Relevant bibliographies by topics / Alpha-Synuclein, Prion Protein, Aggregation

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Academic literature on the topic 'Alpha-Synuclein, Prion Protein, Aggregation'

Author: Grafiati
Published: 14 March 2023
Last updated: 27 July 2025

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Journal articles on the topic "Alpha-Synuclein, Prion Protein, Aggregation"

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de Boni, Laura, Aurelia Hays Watson, Ludovica Zaccagnini та ін. "Brain region-specific susceptibility of Lewy body pathology in synucleinopathies is governed by α-synuclein conformations". Acta Neuropathologica 143, № 4 (2022): 453–69. http://dx.doi.org/10.1007/s00401-022-02406-7.

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AbstractThe protein α-synuclein, a key player in Parkinson’s disease (PD) and other synucleinopathies, exists in different physiological conformations: cytosolic unfolded aggregation-prone monomers and helical aggregation-resistant multimers. It has been shown that familial PD-associated missense mutations within the α-synuclein gene destabilize the conformer equilibrium of physiologic α-synuclein in favor of unfolded monomers. Here, we characterized the relative levels of unfolded and helical forms of cytosolic α-synuclein in post-mortem human brain tissue and showed that the equilibrium of α
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Limanaqi, Fiona, Francesca Biagioni, Carla Letizia Busceti, et al. "Phytochemicals Bridging Autophagy Induction and Alpha-Synuclein Degradation in Parkinsonism." International Journal of Molecular Sciences 20, no. 13 (2019): 3274. http://dx.doi.org/10.3390/ijms20133274.

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Among nutraceuticals, phytochemical-rich compounds represent a source of naturally-derived bioactive principles, which are extensively studied for potential beneficial effects in a variety of disorders ranging from cardiovascular and metabolic diseases to cancer and neurodegeneration. In the brain, phytochemicals produce a number of biological effects such as modulation of neurotransmitter activity, growth factor induction, antioxidant and anti-inflammatory activity, stem cell modulation/neurogenesis, regulation of mitochondrial homeostasis, and counteracting protein aggregation through modula
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Chen, Merry, Julie Vincent, Alexis Ezeanii, Saurabh Wakade, Shobha Yerigenahally та Danielle E. Mor. "Heparan sulfate proteoglycans mediate prion-like α-synuclein toxicity in Parkinson’s in vivo models". Life Science Alliance 5, № 11 (2022): e202201366. http://dx.doi.org/10.26508/lsa.202201366.

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Parkinson’s disease (PD) is a debilitating neurodegenerative disorder characterized by progressive motor decline and the aggregation of α-synuclein protein. Growing evidence suggests that α-synuclein aggregates may spread from neurons of the digestive tract to the central nervous system in a prion-like manner, yet the mechanisms of α-synuclein transmission and neurotoxicity remain poorly understood. Animal models that are amenable to high-throughput investigations are needed to facilitate the discovery of disease mechanisms. Here we describe the first Caenorhabditis elegans models in which fee
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Krawczuk, Daria, Magdalena Groblewska, Jan Mroczko, Izabela Winkel та Barbara Mroczko. "The Role of α-Synuclein in Etiology of Neurodegenerative Diseases". International Journal of Molecular Sciences 25, № 17 (2024): 9197. http://dx.doi.org/10.3390/ijms25179197.

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A presynaptic protein called α-synuclein plays a crucial role in synaptic function and neurotransmitter release. However, its misfolding and aggregation have been implicated in a variety of neurodegenerative diseases, particularly Parkinson’s disease, dementia with Lewy bodies, and multiple system atrophy. Emerging evidence suggests that α-synuclein interacts with various cellular pathways, including mitochondrial dysfunction, oxidative stress, and neuroinflammation, which contributes to neuronal cell death. Moreover, α-synuclein has been involved in the propagation of neurodegenerative proces
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Iljina, Marija, Gonzalo A. Garcia, Mathew H. Horrocks, et al. "Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading." Proceedings of the National Academy of Sciences 113, no. 9 (2016): E1206—E1215. http://dx.doi.org/10.1073/pnas.1524128113.

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The protein alpha-synuclein (αS) self-assembles into small oligomeric species and subsequently into amyloid fibrils that accumulate and proliferate during the development of Parkinson’s disease. However, the quantitative characterization of the aggregation and spreading of αS remains challenging to achieve. Previously, we identified a conformational conversion step leading from the initially formed oligomers to more compact oligomers preceding fibril formation. Here, by a combination of single-molecule fluorescence measurements and kinetic analysis, we find that the reaction in solution involv
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Medvedeva, Maria, Natalia Kitsilovskaya, Yulia Stroylova, Irina Sevostyanova, Ali Akbar Saboury, and Vladimir Muronetz. "Hydroxycinnamic Acid Derivatives from Coffee Extracts Prevent Amyloid Transformation of Alpha-Synuclein." Biomedicines 10, no. 9 (2022): 2255. http://dx.doi.org/10.3390/biomedicines10092255.

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Earlier we showed that derivatives of hydroxycinnamic acids prevent amyloid transformation of alpha-synuclein and prion protein. The aim of this work was to determine the content of 3-hydroxycinnamic acid derivatives in coffee extracts and to evaluate their activity in relation to alpha-synuclein amyloid aggregation. Hydroxycinnamic acid derivatives were identified in aqueous and ethanol extracts of coffee beans by quantitative mass spectrometric analysis. Only 3,4-dimethoxycinnamic acid (13–53 μg/mL) was detected in significant amounts in the coffee extracts, while ferulic acid was present in
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Prusiner, Stanley B., Amanda L. Woerman, Daniel A. Mordes та ін. "Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism". Proceedings of the National Academy of Sciences 112, № 38 (2015): E5308—E5317. http://dx.doi.org/10.1073/pnas.1514475112.

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Prions are proteins that adopt alternative conformations that become self-propagating; the PrPSc prion causes the rare human disorder Creutzfeldt–Jakob disease (CJD). We report here that multiple system atrophy (MSA) is caused by a different human prion composed of the α-synuclein protein. MSA is a slowly evolving disorder characterized by progressive loss of autonomic nervous system function and often signs of parkinsonism; the neuropathological hallmark of MSA is glial cytoplasmic inclusions consisting of filaments of α-synuclein. To determine whether human α-synuclein forms prions, we exami
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Piccardo, Pedro, Juraj Cervenak, Ming Bu, Lindsay Miller та David M. Asher. "Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, α-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys". Journal of General Virology 95, № 7 (2014): 1612–18. http://dx.doi.org/10.1099/vir.0.062083-0.

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Proteins aggregate in several slowly progressive neurodegenerative diseases called ‘proteinopathies’. Studies with cell cultures and transgenic mice overexpressing mutated proteins suggested that aggregates of one protein induced misfolding and aggregation of other proteins as well – a possible common mechanism for some neurodegenerative diseases. However, most proteinopathies are ‘sporadic’, without gene mutation or overexpression. Thus, proteinopathies in WT animals genetically close to humans might be informative. Squirrel monkeys infected with the classical bovine spongiform encephalopathy
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Vaquer-Alicea, Jaime, and Marc I. Diamond. "Propagation of Protein Aggregation in Neurodegenerative Diseases." Annual Review of Biochemistry 88, no. 1 (2019): 785–810. http://dx.doi.org/10.1146/annurev-biochem-061516-045049.

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Most common neurodegenerative diseases feature deposition of protein amyloids and degeneration of brain networks. Amyloids are ordered protein assemblies that can act as templates for their own replication through monomer addition. Evidence suggests that this characteristic may underlie the progression of pathology in neurodegenerative diseases. Many different amyloid proteins, including Aβ, tau, and α-synuclein, exhibit properties similar to those of infectious prion protein in experimental systems: discrete and self-replicating amyloid structures, transcellular propagation of aggregation, an
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Crestini, Alessio, Francesca Santilli, Stefano Martellucci, et al. "Prions and Neurodegenerative Diseases: A Focus on Alzheimer’s Disease." Journal of Alzheimer's Disease 85, no. 2 (2022): 503–18. http://dx.doi.org/10.3233/jad-215171.

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Specific protein misfolding and aggregation are mechanisms underlying various neurodegenerative diseases such as prion disease and Alzheimer’s disease (AD). The misfolded proteins are involved in prions, amyloid-β (Aβ), tau, and α-synuclein disorders; they share common structural, biological, and biochemical characteristics, as well as similar mechanisms of aggregation and self-propagation. Pathological features of AD include the appearance of plaques consisting of deposition of protein Aβ and neurofibrillary tangles formed by the hyperphosphorylated tau protein. Although it is not clear how p
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Dissertations / Theses on the topic "Alpha-Synuclein, Prion Protein, Aggregation"

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Aulic, Suzana. "Alpha-synuclein amyloid accumulation and its interaction with prion protein." Doctoral thesis, SISSA, 2015. http://hdl.handle.net/20.500.11767/4101.

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α-Synuclein (α-syn) plays a central role in the pathogenesis of neurodegenerative disorders collectively known as “synucleinopathies” that include Parkinson’s disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy (MSA). Understanding the underlying molecular mechanisms of neurodegenerative diseases is indispensably important because of the prevalence of these devastating conditions in the elderly population. Several findings from cell culture and in vivo experiments suggest intercellular transfer of α-syn aggregates. The concept of intracellular α-syn pathology spread was
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Roostaee, Alireza. "Importance of dimerization in aggregation and neurotoxicity of Prion and [alpha]-Synuclein in prion and Parkinson's diseases." Thèse, Université de Sherbrooke, 2012. http://hdl.handle.net/11143/6650.

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Abstract: Neurodegenerative diseases are associated with progressive loss of structure or function of neurons which results in cell death. Recent evidence indicate that all neurodegenerative disorders, sporadic or transmissible, may have a common pathological mechanism at the molecular level. This common feature consists of protein aggregation and accumulation of harmful aggregates in neuronal cells resulting in cellular apoptosis and neurotoxicity. Neurodegenerative diseases can affect abstract thinking, skilled movements, emotional feelings, cognition, memory and other abilities. This divers
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Ryazanov, Sergey. "Oligomer modulator anle138b and related compounds in neurodegeneration and beyond." Doctoral thesis, Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2020. http://hdl.handle.net/21.11130/00-1735-0000-0005-1519-8.

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Fonseca, Ornelas Luis Eduardo Verfasser], Markus [Akademischer Betreuer] Zweckstetter, Tiago Fleming [Gutachter] Outeiro, et al. "Modulating the aggregation of alpha-synuclein and prion protein with small molecules. / Luis Eduardo Fonseca Ornelas ; Gutachter: Tiago Fleming Outeiro, Henning Urlaub, Kai Tittmann, Christian Griesinger, Reinhard Jahn ; Betreuer: Markus Zweckstetter." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2016. http://d-nb.info/1118846931/34.

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Morgan, Sophie. "The prion-like properties of assembled human alpha-synuclein." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/277553.

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The pathological hallmark of many age-related neurodegenerative diseases is the presence of proteinaceous inclusions in nerve cells and glial cells. Alpha-synuclein is the main component of the inclusions of Parkinson’s disease, dementia with Lewy bodies and multiple system atrophy, as well as of rarer diseases, collectively called synucleinopathies. For a long time, it was widely believed that neurodegenerative diseases were cell-autonomous; however, a more recent hypothesis has suggested that some misfolded proteins resemble prions. Thus, aggregated alpha-synuclein shares features of PrPSc,
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Iljina, Marija. "Aggregation of alpha-synuclein using single-molecule spectroscopy." Thesis, University of Cambridge, 2017. https://www.repository.cam.ac.uk/handle/1810/263216.

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The aggregation of alpha-synuclein (αS) protein from soluble monomer into solid amyloid fibrils in the brain is associated with a range of devastating neurodegenerative disorders such as Parkinson’s disease. Soluble oligomers formed during the aggregation process are highly neurotoxic and are thought to play a key role in the onset and spreading of disease. Despite their importance, these species are difficult to study by conventional experimental approaches owing to their transient nature, heterogeneity, low abundance and a remarkable sensitivity of the oligomerisation process to the chosen e
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Tosatto, Laura. "Insights on alpha-synuclein interaction network and aggregation pattern." Doctoral thesis, Università degli studi di Padova, 2009. http://hdl.handle.net/11577/3426440.

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Parkinson’s disease (PD) is the most important neurodegenerative disease which regards movement. The 1% of the population over 65 years old is affected by this disorder. The main symptoms are bradykinesia, resting tremor, postural instability, muscle rigidity and sometimes cognitive and personality problems. The cause of the disease is a selective death of dopaminergic neurons in substantia nigra pars compacta. Actually, the best therapy can help to solve only symptoms and it is based on the supply of the precursor of dopamine, which is the neurotransmitter lacking in the disease, or inhibitor
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Plotegher, Nicoletta. "Unraveling the mechanisms of alpha-synuclein aggregation and toxicity." Doctoral thesis, Università degli studi di Padova, 2013. http://hdl.handle.net/11577/3423061.

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Parkinson’s disease is the second most common neurodegenerative disorder after Alzheimer’s disease and affects about 1% of the population over 65 years old. This disorder can be both sporadic and familial and some genetic forms are due to mutations in SNCA gene, encoding for the protein alpha-synuclein (aS). PD pathological hallmarks are the prominent death of the dopaminergic neurons in the substantia nigra pars compacta and the presence of proteins and lipid inclusions, termed Lewy’s body (LBs), in the surviving neurons in parkinsonian brains. The main constituent of LBs is an aggregated fi
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Goodwin, Jacob J. "The Role of Calcium in Alpha-Synuclein Aggregation: A Potential Mechanism of Neurodegeneration." Thesis, Griffith University, 2014. http://hdl.handle.net/10072/366325.

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Abnormal protein aggregation has been implicated in the pathogenesis of many neurological disorders. This study focuses on the protein alpha-synuclein (α-syn), a pre- synaptic protein that is involved in a number of diseases collectively termed alpha- synucleinopathies, which include Parkinson’s disease (PD) and Multiple System Atrophy (MSA). α-syn aggregation and microscopically-visible α-syn-positive intracellular inclusion bodies are common features of these diseases, occurring in multiple cell types and localisation throughout the central nervous system. Although gene mutati
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De, Franceschi Giorgia. "Alpha-Synuclein and polyunsaturated fatty acids molecular characterization of the interaction and implication in protein aggregation." Doctoral thesis, Università degli studi di Padova, 2009. http://hdl.handle.net/11577/3426125.

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The project of my PhD Thesis focuses on the general problem of the protein folding and misfolding in line with the research conducted in the laboratory of Protein Chemistry at CRIBI, where the work was mainly conducted. My research activity can be divided in two parts. In the first year of the PhD course I studied the effect of pH in protein fibrillogenesis using a peptide model. During the second and the third years, my research was focused into the molecular interaction between alpha-synuclein and fatty acids and its implications in alpha-synuclein aggregation. Thus, this PhD Thesis is com
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Book chapters on the topic "Alpha-Synuclein, Prion Protein, Aggregation"

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Fu, YuHong, Onur Tanglay, Hongyun Li, and Glenda M. Halliday. "The Role of Alpha-Synuclein Pathology." In Neuromethods. Springer US, 2024. http://dx.doi.org/10.1007/978-1-0716-4083-8_2.

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AbstractAlpha-synuclein (αSyn) is a conformationally flexible protein that is known to be involved in key neuronal biological processes and the pathogenesis of Parkinson’s disease (PD). The aggregation of αSyn in the brain is not only the neuropathological hallmark of PD but also characterizes other primary synucleinopathies, including dementia with Lewy bodies (DLB) and multiple system atrophy (MSA). These disorders share common clinical motor symptoms, namely, parkinsonism, which is associated with the loss of nigral dopaminergic neurons. Pathologically the selective neurodegeneration in syn
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Banu, Khaji Firdous, Rage Rekha, Sasikala Chinnappan, et al. "Andrographolide and its Neuroprotective Potential in Ameliorating Parkinson’s Disease." In Therapeutic Insights into Herbal Medicine through the Use of Phytomolecules. BENTHAM SCIENCE PUBLISHERS, 2024. http://dx.doi.org/10.2174/9789815238129124030011.

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Neurodegenerative diseases such as Alzheimer’s, Parkinson’s, Huntington’s and Prion-related diseases are age-related progressive disorders. Among neurodegenerative diseases, Parkinson’s disease is the second most common disease after Alzheimer’s. Every year, millions of people were affected by Parkinson’s disease. The formation of α-synuclein protein aggregation associated with degeneration of dopaminergic neurons is the main pathological hallmark of PD. Patients suffering from this disease live in an impairing condition and impose huge financial as well as psychological burdens on society. Ho
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Silva, Igor José Siqueira da, Manuele Figueiredo da Silva, Thiago Santos de Assis Dutra, et al. "Alpha-synuclein aggregation in Parkinson’s disease." In Advances in Protein Chemistry and Structural Biology. Elsevier, 2025. https://doi.org/10.1016/bs.apcsb.2024.11.002.

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Dimitrova-Shumkovska, Jasmina, and Ljupcho Krstanoski. "Alpha-Synuclein Aggregation, Cholesterol Transport, and the 18-kDa Translocator Protein." In Synucleins - Biochemistry and Role in Diseases. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.83459.

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Bagree, Gayatri, Oshadie De Silva, Piyumi Dinusha Liyanage, Sanje Mahasivam, Vipul Bansal, and Rajesh Ramanathan. "Alpha-synuclein as a Molecular Marker for the Diagnosis of Neurological Disorders." In Low-cost Diagnostics. Royal Society of Chemistry, 2024. https://doi.org/10.1039/9781837673216-00286.

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Intracellular deposits of α-synuclein (α-syn) protein are a conventional indicator of synucleinopathies. Despite tremendous advances in understanding the pathophysiology of synucleinopathies, histological investigations and clinical symptoms are still extensively used in diagnosis. Identification of key biomarkers of these diseases using diagnostic techniques is a continuing challenge. As the aggregation of α-syn is an indicator of synucleinopathies, this can be used as a biomarker for developing diagnostic platforms. This chapter highlights the working principle of different diagnostic tools
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Conference papers on the topic "Alpha-Synuclein, Prion Protein, Aggregation"

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Ivey, Paula-Marie E., Arjun Krishnamoorthi, Sehong Min, Jean-Christophe Rochet, and Kevin J. Webb. "Fluorescence Lifetime Imaging of Protein Aggregation to Understand the Etiology of Neurodegenerative Diseases." In CLEO: Applications and Technology. Optica Publishing Group, 2022. http://dx.doi.org/10.1364/cleo_at.2022.jth3a.8.

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Time-domain fluorescence lifetime imaging microscopy is presented for the detection of alpha-synuclein aggregation in neurons and for determining spread, thereby facilitating understanding of the development and progression of Parkinson’s disease.
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Lanza, M., A. Beretz, A. Stierlé, D. Hanau, M. Kubina, and J. P. Cazenave. "ADRENALINE ACTIVATES HUMAN PLATELETS BUT IS NOT PER SE AN AGGREGATING AGENT. EFFECTS ON PLATELET MORPHOLOGY, MEMBRANEFLUIDITY, FIBRINOGEN BINDING, CYTOPLASMIC FREE CALCIUM AND PROTEIN PHOSPHORYLATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643762.

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Adrenaline (Adr) is generally considered as a full agonist able to induce in vitro the aggregation of human platelets and could play an important role in vivo in the appearance of thrombotic disorders when catecholamine levels are increased. Adr 2.5 M) induces the aggregation and secretion of 41 % of preloaded 3H-serotonin in human platelets in citrated plasma. This effect is not seen in plasma collected on 50 ATU/ml hirudin, and is due to the generation of traces of thrombin during blood collection and not to a direct effect of citrate itself, such asthe lowering of plasma free calcium. With
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Crouch, Michael F., and Eduardo G. Lapetina. "PHOSPHOLIPASE A2 ACTIVATION BY A MECHANISM SEPARATE TO THAT RESPONSIBLE FOR PHOSPHOLIPASE C STIMULATION IN ALPHA-THROMBIN-STIMULATED HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644470.

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The ability of cell surface receptor occupation to increase the activity of phospholipase A2 has been thought to be due to the prior activation of phospholipase C and an increase in the intracellular Ca2+ concentration. However, recent evidence from our and other laboratories has suggested that this may not be the case, but rather stimulation of phospholipase A2 may be under the control of separate receptor-activated events. We have investigated this further by comparing the ability of prostacyclin (PGI2) and epinephrine to alter platelet responses to thrombin and examining the resulting phosp
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