| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2013PLoSO...862143F |
| P356 | DOI | 10.1371/JOURNAL.PONE.0062143 |
| P953 | full work available at URL | http://dx.plos.org/10.1371/journal.pone.0062143 |
| https://europepmc.org/articles/PMC3636263 | ||
| https://europepmc.org/articles/PMC3636263?pdf=render | ||
| https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0062143&type=printable | ||
| P3181 | OpenCitations bibliographic resource ID | 2145373 |
| P932 | PMC publication ID | 3636263 |
| P698 | PubMed publication ID | 23634225 |
| P5875 | ResearchGate publication ID | 236600829 |
| P2093 | author name string | Ajay Rana | |
| Christopher O'Connor | |||
| David Freeman | |||
| Kathleen McGuire | |||
| Rudy Cedillos | |||
| Samantha Choyke | |||
| Shauna Marvin | |||
| Stacey Sudholt | |||
| Zana Lukic | |||
| Christopher M. Wiethoff | |||
| Edward M. Campbell | |||
| Andrew M. Burrage | |||
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| Adenovirus membrane penetration activates the NLRP3 inflammasome. | Q39639156 | ||
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| The interaction between the fiber knob domain and the cellular attachment receptor determines the intracellular trafficking route of adenoviruses | Q39732535 | ||
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| Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions | Q48581414 | ||
| Tracking the dynamic interplay between bacterial and host factors during pathogen-induced vacuole rupture in real time | Q48827027 | ||
| Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease | Q48830095 | ||
| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P433 | issue | 4 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | endocytosis | Q189814 |
| reactive oxygen species | Q424361 | ||
| Synuclein | Q24767155 | ||
| P304 | page(s) | e62143 | |
| P577 | publication date | 2013-01-01 | |
| 2013-04-25 | |||
| P1433 | published in | PLOS One | Q564954 |
| P1476 | title | Alpha-synuclein induces lysosomal rupture and cathepsin dependent reactive oxygen species following endocytosis | |
| Alpha-Synuclein Induces Lysosomal Rupture and Cathepsin Dependent Reactive Oxygen Species Following Endocytosis | |||
| P478 | volume | 8 |
| Q57792623 | A Druggable Genome Screen Identifies Modifiers of α-Synuclein Levels via a Tiered Cross-Species Validation Approach |
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| Q28390698 | Activation of Proinflammatory Responses in Cells of the Airway Mucosa by Particulate Matter: Oxidant- and Non-Oxidant-Mediated Triggering Mechanisms |
| Q58596800 | Alpha-synuclein fibrils recruit TBK1 and OPTN to lysosomal damage sites and induce autophagy in microglial cells |
| Q64763405 | Autophagy in Synucleinopathy: The Overwhelmed and Defective Machinery |
| Q38673272 | Beyond starvation: An update on the autophagic machinery and its functions |
| Q38860098 | Binding, internalization and fate of Huntingtin Exon1 fibrillar assemblies in mitotic and nonmitotic neuroblastoma cells |
| Q38180144 | Biophysical groundwork as a hinge to unravel the biology of α-synuclein aggregation and toxicity |
| Q33997655 | Brain disposition of α-Synuclein: roles of brain barrier systems and implications for Parkinson's disease |
| Q92049502 | C-terminal α-synuclein truncations are linked to cysteine cathepsin activity in Parkinson's disease |
| Q26782938 | Cathepsin B is a New Drug Target for Traumatic Brain Injury Therapeutics: Evidence for E64d as a Promising Lead Drug Candidate |
| Q46279808 | Cell Death Pathways: a Novel Therapeutic Approach for Neuroscientists. |
| Q90054708 | Chaperone Mediated Autophagy Degrades TDP-43 Protein and Is Affected by TDP-43 Aggregation |
| Q33603777 | Considerations on the role of environmental toxins in idiopathic Parkinson's disease pathophysiology |
| Q35996987 | Direct Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells |
| Q36678823 | ER Stress and Autophagic Perturbations Lead to Elevated Extracellular α-Synuclein in GBA-N370S Parkinson's iPSC-Derived Dopamine Neurons. |
| Q36744478 | Effects of Serine 129 Phosphorylation on α-Synuclein Aggregation, Membrane Association, and Internalization |
| Q38773604 | Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins |
| Q47136365 | Ethanol preconditioning of rat cerebellar cultures targets NMDA receptors to the synapse and enhances peroxiredoxin 2 expression |
| Q92377188 | Galectin-3 is required for the microglia-mediated brain inflammation in a model of Huntington's disease |
| Q47251029 | Galectin-8-mediated selective autophagy protects against seeded tau aggregation |
| Q89762207 | Healthy Effects of Plant Polyphenols: Molecular Mechanisms |
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| Q35782822 | Iron Toxicity in the Retina Requires Alu RNA and the NLRP3 Inflammasome |
| Q58479932 | Is Parkinson's disease a lysosomal disorder? |
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| Q34073890 | Lys-63-linked ubiquitination by E3 ubiquitin ligase Nedd4-1 facilitates endosomal sequestration of internalized α-synuclein |
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| Q37537087 | Perturbation of neuronal cobalamin transport by lysosomal enzyme inhibition |
| Q64867396 | Prion-like propagation of pathology in Parkinson disease |
| Q90697402 | Protein Aggregation and Dysfunction of Autophagy-Lysosomal Pathway: A Vicious Cycle in Lysosomal Storage Diseases |
| Q47665674 | Prying into the Prion Hypothesis for Parkinson's Disease |
| Q92235387 | Reducing INS-IGF1 signaling protects against non-cell autonomous vesicle rupture caused by SNCA spreading |
| Q94686336 | Restoration of lysosomal function after damage is accompanied by recycling of lysosomal membrane proteins |
| Q28082714 | Role of Different Alpha-Synuclein Strains in Synucleinopathies, Similarities with other Neurodegenerative Diseases |
| Q36234963 | SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation |
| Q41378010 | Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies. |
| Q38652662 | Sorting out release, uptake and processing of alpha-synuclein during prion-like spread of pathology |
| Q52675832 | Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules. |
| Q90073258 | Targeting α-synuclein for PD Therapeutics: A Pursuit on All Fronts |
| Q37566684 | Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations |
| Q38754587 | Targeting α-synuclein: Therapeutic options |
| Q35833984 | The Interplay between Alpha-Synuclein Clearance and Spreading |
| Q99726049 | The Role of Vesicle Trafficking Defects in the Pathogenesis of Prion and Prion-Like Disorders |
| Q51284194 | The Transcellular Propagation and Intracellular Trafficking of α-Synuclein. |
| Q90408376 | The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding |
| Q46249781 | The lysosomal enzyme alpha-Galactosidase A is deficient in Parkinson's disease brain in association with the pathologic accumulation of alpha-synuclein. |
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| Q39445835 | The spread of prion-like proteins by lysosomes and tunneling nanotubes: Implications for neurodegenerative diseases. |
| Q47567656 | Therapeutic approaches to target alpha-synuclein pathology |
| Q38341877 | Trafficking and degradation pathways in pathogenic conversion of prions and prion-like proteins in neurodegenerative diseases |
| Q91559574 | Transmission of α-synuclein seeds in neurodegenerative disease: recent developments |
| Q42388077 | Tunneling nanotubes spread fibrillar α-synuclein by intercellular trafficking of lysosomes |
| Q30274624 | VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy |
| Q28116171 | Zn²⁺ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation |
| Q36608855 | α-Synuclein interferes with the ESCRT-III complex contributing to the pathogenesis of Lewy body disease |
| Q38671037 | α-Synuclein transfer between neurons and astrocytes indicates that astrocytes play a role in degradation rather than in spreading |
| Q28541669 | β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH |
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