Alpha-Synuclein Induces Lysosomal Rupture and Cathepsin Dependent Reactive Oxygen Species Following Endocytosis
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{"title"=>"Alpha-Synuclein Induces Lysosomal Rupture and Cathepsin Dependent Reactive Oxygen Species Following Endocytosis", "type"=>"journal", "authors"=>[{"first_name"=>"David", "last_name"=>"Freeman", "scopus_author_id"=>"55606855400"}, {"first_name"=>"Rudy", "last_name"=>"Cedillos", "scopus_author_id"=>"54919398900"}, {"first_name"=>"Samantha", "last_name"=>"Choyke", "scopus_author_id"=>"55661381300"}, {"first_name"=>"Zana", "last_name"=>"Lukic", "scopus_author_id"=>"54389459100"}, {"first_name"=>"Kathleen", "last_name"=>"McGuire", "scopus_author_id"=>"37031609900"}, {"first_name"=>"Shauna", "last_name"=>"Marvin", "scopus_author_id"=>"7003285868"}, {"first_name"=>"Andrew M.", "last_name"=>"Burrage", "scopus_author_id"=>"55661703200"}, {"first_name"=>"Stacey", "last_name"=>"Sudholt", "scopus_author_id"=>"55661248300"}, {"first_name"=>"Ajay", "last_name"=>"Rana", "scopus_author_id"=>"7004537880"}, {"first_name"=>"Christopher", "last_name"=>"O'Connor", "scopus_author_id"=>"55119109000"}, {"first_name"=>"Christopher M.", "last_name"=>"Wiethoff", "scopus_author_id"=>"35610646500"}, {"first_name"=>"Edward M.", "last_name"=>"Campbell", "scopus_author_id"=>"7402063637"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"84876722731", "doi"=>"10.1371/journal.pone.0062143", "isbn"=>"1932-6203", "pmid"=>"23634225", "issn"=>"19326203", "scopus"=>"2-s2.0-84876722731", "pui"=>"368798921"}, "id"=>"008d5476-4172-36fb-b9d0-4491c5ebb78c", "abstract"=>"α-synuclein dysregulation is a critical aspect of Parkinson's disease pathology. Recent studies have observed that α-synuclein aggregates are cytotoxic to cells in culture and that this toxicity can be spread between cells. However, the molecular mechanisms governing this cytotoxicity and spread are poorly characterized. Recent studies of viruses and bacteria, which achieve their cytoplasmic entry by rupturing intracellular vesicles, have utilized the redistribution of galectin proteins as a tool to measure vesicle rupture by these organisms. Using this approach, we demonstrate that α-synuclein aggregates can induce the rupture of lysosomes following their endocytosis in neuronal cell lines. This rupture can be induced by the addition of α-synuclein aggregates directly into cells as well as by cell-to-cell transfer of α-synuclein. We also observe that lysosomal rupture by α-synuclein induces a cathepsin B dependent increase in reactive oxygen species (ROS) in target cells. Finally, we observe that α-synuclein aggregates can induce inflammasome activation in THP-1 cells. Lysosomal rupture is known to induce mitochondrial dysfunction and inflammation, both of which are well established aspects of Parkinson's disease, thus connecting these aspects of Parkinson's disease to the propagation of α-synuclein pathology in cells.", "link"=>"http://www.mendeley.com/research/alphasynuclein-induces-lysosomal-rupture-cathepsin-dependent-reactive-oxygen-species-following-endoc", "reader_count"=>106, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>6, "Student > Doctoral Student"=>3, "Researcher"=>20, "Student > Ph. D. Student"=>35, "Student > Postgraduate"=>3, "Student > Master"=>19, "Other"=>1, "Student > Bachelor"=>10, "Professor"=>7}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>6, "Student > Doctoral Student"=>3, "Researcher"=>20, "Student > Ph. D. Student"=>35, "Student > Postgraduate"=>3, "Student > Master"=>19, "Other"=>1, "Student > Bachelor"=>10, "Professor"=>7}, "reader_count_by_subject_area"=>{"Engineering"=>1, "Unspecified"=>3, "Biochemistry, Genetics and Molecular Biology"=>13, "Nursing and Health Professions"=>1, "Agricultural and Biological Sciences"=>49, "Medicine and Dentistry"=>9, "Neuroscience"=>16, "Pharmacology, Toxicology and Pharmaceutical Science"=>2, "Chemistry"=>8, "Social Sciences"=>2, "Computer Science"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>9}, "Neuroscience"=>{"Neuroscience"=>16}, "Chemistry"=>{"Chemistry"=>8}, "Social Sciences"=>{"Social Sciences"=>2}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>49}, "Computer Science"=>{"Computer Science"=>1}, "Nursing and Health Professions"=>{"Nursing and Health Professions"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>13}, "Unspecified"=>{"Unspecified"=>3}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>2}}, "reader_count_by_country"=>{"United States"=>1, "China"=>1, "Italy"=>1}, "group_count"=>2}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1036657"], "description"=>"<p>N27 cells stably expressing α-synuclein and treated with MPP<sup>+</sup> for 24 hours. N27chGal3 cells were then added to the culture and co-cultured for 48 hours. Cells were then fixed and stained for α-synuclein (green). The boxed areas in the left panel are enlarged to allow visualization of α-synuclein and chGal3 colocalization.</p>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "rupture"], "article_id"=>692013, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0062143.g006", "stats"=>{"downloads"=>2, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Vesicle_rupture_following_the_cell_to_cell_transfer_of_945_synuclein_/692013", "title"=>"Vesicle rupture following the cell to cell transfer of α-synuclein.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-25 00:33:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/1036673", "https://ndownloader.figshare.com/files/1036684", "https://ndownloader.figshare.com/files/1036687", "https://ndownloader.figshare.com/files/1036689", "https://ndownloader.figshare.com/files/1036690"], "description"=>"<div><p>α-synuclein dysregulation is a critical aspect of Parkinson's disease pathology. Recent studies have observed that α-synuclein aggregates are cytotoxic to cells in culture and that this toxicity can be spread between cells. However, the molecular mechanisms governing this cytotoxicity and spread are poorly characterized. Recent studies of viruses and bacteria, which achieve their cytoplasmic entry by rupturing intracellular vesicles, have utilized the redistribution of galectin proteins as a tool to measure vesicle rupture by these organisms. Using this approach, we demonstrate that α-synuclein aggregates can induce the rupture of lysosomes following their endocytosis in neuronal cell lines. This rupture can be induced by the addition of α-synuclein aggregates directly into cells as well as by cell-to-cell transfer of α-synuclein. We also observe that lysosomal rupture by α-synuclein induces a cathepsin B dependent increase in reactive oxygen species (ROS) in target cells. Finally, we observe that α-synuclein aggregates can induce inflammasome activation in THP-1 cells. Lysosomal rupture is known to induce mitochondrial dysfunction and inflammation, both of which are well established aspects of Parkinson's disease, thus connecting these aspects of Parkinson's disease to the propagation of α-synuclein pathology in cells.</p></div>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "lysosomal", "rupture", "cathepsin", "reactive"], "article_id"=>692027, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0062143.s001", "https://dx.doi.org/10.1371/journal.pone.0062143.s002", "https://dx.doi.org/10.1371/journal.pone.0062143.s003", "https://dx.doi.org/10.1371/journal.pone.0062143.s004", "https://dx.doi.org/10.1371/journal.pone.0062143.s005"], "stats"=>{"downloads"=>1, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Alpha_Synuclein_Induces_Lysosomal_Rupture_and_Cathepsin_Dependent_Reactive_Oxygen_Species_Following_Endocytosis_/692027", "title"=>"Alpha-Synuclein Induces Lysosomal Rupture and Cathepsin Dependent Reactive Oxygen Species Following Endocytosis", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-04-25 00:33:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1036654"], "description"=>"<p>N27chGal3 cells were exposed to Dylight 488 conjugated α-synuclein aggregates for 48 hours. Cells were fixed and imaged using a structured illumination fluorescent microscope, allowing the images to be reconstructed with a resolution below the diffraction limit of light microscopy. The boxed area in the left panel is enlarged in the two panels to reveal the intraluminal localization of α-synuclein.</p>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "illumination", "imaging", "mediated", "vesicle"], "article_id"=>692012, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0062143.g005", "stats"=>{"downloads"=>1, "page_views"=>23, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structured_Illumination_SIM_imaging_of_945_synuclein_mediated_vesicle_rupture_/692012", "title"=>"Structured Illumination (SIM) imaging of α-synuclein mediated vesicle rupture.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-25 00:33:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/1036666"], "description"=>"<p>A. ELISA of the time dependent release of IL-1β by differentiated THP-1 cells left untreated (Mock) or stimulated with α-synuclein (2.4 µg/ml) and/or LPS. B. ELISA of the dose dependent release of IL-1β into supernatants of LPS-primed THP-1 cells left unstimulated (Ctrl) or stimulated with an increasing amount of α-synuclein, or ATP (5 mM). C. Quantification of caspase-1 activation in THP-1 cells. Caspase-1 activation was visualized by incubation with a fluorescent cell-permeable probe that binds only to activated caspase-1 (FLICA). Data represents the means and standard errors from 3 replicates. *p<0.01</p>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "aggregates", "induce", "caspase-1-dependent"], "article_id"=>692020, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0062143.g009", "stats"=>{"downloads"=>0, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_945_synuclein_aggregates_induce_the_caspase_1_dependent_release_of_interleukin_1_946_/692020", "title"=>"α-synuclein aggregates induce the caspase-1-dependent release of interleukin-1β.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-25 00:33:40"}
  • {"files"=>["https://ndownloader.figshare.com/files/1036663"], "description"=>"<p>(A) SH-SY5Y or (B) N27 cells were loaded with H<sub>2</sub>DCFDA reagent and incubated with wt or E46K α-synuclein. Error bars represent the SEM of triplicate samples. Results are representative of at least three independent experiments. C. Purified recombinant E46K α-synuclein aggregates were added to N27 chGal3 cells for 24 hours, stained with an α-synuclein specific antibody (green) and imaged as in previous experiments. Results are representative of at least three independent experiments.</p>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "aggregates", "generated", "e46k", "mutant", "induce", "vesicle", "rupture", "ros", "efficiently", "wt"], "article_id"=>692017, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0062143.g008", "stats"=>{"downloads"=>1, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Large_aggregates_generated_by_the_E46K_mutant_of_945_synuclein_do_not_induce_vesicle_rupture_or_ROS_as_efficiently_as_wt_945_synuclein_/692017", "title"=>"Large aggregates generated by the E46K mutant of α-synuclein do not induce vesicle rupture or ROS as efficiently as wt α-synuclein.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-25 00:33:37"}
  • {"files"=>["https://ndownloader.figshare.com/files/1036639"], "description"=>"<p>A. Wild-type α-synuclein aggregates were generated using <i>in vitro</i> purified protein. Recombinant lyophilized α-synuclein was resuspended and followed by constant agitation for three days at 37°C. The aggregates generated in this fashion were run on a non-denaturing gel (left) or denaturing gel (right), fixed and stained with Coomassie brilliant blue. B. Following incubation for 3 days as described, α-synuclein preparations were fixed with glutaraldehyde at the indicated concentration for 15 minutes at room temperature. C. K114 analysis of α-synuclein which was freshly resuspended or incubated as described. Emission was measured at 550 nm. Error bars represent the standard error of the mean of 3 readings. Results are representative of at least three independent experiments (* indicates a P value <.01). D. Transmission electron micrograph of α-synuclein preparations from freshly resuspended protein or after 3 days of incubation as described. Scale bars = 500 nm.</p>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "aggregate"], "article_id"=>692002, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0062143.g001", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_945_synuclein_aggregate_characterization_/692002", "title"=>"α-synuclein aggregate characterization.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-25 00:33:22"}
  • {"files"=>["https://ndownloader.figshare.com/files/1036660"], "description"=>"<p>SH-SY5Y (A) or N27 (B) cells loaded with the fluorescent substrate H<sub>2</sub>DCFDA reagent and incubated in the presence or absence of α-synuclein aggregates with or without treatment with the cathepsin B inhibitor Ca-074Me. Error bars represent the SEM of triplicate samples. C. SH-SY5Y cells stably expressing mitochondrially targeted roGFP1 were incubated for 72 hours with α-synuclein aggregates and the oxidation state of the mitochondria of individual cells was assessed at described in the text. Error bars represent the SEM of 15 or more cells analyzed for each treatment group. * p<u><0.001.</u></p>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "aggregates", "induce", "cathepsin", "ros"], "article_id"=>692014, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0062143.g007", "stats"=>{"downloads"=>1, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_945_synuclein_aggregates_induce_a_cathepsin_B_dependent_increase_in_ROS_in_cells_/692014", "title"=>"α-synuclein aggregates induce a cathepsin B dependent increase in ROS in cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-25 00:33:34"}
  • {"files"=>["https://ndownloader.figshare.com/files/1036651"], "description"=>"<p>SH-SY5Y chGal3 cell exposed to Dylight 488 conjugated α-synuclein aggregates for 24 hours. The white box in the upper left panel is enlarged in the other three panels to demonstrate colocalization of α-syn and chGal3. White arrows show vesicles demonstrating colocalization between chGal3 and α-syn. The red arrow highlights a ruptured vesicle that does not appear to contain α-synuclein.</p>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "colocalizes", "chgal3", "neuronal"], "article_id"=>692010, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0062143.g004", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_945_synuclein_colocalizes_with_chGal3_in_neuronal_cell_lines_/692010", "title"=>"α-synuclein colocalizes with chGal3 in neuronal cell lines.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-25 00:33:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/1036645"], "description"=>"<p>A. SH-SY5Y chGal3 cells (red) treated with α-synuclein aggregates hibit colocalization between chGal3 and LAMP2 (green). The area shown in the white box in the upper left panel is enlarged in the other three panels. B. SH-SY5Y chGal3 cells (red) treated with α-synuclein, which does not induce colocalization between chGal3 and EEA1 (green). The area shown in the white box in the upper left panel is enlarged in the other three panels. C. Quantitative analysis of the colocalization of fluorescent intensity of EEA1 or LAMP2 staining in individual chGal3 puncta identified using Imaris image analysis software. 7.43% of chGal3-positive vesicles exhibited EEA1 staining above background levels, whereas 91.98% of these vesicles exhibited LAMP2 staining greater than secondary antibody alone. Forty images were collected for each group. More than 190 individual puncta were analyzed for each group.</p>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "aggregates", "induce", "lysosomal"], "article_id"=>692005, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0062143.g003", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_945_synuclein_aggregates_induce_lysosomal_rupture_/692005", "title"=>"α-synuclein aggregates induce lysosomal rupture.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-25 00:33:25"}
  • {"files"=>["https://ndownloader.figshare.com/files/1036641"], "description"=>"<p>SH-SY5Y or N27 cells stably expressing chGal3 were treated with α-synuclein aggregates for 24 hours. In both cell lines a relocalization from the diffuse, untreated state can be clearly visualized after 24 hours. This relocalization is indicative of intracellular vesicular rupture. Images are representative of at least three independent experiments.</p>", "links"=>[], "tags"=>["neurology", "Parkinson disease", "Biochemistry", "Neurochemistry", "Neurochemicals", "dopamine", "proteins", "Protein interactions", "Recombinant proteins", "immunochemistry", "immunology", "immunopathology", "Molecular cell biology", "Membranes and sorting", "neuroscience", "Cellular neuroscience", "Neurobiology of disease and regeneration", "aggregates", "induce", "discrete", "galectin-3"], "article_id"=>692004, "categories"=>["Medicine", "Biological Sciences"], "users"=>["David Freeman", "Rudy Cedillos", "Samantha Choyke", "Zana Lukic", "Kathleen McGuire", "Shauna Marvin", "Andrew M. Burrage", "Stacey Sudholt", "Ajay Rana", "Christopher O'Connor", "Christopher M. Wiethoff", "Edward M. Campbell"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0062143.g002", "stats"=>{"downloads"=>0, "page_views"=>33, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_945_synuclein_aggregates_induce_discrete_Galectin_3_puncta_/692004", "title"=>"α-synuclein aggregates induce discrete Galectin-3 puncta.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-25 00:33:24"}

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Relative Metric

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