Search Results - "Moudjou, Mohammed"

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    Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics by Laferrière, Florent, Tixador, Philippe, Moudjou, Mohammed, Chapuis, Jérôme, Sibille, Pierre, Herzog, Laetitia, Reine, Fabienne, Jaumain, Emilie, Laude, Hubert, Rezaei, Human, Béringue, Vincent

    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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    Pressure Reveals Unique Conformational Features in Prion Protein Fibril Diversity by Torrent, Joan, Martin, Davy, Noinville, Sylvie, Yin, Yi, Doumic, Marie, Moudjou, Mohammed, Béringue, Vincent, Rezaei, Human

    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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    Thermostability as a highly dependent prion strain feature by Marín-Moreno, Alba, Aguilar-Calvo, Patricia, Moudjou, Mohammed, Espinosa, Juan Carlos, Béringue, Vincent, Torres, Juan María

    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 by Moudjou, Mohammed, Sibille, Pierre, Fichet, Guillaume, Reine, Fabienne, Chapuis, Jérôme, Herzog, Laetitia, Jaumain, Emilie, Laferrière, Florent, Richard, Charles-Adrien, Laude, Hubert, Andréoletti, Olivier, Rezaei, Human, Béringue, Vincent

    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 by Igel-Egalon, Angélique, Laferrière, Florent, Tixador, Philippe, Moudjou, Mohammed, Herzog, Laetitia, Reine, Fabienne, Torres, Juan Maria, Laude, Hubert, Rezaei, Human, Béringue, Vincent

    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? by Igel-Egalon, Angélique, Bohl, Jan, Moudjou, Mohammed, Herzog, Laetitia, Reine, Fabienne, Rezaei, Human, Béringue, Vincent

    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 by Dron, Michel, Moudjou, Mohammed, Chapuis, Jérôme, Salamat, Muhammad Khalid Farooq, Bernard, Julie, Cronier, Sabrina, Langevin, Christelle, Laude, Hubert

    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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    Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification by Moudjou, Mohammed, Chapuis, Jérôme, Mekrouti, Mériem, Reine, Fabienne, Herzog, Laetitia, Sibille, Pierre, Laude, Hubert, Vilette, Didier, Andréoletti, Olivier, Rezaei, Human, Dron, Michel, Béringue, Vincent

    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 by Igel-Egalon, Angélique, Moudjou, Mohammed, Martin, Davy, Busley, Alexandra, Knäpple, Tina, Herzog, Laetitia, Reine, Fabienne, Lepejova, Nad'a, Richard, Charles-Adrien, Béringue, Vincent, Rezaei, Human

    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 by TRAN, Thi-Lan, CASTAGNE, Nathalie, DUBOSCLARD, Virginie, NOINVILLE, Sylvie, KOCH, Emmanuelle, MOUDJOU, Mohammed, HENRY, Céline, BERNARD, Julie, YEO, Robert Paul, ELEOUËT, Jean-François

    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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    Glycoform-selective prion formation in sporadic and familial forms of prion disease by Xiao, Xiangzhu, Yuan, Jue, Haïk, Stéphane, Cali, Ignazio, Zhan, Yian, Moudjou, Mohammed, Li, Baiya, Laplanche, Jean-Louis, Laude, Hubert, Langeveld, Jan, Gambetti, Pierluigi, Kitamoto, Tetsuyuki, Kong, Qingzhong, Brandel, Jean-Philippe, Cobb, Brian A, Petersen, Robert B, Zou, Wen-Quan

    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 by Segarra, Christiane, Bougard, Daisy, Moudjou, Mohammed, Laude, Hubert, Béringue, Vincent, Coste, Joliette

    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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    Shadoo binds lipid membranes and undergoes aggregation and fibrillization by Li, Qiaojing, Chevalier, Christophe, Henry, Céline, Richard, Charles-Adrien, Moudjou, Mohammed, Vidic, Jasmina

    “…•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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    Nucleoprotein nanostructures combined with adjuvants adapted to the neonatal immune context: a candidate mucosal RSV vaccine by Remot, Aude, Roux, Xavier, Dubuquoy, Catherine, Fix, Jenna, Bouet, Stephan, Moudjou, Mohammed, Eléouët, Jean-François, Riffault, Sabine, Petit-Camurdan, Agnès

    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 by Martin, Davy, Reine, Fabienne, Herzog, Laetitia, Igel-Egalon, Angélique, Aron, Naima, Michel, Christel, Moudjou, Mohammed, Fichet, Guillaume, Quadrio, Isabelle, Perret-Liaudet, Armand, Andréoletti, Olivier, Rezaei, Human, Béringue, Vincent

    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 by Zhang, Weiguanliu, Xiao, Xiangzhu, Ding, Mingxuan, Yuan, Jue, Foutz, Aaron, Moudjou, Mohammed, Kitamoto, Tetsuyuki, Langeveld, Jan P M, Cui, Li, Zou, Wen-Quan

    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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