Results 81 to 90 of about 68,100 (329)

Ubiquilin-2 regulates pathological alpha-synuclein

Scientific Reports, 2023
AbstractThe key protein implicated in Parkinson’s disease and other synucleinopathies is α-synuclein, and a post-translationally modified form of the protein, phosphorylated at serine 129 (pS129), is a principal component in Lewy bodies, a pathological hallmark of PD. While altered proteostasis has been implicated in the etiology of Parkinson’s disease,
Stephanie S. Sandoval-Pistorius, Julia E. Gerson, Nyjerus Liggans, Jaimie H. Ryou, Kulin Oak, Xingli Li, Keyshla Y. Negron-Rios, Svetlana Fischer, Henry Barsh, Emily V. Crowley, Mary E. Skinner, Lisa M. Sharkey, Sami J. Barmada, Henry L. Paulson   +13 more
openaire   +3 more sources

NDST3‐Induced Epigenetic Reprogramming Reverses Neurodegeneration in Parkinson's Disease

Advanced Science, EarlyView.
NDST3‐mediated epigenetic reprogramming revitalizes neuronal circuits in the substantia nigra and striatum to halt dopaminergic neuron degeneration and restore motor function in Parkinson's disease models. This strategy promotes neuronal maintenance and functional recovery, highlighting NDST3's therapeutic potential in neurodegenerative disorders ...
Yujung Chang, Yongwoo Na, Hyeonjoo Im, Garam Yang, Seungseon Yang, Hyun Soo Shim, Chunggoo Kim, GyeungYun Kim, Hyeok Ju Park, Hee Young Kim, Seung Eun Lee, Wonwoong Lee, Yoon Ha, Sungho Park, Jieun Kim, Won‐Young Cho, Woong Sun, Jong‐Seo Kim, Junsang Yoo   +18 more
wiley   +1 more source

ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication

Advanced Science, EarlyView.
During RSV infection, nucleoprotein (N) forms RNA‐bound oligomers. The host protein ZNRD2 binds to these oligomers, promoting their transition into insoluble aggregates. These aggregates simultaneously sequester functional N to restrict viral production and disrupt chaperonin assembly quality control by interfering with ZNRD2's role as an adaptor ...
Haiwu Zhou, Mingbin He, Jinhong Du, Cong Liu, Weiwei Wang, Yuewen Han, Zhifei Li, Yali Qin, Mingzhou Chen   +8 more
wiley   +1 more source

TBK1 Induces the Formation of Optineurin Filaments That Condensate with Polyubiquitin and LC3 for Cargo Sequestration

Advanced Science, EarlyView.
Phosphorylation of Optineurin by TBK1 induces the formation of filaments that condensate upon binding to linear polyubiquitin. Membrane‐anchored LC3 partitions into these condensates, suggesting that phase separation of filamentous Optineurin with ubiquitylated cargo promotes the sequestration of cargo and its subsequent alignment with LC3‐positive ...
Maria G. Herrera, Lena Kühn, Lisa Jungbluth, Verian Bader, Laura J. Krause, David Kartte, Elias Adriaenssens, Sascha Martens, Jörg Tatzelt, Carsten Sachse, Konstanze F. Winklhofer   +10 more
wiley   +1 more source

Examining a Link between Paraquat, Alpha-Synuclein Fibrillation and Neurodegeneration: A Review [PDF]

, 2014
Parkinson’s disease is a progressive and chronic disorder that causes motor system dysfunction due to a lack of dopamine in the central nervous system.
Ailaney, Nikhil
core   +4 more sources

Prolyl Oligopeptidase Regulates Dopamine Transporter Phosphorylation in the Nigrostriatal Pathway of Mouse [PDF]

, 2018
Alpha-synuclein is the main component of Lewy bodies, a histopathological finding of Parkinson's disease. Prolyl oligopeptidase (PREP) is a serine protease that binds to alpha-synuclein and accelerates its aggregation in vitro.
Julku, Ulrika H., Myöhänen, Timo T., Panhelainen, Anne E., Piepponen, T. Petteri, Savolainen, Mari H., Svarcbahs, Reinis, Tammimäki, Anne E., Tiilikainen, Saija E.   +7 more
core   +1 more source

Phospho-S129 Alpha-Synuclein Is Present in Human Plasma but Not in Cerebrospinal Fluid as Determined by an Ultrasensitive Immunoassay

Frontiers in Neuroscience, 2019
Accumulation and aggregation of misfolded alpha-synuclein is believed to be a cause of Parkinson’s disease (PD). Phosphorylation of alpha-synuclein at S129 is known to be associated with the pathological misfolding process, but efforts to investigate the
Cristina Cariulo, Paola Martufi, Margherita Verani, Lucia Azzollini, Giordana Bruni, Andreas Weiss, Sean M. Deguire, Hilal A. Lashuel, Eugenia Scaricamazza, Giulia Maria Sancesario, Tommaso Schirinzi, Nicola Biagio Mercuri, Nicola Biagio Mercuri, Giuseppe Sancesario, Andrea Caricasole, Lara Petricca   +15 more
doaj   +1 more source

Protein-Protein Interactions in Alpha-Synuclein Biogenesis: New Potential Targets in Parkinson’s Disease

Frontiers in Aging Neuroscience, 2020
Parkinson’s disease (PD) is a debilitating neurodegenerative disorder defined by a loss of dopamine-producing neurons in the substantia nigra in the brain. It is associated with cytosolic inclusions known as Lewy bodies.
Sarah M. Hernandez, Elena B. Tikhonova, Andrey L. Karamyshev   +2 more
doaj   +1 more source

Assessment of the direct and indirect effects of MPP+ and dopamine on the human proteasome: implications for Parkinson's disease aetiology [PDF]

, 2008
Mitochondrial impairment, glutathione depletion and oxidative stress have been implicated in the pathogenesis of Parkinson’s disease (PD), linked recently to proteasomal dysfunction.
Beck, KE, Billett, EE, Caneda-Ferrón, B, Costa, T, De, Girolamo, Layfield, R   +5 more
core   +1 more source

Inhibition of SLC11A1‐Mediated Lysosomal Iron Accumulation in Microglia Promotes Repair Following White Matter Stroke

Advanced Science, EarlyView.
Genetic and pharmacological inhibition of SLC11A1 functioning as an H+/Fe2+ antiporter–mediated lysosomal iron accumulation in microglia promotes lysosomal lumen acidification, increases CTSD expression, enhances lysosomal myelin debris uptake and degradation, and promotes repair following white matter stroke. ABSTRACT White matter stroke (WMS) results
Lingling Qiu, Yajie Zhang, Yushi Tang, Hongli Hu, Ying Zhang, Junwen Xue, Hao Wang, Yecheng Wang, Chunfeng Liu, Jia Jia, Jian Cheng, Yongjun Cao   +11 more
wiley   +1 more source