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https://www.readbyqxmd.com/read/28538692/exploring-anti-prion-glyco-based-and-aromatic-scaffolds-a-chemical-strategy-for-the-quality-of-life
#1
REVIEW
María Teresa Blázquez-Sánchez, Ana M de Matos, Amélia P Rauter
Prion diseases are fatal neurodegenerative disorders caused by protein misfolding and aggregation, affecting the brain progressively and consequently the quality of life. Alzheimer's is also a protein misfolding disease, causing dementia in over 40 million people worldwide. There are no therapeutics able to cure these diseases. Cellular prion protein is a high-affinity binding partner of amyloid β (Aβ) oligomers, the most toxic species in Alzheimer's pathology. These findings motivate the development of new chemicals for a better understanding of the events involved...
May 24, 2017: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://www.readbyqxmd.com/read/28533442/the-role-of-shed-prp-c-in-the-neuropathogenesis-of-hiv-infection
#2
Bezawit W Megra, Eliseo A Eugenin, Joan W Berman
HIV-1 enters the CNS soon after peripheral infection and causes chronic neuroinflammation and neuronal damage that leads to cognitive impairment in 40-70% of HIV-infected people. The nonpathogenic cellular isoform of the human prion protein (PrP(c)) is an adhesion molecule constitutively expressed in the CNS. Previously, our laboratory showed that shed PrP(c) (sPrP(c)) is increased in the cerebrospinal fluid of HIV-infected people with cognitive deficits as compared with infected people with no impairment. In this article, we demonstrate that CCL2 and TNF-α, inflammatory mediators that are elevated in the CNS of HIV-infected people, increase shedding of PrP(c) from human astrocytes by increasing the active form of the metalloprotease ADAM10...
May 22, 2017: Journal of Immunology: Official Journal of the American Association of Immunologists
https://www.readbyqxmd.com/read/28532450/lps-induced-systemic-inflammation-reveals-an-immunomodulatory-role-for-the-prion-protein-at-the-blood-brain-interface
#3
Ø Salvesen, M R Reiten, A Espenes, M K Bakkebø, M A Tranulis, C Ersdal
BACKGROUND: The cellular prion protein (PrP(C)) is an evolutionary conserved protein abundantly expressed not only in the central nervous system but also peripherally including the immune system. A line of Norwegian dairy goats naturally devoid of PrP(C) (PRNP (Ter/Ter)) provides a novel model for studying PrP(C) physiology. METHODS: In order to explore putative roles for PrP(C) in acute inflammatory responses, we performed a lipopolysaccharide (LPS, Escherichia coli O26:B6) challenge of 16 goats (8 PRNP (+/+) and 8 PRNP (Ter/Ter)) and included 10 saline-treated controls (5 of each PRNP genotype)...
May 22, 2017: Journal of Neuroinflammation
https://www.readbyqxmd.com/read/28531192/overexpression-of-the-essential-sis1-chaperone-reduces-tdp-43-effects-on-toxicity-and-proteolysis
#4
Sei-Kyoung Park, Joo Y Hong, Fatih Arslan, Vydehi Kanneganti, Basant Patel, Alex Tietsort, Elizabeth M H Tank, Xingli Li, Sami J Barmada, Susan W Liebman
Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disease characterized by selective loss of motor neurons with inclusions frequently containing the RNA/DNA binding protein TDP-43. Using a yeast model of ALS exhibiting TDP-43 dependent toxicity, we now show that TDP-43 overexpression dramatically alters cell shape and reduces ubiquitin dependent proteolysis of a reporter construct. Furthermore, we show that an excess of the Hsp40 chaperone, Sis1, reduced TDP-43's effect on toxicity, cell shape and proteolysis...
May 22, 2017: PLoS Genetics
https://www.readbyqxmd.com/read/28527237/the-n-terminus-of-the-prion-protein-is-a-toxic-effector-regulated-by-the-c-terminus
#5
Bei Wu, Alex J McDonald, Kathleen Markham, Celeste B Rich, Kyle P Mchugh, Jörg Tatzelt, David W Colby, Glenn L Millhauser, David A Harris
PrP(C), the cellular isoform of the prion protein, serves to transduce the neurotoxic effects of PrP(Sc), the infectious isoform, but how this occurs is mysterious. Here, using a combination of electrophysiological, cellular, and biophysical techniques, we show that the flexible, N-terminal domain of PrP(C) functions as a powerful toxicity-transducing effector whose activity is tightly regulated in cis by the globular C-terminal domain. Ligands binding to the N-terminal domain abolish the spontaneous ionic currents associated with neurotoxic mutants of PrP, and the isolated N-terminal domain induces currents when expressed in the absence of the C-terminal domain...
May 20, 2017: ELife
https://www.readbyqxmd.com/read/28521568/prion-based-memory-of-heat-stress-in-yeast
#6
Tatiana A Chernova, Yury O Chernoff, Keith D Wilkinson
Amyloids and amyloid-based prions are self-perpetuating protein aggregates which can spread by converting a normal protein of the same sequence into a prion form. They are associated with diseases in humans and mammals, and control heritable traits in yeast and other fungi. Some amyloids are implicated in biologically beneficial processes. As prion formation generates reproducible memory of a conformational change, prions can be considered as molecular memory devices.  We have demonstrated that in yeast, stress-inducible cytoskeleton-associated protein Lsb2 forms a metastable prion in response to high temperature...
May 19, 2017: Prion
https://www.readbyqxmd.com/read/28520598/imaging-plus-x-multimodal-models-of-neurodegenerative-disease
#7
Neil P Oxtoby, Daniel C Alexander
PURPOSE OF REVIEW: This article argues that the time is approaching for data-driven disease modelling to take centre stage in the study and management of neurodegenerative disease. The snowstorm of data now available to the clinician defies qualitative evaluation; the heterogeneity of data types complicates integration through traditional statistical methods; and the large datasets becoming available remain far from the big-data sizes necessary for fully data-driven machine-learning approaches...
May 16, 2017: Current Opinion in Neurology
https://www.readbyqxmd.com/read/28518033/distribution-and-quantitative-estimates-of-variant-creutzfeldt-jakob-disease-prions-in-tissues-of-clinical-and-asymptomatic-patients
#8
Jean Y Douet, Caroline Lacroux, Naima Aron, Mark W Head, Séverine Lugan, Cécile Tillier, Alvina Huor, Hervé Cassard, Mark Arnold, Vincent Beringue, James W Ironside, Olivier Andréoletti
In the United-Kingdom, ≈1 of 2,000 persons could be infected with variant Creutzfeldt-Jakob disease (vCJD). Therefore, risk of transmission of vCJD by medical procedures remains a major concern for public health authorities. In this study, we used in vitro amplification of prions by protein misfolding cyclic amplification (PMCA) to estimate distribution and level of the vCJD agent in 21 tissues from 4 patients who died of clinical vCJD and from 1 asymptomatic person with vCJD. PMCA identified major levels of vCJD prions in a range of tissues, including liver, salivary gland, kidney, lung, and bone marrow...
June 2017: Emerging Infectious Diseases
https://www.readbyqxmd.com/read/28516990/cross-talk-between-neurometals-and-amyloidogenic-proteins-at-the-synapse-and-the-pathogenesis-of-neurodegenerative-diseases
#9
REVIEW
M Kawahara, M Kato-Negishi, K Tanaka
Increasing evidence suggests that disruption of metal homeostasis contributes to the pathogenesis of various neurodegenerative diseases, including Alzheimer's disease, prion diseases, Lewy body diseases, and vascular dementia. Conformational changes of disease-related proteins (amyloidogenic proteins), such as β-amyloid protein, prion proteins, and α-synuclein, are well-established contributors to neurotoxicity and to the pathogenesis of these diseases. Recent studies have demonstrated that these amyloidogenic proteins are metalloproteins that bind trace elements, including zinc, iron, copper, and manganese, and play significant roles in the maintenance of metal homeostasis...
May 18, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28515679/downregulation-of-the-repressor-element-1-silencing-transcription-factor-rest-is-associated-with-akt-mtor-and-wnt-%C3%AE-catenin-signaling-in-prion-diseases-models
#10
Zhiqi Song, Syed Z A Shah, Wei Yang, Haodi Dong, Lifeng Yang, Xiangmei Zhou, Deming Zhao
Prion diseases are a group of infectious diseases characterized by multiple neuropathological changes, yet the mechanisms that preserve function and protect against prion-associated neurodegeneration are still unclear. We previously reported that the repressor element 1-silencing transcription factor (REST) alleviates neurotoxic prion peptide (PrP106-126)-induced toxicity in primary neurons. Here we confirmed the findings of the in vitro model in 263K infected hamsters, an in vivo model of prion diseases and further showed the relationships between REST and related signaling pathways...
2017: Frontiers in Molecular Neuroscience
https://www.readbyqxmd.com/read/28513534/unraveling-prion-protein-interactions-with-aptamers-and-other-prp-binding-nucleic-acids
#11
REVIEW
Bruno Macedo, Yraima Cordeiro
Transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative disorders that affect humans and other mammals. The etiologic agents common to these diseases are misfolded conformations of the prion protein (PrP). The molecular mechanisms that trigger the structural conversion of the normal cellular PrP (PrP(C)) into the pathogenic conformer (PrP(Sc)) are still poorly understood. It is proposed that a molecular cofactor would act as a catalyst, lowering the activation energy of the conversion process, therefore favoring the transition of PrP(C) to PrP(Sc)...
May 17, 2017: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/28509623/gastrostomy-in-patients-with-prion-disease
#12
Yasushi Iwasaki, Keiko Mori, Masumi Ito, Yoshinari Kawai, Ken-Ichiro Hoshino, Yuko Kawabata, Maya Mimuro, Mari Yoshida
Patients with prion diseases can live for long periods of time in a state of akinetic mutism given appropriate management of their symptoms. To study symptom support in these cases, we performed gastrostomies on three patients with V180I genetic Creutzfeldt-Jakob disease (CJD) who had become akinetic and mute, and compared them to 14 other similar patients being fed by tube. In the three gastrostomy cases, there were no direct complications due to the gastrostomy or tube feeding, nor were there episodes of discontinuation of tube feeding or initiation of continuous drip infusion due to severe complications...
May 16, 2017: Prion
https://www.readbyqxmd.com/read/28509609/amyloid-and-fdg-pet-in-sporadic-creutzfeldt-jakob-disease-correlation-with-pathological-prion-protein-in-neuropathology
#13
Jordi A Matías-Guiu, Carmen Guerrero-Márquez, María Nieves Cabrera-Martín, Ulises Gómez-Pinedo, María Romeral, Diego Mayo, Jesús Porta-Etessam, Teresa Moreno-Ramos, José Luis Carreras, Jorge Matías-Guiu
INTRODUCTION: The role of positron emission tomography (PET) in Creutzfeldt-Jakob disease is less defined than in other neurodegenerative diseases. We studied the correlation between the uptake of (18)F-florbetaben and (18)F-fluorodeoxyglucose with pathological prion protein deposition in histopathology in a case. METHODS: A patient with 80 y old with a rapid neurological deterioration with a confirmed diagnosis of CJD was studied. PET and MRI studies were performed between 13-20 d before the death...
May 16, 2017: Prion
https://www.readbyqxmd.com/read/28509424/inhibition-of-prion-propagation-by-3-4-dimethoxycinnamic-acid
#14
Ivan Zanyatkin, Yulia Stroylova, Sofia Tishina, Victor Stroylov, Aleksandra Melnikova, Thomas Haertle, Vladimir Muronetz
Neurodegenerative diseases are associated with accumulation of amyloid-type protein misfolding products. Prion protein (PrP) is known for its ability to aggregate into soluble oligomers that in turn associate into amyloid fibrils. Preventing the formation of these infective and neurotoxic entities represents a viable strategy to control prion diseases. Numerous attempts to find dietary compounds with anti-prion properties have been made; however, the most promising agent found so far was curcumin, which is poorly soluble and merely bioavailable...
May 16, 2017: Phytotherapy Research: PTR
https://www.readbyqxmd.com/read/28508264/biological-safety-of-a-highly-purified-10-liquid-intravenous-immunoglobulin-preparation-from-human-plasma
#15
Caroline Goussen, Steve Simoneau, Soline Bérend, Christine Jehan-Kimmel, Anne Bellon, Céline Ducloux, Bruno You, Philippe Paolantonacci, Monique Ollivier, Ludovic Burlot, Sami Chtourou, Benoît Flan
BACKGROUND: A highly purified 10% liquid intravenous immunoglobulin, IQYMUNE(®), has been developed using an innovative manufacturing process including an affinity chromatography step for the removal of anti-A and anti-B hemagglutinins. OBJECTIVES: The pathogen (viruses and prions) clearance efficacy of the manufacturing process and its robustness for critical steps were investigated. METHODS: The manufacturing process of IQYMUNE(®) includes two dedicated complementary virus reduction steps: solvent/detergent (S/D) treatment and 20 nm nanofiltration as well as two contributing steps, namely caprylic acid fractionation and anion-exchange chromatography...
May 15, 2017: BioDrugs: Clinical Immunotherapeutics, Biopharmaceuticals and Gene Therapy
https://www.readbyqxmd.com/read/28507517/the-role-of-unfolded-protein-response-and-mitogen-activated-protein-kinase-signaling-in-neurodegenerative-diseases-with-special-focus-on-prion-diseases
#16
REVIEW
Syed Zahid Ali Shah, Deming Zhao, Tariq Hussain, Lifeng Yang
Prion diseases are neurodegenerative pathologies characterized by the accumulation of a protease-resistant form of the cellular prion protein named prion protein scrapie (PrP(Sc)) in the brain. PrP(Sc) accumulation in the endoplasmic reticulum (ER) result in a dysregulated calcium (Ca(2+)) homeostasis and subsequent initiation of unfolded protein response (UPR) leading to neuronal dysfunction and apoptosis. The molecular mechanisms for the transition between adaptation to ER stress and ER stress-induced apoptosis are still unclear...
2017: Frontiers in Aging Neuroscience
https://www.readbyqxmd.com/read/28506438/prion-like-spreading-in-tauopathies
#17
REVIEW
Jacob I Ayers, Benoit I Giasson, David R Borchelt
Tau is a microtubule-associated protein that functions in regulating cytoskeleton dynamics, especially in neurons. Misfolded and aggregated forms of tau produce pathological structures in a number of neurodegenerative diseases, including Alzheimer's disease (AD) and tauopathy dementias. These disorders can present with a sporadic etiology, such as in AD, or a familial etiology, such as in some cases of frontotemporal dementia with parkinsonism. Notably, the pathological features of tau pathology in these diseases can be very distinct...
April 13, 2017: Biological Psychiatry
https://www.readbyqxmd.com/read/28503968/the-five-stages-of-prisoner-reentry-toward-a-process-theory
#18
Ioan Durnescu
This article is based on an ethnographic study involving 58 Roma and Romanian participants who were released from Jilava Prion in Romania between January and July 2015. The methodology involved interviews, observation, questionnaires, and photovoice. The findings seem to suggest that most of the factors associated with desistance and reentry in the literature are relevant to the ex-prisoner's experiences. The main contribution of this article is the observation that these factors come into play at different times and in different stages of the reentry process...
May 1, 2017: International Journal of Offender Therapy and Comparative Criminology
https://www.readbyqxmd.com/read/28502793/salt-mediated-oligomerization-of-the-mouse-prion-protein-monitored-by-real-time-nmr
#19
Ishita Sengupta, Suhas H Bhate, Ranabir Das, Jayant B Udgaonkar
The prion protein forms ß-rich soluble oligomers in vitro at pH4 in the presence of physiological concentrations of salt. In the absence of salt, oligomerization and misfolding does not take place in an experimentally tractable timescale. While it is well established that a lowering of pH facilitates misfolding and oligomerization of this protein, the role of salt remains poorly understood. Here, solution-state NMR was used to probe perturbations in the monomeric mouse prion protein moPrP) structure immediately upon salt-addition, prior to the commencement of the oligomerization reaction...
May 11, 2017: Journal of Molecular Biology
https://www.readbyqxmd.com/read/28491313/positron-emission-tomography-imaging-in-a-case-of-e200k-mutation-related-spongiform-encephalopathy-with-non-diagnostic-magnetic-resonance-imaging-and-cerebrospinal-fluid-testing
#20
Pravin George, Christopher R Newey, Karin P Mente, Erik P Pioro
OBJECTIVE: Creutzfeldt-Jakob disease is a rapidly progressive spongiform encephalopathy. The E200K mutation is found in a majority of genetically transmitted Creutzfeldt-Jakob disease cases. METHODS: We describe the case and associated neuroimaging of an E200K-129M gene-mutation-related fatal spongiform encephalopathy with resultant clinical insomnia and thalamic changes. RESULTS: A 46-year-old Caucasian male presented with, who was well until 2 months prior to admission, a rapidly progressive dementia followed by a change in personality with auditory and visual hallucinations...
2017: SAGE open medical case reports
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