatory mediators in the brain. Through their phagocytic actions, microglia are significant in the CNS when it comes to the body's response to physiological insults by promoting repair of impaired brain function. They do so by engulfing and degrading microbes as well as brain-derived debris and proteins such as myelin and axonal fragments, amyloid-beta, and apoptotic cells. This mitophagic activity of microglia is of importance in neurodegeneration. In most neurodegenerative disorders, m
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Journal articles
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