Results 311 to 320 of about 68,100 (329)

Dimerization of Tyr136Cys alpha-synuclein prevents amyloid transformation of wild type alpha-synuclein

International Journal of Biological Macromolecules, 2017
Expression of human alpha-synuclein in E. coli cells is known to result in a mixture of the wild type alpha-synuclein and the protein containing Tyr136Cys substitution due to the translational error. The amount of Cys136 alpha-synuclein (Cys136-AS) may reach approximately 50% of the recombinant protein.
K V, Barinova, M L, Kuravsky, A M, Arutyunyan, M V, Serebryakova, E V, Schmalhausen, V I, Muronetz   +5 more
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Agrin binds alpha-synuclein and modulates alpha-synuclein fibrillation.

Glycobiology, 2006
Recent studies have begun to investigate the role of agrin in brain and suggest that agrin's function likely extends beyond that of a synaptogenic protein. Particularly, it has been shown that agrin is associated with the pathological lesions of Alzheimer's disease (AD) and may contribute to the formation of beta-amyloid (Abeta) plaques in AD.
I-Hsuan, Liu, Vladimir N, Uversky, Larissa A, Munishkina, Anthony L, Fink, Willi, Halfter, Gregory J, Cole   +5 more
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Ubiquitination of alpha-synuclein.

Biochemistry, 2005
Filamentous alpha-synuclein depositions are the defining hallmarks of a subset of neurodegenerative diseases including Parkinson's disease (PD), dementia with Lewy bodies, and multiple system atrophy. We previously reported that alpha-synuclein in those brains are extensively phosphorylated at Ser129 [Fujiwara et al. (2002) Nat. Cell Biol.
Takashi, Nonaka, Takeshi, Iwatsubo, Masato, Hasegawa   +2 more
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Alpha-synuclein aggregation.

Protein and peptide letters, 2004
Alpha-synuclein is a major component of Lewy bodies in Parkinson's disease and is found associated with several other forms of dementia. As with other neurodegenerative diseases, the ability of alpha-synuclein to aggregate and form fibrillar deposits seems central to its pathology.
Bodles, A.M., Irvine, Brent
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Alpha-synuclein and neurodegenerative diseases

Nature Reviews Neuroscience, 2001
In recent years, two developments have imparted a new direction to research on the aetiology and pathogenesis of Parkinson's disease. First, the discovery that a missense mutation in the α-synuclein gene is a rare genetic cause of Parkinson's disease.
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Alpha-Synuclein

Journal of the Neurological Sciences, 2017
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Alpha-synuclein overexpression model.

Journal of neural transmission. Supplementum, 2006
To elucidate the role of alpha-synuclein in the pathogenesis of Parkinson's disease (PD), both human alpha-synuclein transgenic mice and targeted overexpression of human alpha-synuclein in rat substantia nigra (SN) by viral vector-based methods have been studied, however little is known about the pathogenetic changes of dopaminergic neuron loss ...
H, Mochizuki, M, Yamada, Y, Mizuno
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Neurobiology of alpha-synuclein.

Molecular neurobiology, 2004
Alpha-synuclein is an abundant neuronal protein that has been linked both to normal synaptic function and to neurodegeneration. Most significantly, mutations in the gene encoding for alpha-synuclein are responsible for Parkinson's disease (PD) in rare familial cases, and the aggregated protein is a major component of Lewy bodies found in sporadic PD ...
Kostas, Vekrellis, Hardy J, Rideout, Leonidas, Stefanis   +2 more
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Deamidation of alpha-synuclein.

Protein science : a publication of the Protein Society, 2009
The rates of deamidation of alpha-synuclein and single Asn residues in 13 Asn-sequence mutants have been measured for 5 x 10(-5)M protein in both the absence and presence of 10(-2)M sodium dodecyl sulfate (SDS). In the course of these experiments, 370 quantitative protein deamidation measurements were performed and 37 deamidation rates were determined ...
Noah E, Robinson, Matthew L, Robinson, Stephanie E S, Schulze, Bert T, Lai, Harry B, Gray   +4 more
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Beta-synuclein modulates alpha-synuclein neurotoxicity by reducing alpha-synuclein protein expression.

Human molecular genetics, 2006
Parkinson's disease (PD) is a neurodegenerative disorder characterized by fibrillar aggregates of alpha-synuclein in characteristic inclusions known as "Lewy bodies". As mutations altering alpha-synuclein structure or increasing alpha-synuclein expression level can cause familial forms of PD or related Lewy body disorders, alpha-synuclein is believed ...
Yuxin, Fan, Pornprot, Limprasert, Ian V J, Murray, Annette C, Smith, Virginia M-Y, Lee, John Q, Trojanowski, Bryce L, Sopher, Albert R, La Spada   +7 more
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