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https://www.readbyqxmd.com/read/29349578/in-situ-tissue-labeling-of-cerebral-amyloid-using-hiv-related-tat-peptide
#1
E Maderna, L Colombo, A Cagnotto, G Di Fede, A Indaco, F Tagliavini, M Salmona, G Giaccone
Delivering peptide-based drugs to the brain is a major challenge because of the existence of the blood-brain barrier (BBB). To overcome this problem, cell-penetrating peptides derived from proteins that are able to cross biological membranes have been used as cell-permeable and brain-penetrant compounds. An example is the transactivator of transcription protein transduction domain (Tat) of the human immunodeficiency virus. The basic domain of Tat is formed of arginine and lysine amino acid residues. Tat has been used as brain-penetrant carrier also in therapies for Alzheimer disease (AD), the most common form of dementia characterized by extracellular cerebral deposits of amyloid made up of Aβ peptide...
January 19, 2018: Molecular Neurobiology
https://www.readbyqxmd.com/read/29346380/rapidly-progressive-dementia-an-eight-year-2008-2016-retrospective-study
#2
Patil Anuja, Vishnu Venugopalan, Naheed Darakhshan, Pandit Awadh, Vinny Wilson, Goyal Manoj, Modi Manish, Lal Vivek
BACKGROUND AND PURPOSE: Rapidly progressive dementia (RPD) is an emergency in cognitive neurology, defined as cognitive impairment affecting the daily living activities developed over less than 1 year. This study investigated the profile of patients with rapidly progressive dementia at first presentation. METHODS: Retrospective case analysis was done in 187 patients with rapidly progressive dementia who presented to the Postgraduate Institute of Medical Education and Research, Chandigarh, India from January 2008 to August 2016...
2018: PloS One
https://www.readbyqxmd.com/read/29345730/regional-pattern-of-microgliosis-in-sporadic-creutzfeldt-jakob-disease-in-relation-to-phenotypic-variants-and-disease-progression
#3
Alessia Franceschini, Rosaria Strammiello, Sabina Capellari, Armin Giese, Piero Parchi
AIMS: To describe the regional profiles of microglial activation in sporadic Creutzfeldt-Jakob disease (sCJD) subtypes and analyse the influence of prion strain, disease duration and codon 129 genotype. METHODS: We studied the amount/severity and distribution of activated microglia, protease-resistant prion protein (PrPSc ) spongiform change, and astrogliosis in 8 regions of 57 brains representative of the entire spectrum of sCJD subtypes. RESULTS: In each individual subtype, the regional extent and distribution of microgliosis significantly correlated with PrPSc deposition and spongiform change, leading to subtype-specific "lesion profiles"...
January 18, 2018: Neuropathology and Applied Neurobiology
https://www.readbyqxmd.com/read/29338055/a-novel-gerstmann-str%C3%A3-ussler-scheinker-disease-mutation-defines-a-precursor-for-amyloidogenic-8-kda-prp-fragments-and-reveals-n-terminal-structural-changes-shared-by-other-gss-alleles
#4
Robert C C Mercer, Nathalie Daude, Lyudmyla Dorosh, Ze-Lin Fu, Charles E Mays, Hristina Gapeshina, Serene L Wohlgemuth, Claudia Y Acevedo-Morantes, Jing Yang, Neil R Cashman, Michael B Coulthart, Dawn M Pearson, Jeffrey T Joseph, Holger Wille, Jiri G Safar, Gerard H Jansen, Maria Stepanova, Brian D Sykes, David Westaway
To explore pathogenesis in a young Gerstmann-Sträussler-Scheinker Disease (GSS) patient, the corresponding mutation, an eight-residue duplication in the hydrophobic region (HR), was inserted into the wild type mouse PrP gene. Transgenic (Tg) mouse lines expressing this mutation (Tg.HRdup) developed spontaneous neurologic syndromes and brain extracts hastened disease in low-expressor Tg.HRdup mice, suggesting de novo formation of prions. While Tg.HRdup mice exhibited spongiform change, PrP aggregates and the anticipated GSS hallmark of a proteinase K (PK)-resistant 8 kDa fragment deriving from the center of PrP, the LGGLGGYV insertion also imparted alterations in PrP's unstructured N-terminus, resulting in a 16 kDa species following thermolysin exposure...
January 16, 2018: PLoS Pathogens
https://www.readbyqxmd.com/read/29337365/loss-of-sti1-mediated-neuronal-survival-and-differentiation-in-disease-associated-mutations-of-prion-protein
#5
M C Landemberger, G P Oliveira, C F Machado, K J Gollob, V R Martins
Cellular prion protein (PrPC ) is widely expressed and displays a variety of well-described functions in the central nervous system (CNS). Mutations of the PRNP gene are known to promote genetic human spongiform encephalopathies, but the components of gain- or loss-of-function mutations to PrPC remain a matter for debate. Among the proteins described to interact with PrPC is stress inducible protein 1 (STI1), a co-chaperonin that is secreted from astrocytes and triggers neuroprotection and neuritogenesis through its interaction with PrPC ...
January 16, 2018: Journal of Neurochemistry
https://www.readbyqxmd.com/read/29335561/sub-%C3%A3-ngstr%C3%A3-m-cryo-em-structure-of-a-prion-protofibril-reveals-a-polar-clasp
#6
Marcus Gallagher-Jones, Calina Glynn, David R Boyer, Michael W Martynowycz, Evelyn Hernandez, Jennifer Miao, Chih-Te Zee, Irina V Novikova, Lukasz Goldschmidt, Heather T McFarlane, Gustavo F Helguera, James E Evans, Michael R Sawaya, Duilio Cascio, David S Eisenberg, Tamir Gonen, Jose A Rodriguez
The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the β2-α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named 'polar clasps'.
January 15, 2018: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/29331212/prion-protein-as-a-toxic-acceptor-of-amyloid-%C3%AE-oligomers
#7
REVIEW
Silvia A Purro, Andrew J Nicoll, John Collinge
The initial report that cellular prion protein (PrPC) mediates toxicity of amyloid-β species linked to Alzheimer's disease was initially treated with scepticism, but growing evidence supports this claim. That there is a high-affinity interaction is now clear, and its molecular basis is being unraveled, while recent studies have identified possible downstream toxic mechanisms. Determination of the clinical significance of such interactions between PrPC and disease-associated amyloid-β species will require experimental medicine studies in humans...
February 15, 2018: Biological Psychiatry
https://www.readbyqxmd.com/read/29330304/efficient-prion-disease-transmission-through-common-environmental-materials
#8
Sandra Pritzkow, Rodrigo Morales, Adam Lyon, Luis Concha-Marambio, Akihiko Urayama, Claudio Soto
Prion diseases are a group of fatal neurodegenerative diseases associated with a protein-based infectious agent, termed prion. Compelling evidence suggests that natural transmission of prion diseases is mediated by environmental contamination with infectious prions. We hypothesized that several natural and man-made materials, commonly found in the environments of wild and captive animals, can bind prions and may act as vectors for disease transmission. To test our hypothesis, we exposed surfaces composed of various common environmental materials (i...
January 12, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29330303/mammalian-amyloidogenic-proteins-promote-prion-nucleation-in-yeast
#9
Pavithra Chandramowlishwaran, Meng Sun, Kristin L Casey, Andrey V Romanyuk, Anastasiya V Grizel, Julia V Sopova, Aleksandr A Rubel, Carmen Nussbaum-Krammer, Ina M Vorberg, Yury O Chernoff
Fibrous cross-β aggregates (amyloids) and their transmissible forms (prions) cause diseases in mammals (including humans) and control heritable traits in yeast. Initial nucleation of a yeast prion by transiently overproduced prion-forming protein or its (typically, QN-rich) prion domain is efficient only in the presence of another aggregated (in most cases, QN-rich) protein. Here, we demonstrate that a fusion of the prion domain of yeast protein Sup35 to some non-QN-rich mammalian proteins, associated with amyloid diseases, promotes nucleation of Sup35 prions in the absence of preexisting aggregates...
January 12, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29330300/real-time-imaging-of-yeast-cells-reveals-several-distinct-mechanisms-of-curing-of-the-ure3-prion
#10
Xiaohong Zhao, Jenna Lanz, Danielle Steinberg, Tyler Pease, Joseph M Ahearn, Evgeny E Bezsonov, Elena Staguhn, Evan Eisenberg, Daniel C Masison, Lois E Greene
The [URE3] yeast prion is the self-propagating amyloid form of the Ure2 protein. [URE3] is cured by overexpression of several yeast proteins, including Ydj1, Btn2, Cur1, Hsp42, and human DnaJB6. To better understand [URE3] curing, we used real-time imaging with a yeast strain expressing a GFP-labeled full-length Ure2 construct to monitor the curing of [URE3] over time. [URE3] yeast cells exhibited numerous fluorescent foci, and expression of the GFP-labeled Ure2 affected neither mitotic stability of [URE3] nor the rate of [URE3] curing by the curing proteins...
January 12, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29329958/contact-tracing-for-the-control-of-infectious-disease-epidemics-chronic-wasting-disease-in-deer-farms
#11
Chris Rorres, Maria Romano, Jennifer A Miller, Jana M Mossey, Tony H Grubesic, David E Zellner, Gary Smith
Contact tracing is a crucial component of the control of many infectious diseases, but is an arduous and time consuming process. Procedures that increase the efficiency of contact tracing increase the chance that effective controls can be implemented sooner and thus reduce the magnitude of the epidemic. We illustrate a procedure using Graph Theory in the context of infectious disease epidemics of farmed animals in which the epidemics are driven mainly by the shipment of animals between farms. Specifically, we created a directed graph of the recorded shipments of deer between deer farms in Pennsylvania over a timeframe and asked how the properties of the graph could be exploited to make contact tracing more efficient should Chronic Wasting Disease (a prion disease of deer) be discovered in one of the farms...
December 14, 2017: Epidemics
https://www.readbyqxmd.com/read/29329906/development-of-a-quick-bioassay-for-the-evaluation-of-transmission-properties-of-acquired-prion-diseases
#12
Yoshiko Munesue, Taishi Shimazaki, Zechen Qi, Norikazu Isoda, Hirofumi Sawa, Keisuke Aoshima, Takashi Kimura, Shirou Mohri, Tetsuyuki Kitamoto, Atsushi Kobayashi
Evaluation of transmission properties is important for the differential diagnosis of a subgroup of acquired Creutzfeldt-Jakob disease (CJD) with methionine homozygosity at polymorphic codon 129 of the PRNP gene, an intermediate type abnormal prion protein (PrP), and kuru plaques, denoted as acquired CJD-MMiK. The present study aimed to develop a quick evaluation system of the transmission properties of acquired CJD-MMiK. In the PrP-humanized mice intraperitoneally inoculated with brain homogenates from an acquired CJD-MMiK patient, accumulation of abnormal PrP was observed in follicular dendritic cells of the spleen at 75 days post-inoculation...
January 9, 2018: Neuroscience Letters
https://www.readbyqxmd.com/read/29321951/utility-of-the-phenacyl-protecting-group-in-traceless-protein-semisynthesis-through-ligation-desulfurization-chemistry
#13
Maria Matveenko, Stefanie Hackl, Christian F W Becker
Semisynthesis of proteins via expressed protein ligation is a widely applicable method, even more so because of the possibility of ligation at non-cysteine sites using β-mercapto amino acids that can be converted to the corresponding native amino acids by desulfurization. A drawback of this ligation- desulfurization approach is the removal of any unprotected native cysteine residues within the ligated protein segments. Here, we show that the phenacyl (PAc) moiety can be successfully used to protect cysteines within recombinantly generated protein segments...
January 2018: ChemistryOpen
https://www.readbyqxmd.com/read/29312526/amyotrophic-lateral-sclerosis-as-a-protein-level-non-genomic-disease-therapy-with-s2rm-exosome-released-molecules
#14
REVIEW
Greg Maguire
Amyotrophic lateral sclerosis (ALS) is a rapidly progressing neurodegenerative disease that leads to death. No effective treatments are currently available. Based on data from epidemiological, etiological, laboratory, and clinical studies, I offer a new way of thinking about ALS and its treatment. This paper describes a host of extrinsic factors, including the exposome, that disrupt the extracellular matrix and protein function such that a spreading, prion-like disease leads to neurodegeneration in the motor tracts...
November 26, 2017: World Journal of Stem Cells
https://www.readbyqxmd.com/read/29311311/structural-heterogeneity-and-intersubject-variability-of-a%C3%AE-in-familial-and-sporadic-alzheimer-s-disease
#15
Carlo Condello, Thomas Lemmin, Jan Stöhr, Mimi Nick, Yibing Wu, Alison M Maxwell, Joel C Watts, Christoffer D Caro, Abby Oehler, C Dirk Keene, Thomas D Bird, Sjoerd G van Duinen, Lars Lannfelt, Martin Ingelsson, Caroline Graff, Kurt Giles, William F DeGrado, Stanley B Prusiner
Point mutations in the amyloid-β (Aβ) coding region produce a combination of mutant and WT Aβ isoforms that yield unique clinicopathologies in familial Alzheimer's disease (fAD) and cerebral amyloid angiopathy (fCAA) patients. Here, we report a method to investigate the structural variability of amyloid deposits found in fAD, fCAA, and sporadic AD (sAD). Using this approach, we demonstrate that mutant Aβ determines WT Aβ conformation through prion template-directed misfolding. Using principal component analysis of multiple structure-sensitive fluorescent amyloid-binding dyes, we assessed the conformational variability of Aβ deposits in fAD, fCAA, and sAD patients...
January 8, 2018: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29310723/iatrogenic-creutzfeldt-jakob-disease-with-amyloid-%C3%AE-pathology-an-international-study
#16
Ignazio Cali, Mark L Cohen, Stéphane Haїk, Piero Parchi, Giorgio Giaccone, Steven J Collins, Diane Kofskey, Han Wang, Catriona A McLean, Jean-Philippe Brandel, Nicolas Privat, Véronique Sazdovitch, Charles Duyckaerts, Tetsuyuki Kitamoto, Ermias D Belay, Ryan A Maddox, Fabrizio Tagliavini, Maurizio Pocchiari, Ellen Leschek, Brian S Appleby, Jiri G Safar, Lawrence B Schonberger, Pierluigi Gambetti
The presence of pathology related to the deposition of amyloid-β (Aβ) has been recently reported in iatrogenic Creutzfeldt-Jakob disease (iCJD) acquired from inoculation of growth hormone (GH) extracted from human cadaveric pituitary gland or use of cadaveric dura mater (DM) grafts.To investigate this phenomenon further, a cohort of 27 iCJD cases - 21 with adequate number of histopathological sections - originating from Australia, France, Italy, and the Unites States, were examined by immunohistochemistry, amyloid staining, and Western blot analysis of the scrapie prion protein (PrPSc), and compared with age-group matched cases of sporadic CJD (sCJD), Alzheimer disease (AD) or free of neurodegenerative diseases (non-ND)...
January 8, 2018: Acta Neuropathologica Communications
https://www.readbyqxmd.com/read/29310497/differential-effects-of-divalent-cations-on-elk-prion-protein-fibril-formation-and-stability
#17
Daniel Samorodnitsky, Eric M Nicholson
Misfolding of the normally folded prion protein of mammals (PrPC) into infectious fibrils causes a variety of diseases, from scrapie in sheep to chronic wasting disease (CWD) in cervids. The misfolded form of PrPC, termed PrPSc, or in this case PrPCWD, interacts with PrPC to create more PrPCWD. This process is not clearly defined but is affected by the presence and interactions of biotic and abiotic cofactors. These include nucleic acids, lipids, glycosylation, pH, and ionic character. PrPC has been shown to act as a copper-binding protein in vivo, though it also binds to other divalents as well...
January 9, 2018: Prion
https://www.readbyqxmd.com/read/29310343/cerebrospinal-fluid-real-time-quaking-induced-conversion-test-for-sporadic-creutzfeldt-jakob-disease-in-an-18-year-old-woman-a-case-report
#18
Yuan Yao, Xiaoping Dong, Hongzhi Guan, Qiang Lu
RATIONALE: Sporadic Creutzfeldt-Jakob disease (sCJD) mainly occurs in the elderly, with the peak age of onset ranging from 55 to 75 years. The symptoms of sCJD are not unique, and laboratory tests such as magnetic resonance imaging (MRI), electroencephalogram (EEG) and cerebrospinal fluid (CSF)14-3-3 protein have low sensitivity or specificity. Therefore, excluding treatable diseases and establishing a diagnosis could be difficult in young patients with suspected sCJD. Recently, real-time quaking-induced conversion (RT-QuIC) has been used in the diagnosis of sCJD, with more than 95% sensitivity and 100% specificity...
December 2017: Medicine (Baltimore)
https://www.readbyqxmd.com/read/29310300/a-new-electrochemical-immunosensor-for-sensitive-detection-of-prion-based-on-prussian-blue-analogue
#19
Junjing Li, Xiaoxia Yan, Xiaoyu Li, Xiaohua Zhang, Jinhua Chen
Based on Co-Co Prussian blue analogue (Co-Co PBA), a novel immunosensor has been developed for sensitive detection of prion protein (PrPC). Gold nanoparticles (AuNPs)-modified Co-Co PBA nanocubes (PBA-AuNPs) worked as a support of the antibody (Ab2) of PrPC to obtain Ab2-PBA-AuNPs composite and also as the signal source for PrPC assay. When PrPC existed, Ab2-PBA-AuNPs could be introduced to the surface of another antibody of PrPC (Ab1) modified AuNPs/GC electrode (the gold nanoparticles-modified glassy carbon electrode) through specific antigen-antibody interaction between PrPC and its antibodies to form the Ab1-PrPC-Ab2 sandwich structure...
March 1, 2018: Talanta
https://www.readbyqxmd.com/read/29308725/the-role-of-the-prion-protein-in-the-internalization-of-%C3%AE-synuclein-amyloids
#20
Elena De Cecco, Giuseppe Legname
Synucleinopathies are a group of neurodegenerative diseases characterized by the accumulation of α-synuclein amyloids in several regions of the brain. α-Synuclein fibrils are able to spread via cell-to-cell transfer, and once inside the cells, they can template the misfolding and aggregation of the endogenous α-synuclein. Multiple mechanisms have been shown to participate in the process of propagation: endocytosis, tunneling nanotubes and micropinocytosis. Recently, we published a research showing that the cellular form of the prion protein (PrPC) acts as a receptor for α-synuclein amyloid fibrils, facilitating their internalization through and endocytic pathway...
January 8, 2018: Prion
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