Relevant bibliographies by topics / Cellular prion protein physiological function

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

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"

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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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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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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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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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Das, Alvin S., and Wen-Quan Zou. "Prions: Beyond a Single Protein." Clinical Microbiology Reviews 29, no. 3 (2016): 633–58. http://dx.doi.org/10.1128/cmr.00046-15.

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SUMMARYSince the term protein was first coined in 1838 and protein was discovered to be the essential component of fibrin and albumin, all cellular proteins were presumed to play beneficial roles in plants and mammals. However, in 1967, Griffith proposed that proteins could be infectious pathogens and postulated their involvement in scrapie, a universally fatal transmissible spongiform encephalopathy in goats and sheep. Nevertheless, this novel hypothesis had not been evidenced until 1982, when Prusiner and coworkers purified infectious particles from scrapie-infected hamster brains and demons
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Dondapati, Divya Teja, Pradeep Reddy Cingaram, Ferhan Ayaydin, et al. "Membrane Domain Localization and Interaction of the Prion-Family Proteins, Prion and Shadoo with Calnexin." Membranes 11, no. 12 (2021): 978. http://dx.doi.org/10.3390/membranes11120978.

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The cellular prion protein (PrPC) is renowned for its infectious conformational isoform PrPSc, capable of templating subsequent conversions of healthy PrPCs and thus triggering the group of incurable diseases known as transmissible spongiform encephalopathies. Besides this mechanism not being fully uncovered, the protein’s physiological role is also elusive. PrPC and its newest, less understood paralog Shadoo are glycosylphosphatidylinositol-anchored proteins highly expressed in the central nervous system. While they share some attributes and neuroprotective actions, opposing roles have also b
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Gavín, Rosalina, Laia Lidón, Isidre Ferrer, and José Antonio del Río. "The Quest for Cellular Prion Protein Functions in the Aged and Neurodegenerating Brain." Cells 9, no. 3 (2020): 591. http://dx.doi.org/10.3390/cells9030591.

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Cellular (also termed ‘natural’) prion protein has been extensively studied for many years for its pathogenic role in prionopathies after misfolding. However, neuroprotective properties of the protein have been demonstrated under various scenarios. In this line, the involvement of the cellular prion protein in neurodegenerative diseases other than prionopathies continues to be widely debated by the scientific community. In fact, studies on knock-out mice show a vast range of physiological functions for the protein that can be supported by its ability as a cell surface scaffold protein. In this
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Yoon, Sungtae, Gyeongyun Go, Yeomin Yoon, Jiho Lim, Gaeun Lee, and Sanghun Lee. "Harnessing the Physiological Functions of Cellular Prion Protein in the Kidneys: Applications for Treating Renal Diseases." Biomolecules 11, no. 6 (2021): 784. http://dx.doi.org/10.3390/biom11060784.

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A cellular prion protein (PrPC) is a ubiquitous cell surface glycoprotein, and its physiological functions have been receiving increased attention. Endogenous PrPC is present in various kidney tissues and undergoes glomerular filtration. In prion diseases, abnormal prion proteins are found to accumulate in renal tissues and filtered into urine. Urinary prion protein could serve as a diagnostic biomarker. PrPC plays a role in cellular signaling pathways, reno-protective effects, and kidney iron uptake. PrPC signaling affects mitochondrial function via the ERK pathway and is affected by the regu
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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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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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Dissertations / Theses on the topic "Cellular prion protein physiological function"

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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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Isaacs, J. D. "Immunogenicity and immune function of the cellular prion protein." Thesis, University College London (University of London), 2007. http://discovery.ucl.ac.uk/1444752/.

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Prion protein (PrP) is the only factor known to be essential in the pathogenesis of the transmissible spongiform encephalopathies (TSEs) or prion diseases. The cellular isoform (PrPc), a GPI-anchored sialoglycoprotein of unknown function, has an identical primary structure to the disease-associated conformer (PrPSc). Thus, animals are tolerant to PrPSc and TSEs do not trigger a classical immune response. Vaccine development for human TSEs requires elucidation of the immunodominant human T cell epitopes within PrP. Further, successful immunotherapy requires that the function of PrPc in lymphocy
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Dodelet, Vincent C. "Distribution and function of the normal cellular isoform of the prion protein." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0023/NQ50322.pdf.

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Poggiolini, Ilaria. "Insights in the Regional Distribution and Physiological Role of the Cellular Prion Protein in the Central Nervous System of Mammalian Organisms." Doctoral thesis, SISSA, 2012. http://hdl.handle.net/20.500.11767/4880.

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The cellular form of the prion protein (PrPC) is a sialoglycoprotein ubiquitously expressed in the central nervous system (CNS) of mammalian species along the neurodevelopment and in the adulthood. The PrPC localization in the brain has attracted interest because of its involvement in fatal neurodegenerative disorders, denoted as transmissible spongiform encephalopathies. In mammals, PrPC is expressed early in embryogenesis, and in the adulthood it reaches its highest levels in the neurons of the encephalon and spinal cord. The protein is also found at lower levels in glial cells of the CNS, a
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Weiß, Eva Annabelle. "Analyse der Proteinexpression zur Untersuchung der physiologischen Funktion des zellulären Prionproteins (PrPc)." Doctoral thesis, 2012. http://hdl.handle.net/11858/00-1735-0000-0006-B2B7-B.

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Glier, Hana. "Exprese a funkce buněčného prionového proteinu na krevních buňkách." Doctoral thesis, 2012. http://www.nusl.cz/ntk/nusl-322648.

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The cellular prion protein (PrPc) is essential for pathogenesis of fatal neurodegenerative prion diseases. Recently reported four cases of vCJD transmission by blood transfusion raise concerns about the safety of blood products. Proper understanding of PrPc in blood is necessary for development of currently unavailable blood screening tests for prion diseases. Flow cytometry is an attractive method for prion detection, however, the reports on the quantity of PrPc on human blood cells are contradictory. We showed that the majority of PrPc in resting platelets is present in the intracellular poo
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Books on the topic "Cellular prion protein physiological function"

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R, Means Anthony, ed. Calcium regulation of cellular function. Raven Press, 1995.

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Means, Anthony R. Calcium regulation of cellular function. Raven Press, 1995.

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A, Wirtz Karel W., and NATO Advanced Study Institute on New Developments in Lipid-Protein Interactions and Receptor Function (1992 : Spetsai, Greece), eds. New developments in lipid-protein interactions and receptor function. Plenum Press, 1993.

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NATO, Advanced Study Institute on Structure and Function of Interacting Protein Domains in Signal and Energy Transduction (1996 Acquafredda di Maratea Italy). Interacting protein domains: Their role in signal and energy transduction : [proceedings of the NATO Advanced Study Institute on Structure and Function of Interacting Protein Domains in Signal and Energy Transduction, held at Acquafredda di Maratea, Italy, September 10-19, 1996]. Springer, 1997.

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

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Landrier, Jean-François, Jacques Grober, Isabelle Zaghini, and Philippe Besnard. "Regulation of the ileal bile acid-binding protein gene: An approach to determine its physiological function(s)." In Cellular Lipid Binding Proteins. Springer US, 2002. http://dx.doi.org/10.1007/978-1-4419-9270-3_19.

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James, Dominika Lipowska, and Maryam Jowza. "Protein Function as Immunoglobulins and Hormones." In Basic Anesthesia Review, edited by Alaa Abd-Elsayed. Oxford University PressNew York, 2024. http://dx.doi.org/10.1093/med/9780197584569.003.0323.

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Abstract All living things depend on proteins for their existence. Proteins are some of the most structurally complex biological molecules, whose three-dimensional configuration is inherently correlated with their function. Proteins serve a wide array of physiological processes within the human body; they not only are the primary building blocks of many tissues, but also serve as hormones coordinating physiological activities, as well as carrying immune function as immunoglobulins. Protein hormones are specific proteins involved in cell signaling and communication. They are secreted by endocri
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Hidaka, Hiroyoshi, and Ryoji Kobayashi. "Use of protein (serine/threonine) kinase activators and inhibitors to study protein phosphorylation in intact cells." In Protein Phosphorylation. Oxford University PressOxford, 1993. http://dx.doi.org/10.1093/oso/9780199633067.003.0004.

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Abstract A complete understanding of the organization and functioning of a protein phosphorylation system requires the co-operation of several different approaches, such as molecular pharmacology, genetic manipulation, bio¬ chemistry, and cell biology. The advent of a new class of effective pharmacological agents is always an event of considerable interest, in particular for new types of antagonists, i.e. potentially important groups of compounds that act by specifically blocking one or more of the steps in intracellular signalling systems (1). There is now convincing evidence that intracellul
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Skolnick, Jeffrey, and Yang Zhang. "Protein Structure Prediction." In Systems Biology. Oxford University PressNew York, NY, 2006. http://dx.doi.org/10.1093/oso/9780195300819.003.0007.

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Abstract Over the past decade, the success of genome sequence efforts has brought about a paradigm shift in biology [1]. There is increasing emphasis on the large-scale, high-throughput examination of all genes and gene products of an organism, with the aim of assigning their functions [2]. Of course, biological function is multifaceted, ranging from molecular/biochemical to cellular or physiological to phenotypical [3]. In practice, knowledge of the DNA sequence of an organism and the identification of its open reading frames (ORFs) does not directly provide functional insight. Here, the focu
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Naito, Yasuhito, Ryoji Kobayashi, and Hiroyoshi Hidaka. "Analysis of signal transduction pathways using protein kinase inhibitors and activators." In Protein Phosphorylation. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780199637294.003.0002.

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Abstract A complete understanding of the organization and functioning of the protein phosphorylation system requires the pooling of expertise in several different fields, such as molecular pharmacology, genetic manipulation, biochemistry, and cell biology. The advent of a new class of effective pharmacological agents is always an event of considerable interest, in particular for new types of antagonists, i.e. potentially important groups of compounds that act by specifically blocking one or more of the steps in intracellular signalling systems (1). There is now convincing evidence that intrace
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Assefi, Marjan, Kai Uwe Lewandrowski, Alireza Sharafshah, and Seyed Majid Hosseini. "Cellular Aging from Physiological and Economical Perspectives." In Cell Physiology - Annual Volume 2023 [Working Title]. IntechOpen, 2023. http://dx.doi.org/10.5772/intechopen.111516.

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The study of biological processes and functions of the human body under normal circumstances is known as physiology. Cellular physiology is the study of biophysical and biochemistry processes taking place in a cell. Cells age with time. They all have a certain lifespan after which they die common features that can be observed in an aging cell include damaged protein and organelles accumulation even when there is the absence of mutation. Many physiological changes are experienced as cell ages, resulting in the deterioration of normal cell functioning. Examples of such changes include: Cells may
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"7. Function of Cellular Prion Protein (PrPC) in Copper Homeostasis and Redox Signaling at the Synapse." In Prions in Humans and Animals, edited by Beat Hörnlimann, Detlev Riesner, and Hans A. Kretzschmar. Walter de Gruyter, 2006. http://dx.doi.org/10.1515/9783110200171.2.95.

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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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Brown, Dennis. "Analysis of protein expression by immunocytochemistry." In Gene probes 2. Oxford University PressOxford, 1995. http://dx.doi.org/10.1093/oso/9780199634156.003.0011.

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Abstract Immunocytochemistry is a major technique in unravelling the roles of proteins expressed by cells. This is true whether the protein is endogenous, or whether it is expressed as a result of transfection of a cell with a specific cDNA. Remarkable insights into the complex physiology and cell biology of cells, tissues, and organs have been obtained by combining immunocytochemical observations with the powerful tools of molecular biology, and with measurements of physiological and cellular function. In view of the increasing use of such detection techniques in multidisciplinary studies, it
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Balchin, D., M. Aguilar Rangel, and R. S. Samant. "Introduction: Molecular Chaperones and Protein Quality Control." In Biophysics of Molecular Chaperones. Royal Society of Chemistry, 2023. http://dx.doi.org/10.1039/bk9781839165986-00001.

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Most proteins need to attain and maintain a defined, native three-dimensional structure to carry out their physiological function. In the crowded macromolecular environment of a cell, a specialised and conserved set of machineries called molecular chaperones have evolved to maintain protein homeostasis, or “proteostasis”, and protect the cell from the deleterious accumulation of non-functional and potentially toxic misfolded protein species. In this chapter, we (i) lay out some of the challenges faced during a protein’s lifecycle; (ii) discuss protein aggregation from both biophysical and cell
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Conference papers on the topic "Cellular prion protein physiological function"

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Carruthers, Christopher A., Bryan Good, Antonio D’Amore, Rouzbeh Amini, Joseph H. Gorman, and Michael S. Sacks. "Physiological Micromechanics of the Anterior Mitral Valve Leaflet." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53637.

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An improved understanding of mitral valve (MV) function remains an important goal for determining mechanisms underlying valve disease and for developing novel therapies. Critical to heart valve tissue homeostasis is the valvular interstitial cells (VICs), which reside in the interstitium and maintain the extracellular matrix (ECM) through both protein synthesis and enzymatic degradation [1]. There is scant experimental data on the alterations of the MV fiber network reorganization as a function of load, which is critical for implementation of computational strategies that attempt to link this
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Tran, Phat L., Jessica R. Gamboa, Katherine E. McCracken, Jeong-Yeol Yoon, and Marvin J. Slepian. "Interaction With Nanoscale Topography: The Use of Nanowell-Trapped Charged Ligand-Bearing Nanoparticle Surfaces To Modulate Physiological Focal Adhesions in Endothelial Cells." In ASME 2013 2nd Global Congress on NanoEngineering for Medicine and Biology. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/nemb2013-93345.

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Achieving cell adhesion, growth and homeostasis on an underlying biomaterial surface may be a desirable feature in implant device design and tissue engineering. Insight has been gained from numerous cell patterning strategies where spatial cues and physical constraints have been shown to regulate the structure and function of cells. Despite significant advances in modifying substrates for cellular attachment, migration and proliferation, the achievement of confluent and aligned growth of functional endothelial cells on cardiovascular blood-contacting implants under physiologically significant
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