Результаты поиска - Joseph R. Mazzulli

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  1. 1
    Is Parkinson’s disease a lysosomal disorder?

    Is Parkinson’s disease a lysosomal disorder? по Andrés D. Klein, Joseph R. Mazzulli

    Опубликовано 2018
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  2. 2
    Molecular mechanisms of α-synuclein and GBA1 in Parkinson’s disease

    Molecular mechanisms of α-synuclein and GBA1 in Parkinson’s disease по Iva Stojkovska, Dimitri Krainc, Joseph R. Mazzulli

    Опубликовано 2017
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  3. 3
    Dysregulation of the autophagic-lysosomal pathway in Gaucher and Parkinson's disease

    Dysregulation of the autophagic-lysosomal pathway in Gaucher and Parkinson's disease по Caleb Pitcairn, Willayat Yousuf Wani, Joseph R. Mazzulli

    Опубликовано 2018
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  4. 4
    Characterization of Hydrophobic Residue Requirements for α-Synuclein Fibrillization

    Characterization of Hydrophobic Residue Requirements for α-Synuclein Fibrillization по Elisa A. Waxman, Joseph R. Mazzulli, Benoit I. Giasson

    Опубликовано 2009
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  5. 5
    Cellular Oligomerization of α-Synuclein Is Determined by the Interaction of Oxidized Catechols with a C-terminal Sequence

    Cellular Oligomerization of α-Synuclein Is Determined by the Interaction of Oxidized Catechols with a C-terminal Sequence по Joseph R. Mazzulli, Maria Armakola, Michelle Dumoulin, Ioannis Parastatidis, Harry Ischiropoulos

    Опубликовано 2007
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  6. 6
    α-Synuclein–induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models

    α-Synuclein–induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models по Joseph R. Mazzulli, Friederike Zunke, Ole Isacson, Lorenz Studer, Dimitri Krainc

    Опубликовано 2016
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  7. 7
    Deficiency of ATP13A2 Leads to Lysosomal Dysfunction, α-Synuclein Accumulation, and Neurotoxicity

    Deficiency of ATP13A2 Leads to Lysosomal Dysfunction, α-Synuclein Accumulation, and Neurotoxicity по Marija Usenovic, Emilie Tresse, Joseph R. Mazzulli, J. Paul Taylor, Dimitri Krainc

    Опубликовано 2012
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  8. 8
    AAV9/MFSD8 gene therapy is effective in preclinical models of neuronal ceroid lipofuscinosis type 7 disease

    AAV9/MFSD8 gene therapy is effective in preclinical models of neuronal ceroid lipofuscinosis type 7 disease по Xin Chen, Thomas Dong, Yuhui Hu, Frances C. Shaffo, Nandkishore R. Belur, Joseph R. Mazzulli, Steven J. Gray

    Опубликовано 2022
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  9. 9
    Rescue of α-synuclein aggregation in Parkinson’s patient neurons by synergistic enhancement of ER proteostasis and protein trafficking

    Rescue of α-synuclein aggregation in Parkinson’s patient neurons by synergistic enhancement of ER proteostasis and protein trafficking по Iva Stojkovska, Willayat Yousuf Wani, Friederike Zunke, Nandkishore R. Belur, Egor Pavlenko, Nkatha Mwenda, Karan Sharma, Laetitia Francelle, Joseph R. Mazzulli

    Опубликовано 2021
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  10. 10
    Cytosolic Catechols Inhibit α-Synuclein Aggregation and Facilitate the Formation of Intracellular Soluble Oligomeric Intermediates

    Cytosolic Catechols Inhibit α-Synuclein Aggregation and Facilitate the Formation of Intracellular Soluble Oligomeric Intermediates по Joseph R. Mazzulli, Amanda J. Mishizen, Benoit I. Giasson, David R. Lynch, Steven Thomas, Akira Nakashima, Toshiharu Nagatsu, Akira Ota, Harry Ischiropoulos

    Опубликовано 2006
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    Artigo
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  11. 11
    Distinct Region-Specific α-Synuclein Oligomers in A53T Transgenic Mice: Implications for Neurodegeneration

    Distinct Region-Specific α-Synuclein Oligomers in A53T Transgenic Mice: Implications for Neurodegeneration по Elpida Tsika, Maria Moysidou, Jing Guo, Mimi Cushman, Patrick J. Gannon, Raphael Sandaltzopoulos, Benoit I. Giasson, Dimitri Krainc, Harry Ischiropoulos, Joseph R. Mazzulli

    Опубликовано 2010
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    Artigo
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  12. 12
    Characterization of the complex formed by β-glucocerebrosidase and the lysosomal integral membrane protein type-2

    Characterization of the complex formed by β-glucocerebrosidase and the lysosomal integral membrane protein type-2 по Friederike Zunke, Lisa Andresen, Sophia Wesseler, Johann Groth, Philipp Arnold, Michelle Rothaug, Joseph R. Mazzulli, Dimitri Krainc, Judith Blanz, Paul Säftig, Michael Schwake

    Опубликовано 2016
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  13. 13
    Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide

    Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide по Friederike Zunke, Alexandra C. Moise, Nandkishore R. Belur, Eilrayna Gelyana, Iva Stojkovska, Haris Dzaferbegovic, Nicholas Toker, Sohee Jeon, Kristina Fredriksen, Joseph R. Mazzulli

    Опубликовано 2017
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  14. 14
    Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway

    Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway по Hyunkyung Jeong, Dena E. Cohen, Libin Cui, Andrea Supinski, Jeffrey N. Savas, Joseph R. Mazzulli, John R. Yates, Laura Bordone, Leonard Guarente, Dimitri Krainc

    Опубликовано 2011
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  15. 15
    Gaucher Disease Glucocerebrosidase and α-Synuclein Form a Bidirectional Pathogenic Loop in Synucleinopathies

    Gaucher Disease Glucocerebrosidase and α-Synuclein Form a Bidirectional Pathogenic Loop in Synucleinopathies по Joseph R. Mazzulli, You-Hai Xu, Ying Sun, Adam L. Knight, Pamela J. McLean, Guy A. Caldwell, Ellen Sidransky, Gregory A. Grabowski, Dimitri Krainc

    Опубликовано 2011
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  16. 16
    Activation of -Glucocerebrosidase Reduces Pathological -Synuclein and Restores Lysosomal Function in Parkinson's Patient Midbrain Neurons

    Activation of -Glucocerebrosidase Reduces Pathological -Synuclein and Restores Lysosomal Function in Parkinson's Patient Midbrain Neurons по Joseph R. Mazzulli, Friederike Zunke, Taiji Tsunemi, Nicholas Toker, Sohee Jeon, Lena F. Burbulla, Samarjit Patnaik, Ellen Sidransky, Juan Marugán, Carolyn M. Sue, Dimitri Krainc

    Опубликовано 2016
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  17. 17
    Acetylation Targets Mutant Huntingtin to Autophagosomes for Degradation

    Acetylation Targets Mutant Huntingtin to Autophagosomes for Degradation по Hyunkyung Jeong, Florian Then, Thomas J. Melia, Joseph R. Mazzulli, Libin Cui, Jeffrey N. Savas, Cindy Voisine, Paolo Paganetti, Naoko Tanese, Anne C. Hart, Ai Yamamoto, Dimitri Krainc

    Опубликовано 2009
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  18. 18
    Reciprocal effects of alpha-synuclein aggregation and lysosomal homeostasis in synucleinopathy models

    Reciprocal effects of alpha-synuclein aggregation and lysosomal homeostasis in synucleinopathy models по Alice Drobny, Fanni Annamária Boros, Denise Balta, Susy Prieto Huarcaya, Deniz Caylioglu, Niyeti Qazi, Julia Vandrey, Yanni Schneider, Jan Philipp Dobert, Caleb Pitcairn, Joseph R. Mazzulli, Friederike Zunke

    Опубликовано 2023
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  19. 19
    Increased Lysosomal Exocytosis Induced by Lysosomal Ca<sup>2+</sup> Channel Agonists Protects Human Dopaminergic Neurons from α-Synuclein Toxicity

    Increased Lysosomal Exocytosis Induced by Lysosomal Ca<sup>2+</sup> Channel Agonists Protects Human Dopaminergic Neurons from α-Synuclein Toxicity по Taiji Tsunemi, Tamara Perez‐Rosello, Yuta Ishiguro, Asako Yoroisaka, Sohee Jeon, Kana Hamada, Malini Rammonhan, Yvette C. Wong, Zhong Xie, Wado Akamatsu, Joseph R. Mazzulli, D. James Surmeier, Nobutaka Hattori, Dimitri Krainc

    Опубликовано 2019
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  20. 20
    Parkin and PINK1 Patient iPSC-Derived Midbrain Dopamine Neurons Exhibit Mitochondrial Dysfunction and α-Synuclein Accumulation

    Parkin and PINK1 Patient iPSC-Derived Midbrain Dopamine Neurons Exhibit Mitochondrial Dysfunction and α-Synuclein Accumulation по Sun Young Chung, Sarah Kishinevsky, Joseph R. Mazzulli, John J. Graziotto, Ana Mrejeru, Eugene V. Mosharov, Lesly Puspita, Parvin Valiulahi, David Sulzer, Teresa A. Milner, Tony Taldone, Dimitri Krainc, Lorenz Studer, Jae-won Shim

    Опубликовано 2016
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