168 results match your criteria Prion-Related Diseases


Genetic Perturbation of TIA1 Reveals a Physiological Role in Fear Memory.

Cell Rep 2019 Mar;26(11):2970-2983.e4

Department of Neuroscience, Mortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Psychiatry, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA; Howard Hughes Medical Institute at Columbia University, New York, NY 10032, USA; Kavli Institute for Brain Science, Columbia University, New York, NY 10032, USA. Electronic address:

TIA1 is a prion-related RNA-binding protein whose capacity to form various types of intracellular aggregates has been implicated in neurodegenerative disease. However, its role in normal brain function is poorly understood. Here, we show that TIA1 bidirectionally modulates stress-dependent synaptic plasticity in the hippocampus, a brain region involved in fear memory and olfactory discrimination learning. Read More

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http://dx.doi.org/10.1016/j.celrep.2019.02.048DOI Listing
March 2019
2 Reads

Prion-like protein gene (PRND) polymorphisms associated with scrapie susceptibility in Korean native black goats.

PLoS One 2018 25;13(10):e0206209. Epub 2018 Oct 25.

Korea Zoonosis Research Institute, Chonbuk National University, Iksan, Jeonbuk, Republic of Korea.

The polymorphisms of the prion protein (PRNP) gene, which encodes normal prion proteins (PrP), are known to be involved in the susceptibility of prion diseases. The prion-like protein (Doppel) gene (PRND) is the paralog of the PRNP gene and is closely located downstream of the PRNP gene. In addition, the polymorphisms of PRND correlate with disease susceptibility in several animals. Read More

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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0206209PLOS
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6201918PMC
April 2019
25 Reads

Prion-related peripheral neuropathy in sporadic Creutzfeldt-Jakob disease.

J Neurol Neurosurg Psychiatry 2019 Apr 24;90(4):424-427. Epub 2018 Oct 24.

IRCCS Istituto delle Scienze Neurologiche di Bologna, Bologna, Italy

Objective: To assess whether the involvement of the peripheral nervous system (PNS) belongs to the phenotypic spectrum of sporadic Creutzfeldt-Jakob disease (sCJD).

Methods: We examined medical records of 117 sCJDVV2 (ataxic type), 65 sCJDMV2K (kuru-plaque type) and 121 sCJDMM(V)1 (myoclonic type) subjects for clinical symptoms, objective signs and neurophysiological data. We reviewed two diagnostic nerve biopsies and looked for abnormal prion protein (PrP) by western blotting and real-time quaking-induced conversion (RT-QuIC) in postmortem PNS samples from 14 subjects. Read More

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http://dx.doi.org/10.1136/jnnp-2018-319221DOI Listing
April 2019
4 Reads

Mammalian prion propagation in PrP transgenic Drosophila.

Brain 2018 Sep;141(9):2700-2710

University of Cambridge, Department of Veterinary Medicine, Madingley Road, Cambridge, CB3 OES, UK.

Mammalian prions propagate by template-directed misfolding and aggregation of normal cellular prion related protein PrPC as it converts into disease-associated conformers collectively referred to as PrPSc. Mammalian species may be permissive for prion disease because these hosts have co-evolved specific co-factors that assist PrPC conformational change and prion propagation. We have tested this hypothesis by examining whether faithful prion propagation occurs in the normally PrPC-null invertebrate host Drosophila melanogaster. Read More

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http://dx.doi.org/10.1093/brain/awy183DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6113635PMC
September 2018
38 Reads

First report of prion-related protein gene () polymorphisms in cattle.

Vet Rec 2018 06 17;182(25):717. Epub 2018 Apr 17.

Department of Bioactive Material Sciences, Chonbuk National University, Jeonju, Jeonbuk, Republicof Korea.

Prion diseases are caused by structural changes in normal prion protein (PrP). The prion gene family includes four members: prion protein (), prion-like protein (), shadow of () and prion-related protein (). Genetic association studies of prion diseases and the other genes in the prion gene family, except for , have been performed in cattle. Read More

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http://veterinaryrecord.bmj.com/lookup/doi/10.1136/vr.104123
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http://dx.doi.org/10.1136/vr.104123DOI Listing
June 2018
5 Reads

Discovery of small molecules binding to the normal conformation of prion by combining virtual screening and multiple biological activity evaluation methods.

J Comput Aided Mol Des 2017 12 20;31(12):1053-1062. Epub 2017 Nov 20.

State Key Laboratory of Applied Organic Chemistry and Department of Chemistry, Lanzhou University, Lanzhou, 730000, People's Republic of China.

Conformational conversion of the normal cellular prion protein, PrP, into the misfolded isoform, PrP, is considered to be a central event in the development of fatal neurodegenerative diseases. Stabilization of prion protein at the normal cellular form (PrP) with small molecules is a rational and efficient strategy for treatment of prion related diseases. However, few compounds have been identified as potent prion inhibitors by binding to the normal conformation of prion. Read More

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http://dx.doi.org/10.1007/s10822-017-0086-6DOI Listing
December 2017
12 Reads

Semisynthetic prion protein (PrP) variants carrying glycan mimics at position 181 and 197 do not form fibrils.

Chem Sci 2017 Sep 24;8(9):6626-6632. Epub 2017 Jul 24.

Institute of Biological Chemistry , Department of Chemistry , University of Vienna , Waehringer Strasse 38 , 1090 , Vienna-AT , Austria . Email:

The prion protein (PrP) is an -glycosylated protein attached to the outer leaflet of eukaryotic cell membranes a glycosylphosphatidylinositol (GPI) anchor. Different prion strains have distinct glycosylation patterns and the extent of glycosylation of potentially pathogenic misfolded prion protein (PrP) has a major impact on several prion-related diseases (transmissible spongiform encephalopathies, TSEs). Based on these findings it is hypothesized that posttranslational modifications (PTMs) of PrP influence conversion of cellular prion protein (PrP) into PrP and, as such, modified PrP variants are critical tools needed to investigate the impact of PTMs on the pathogenesis of TSEs. Read More

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http://dx.doi.org/10.1039/c7sc02719bDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5625290PMC
September 2017
16 Reads

Chicken RNA-binding protein T-cell internal antigen-1 contributes to stress granule formation in chicken cells and tissues.

J Vet Sci 2018 Jan;19(1):3-12

Department of Avian Infectious Diseases, Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Science, Shanghai 200241, China.

T-cell internal antigen-1 (TIA-1) has roles in regulating alternative pre-mRNA splicing, mRNA translation, and stress granule (SG) formation in human cells. As an evolutionarily conserved response to environmental stress, SGs have been reported in various species. However, SG formation in chicken cells and the role of chicken TIA-1 (cTIA-1) in SG assembly has not been elucidated. Read More

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http://dx.doi.org/10.4142/jvs.2018.19.1.3DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5799397PMC
January 2018
59 Reads
1.164 Impact Factor

The first report of prion-related protein gene (PRNT) polymorphisms in goat.

Acta Vet Hung 2017 06;65(2):291-300

Korea Zoonosis Research Institute, Chonbuk National University , 820-120, Hana-ro, Iksan, Jeonbuk 570-390 , Republic of Korea.

Prion protein is encoded by the prion protein gene (PRNP). Polymorphisms of several members of the prion gene family have shown association with prion diseases in several species. Recent studies on a novel member of the prion gene family in rams have shown that prion-related protein gene (PRNT) has a linkage with codon 26 of prion-like protein (PRND). Read More

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http://dx.doi.org/10.1556/004.2017.028DOI Listing
June 2017
17 Reads

Regulation of RhoA activity by the cellular prion protein.

Cell Death Dis 2017 03 16;8(3):e2668. Epub 2017 Mar 16.

Ilsong Institute of Life Science, Hallym University, Anyang, Republic of Korea.

The cellular prion protein (PrP) is a highly conserved glycosylphosphatidylinositol (GPI)-anchored membrane protein that is involved in the signal transduction during the initial phase of neurite outgrowth. The Ras homolog gene family member A (RhoA) is a small GTPase that is known to have an essential role in regulating the development, differentiation, survival, and death of neurons in the central nervous system. Although recent studies have shown the dysregulation of RhoA in a variety of neurodegenerative diseases, the role of RhoA in prion pathogenesis remains unclear. Read More

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http://dx.doi.org/10.1038/cddis.2017.37DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5386549PMC
March 2017
13 Reads

Prion Function and Pathophysiology in Non-Mammalian Models.

Curr Mol Med 2017 ;17(1):13-23

Institute of Biomedical Sciences (Sector A, Second Floor), Universidad de Chile, Independencia 1027, Santiago, P.O. Box 70031. Chile.

More than thirty years have passed since the discovery of the prion protein (PrP) and its causative role in transmissible spongiform encephalopathy. Since a combination of both gain- and loss-of-function mechanisms may underlay prion pathogenesis, understanding the physiological role of PrP may give important clues about disease mechanisms. Historically, the primary strategy for prion research has involved the use of human tissue, cell cultures and mammalian animal models. Read More

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http://dx.doi.org/10.2174/1566524017666170220100715DOI Listing
May 2018
3 Reads

TIA-1 Is a Functional Prion-Like Protein.

Cold Spring Harb Perspect Biol 2017 May 1;9(5). Epub 2017 May 1.

Department of Neuroscience, College of Physicians and Surgeons of Columbia University, New York, New York 10032.

Prions are self-propagating protein conformations that are traditionally regarded as agents of neurodegenerative disease in animals. However, it has become evident that prion-like aggregation of endogenous proteins can also occur under normal physiological conditions (e.g. Read More

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http://dx.doi.org/10.1101/cshperspect.a030718DOI Listing
May 2017
6 Reads

Differentially expressed genes in iron-induced prion protein conversion.

Biochem Biophys Res Commun 2016 11 29;480(4):734-740. Epub 2016 Oct 29.

Laboratory of Immunology and Research Institute for Veterinary Science, College of Veterinary Medicine, Seoul National University, Seoul 08826, Republic of Korea. Electronic address:

The conversion of the cellular prion protein (PrP) to the protease-resistant isoform is the key event in chronic neurodegenerative diseases, including transmissible spongiform encephalopathies (TSEs). Increased iron in prion-related disease has been observed due to the prion protein-ferritin complex. Additionally, the accumulation and conversion of recombinant PrP (rPrP) is specifically derived from Fe(III) but not Fe(II). Read More

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http://dx.doi.org/10.1016/j.bbrc.2016.10.117DOI Listing
November 2016
3 Reads

Insights from Therapeutic Studies for PrP Prion Disease.

Cold Spring Harb Perspect Med 2017 Mar 1;7(3). Epub 2017 Mar 1.

Department of Neurochemistry, Tohoku University Graduate School of Medicine, Seiryo-cho, Aoba-ku, Sendai 980-8575, Japan.

Although an effective therapy for prion disease has not yet been established, many advances have been made toward understanding its pathogenesis, which has facilitated research into therapeutics for the disease. Several compounds, including flupirtine, quinacrine, pentosan polysulfate, and doxycycline, have recently been used on a trial basis for patients with prion disease. Concomitantly, several lead antiprion compounds, including compound B (compB), IND series, and anle138b, have been discovered. Read More

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http://dx.doi.org/10.1101/cshperspect.a024430DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5334251PMC
March 2017
12 Reads

Almost a century of prion protein(s): From pathology to physiology, and back to pathology.

Biochem Biophys Res Commun 2017 02 28;483(4):1148-1155. Epub 2016 Aug 28.

Department of Biomedical Sciences, University of Padova, Via Bassi 58/B, 35131 Padova, Italy; C.N.R. Institute of Neuroscience, University of Padova, Via Bassi 58/B, 35131 Padova, Italy. Electronic address:

Prions are one of the few pathogens whose name is renowned at all population levels, after the dramatic years pervaded by the fear of eating prion-infected food. If now this, somehow irrational, scare of bovine meat inexorably transmitting devastating brain disorders is largely subdued, several prion-related issues are still unsolved, precluding the design of therapeutic approaches that could slow, if not halt, prion diseases. One unsolved issue is, for example, the role of the prion protein (PrP), whole conformational misfolding originates the prion but whose physiologic reason d'etre in neurons, and in cells at large, remains enigmatic. Read More

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http://dx.doi.org/10.1016/j.bbrc.2016.07.118DOI Listing
February 2017
9 Reads

Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND) Variation in Domestic Cattle.

PLoS One 2016 25;11(5):e0155924. Epub 2016 May 25.

Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, College Station, Texas 77843-4467, United States of America.

Previous investigations aimed at determining whether the mammalian prion protein actually facilitates tangible molecular aspects of either a discrete or pleiotropic functional niche have been debated, especially given the apparent absence of overt behavioral or physiological phenotypes associated with several mammalian prion gene (PRNP) knockout experiments. Moreover, a previous evaluation of PRNP knockout cattle concluded that they were normal, suggesting that the bovine prion protein is physiologically dispensable. Herein, we examined the frequency and distribution of nucleotide sequence variation within the coding regions of bovine PRNP and the adjacent Doppel (PRND) gene, a proximal paralogue to PRNP on BTA13. Read More

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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0155924PLOS
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4880211PMC
July 2017
3 Reads

Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data.

Data Brief 2016 Jun 4;7:1643-51. Epub 2016 May 4.

Biomaterials and Advanced Drug Delivery Laboratory, School of Medicine, Stanford University, Palo Alto, CA 94304, USA; Cardiovascular Pharmacology Division, Cardiovascular Institute, School of Medicine, Stanford University, Stanford, CA 94305, USA.

Protein misfolding and aggregation are responsible for a large number of diseases called protein conformational diseases or disorders that include Alzheimer׳s disease, Huntington׳s diseases, Prion related encephalopathies and type-II diabetes (http://dx.doi.org/10. Read More

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http://dx.doi.org/10.1016/j.dib.2016.04.070DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4872718PMC
June 2016
3 Reads

Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies.

Ultramicroscopy 2016 06 30;165:26-33. Epub 2016 Mar 30.

Department of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198, United States. Electronic address:

Aggregation of prion proteins is the cause of various prion related diseases. The infectious form of prions, amyloid aggregates, exist as multiple strains. The strains are thought to represent structurally different prion protein molecules packed into amyloid aggregates, but the knowledge on the structure of different types of aggregates is limited. Read More

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http://dx.doi.org/10.1016/j.ultramic.2016.03.011DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4879610PMC
June 2016
6 Reads

Metallothioneins in Prion- and Amyloid-Related Diseases.

J Alzheimers Dis 2016 ;51(3):637-56

Department of Chemistry and Biochemistry, Mendel University in Brno, Zemedelska 1, Brno, Czech Republic.

Prion and other amyloid-forming diseases represent a group of neurodegenerative disorders that affect both animals and humans. The role of metal ions, especially copper and zinc is studied intensively in connection with these diseases. Their involvement in protein misfolding and aggregation and their role in creation of reactive oxygen species have been shown. Read More

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http://dx.doi.org/10.3233/JAD-150984DOI Listing
December 2016
19 Reads

ERp57 as a novel cellular factor controlling prion protein biosynthesis: Therapeutic potential of protein disulfide isomerases.

Prion 2016 ;10(1):50-6

a Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile , Santiago , Chile.

Disturbance of endoplasmic reticulum (ER) proteostasis is observed in Prion-related disorders (PrDs). The protein disulfide isomerase ERp57 is a stress-responsive ER chaperone up-regulated in the brain of Creutzfeldt-Jakob disease patients. However, the actual role of ERp57 in prion protein (PrP) biogenesis and the ER stress response remained poorly defined. Read More

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http://dx.doi.org/10.1080/19336896.2015.1129485DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4981197PMC
January 2017
10 Reads

Prion Diseases.

Continuum (Minneap Minn) 2015 Dec;21(6 Neuroinfectious Disease):1612-38

Purpose Of Review: This article presents an update on the clinical aspects of human prion disease, including the wide spectrum of their presentations.

Recent Findings: Prion diseases, a group of disorders caused by abnormally shaped proteins called prions, occur in sporadic (Jakob-Creutzfeldt disease), genetic (genetic Jakob-Creutzfeldt disease, Gerstmann-Sträussler-Scheinker syndrome, and fatal familial insomnia), and acquired (kuru, variant Jakob-Creutzfeldt disease, and iatrogenic Jakob-Creutzfeldt disease) forms. This article presents updated information on the clinical features and diagnostic methods for human prion diseases. Read More

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https://insights.ovid.com/crossref?an=00132979-201512000-000
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http://dx.doi.org/10.1212/CON.0000000000000251DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4879966PMC
December 2015
6 Reads

Effects of lysine residues on structural characteristics and stability of tau proteins.

Biochem Biophys Res Commun 2015 Oct 14;466(3):486-92. Epub 2015 Sep 14.

Department of Mechanical Engineering Korea University, Seoul 136-701, Republic of Korea. Electronic address:

Pathological amyloid proteins have been implicated in neuro-degenerative diseases, specifically Alzheimer's, Parkinson's, Lewy-body diseases and prion related diseases. In prion related diseases, functional tau proteins can be transformed into pathological agents by environmental factors, including oxidative stress, inflammation, Aβ-mediated toxicity and covalent modification. These pathological agents are stable under physiological conditions and are not easily degraded. Read More

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http://dx.doi.org/10.1016/j.bbrc.2015.09.056DOI Listing
October 2015
4 Reads

Neuroprotective effect of cellular prion protein (PrPC) is related with activation of alpha7 nicotinic acetylcholine receptor (α7nAchR)-mediated autophagy flux.

Oncotarget 2015 Sep;6(28):24660-74

Biosafety Research Institute, College of Veterinary Medicine, Chonbuk National University, Jeonju, Korea.

Activation of the alpha7 nicotinic acetylcholine receptor (α7nAchR) is regulated by prion protein (PrPC) expression and has a neuroprotective effect by modulating autophagic flux. In this study, we hypothesized that PrPC may regulate α7nAchR activation and that may prevent prion-related neurodegenerative diseases by regulating autophagic flux. PrP(106-126) treatment decreased α7nAchR expression and activation of autophagic flux. Read More

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http://dx.doi.org/10.18632/oncotarget.4953DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4694786PMC
September 2015
4 Reads

Antioxidant peroxiredoxin 6 protein rescues toxicity due to oxidative stress and cellular hypoxia in vitro, and attenuates prion-related pathology in vivo.

Neurochem Int 2015 Nov 8;90:152-65. Epub 2015 Aug 8.

Department of Neurology, New York University School of Medicine, New York, NY 10016, USA; Department of Psychiatry, New York University School of Medicine, New York, NY 10016, USA; Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016, USA. Electronic address:

Protein misfolding, mitochondrial dysfunction and oxidative stress are common pathomechanisms that underlie neurodegenerative diseases. In prion disease, central to these processes is the post-translational transformation of cellular prion protein (PrP(c)) to the aberrant conformationally altered isoform; PrP(Sc). This can trigger oxidative reactions and impair mitochondrial function by increasing levels of peroxynitrite, causing damage through formation of hydroxyl radicals or via nitration of tyrosine residues on proteins. Read More

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http://dx.doi.org/10.1016/j.neuint.2015.08.006DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4641785PMC
November 2015
5 Reads

The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein.

J Biol Chem 2015 Sep 13;290(39):23631-45. Epub 2015 Jul 13.

From the Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago 8380453, Chile, the Program of Cellular and Molecular Biology, Institute of Biomedical Sciences, Center for Molecular Studies of the Cell, University of Chile, Santiago 8380453, Chile, the Harvard School of Public Health, Boston, Massachusetts 02115

Although the accumulation of a misfolded and protease-resistant form of the prion protein (PrP) is a key event in prion pathogenesis, the cellular factors involved in its folding and quality control are poorly understood. PrP is a glycosylated and disulfide-bonded protein synthesized at the endoplasmic reticulum (ER). The ER foldase ERp57 (also known as Grp58) is highly expressed in the brain of sporadic and infectious forms of prion-related disorders. Read More

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http://www.jbc.org/content/290/39/23631.full.pdf
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http://www.jbc.org/lookup/doi/10.1074/jbc.M114.635565
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http://dx.doi.org/10.1074/jbc.M114.635565DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4583042PMC
September 2015
25 Reads

Modulation of endoplasmic reticulum stress: an opportunity to prevent neurodegeneration?

CNS Neurol Disord Drug Targets 2015 ;14(4):518-33

Institute of Physiology - Faculty of Medicine, University of Coimbra & CNC - Center for Neuroscience and Cell Biology, University of Coimbra, 3004-504 Coimbra, Portugal.

Neurodegenerative diseases (e.g. Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis and prion-related diseases) have in common the presence of protein aggregates in specific brain areas where significant neuronal loss is detected. Read More

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February 2016
11 Reads
8 Citations
2.630 Impact Factor

Death Receptor 6 and Caspase-6 Regulate Prion Peptide-Induced Axonal Degeneration in Rat Spinal Neurons.

J Mol Neurosci 2015 Aug 22;56(4):966-976. Epub 2015 Apr 22.

State Key Laboratories for Agrobiotechnology, Key Lab of Animal Epidemiology and Zoonosis, Ministry of Agriculture, National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China Agricultural University, Beijing, 100193, China.

Axonal degeneration is a hallmark of many neurodegenerative disorders including transmissible spongiform encephalopathies (TSE). However, the full complement of axonal degeneration triggers is not fully understood. In an in vitro prion model, we observed that treatment of rat spinal neurons with the prion peptide, PrP106-126, activated death receptor 6 (DR6, also known as TNFRSF21), caspase-6, caspase-3, and induced axonal degeneration. Read More

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http://link.springer.com/content/pdf/10.1007/s12031-015-0562
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http://link.springer.com/10.1007/s12031-015-0562-1
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http://dx.doi.org/10.1007/s12031-015-0562-1DOI Listing
August 2015
2 Reads
2 Citations
2.343 Impact Factor

Polo-like kinase 3 (PLK3) mediates the clearance of the accumulated PrP mutants transiently expressed in cultured cells and pathogenic PrP(Sc) in prion infected cell line via protein interaction.

Int J Biochem Cell Biol 2015 May 25;62:24-35. Epub 2015 Feb 25.

State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Chang-Bai Rd 155, Beijing 102206, China; Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Zhejiang University, Hangzhou 310003, China; Chinese Academy of Sciences Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China. Electronic address:

Polo-like kinases (PLKs) family has long been known to be critical for cell cycle and recent studies have pointed to new dimensions of PLKs function in the nervous system. Our previous study has verified that the levels of PLK3 in the brain are severely downregulated in prion-related diseases. However, the associations of PLKs with prion protein remain unclear. Read More

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http://dx.doi.org/10.1016/j.biocel.2015.02.011DOI Listing
May 2015
16 Reads

Role of mitochondrial raft-like microdomains in the regulation of cell apoptosis.

Apoptosis 2015 May;20(5):621-34

Department of Experimental Medicine, Sapienza University of Rome, Viale Regina Elena 324, 00161, Rome, Italy.

Lipid rafts are envisaged as lateral assemblies of specific lipids and proteins that dissociate and associate rapidly and form functional clusters in cell membranes. These structural platforms are not confined to the plasma membrane; indeed lipid microdomains are similarly formed at subcellular organelles, which include endoplasmic reticulum, Golgi and mitochondria, named raft-like microdomains. In addition, some components of raft-like microdomains are present within ER-mitochondria associated membranes. Read More

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http://link.springer.com/10.1007/s10495-015-1100-x
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http://dx.doi.org/10.1007/s10495-015-1100-xDOI Listing
May 2015
28 Reads

ER stress signaling and neurodegeneration: At the intersection between Alzheimer's disease and Prion-related disorders.

Virus Res 2015 Sep 31;207:69-75. Epub 2014 Dec 31.

Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; Center for Molecular Studies of the Cell, Institute of Biomedical Sciences, University of Chile, Santiago, Chile; Neurounion Biomedical Foundation, Santiago, Chile; Harvard School of Public Health, Boston, USA. Electronic address:

Alzheimer's and Prion diseases are two neurodegenerative conditions sharing different pathophysiological characteristics. Disease symptoms are associated with the abnormal accumulation of protein aggregates, which are generated by the misfolding and oligomerization of specific proteins. Recent functional studies uncovered a key role of endoplasmic reticulum (ER) stress and the unfolded protein response (UPR) in the occurrence of synaptic dysfunction and neurodegeneration in Prion-related disorders and Alzheimer's disease. Read More

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http://dx.doi.org/10.1016/j.virusres.2014.12.018DOI Listing
September 2015
33 Reads

Melatonin-mediated β-catenin activation protects neuron cells against prion protein-induced neurotoxicity.

J Pineal Res 2014 Nov 16;57(4):427-34. Epub 2014 Oct 16.

Bio-Safety Research Institute, College of Veterinary Medicine, Chonbuk National University, Jeonju, Jeonbuk, South Korea.

Activation of β-catenin in neurons regulates mitochondrial function and protects against protein misfolding disorders, including Alzheimer's disease and Huntington's disease. Melatonin, a natural secretory product of the pineal gland, exerts neuroprotective effects through the activation of β-catenin. In this study, melatonin increased β-catenin protein expression and activation in human neuroblastoma cell lines SH-SY5Y cells. Read More

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http://dx.doi.org/10.1111/jpi.12182DOI Listing
November 2014
24 Reads

Sensitive electrical detection of human prion proteins using field effect transistor biosensor with dual-ligand binding amplification.

Biosens Bioelectron 2015 May 20;67:256-62. Epub 2014 Aug 20.

Graduate School of Advanced Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan; Institute for Nanoscience & Nanotechnology, Waseda University, 513 Waseda-tsurumaki-cho, Shinjuku-ku, Tokyo 162-0041, Japan. Electronic address:

Simple and accurate detection of prion proteins in biological samples is of utmost importance in recent years. In this study, we developed a label-free electrical detection-based field effect transistor (FET) biosensor using thiamine as a probe molecule for a non-invasive and specific test of human prion protein detection. We found that thiamine-immobilized FETs can be used to observe the prion protein oligomer, and might be a significant test for the early diagnosis of prion-related diseases. Read More

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http://dx.doi.org/10.1016/j.bios.2014.08.028DOI Listing
May 2015
9 Reads

Initial diagnoses of patients ultimately diagnosed with prion disease.

J Alzheimers Dis 2014 ;42(3):833-9

Veterans Affairs Healthcare System, Department of Neurology, Washington, DC, USA Department of Neurology, Georgetown University Hospital, Washington, DC, USA.

Background: Prion diseases are rapidly progressive neurodegenerative diseases that frequently mimic other forms of dementia making them difficult to diagnose.

Objective: To explore factors associated with the initial diagnoses of cases later determined to be caused by prion disease in an attempt to recognize key clinical variables that impact the timely diagnosis of prion disease.

Methods: A retrospective chart review performed at Johns Hopkins Medicine and the Department of Veterans Affairs Health Care System (1995-2008) was conducted. Read More

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http://dx.doi.org/10.3233/JAD-132465DOI Listing
August 2015
6 Reads

Cellular prion protein is present in dopaminergic neurons and modulates the dopaminergic system.

Eur J Neurosci 2014 Aug 26;40(3):2479-86. Epub 2014 Apr 26.

Departamento de Farmacologia, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, UFSC, Florianópolis, Brazil; Center for Neuroscience and Cell Biology, Faculty of Medicine, Rua Larga University of Coimbra, 3004-504 Coimbra, Portugal.

Cellular prion protein (PrP(C) ) is widely expressed in the brain. Although the precise role of PrP(C) remains uncertain, it has been proposed to be a pivotal modulator of neuroplasticity events by regulating the glutamatergic and serotonergic systems. Here we report the existence of neurochemical and functional interactions between PrP(C) and the dopaminergic system. Read More

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http://dx.doi.org/10.1111/ejn.12600DOI Listing
August 2014
10 Reads

Role of proteolytic activation of protein kinase Cδ in the pathogenesis of prion disease.

Prion 2014 Jan-Feb;8(1):143-53

Prion diseases are infectious and inevitably fatal neurodegenerative diseases characterized by prion replication, widespread protein aggregation and spongiform degeneration of major brain regions controlling motor function. Oxidative stress has been implicated in prion-related neuronal degeneration, but the molecular mechanisms underlying prion-induced oxidative damage are not well understood. In this study, we evaluated the role of oxidative stress-sensitive, pro-apoptotic protein kinase Cδ (PKCδ) in prion-induced neuronal cell death using cerebellar organotypic slice cultures (COSC) and mouse models of prion diseases. Read More

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4988799PMC
February 2015
7 Reads

In vivo and in vitro analyses of amygdalar function reveal a role for copper.

J Neurophysiol 2014 May 19;111(10):1927-39. Epub 2014 Feb 19.

Neuroscience Department, University of Connecticut Health Center, Farmington, Connecticut;

Mice with a single copy of the peptide amidating monooxygenase (Pam) gene (PAM(+/-)) are impaired in contextual and cued fear conditioning. These abnormalities coincide with deficient long-term potentiation (LTP) at excitatory thalamic afferent synapses onto pyramidal neurons in the lateral amygdala. Slice recordings from PAM(+/-) mice identified an increase in GABAergic tone (Gaier ED, Rodriguiz RM, Ma XM, Sivaramakrishnan S, Bousquet-Moore D, Wetsel WC, Eipper BA, Mains RE. Read More

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http://dx.doi.org/10.1152/jn.00631.2013DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4044343PMC
May 2014
9 Reads

Prion diseases.

Semin Neurol 2013 Sep 14;33(4):348-56. Epub 2013 Nov 14.

Cognitive and Behavioral Neurology Unit, Department of Neurology, University of Sao Paulo Medical School, Sao Paulo, Brazil.

Prion diseases are a group of diseases caused by abnormally conformed infectious proteins, called prions. They can be sporadic (Jakob-Creutzfeldt disease [JCD]), genetic (genetic JCD, Gerstmann-Sträussler-Scheinker, and familial fatal insomnia), or acquired (kuru, variant JCD, and iatrogenic JCD). The clinical features associated with each form of prion disease, the neuroimaging findings, cerebrospinal fluid markers, and neuropathological findings are reviewed. Read More

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http://www.thieme-connect.de/DOI/DOI?10.1055/s-0033-1359314
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http://dx.doi.org/10.1055/s-0033-1359314DOI Listing
September 2013
6 Reads

Pan-amyloid oligomer specific scFv antibody attenuates memory deficits and brain amyloid burden in mice with Alzheimer's disease.

Curr Alzheimer Res 2014 Jan;11(1):69-78

National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China.

Amyloid oligomers have a critical function in the pathologic processes of various amyloidoses, such as Alzheimer's disease (AD), Parkinson disease (PD), Huntington's disease, prion-related diseases, type 2 diabetes, and hereditary renal amyloidosis. Our previous reports demonstrated that a conformation-dependent oligomer-specific single-chain variable fragment (scFv) antibody, W20, isolated from a naïve human scFv library, can recognize oligomers assembled from α-synuclein, amylin, insulin, Aβ40/42, prion peptide 106-126, and lysozyme, inhibit the aggregation of various amyloid, and attenuate amyloid oligomer-induced cytotoxicity In vitro. Furthermore, W20 recognized the amyloid oligomers in all types of plaques, Lewy bodies, and amylin deposits in the brain tissues of AD and PD patients and in the pancreas of type 2 diabetes patients. Read More

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January 2014
9 Reads

Creutzfeldt-Jakob Disease in the hospital setting: a case report and review.

Minn Med 2013 May;96(5):46-9

University of Minnesota, USA.

Rapidly progressive dementia is a neurological condition that results in subacute deterioration in cognitive, behavioral and motor function. The most serious diagnosis for a patient with rapidly progressive dementia is Creutzfeldt-Jakob Disease (CJD), a prion-related illness that typically results in death within one year. However, there are numerous autoimmune, infectious and toxic-metabolic causes of rapidly progressive dementia that are potentially reversible with treatment. Read More

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May 2013
2 Reads

[Wilson disease - factors affecting clinical presentation].

Neurol Neurochir Pol 2013 Mar-Apr;47(2):161-9

Instytut Psychiatrii i Neurologii, II Klinika Neurologii, ul. Sobieskiego 9, 02-957 Warszawa.

Wilson disease (WD) is a genetic disorder with copper metabolism disturbances leading to copper accumulation in many organs with their secondary damage. It is caused by mutation in the ATP7B gene on chromosome 13, which encodes ATP-ase 7B involved in copper transport. The age of neurologic symptom onset in WD is 20-30 years, but there is a wide spectrum of disease including: age at onset, clinical signs and treatment efficacy. Read More

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August 2013
4 Reads

Protein aggregates and regional disease spread in ALS is reminiscent of prion-like pathogenesis.

Authors:
Ashok Verma

Neurol India 2013 Mar-Apr;61(2):107-10

Department of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA.

Amyotrophic lateral sclerosis (ALS) typically commences in a discrete location in a limb or bulbar territory muscles and then spreads to the adjacent anatomical regions. This pattern is consistent with a contiguous spread of the disease process in motor neuron network resulting in progressive motor weakness. The etiology of ALS onset and the mechanism of the regional ALS spread remain elusive. Read More

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http://dx.doi.org/10.4103/0028-3886.111109DOI Listing
June 2013
2 Reads

Molecular dynamics simulations of amyloid fibrils: an in silico approach.

Acta Biochim Biophys Sin (Shanghai) 2013 Jun 26;45(6):503-8. Epub 2013 Mar 26.

State Key Laboratory of Microbial Metabolism, Department of Bioinformatics and Biostatistics, College of Life Sciences and Biotechnology, Shanghai Jiaotong University, Shanghai 200240, China.

Amyloid fibrils play causal roles in the pathogenesis of amyloid-related degenerative diseases such as Alzheimer's disease, type II diabetes mellitus, and the prion-related transmissible spongiform encephalopathies. The mechanism of fibril formation and protein aggregation is still hotly debated and remains an important open question in order to develop therapeutic method of these diseases. However, traditional molecular biological and crystallographic experiments could hardly observe atomic details and aggregation process. Read More

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http://dx.doi.org/10.1093/abbs/gmt026DOI Listing
June 2013
3 Reads

Gene and protein patterns of potential prion-related markers in the central nervous system of clinical and preclinical infected sheep.

Vet Res 2013 Mar 11;44:14. Epub 2013 Mar 11.

Centro de Investigación en Encefalopatías y Enfermedades Transmisibles Emergentes, Facultad de Veterinaria, Universidad de Zaragoza, Zaragoza, Spain.

The molecular pathogenic mechanisms of prion diseases are far from clear. Genomic analyses have revealed genetic biomarkers potentially involved in prion neuropathology in naturally scrapie-infected sheep, a good animal model of infectious prionopathies. However, these biomarkers must be validated in independent studies at different stages of the disease. Read More

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http://dx.doi.org/10.1186/1297-9716-44-14DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3608070PMC
March 2013
7 Reads

Neuroimaging of rapidly progressive dementias, part 1: neurodegenerative etiologies.

Authors:
A J Degnan L M Levy

AJNR Am J Neuroradiol 2014 Mar 22;35(3):418-23. Epub 2013 Feb 22.

From the University of Pittsburgh Medical Center (A.J.D.), Pittsburgh, Pennsylvania.

Most dementias begin insidiously, developing slowly and generally occurring in the elderly age group. The so-called rapidly progressive dementias constitute a different, diverse collection of conditions, many of which are reversible or treatable. For this reason, prompt identification and assessment of acute and subacute forms of dementia are critical to effective treatment. Read More

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http://www.ajnr.org/content/early/2013/03/21/ajnr.A3454.full
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http://www.ajnr.org/content/early/2013/02/14/ajnr.A3455.full
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http://www.ajnr.org/cgi/doi/10.3174/ajnr.A3454
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http://dx.doi.org/10.3174/ajnr.A3454DOI Listing
March 2014
4 Reads

Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis.

Proc Natl Acad Sci U S A 2013 Jan 24;110(2):519-24. Epub 2012 Dec 24.

Institute of Bioengineering and Nanotechnology, Singapore 138669.

The self-assembly of abnormally folded proteins into amyloid fibrils is a hallmark of many debilitating diseases, from Alzheimer's and Parkinson diseases to prion-related disorders and diabetes type II. However, the fundamental mechanism of amyloid aggregation remains poorly understood. Core sequences of four to seven amino acids within natural amyloid proteins that form toxic fibrils have been used to study amyloidogenesis. Read More

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http://dx.doi.org/10.1073/pnas.1217742110DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3545743PMC
January 2013
19 Reads
18 Citations
9.810 Impact Factor

Medulla oblongata transcriptome changes during presymptomatic natural scrapie and their association with prion-related lesions.

BMC Genomics 2012 Aug 16;13:399. Epub 2012 Aug 16.

Centro de Investigación en Encefalopatías y Enfermedades Transmisibles Emergentes, Facultad de Veterinaria, Universidad de Zaragoza, Zaragoza, Spain.

Background: The pathogenesis of natural scrapie and other prion diseases is still poorly understood. Determining the variations in the transcriptome in the early phases of the disease might clarify some of the molecular mechanisms of the prion-induced pathology and allow for the development of new biomarkers for diagnosis and therapy. This study is the first to focus on the identification of genes regulated during the preclinical phases of natural scrapie in the ovine medulla oblongata (MO) and the association of these genes with prion deposition, astrocytosis and spongiosis. Read More

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http://dx.doi.org/10.1186/1471-2164-13-399DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3495657PMC
August 2012
6 Reads

Alzheimer Aβ peptide interactions with lipid membranes: fibrils, oligomers and polymorphic amyloid channels.

Prion 2012 Sep-Oct;6(4):339-45. Epub 2012 Aug 9.

School of Physics, University College Dublin, Dublin, Ireland.

Fibrillar aggregates of misfolded amyloid proteins are involved in a variety of diseases such as Alzheimer disease (AD), type 2 diabetes, Parkinson, Huntington and prion-related diseases. In the case of AD amyloid β (Aβ) peptides, the toxicity of amyloid oligomers and larger fibrillar aggregates is related to perturbing the biological function of the adjacent cellular membrane. We used atomistic molecular dynamics (MD) simulations of Aβ 9-40 fibrillar oligomers modeled as protofilament segments, including lipid bilayers and explicit water molecules, to probe the first steps in the mechanism of Aβ-membrane interactions. Read More

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http://dx.doi.org/10.4161/pri.21022DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3609060PMC
February 2013
2 Reads

Protein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applications.

FEBS Lett 2012 Aug 22;586(18):2826-34. Epub 2012 Jul 22.

Institute of Biomedical Sciences, Program of Cellular and Molecular Biology, University of Chile, Santiago, Chile.

Protein disulfide isomerases (PDIs) are a family of foldases and chaperones primarily located at the endoplasmic reticulum that catalyze the formation and isomerization of disulfide bonds thereby facilitating protein folding. PDIs also perform important physiological functions in protein quality control, cell death, and cell signaling. Protein misfolding is involved in the etiology of the most common neurodegenerative diseases, including Alzheimer, Parkinson, amyotrophic lateral sclerosis, Prion-related disorders, among others. Read More

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http://dx.doi.org/10.1016/j.febslet.2012.07.023DOI Listing
August 2012
7 Reads

Altered Prion protein expression pattern in CSF as a biomarker for Creutzfeldt-Jakob disease.

PLoS One 2012 27;7(4):e36159. Epub 2012 Apr 27.

Neuroscience Biomedical Institute, Faculty of Medicine, University of Chile, Santiago, Chile.

Creutzfeldt-Jakob disease (CJD) is the most frequent human Prion-related disorder (PrD). The detection of 14-3-3 protein in the cerebrospinal fluid (CSF) is used as a molecular diagnostic criterion for patients clinically compatible with CJD. However, there is a pressing need for the identification of new reliable disease biomarkers. Read More

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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0036159PLOS
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3338608PMC
September 2012
29 Reads