UB Paderborn / Katalog / Suche / in CDI

Sortiert nach

Einfacher Volltextzugriff von (fast) überall

Installieren Sie die LibKey Nomad-Browsererweiterung und erhalten Sie von vielen Webseiten einfachen Zugriff auf lizenzierte Volltexte oder Open Access Publikationen. Mehr erfahren...

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

Proceedings of the National Academy of Sciences - PNAS, 2016-02, Vol.113 (7), p.1931-1936

2016

Volltextzugriff (PDF)

Molecular mechanisms of α-synuclein and GBA1 in Parkinson’s disease

Cell and tissue research, 2018-07, Vol.373 (1), p.51-60

2018

Volltextzugriff (PDF)

Gaucher Disease Glucocerebrosidase and α-Synuclein Form a Bidirectional Pathogenic Loop in Synucleinopathies

Cell, 2011-07, Vol.146 (1), p.37-52

2011

Volltextzugriff (PDF)

Is Parkinson's disease a lysosomal disorder?

Brain (London, England : 1878), 2018-08, Vol.141 (8), p.2255-2262

2018

Volltextzugriff (PDF)

Dopamine oxidation mediates mitochondrial and lysosomal dysfunction in Parkinson’s disease

Science (American Association for the Advancement of Science), 2017-09, Vol.357 (6357), p.1255-1261

2017

Volltextzugriff (PDF)

Neuroinflammation in Gaucher disease, neuronal ceroid lipofuscinosis, and commonalities with Parkinson’s disease

Brain research, 2022-04, Vol.1780, p.147798-147798, Article 147798

2022

Volltextzugriff (PDF)

Dysregulation of the autophagic-lysosomal pathway in Gaucher and Parkinson's disease

Neurobiology of disease, 2019-02, Vol.122, p.72-82

2019

Volltextzugriff (PDF)

Modeling neuronopathic storage diseases with patient-derived culture systems

Neurobiology of disease, 2019-07, Vol.127, p.147-162

2019

Volltextzugriff (PDF)

Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity

The Journal of neuroscience, 2012-03, Vol.32 (12), p.4240-4246

2012

Volltextzugriff (PDF)

Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide

Neuron (Cambridge, Mass.), 2018-01, Vol.97 (1), p.92-107.e10

2018

Volltextzugriff (PDF)

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

Stem cell reports, 2016-10, Vol.7 (4), p.664-677

2016

Volltextzugriff (PDF)

Increased Lysosomal Exocytosis Induced by Lysosomal Ca2+ Channel Agonists Protects Human Dopaminergic Neurons from α-Synuclein Toxicity

The Journal of neuroscience, 2019-07, Vol.39 (29), p.5760-5772

2019

Volltextzugriff (PDF)

Rapamycin reverses cellular phenotypes and enhances mutant protein clearance in Hutchinson-Gilford progeria syndrome cells

Science translational medicine, 2011-06, Vol.3 (89), p.89ra58

2011

Volltextzugriff (PDF)

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

Neuron (Cambridge, Mass.), 2022-02, Vol.110 (3), p.436-451.e11

2022

Volltextzugriff (PDF)

The hexosamine biosynthetic pathway rescues lysosomal dysfunction in Parkinson’s disease patient iPSC derived midbrain neurons

Nature communications, 2024-06, Vol.15 (1), p.5206-17, Article 5206

2024

Volltextzugriff (PDF)

Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway

Nature medicine, 2012-01, Vol.18 (1), p.159-165

2012

Volltextzugriff (PDF)

Impaired Autophagic-Lysosomal Fusion in Parkinson's Patient Midbrain Neurons Occurs through Loss of ykt6 and Is Rescued by Farnesyltransferase Inhibition

The Journal of neuroscience, 2023-04, Vol.43 (14), p.2615-2629

2023

Volltextzugriff (PDF)

α-Synuclein: Multiple pathogenic roles in trafficking and proteostasis pathways in Parkinson’s disease

The Neuroscientist, 2024-10, Vol.30 (5), p.612-635

2024

Volltextzugriff (PDF)

Activation of β-Glucocerebrosidase Reduces Pathological α-Synuclein and Restores Lysosomal Function in Parkinson's Patient Midbrain Neurons

The Journal of neuroscience, 2016-07, Vol.36 (29), p.7693-7706

2016

Volltextzugriff (PDF)

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

The Journal of clinical investigation, 2022-03, Vol.132 (5), p.1-14

2022

Volltextzugriff (PDF)

Dopamine induces soluble α-synuclein oligomers and nigrostriatal degeneration

Nature neuroscience, 2017-11, Vol.20 (11), p.1560-1568

2017

Volltextzugriff (PDF)

Nuclear aggregates of NONO/SFPQ and A-to-I-edited RNA in Parkinson’s disease and dementia with Lewy bodies

Neuron (Cambridge, Mass.), 2024-08, Vol.112 (15), p.2558-2580.e13

2024

Volltextzugriff (PDF)

Acetylation Targets Mutant Huntingtin to Autophagosomes for Degradation

Cell, 2009-04, Vol.137 (1), p.60-72

2009

Volltextzugriff (PDF)

Pathological α-syn aggregation is mediated by glycosphingolipid chain length and the physiological state of α-syn in vivo

Proceedings of the National Academy of Sciences - PNAS, 2021-12, Vol.118 (50), p.1

2021

Volltextzugriff (PDF)

LIMP-2 expression is critical for β-glucocerebrosidase activity and α-synuclein clearance

Proceedings of the National Academy of Sciences - PNAS, 2014-10, Vol.111 (43), p.15573-15578

2014

Volltextzugriff (PDF)

1 – 25 von 70

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(69)
Mit Volltextzugriff
(64)

Publikationsform

Artikel
(69)
Dissertationen
(1)

Sprache

Englisch
(70)
Japanisch
(7)

Erscheinungsjahr

n.n

Thema

15 weitere anzeigen...

Weniger anzeigen...

Menü

Weitere Dienste

Einstellungen

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

Molecular mechanisms of α-synuclein and GBA1 in Parkinson’s disease

Gaucher Disease Glucocerebrosidase and α-Synuclein Form a Bidirectional Pathogenic Loop in Synucleinopathies

Is Parkinson's disease a lysosomal disorder?

Dopamine oxidation mediates mitochondrial and lysosomal dysfunction in Parkinson’s disease

Neuroinflammation in Gaucher disease, neuronal ceroid lipofuscinosis, and commonalities with Parkinson’s disease

Dysregulation of the autophagic-lysosomal pathway in Gaucher and Parkinson's disease

Modeling neuronopathic storage diseases with patient-derived culture systems

Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity

Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide

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

Increased Lysosomal Exocytosis Induced by Lysosomal Ca2+ Channel Agonists Protects Human Dopaminergic Neurons from α-Synuclein Toxicity

Rapamycin reverses cellular phenotypes and enhances mutant protein clearance in Hutchinson-Gilford progeria syndrome cells

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

The hexosamine biosynthetic pathway rescues lysosomal dysfunction in Parkinson’s disease patient iPSC derived midbrain neurons

Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway

Impaired Autophagic-Lysosomal Fusion in Parkinson's Patient Midbrain Neurons Occurs through Loss of ykt6 and Is Rescued by Farnesyltransferase Inhibition

α-Synuclein: Multiple pathogenic roles in trafficking and proteostasis pathways in Parkinson’s disease

Activation of β-Glucocerebrosidase Reduces Pathological α-Synuclein and Restores Lysosomal Function in Parkinson's Patient Midbrain Neurons

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

Dopamine induces soluble α-synuclein oligomers and nigrostriatal degeneration

Nuclear aggregates of NONO/SFPQ and A-to-I-edited RNA in Parkinson’s disease and dementia with Lewy bodies

Acetylation Targets Mutant Huntingtin to Autophagosomes for Degradation

Pathological α-syn aggregation is mediated by glycosphingolipid chain length and the physiological state of α-syn in vivo

LIMP-2 expression is critical for β-glucocerebrosidase activity and α-synuclein clearance

Suchergebnisse filtern