Search Results - "Moudjou, Mohammed"
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Preclinical detection of variant CJD and BSE prions in blood
Published in PLoS pathogens (01-06-2014)“…The emergence of variant Creutzfeldt Jakob Disease (vCJD) is considered a likely consequence of human dietary exposure to Bovine Spongiform Encephalopathy…”
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Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics
Published in PLoS pathogens (01-10-2013)“…Prions are proteinaceous infectious agents responsible for fatal neurodegenerative diseases in animals and humans. They are essentially composed of PrP(Sc), an…”
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3
Identification and characterization of the binding site of the respiratory syncytial virus phosphoprotein to RNA-free nucleoprotein
Published in Journal of virology (01-04-2015)“…The RNA genome of respiratory syncytial virus (RSV) is constitutively encapsidated by the viral nucleoprotein N, thus forming a helical nucleocapsid…”
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4
Pressure Reveals Unique Conformational Features in Prion Protein Fibril Diversity
Published in Scientific reports (26-02-2019)“…The prion protein (PrP) misfolds and assembles into a wide spectrum of self-propagating quaternary structures, designated PrP Sc . These various PrP…”
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5
Thermostability as a highly dependent prion strain feature
Published in Scientific reports (06-08-2019)“…Prion diseases are caused by the conversion of physiological PrP C into the pathogenic misfolded protein PrP Sc , conferring new properties to PrP Sc that vary…”
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Highly infectious prions generated by a single round of microplate-based protein misfolding cyclic amplification
Published in mBio (31-12-2013)“…Measurements of the presence of prions in biological tissues or fluids rely more and more on cell-free assays. Although protein misfolding cyclic amplification…”
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Crossing Species Barriers Relies on Structurally Distinct Prion Assemblies and Their Complementation
Published in Molecular neurobiology (01-06-2020)“…Prion replication results from the autocatalytic templated assisted conversion of the host-encoded prion protein PrP C into misfolded, polydisperse PrP Sc…”
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Heterogeneity and Architecture of Pathological Prion Protein Assemblies: Time to Revisit the Molecular Basis of the Prion Replication Process?
Published in Viruses (10-05-2019)“…Prions are proteinaceous infectious agents responsible for a range of neurodegenerative diseases in animals and humans. Prion particles are assemblies formed…”
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Endogenous Proteolytic Cleavage of Disease-associated Prion Protein to Produce C2 Fragments Is Strongly Cell- and Tissue-dependent
Published in The Journal of biological chemistry (02-04-2010)“…The abnormally folded form of the prion protein (PrPSc) accumulating in nervous and lymphoid tissues of prion-infected individuals can be naturally cleaved to…”
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10
Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification
Published in Scientific reports (07-07-2016)“…Prions are formed of misfolded assemblies (PrP Sc ) of the variably N-glycosylated cellular prion protein (PrP C ). In infected species, prions replicate by…”
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Reversible unfolding of infectious prion assemblies reveals the existence of an oligomeric elementary brick
Published in PLoS pathogens (07-09-2017)“…Mammalian prions, the pathogens that cause transmissible spongiform encephalopathies, propagate by self-perpetuating the structural information stored in the…”
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The Respiratory Syncytial Virus M2-1 Protein Forms Tetramers and Interacts with RNA and P in a Competitive Manner
Published in Journal of Virology (01-07-2009)“…Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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The Prion-like protein Shadoo is involved in mouse embryonic and mammary development and differentiation
Published in Scientific reports (21-04-2020)“…Shadoo belongs to the prion protein family, an evolutionary conserved and extensively studied family due to the implication of PrP in Transmissible Spongiform…”
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14
Glycoform-selective prion formation in sporadic and familial forms of prion disease
Published in PloS one (19-03-2013)“…The four glycoforms of the cellular prion protein (PrP(C)) variably glycosylated at the two N-linked glycosylation sites are converted into their pathological…”
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Plasminogen-based capture combined with amplification technology for the detection of PrP(TSE) in the pre-clinical phase of infection
Published in PloS one (2013)“…Variant Creutzfeldt-Jakob disease (vCJD) is a neurodegenerative infectious disorder, characterized by a prominent accumulation of pathological isoforms of the…”
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PB1-F2 Influenza A Virus Protein Adopts a β-Sheet Conformation and Forms Amyloid Fibers in Membrane Environments
Published in The Journal of biological chemistry (23-04-2010)“…The influenza A virus PB1-F2 protein, encoded by an alternative reading frame in the PB1 polymerase gene, displays a high sequence polymorphism and is reported…”
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Shadoo binds lipid membranes and undergoes aggregation and fibrillization
Published in Biochemical and biophysical research communications (30-08-2013)“…•Shadoo is monomeric disordered protein at acidic pH, but aggregates at pH⩾7.•Shadoo binds anionic lipid vesicles.•Shadoo destabilizes negatively charged…”
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18
Nucleoprotein nanostructures combined with adjuvants adapted to the neonatal immune context: a candidate mucosal RSV vaccine
Published in PloS one (24-05-2012)“…The human respiratory syncytial virus (hRSV) is the leading cause of severe bronchiolitis in infants worldwide. The most severe RSV diseases occur between 2…”
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Prion potentiation after life-long dormancy in mice devoid of PrP
Published in Brain communications (01-01-2021)“…Abstract Prions are neurotropic pathogens composed of misfolded assemblies of the host-encoded prion protein PrPC which replicate by recruitment and conversion…”
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Further Characterization of Glycoform-Selective Prions of Variably Protease-Sensitive Prionopathy
Published in Pathogens (Basel) (23-04-2021)“…Prion is an infectious protein (PrP ) that is derived from a cellular glycoprotein (PrP ) through a conformational transition and associated with a group of…”
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