Search Results - "Ma, Jiyan"
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The role of cofactors in prion propagation and infectivity
Published in PLoS pathogens (01-04-2012)“…The simultaneous propagation of protease-resistant PrPSc and prion infectivity in sPMCA provides strong evidence supporting the prion hypothesis [5]. Because…”
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Generating a Prion with Bacterially Expressed Recombinant Prion Protein
Published in Science (American Association for the Advancement of Science) (26-02-2010)“…The prion hypothesis posits that a misfolded form of prion protein (PrP) is responsible for the infectivity of prion disease. Using recombinant murine PrP…”
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Preparation,characterization and photocatalytic properties of BiOBr/ZnO composites
Published in Journal of energy chemistry (01-05-2017)“…BiOBr/ZnO composite photocatalysts were prepared by a simple hydrothermal method. The as-prepared samples were characterized by X-ray diffraction(XRD),…”
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Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids
Published in Proceedings of the National Academy of Sciences - PNAS (29-05-2012)“…Infectious prions containing the pathogenic conformer of the mammalian prion protein (PrPSc) can be produced de novo from a mixture of the normal conformer…”
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Pathogenic alpha-synuclein aggregates preferentially bind to mitochondria and affect cellular respiration
Published in Acta neuropathologica communications (14-03-2019)“…Misfolded alpha-synuclein (αSyn) is a major constituent of Lewy bodies and Lewy neurites, which are pathological hallmarks of Parkinson's disease (PD). The…”
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Prion protein lowering is a disease-modifying therapy across prion disease stages, strains and endpoints
Published in Nucleic acids research (04-11-2020)“…Abstract Lowering of prion protein (PrP) expression in the brain is a genetically validated therapeutic hypothesis in prion disease. We recently showed that…”
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Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers
Published in Viruses (31-08-2022)“…Generating a prion with exogenously produced recombinant prion protein is widely accepted as the ultimate proof of the prion hypothesis. Over the years, a…”
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Detecting Alpha Synuclein Seeding Activity in Formaldehyde-Fixed MSA Patient Tissue by PMCA
Published in Molecular neurobiology (01-11-2018)“…Alpha synuclein (α-syn) is central to the pathogenesis of a group of neurodegenerative disorders known as synucleinopathies, including Parkinson’s disease…”
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Immunotherapy against Prion Disease
Published in Pathogens (Basel) (14-03-2020)“…The term "prion disease" encompasses a group of neurodegenerative diseases affecting both humans and animals. Currently, there is no effective therapy and all…”
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Streamlined alpha-synuclein RT-QuIC assay for various biospecimens in Parkinson's disease and dementia with Lewy bodies
Published in Acta neuropathologica communications (07-04-2021)“…Definitive diagnosis of Parkinson's disease (PD) and dementia with Lewy bodies (DLB) relies on postmortem finding of disease-associated alpha-synuclein (αSyn )…”
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Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions
Published in Proceedings of the National Academy of Sciences - PNAS (10-07-2012)“…Prions containing misfolded prion protein (PrP Sᶜ) can be formed with cofactor molecules using the technique of serial protein misfolding cyclic amplification…”
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Barriers to and Facilitators of the Implementation of a Micronutrient Powder Program for Children: A Systematic Review Based on the Consolidated Framework for Implementation Research
Published in Nutrients (01-12-2023)“…As one of the most cost-effective investments for improving child nutrition, micronutrient powder (MNP) has been widely used in many countries to underpin the…”
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13
Prion disease and the 'protein-only hypothesis'
Published in Essays in biochemistry (01-01-2014)“…Prion disease is the only naturally occurring infectious protein misfolding disorder. The chemical nature of the infectious agent has been debated for more…”
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Biochemical Profiling of the Brain and Blood Metabolome in a Mouse Model of Prodromal Parkinson’s Disease Reveals Distinct Metabolic Profiles
Published in Journal of proteome research (06-07-2018)“…Parkinson’s disease is the second most common neurodegenerative disease. In the vast majority of cases the origin is not genetic and the cause is not well…”
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Prion protein amino acid sequence influences formation of authentic synthetic PrPSc
Published in Scientific reports (09-01-2023)“…Synthetic prions, generated de novo from minimal, non-infectious components, cause bona fide prion disease in animals. Transmission of synthetic prions to…”
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Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion
Published in PLoS pathogens (01-12-2019)“…Prion or PrPSc is the proteinaceous infectious agent causing prion diseases in various mammalian species. Despite decades of research, the structural basis for…”
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Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol
Published in Science (American Association for the Advancement of Science) (29-11-2002)“…A rare conformation of the prion protein, PrPSc, is found only in mammals with transmissible prion diseases and represents either the infectious agent itself…”
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Access to DTP-Based Combination Vaccines in Asia-Pacific Countries between 2019 and 2022
Published in Vaccines (Basel) (28-12-2023)“…The Asia-Pacific countries are highly diverse in health and economic conditions that may impact vaccine access and uptake. Our study aimed to characterize…”
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Neurotoxicity and Neurodegeneration When PrP Accumulates in the Cytosol
Published in Science (American Association for the Advancement of Science) (29-11-2002)“…Changes in prion protein (PrP) folding are associated with fatal neurodegenerative disorders, but the neurotoxic species is unknown. Like other proteins that…”
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Wild-Type PrP and a Mutant Associated with Prion Disease are Subject to Retrograde Transport and Proteasome Degradation
Published in Proceedings of the National Academy of Sciences - PNAS (18-12-2001)“…The cytoplasm seems to provide an environment that favors conversion of the prion protein (PrP) to a form with the physical characteristics of the…”
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