Results 1 to 10 of about 83,002 (289)

Mannose 6-Phosphate Receptor Is Reduced in -Synuclein Overexpressing Models of Parkinsons Disease [PDF]

PLoS ONE, 2016
Increasing evidence points to defects in autophagy as a common denominator in most neurodegenerative conditions. Progressive functional decline in the autophagy-lysosomal pathway (ALP) occurs with age, and the consequent impairment in protein processing ...
Andresen, Thomas Lars, Dzamko, Nicolas, Halliday, Glenda M., Jensen, Poul Henning, Lassen, Louise B., Madsen, Peder, Matrone, Carmela, Nielsen, Morten S., Nyegaard, Mette, Pohlmann, Regina, Søndergaard, Rikke Vicki   +10 more
core   +18 more sources

Recruitment of Aβ into α‑Synuclein Condensates Catalyzes Primary Nucleation of α‑Synuclein Aggregation [PDF]

ACS Central Science
Owen M. Morris, Alexander Röntgen, Zenon Toprakcioglu, Mariana Cali, Samuel Dada, Michele Vendruscolo   +5 more
doaj   +2 more sources

Resistance to MPTP-neurotoxicity in α-synuclein knockout mice is complemented by human α-synuclein and associated with increased β-synuclein and Akt activation. [PDF]

PLoS ONE, 2011
Genetic and biochemical abnormalities of α-synuclein are associated with the pathogenesis of Parkinson's disease. In the present study we investigated the in vivo interaction of mouse and human α-synuclein with the potent parkinsonian neurotoxin, MPTP ...
Bobby Thomas, Allen S Mandir, Neva West, Ying Liu, Shaida A Andrabi, Wanda Stirling, Valina L Dawson, Ted M Dawson, Michael K Lee   +8 more
doaj   +1 more source

Pathological Relevance of Post-Translationally Modified Alpha-Synuclein (pSer87, pSer129, nTyr39) in Idiopathic Parkinson’s Disease and Multiple System Atrophy

Cells, 2022
Aggregated alpha-synuclein (α-synuclein) is the main component of Lewy bodies (LBs), Lewy neurites (LNs), and glial cytoplasmic inclusions (GCIs), which are pathological hallmarks of idiopathic Parkinson’s disease (IPD) and multiple system atrophy (MSA).
Berkiye Sonustun, Melek Firat Altay, Catherine Strand, Kirsten Ebanks, Geshanthi Hondhamuni, Thomas T. Warner, Hilal A. Lashuel, Rina Bandopadhyay   +7 more
doaj   +1 more source

Central and peripheral α‐synuclein in Parkinson disease detected by seed amplification assay

Annals of Clinical and Translational Neurology, 2023
Objectives Detection of α‐synuclein aggregates by seed amplification is a promising Parkinson disease biomarker assay. Understanding intraindividual relationships of α‐synuclein measures could inform optimal biomarker development.
Lana M. Chahine, Thomas G. Beach, Charles H. Adler, Monica Hepker, Anumantha Kanthasamy, Scott Appel, Sandra Pritzkow, Michelle Pinho, Sherri Mosovsky, Geidy E. Serrano, Christopher Coffey, Michael C. Brumm, Luis M. A. Oliveira, Jamie Eberling, Brit Mollenhauer, For the Systemic Synuclein Sampling Study   +15 more
doaj   +1 more source

Effects of Excess Brain-Derived Human α-Synuclein on Synaptic Vesicle Trafficking

Frontiers in Neuroscience, 2021
α-Synuclein is a presynaptic protein that regulates synaptic vesicle trafficking under physiological conditions. However, in several neurodegenerative diseases, including Parkinson’s disease, dementia with Lewy bodies, and multiple system atrophy, α ...
Cristina Román-Vendrell, Audrey T. Medeiros, John B. Sanderson, Haiyang Jiang, Tim Bartels, Jennifer R. Morgan   +5 more
doaj   +1 more source

Gut mucosal cells transfer α-synuclein to the vagus nerve

JCI Insight, 2023
Epidemiological and histopathological findings have raised the possibility that misfolded α-synuclein protein might spread from the gut to the brain and increase the risk of Parkinson’s disease.
Rashmi Chandra, Arpine Sokratian, Katherine R. Chavez, Stephanie King, Sandip M. Swain, Joshua C. Snyder, Andrew B. West, Rodger A. Liddle   +7 more
doaj   +1 more source

A β-Wrapin Targeting the N-Terminus of α-Synuclein Monomers Reduces Fibril-Induced Aggregation in Neurons

Frontiers in Neuroscience, 2021
Reducing α-synuclein pathology constitutes a plausible strategy against Parkinson’s disease. As we recently demonstrated, the β-wrapin protein AS69 binds an N-terminal region in monomeric α-synuclein, interferes with fibril nucleation, and reduces α ...
Éva M. Szegő, Fabian Boß, Daniel Komnig, Charlott Gärtner, Lennart Höfs, Hamed Shaykhalishahi, Hamed Shaykhalishahi, Michael M. Wördehoff, Theodora Saridaki, Jörg B. Schulz, Jörg B. Schulz, Wolfgang Hoyer, Wolfgang Hoyer, Björn H. Falkenburger, Björn H. Falkenburger, Björn H. Falkenburger, Björn H. Falkenburger   +16 more
doaj   +1 more source

p62/SQSTM1-dependent autophagy of Lewy body-like α-synuclein inclusions. [PDF]

PLoS ONE, 2012
α-Synuclein is the main component of Lewy bodies, the intraneuronal inclusion bodies characteristic of Parkinson's disease. Although α-synuclein accumulation is caused by inhibition of proteasome and autophagy-lysosome, the degradation of α-synuclein ...
Yoshihisa Watanabe, Harutsugu Tatebe, Katsutoshi Taguchi, Yasuhisa Endo, Takahiko Tokuda, Toshiki Mizuno, Masanori Nakagawa, Masaki Tanaka   +7 more
doaj   +1 more source

Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization. [PDF]

PLoS ONE, 2013
Amyloid fibrils of α-synuclein are the main constituent of Lewy bodies deposited in substantial nigra of Parkinson's disease brains. α-Synuclein is an intrinsically disordered protein lacking compact secondary and tertiary structures.
Winny Ariesandi, Chi-Fon Chang, Tseng-Erh Chen, Yun-Ru Chen   +3 more
doaj   +1 more source