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1. Full Text Protein aggregation diseases: pathogenicity and therapeutic perspectives
by Aguzzi, Adriano and O'Connor, Tracy
Nature Reviews Drug Discovery, ISSN 1474-1776, 03/2010, Volume 9, Issue 3, pp. 237 - 248
A growing number of diseases seem to be associated with inappropriate deposition of protein aggregates. Some of these diseases - such as Alzheimer's disease... 
GAMMA-SECRETASE INHIBITOR | BETA PEPTIDE GENERATION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | GATED SODIUM-CHANNELS | FOLLICULAR DENDRITIC CELLS | FAMILIAL ALZHEIMERS-DISEASE | PHARMACOLOGY & PHARMACY | AMYLOID PRECURSOR PROTEIN | INTRANEURONAL A-BETA-42 ACCUMULATION | TRANSGENIC MOUSE MODEL | SHEET BREAKER PEPTIDES | OLIGOMERIC A-BETA | Immunotherapy - methods | Humans | Alzheimer Disease - pathology | Anti-Inflammatory Agents, Non-Steroidal - pharmacology | Brain - metabolism | Amyloid - metabolism | Amyloidosis - immunology | Amyloid - biosynthesis | Amyloidosis - etiology | Alzheimer Disease - immunology | Drug Evaluation, Preclinical - methods | Prion Diseases - drug therapy | Prion Diseases - immunology | Alzheimer Disease - drug therapy | Central Nervous System Diseases - immunology | Amyloidosis - drug therapy | Prion Diseases - pathology | Peptides - pharmacology | Brain - drug effects | Central Nervous System Diseases - etiology | Animals | Anti-Inflammatory Agents, Non-Steroidal - therapeutic use | Central Nervous System Diseases - drug therapy | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Peptides - therapeutic use | Amyloidosis | Research | Drug therapy | Alzheimer's disease | Health aspects | Risk factors | Index Medicus
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2. Full Text A General Model of Prion Strains and Their Pathogenicity
by John Collinge and Anthony R. Clarke
Science, ISSN 0036-8075, 11/2007, Volume 318, Issue 5852, pp. 930 - 936
Prions are lethal mammalian pathogens composed of aggregated conformational isomers of a host-encoded glycoprotein and which appear to lack nucleic acids.... 
Nervous system diseases | Disease transmission | Inbred strains | Neurodegenerative diseases | Prions | Humans | Prion diseases | Mice | Infections | Review | Genetic mutation | FATAL FAMILIAL INSOMNIA | TRANSMISSIBLE MINK ENCEPHALOPATHY | BOVINE SPONGIFORM ENCEPHALOPATHY | MULTIDISCIPLINARY SCIENCES | CREUTZFELDT-JAKOB-DISEASE | VARIANT CJD | PROTEIN GENE | MOLECULAR-BASIS | BSE AGENT | TRANSGENIC MICE | SPECIES-BARRIER | Prions - pathogenicity | Species Specificity | Recombinant Proteins - chemistry | Prions - chemistry | PrPSc Proteins - isolation & purification | PrPC Proteins - chemistry | PrPSc Proteins - chemistry | Protein Folding | PrPC Proteins - isolation & purification | PrPSc Proteins - metabolism | Animals | Prion Diseases - transmission | Models, Biological | Prions - isolation & purification | Protein Conformation | Brain Chemistry | PrPC Proteins - metabolism | PrPSc Proteins - pathogenicity | Prion Diseases - metabolism | Neurosciences | Models | Biochemistry | Molecular biology | Public health | Risk factors
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3. Full Text Mechanism of Amyloid Plaque Formation Suggests an Intracellular Basis of Aβ Pathogenicity
by Ralf P. Friedrich and Katharina Tepper and Raik Rönicke and Malle Soom and Martin Westermann and Klaus Reymann and Christoph Kaether and Marcus Fändrich and David S. Eisenberg
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2010, Volume 107, Issue 5, pp. 1942 - 1947
The formation of extracellular amyloid plaques is a common pathobiochemical event underlying several debilitating human conditions, including Alzheimer's... 
Amyloid plaque | Aggregation | Cell culture techniques | Neurons | Cell lines | Fluorescence | Kidney cells | Amyloids | Solar fibrils | Alzheimers disease | Prion | Protein misfolding | Neurodegeneration | Alzheimer | A-BETA-42 | PROTEIN | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | neurodegeneration | aggregation | PEPTIDE | FIBRILS | MULTIVESICULAR BODIES | protein misfolding | prion | ACCUMULATION | TRANSGENIC MICE | Biological Sciences
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4. Full Text Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity
by Wang, Fei and Wang, Xinhe and Orrú, Christina D and Groveman, Bradley R and Surewicz, Krystyna and Abskharon, Romany and Imamura, Morikazu and Yokoyama, Takashi and Kim, Yong-Sun and Vander Stel, Kayla J and Sinniah, Kumar and Priola, Suzette A and Surewicz, Witold K and Caughey, Byron and Ma, Jiyan
PLoS Pathogens, ISSN 1553-7366, 07/2017, Volume 13, Issue 7, p. e1006491
Prions, characterized by self-propagating protease-resistant prion protein (PrP) conformations, are agents causing prion disease. Recent studies generated... 
MAMMALIAN PRIONS | CONVERSION | MICROBIOLOGY | CONFORMATION | MISFOLDING CYCLIC AMPLIFICATION | PRP | TRANSMISSION | AMYLOID FIBRILS | VIROLOGY | DISEASE | ABSENCE | GENERATION | PARASITOLOGY | Recombinant Proteins - metabolism | Endopeptidases - metabolism | Prion Diseases - genetics | Biocatalysis | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | RNA - chemistry | Prion Proteins - metabolism | RNA - genetics | Endopeptidases - chemistry | Animals | Protein Binding | Protein Conformation | Mice | Prion Proteins - chemistry | Prion Proteins - genetics | Dimerization | Phosphatidylglycerols - metabolism | Prion Diseases - metabolism | RNA - metabolism | Proteins | Prions | Disease susceptibility | Genetic aspects | Structure | Health aspects | Testing | Visualization | Funding | Guanidine | Proteinase | Antibodies | Science | Lipids | Biochemistry | Agglomeration | Seeding | Cofactors | Protease | Phosphatidylglycerol | Physiology | Prion protein | Research centers | Supervision | Recombinant | Pathogens | Phosphatidylethanolamine | Denaturation | Roles | Biophysics | Ribonucleic acid--RNA | Pathogenicity | Infectious diseases | Guanidine hydrochloride | In vivo methods and tests | Stochasticity | Methods | RNA | Ribonucleic acid
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5. Full Text Disease genetics: Prion variant pathogenicity through large-scale population sequencing
by Burgess, Darren J
Nature Reviews Genetics, ISSN 1471-0056, 03/2016, Volume 17, Issue 3, pp. 127 - 127
GENETICS & HEREDITY | Genetic Variation | Humans | Prions | Virulence
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6. Full Text Prion variant pathogenicity through large-scale population sequencing
by Burgess, Darren J
Nature Reviews Genetics, ISSN 1471-0056, 03/2016, Volume 17, Issue 3, pp. 127 - 127
Genetic variation | Prion diseases | Development and progression | Disease susceptibility | Genetic aspects | Nucleotide sequencing | Health aspects | Methods | DNA sequencing
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7. Full Text Generating a Prion with Bacterially Expressed Recombinant Prion Protein
by Fei Wang and Xinhe Wang and Chong-Gang Yuan and Jiyan Ma
Science, ISSN 0036-8075, 2/2010, Volume 327, Issue 5969, pp. 1132 - 1135
The prion hypothesis posits that a misfolded form of prion protein (PrP) is responsible for the infectivity of prion disease. Using recombinant murine PrP... 
Nervous system diseases | RNA | Neurons | Prions | Cell lines | Antibodies | Prion diseases | Lipids | Reports | Mice | Inoculum | STRAINS | SCRAPIE | RESISTANT | IN-VITRO | MULTIDISCIPLINARY SCIENCES | MICE | CONFORMATION | PROPAGATION | PRP | MOLECULES | Cell Line | Neurons - chemistry | Prions - pathogenicity | PrPSc Proteins - analysis | Recombinant Proteins - chemistry | Glycosylation | Prion Diseases - pathology | Prions - chemistry | RNA - chemistry | Liver - chemistry | PrPC Proteins - chemistry | PrPSc Proteins - chemistry | Protein Folding | Phosphatidylglycerols - chemistry | Animals | Escherichia coli - genetics | Endopeptidase K - metabolism | Prion Diseases - etiology | Brain - pathology | Female | Brain Chemistry | PrPSc Proteins - pathogenicity | PrPC Proteins - pathogenicity | Research | Properties | Protein folding | Bacterial proteins | Genetic recombination | Rodents | Neurological disorders
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8. Prions
: new research
by Doupher, Bridgette V
2006, ISBN 1600210198, xiii, 311
Prion diseases | Prions
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9. Fatal flaws
: how a misfolded protein baffled scientists and changed the way we look at the brain
by Ingram, Jay
2013, ISBN 9780300189896
"Discovered and identified as the cause of mad cow disease only three decades ago, the prion is a protein molecule that, when misshapen in the brain, becomes... 
pathogenicity | Prion Diseases | physiopathology | Prions | history
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10. Preventing prion pathogenicity by targeting the cellular prion protein
by Nicoll, Andrew J and Collinge, John
Infectious Disorders - Drug Targets, ISSN 1871-5265, 2009, Volume 9, Issue 1, pp. 48 - 57
High throughput screening | Ligand binding | Prion disease | Mass action | Prion protein | Therapeutics
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11. Full Text Olfactory transmission of neurotropic viruses
by Mori, Isamu and Nishiyama, Yukihiro and Yokochi, Takashi and Kimura, Yoshinobu
Journal of NeuroVirology, ISSN 1355-0284, 2005, Volume 11, Issue 2, pp. 129 - 137
Olfactory receptor neurons are unique in their anatomical structure and function. Each neuron is directly exposed to the external environment at the site of... 
dendrite | prion | nervous system | axon | virus | olfactory receptor neuron | Neurology | Neurosciences | Biomedicine | Immunology | Infectious Diseases | Virology | Virus | Axon | Nervous system | Prion | Olfactory receptor neuron | Dendrite | BRAIN-STEM ENCEPHALITIS | NEUROSCIENCES | VIROLOGY | INFLUENZA-A VIRUS | EQUINE HERPESVIRUS-9 | CENTRAL-NERVOUS-SYSTEM | CREUTZFELDT-JAKOB-DISEASE | RABIES VIRUS | BORNA-DISEASE | HERPES-SIMPLEX ENCEPHALITIS | INTRANASAL INOCULATION | EXPERIMENTAL-INFECTION | Influenza A virus - physiology | Borna disease virus - physiology | Simplexvirus - physiology | Prions - pathogenicity | Humans | Lyssavirus - pathogenicity | Simplexvirus - pathogenicity | Virus Diseases - virology | Olfactory Mucosa - virology | Borna disease virus - pathogenicity | Central Nervous System Viral Diseases - virology | Lyssavirus - physiology | Animals | Prions - physiology | Prion Diseases - etiology | Influenza A virus - pathogenicity | Olfactory Receptor Neurons - virology | Paramyxovirinae - pathogenicity | Nervous System - virology | Synapses - virology
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12. Properties and pathogenicity of prion-derived peptides
by Vassallo, Neville
Protein and Peptide Letters, ISSN 0929-8665, 03/2009, Volume 16, Issue 3, pp. 230 - 238
Prion diseases are neurodegenerative disorders characterized by a hallmark event involving the post-translational misfolding of the normal cellular prion... 
Oxidative stress | Neurotoxicity | Intracellular signaling | Ion channel-forming peptides | Synthetic peptide | Prion protein | Amyloidoses | Calcium homeostasis | Apoptosis | Membrane physiology | Y145STOP VARIANT | APOPTOTIC CELL-DEATH | BIOCHEMISTRY & MOLECULAR BIOLOGY | amyloidoses | apoptosis | calcium homeostasis | LIPID-MEMBRANES | NEURODEGENERATIVE DISEASES | ion channel-forming peptides | PROTEIN PRP FRAGMENT | IN-VITRO | neurotoxicity | intracellular signaling | ENDOPLASMIC-RETICULUM | membrane physiology | oxidative stress | synthetic peptide | SOLUBLE AMYLOID OLIGOMERS | TRANSGENIC MICE | Prion Diseases - physiopathology | Prions - metabolism | Peptide Fragments - chemistry | Peptide Fragments - metabolism | Animals | Prions - genetics | Humans | Prions - chemistry | Peptide Fragments - genetics
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13. Full Text The Heat-Induced Molecular Disaggregase Hsp104 of Candida albicans Plays a Role in Biofilm Formation and Pathogenicity in a Worm Infection Model
by Alessandro Fiori and Soňa Kucharíková and Gilmer Govaert and Bruno P. A. Cammue and Karin Thevissen and Patrick Van Dijck
Eukaryotic Cell, ISSN 1535-9778, 08/2012, Volume 11, Issue 8, pp. 1012 - 1020
Classifications Services EC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit... 
YEAST | FUNGAL PATHOGEN | PSI+ PRION | IN-VIVO | GENE-EXPRESSION | MYCOLOGY | THERMOTOLERANCE | STRESS | SACCHAROMYCES-CEREVISIAE | Candida albicans - pathogenicity | Caenorhabditis elegans - microbiology | Heat-Shock Proteins - metabolism | Biofilms - growth & development | Fungal Proteins - genetics | Candidiasis - microbiology | Candida albicans - genetics | Heat-Shock Proteins - genetics | Animals | Gene Deletion | Candida albicans - physiology | Disease Models, Animal | Fungal Proteins - metabolism | Adaptations | Pathogens | Virulence | polystyrene | Chaperones | Promoters | Stress | Environmental conditions | Infection | Pathogenicity | Biofilms | Molecular modelling | Temperature effects | Hyphae | Extracellular matrix | polyurethane | Heat shock
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14. Prion protein protocols
by Hill, A. F. (Andrew F.)
2008, Methods in molecular biology, ISBN 1588298973, Volume 459
pathogenicity | Prions | isolation & purification
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15. Full Text Darwinian Evolution of Prions in Cell Culture
by Jiali Li and Shawn Browning and Sukhvir P. Mahal and Anja M. Oelschlegel and Charles Weissmann
Science, ISSN 0036-8075, 2/2010, Volume 327, Issue 5967, pp. 869 - 872
Prions are infectious proteins consisting mainly of PrP Sc , a p sheet-rich conformer of the normal host protein PrP c , and occur in different strains. Strain... 
Cell culture techniques | Polysaccharides | Nervous system diseases | Prions | Cultured cells | Evolution | Reports | Infections | Darwinism | Genetic mutation | STRAINS | AGENT | PROTEIN | ASSAY | HAMSTERS | MULTIDISCIPLINARY SCIENCES | CREUTZFELDT-JAKOB-DISEASE | CONFORMATION | MOUSE SCRAPIE | Cell Line | Prions - pathogenicity | Mice, Inbred C57BL | Prions - classification | Prions - chemistry | PrPSc Proteins - chemistry | Culture Media, Conditioned | PrPSc Proteins - classification | Prion Diseases | Animals | Prions - physiology | Culture Media | Cell Line, Tumor | Protein Conformation | Brain Chemistry | Mice | Mutation | PrPSc Proteins - pathogenicity | Swainsonine - pharmacology | Evolution, Molecular | Molecular evolution | Cell culture | Usage | Research | Properties | Proteins | Evolutionary biology | Cellular biology
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