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Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
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Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

Li, Binsen ; Ge, Peng ; Murray, Kevin A ; Sheth, Phorum ; Zhang, Meng ; Nair, Gayatri ; Sawaya, Michael R ; Shin, Woo Shik ; Boyer, David R ; Ye, Shulin ; Eisenberg, David S ; Zhou, Z Hong ; Jiang, Lin

Nature communications, 2018-09, Vol.9 (1), p.3609-10, Article 3609 [Periódico revisado por pares]

England: Nature Publishing Group

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2
Alpha-Synuclein as a Biomarker for Parkinson's Disease
Alpha-Synuclein as a Biomarker for Parkinson's Disease
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Alpha-Synuclein as a Biomarker for Parkinson's Disease

Atik, Anzari ; Stewart, Tessandra ; Zhang, Jing

Brain pathology (Zurich, Switzerland), 2016-05, Vol.26 (3), p.410-418 [Periódico revisado por pares]

Switzerland: Blackwell Publishing Ltd

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3
Structural and functional characterization of two alpha-synuclein strains
Structural and functional characterization of two alpha-synuclein strains
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Structural and functional characterization of two alpha-synuclein strains

Bousset, Luc ; Pieri, Laura ; Ruiz-Arlandis, Gemma ; Gath, Julia ; Jensen, Poul Henning ; Habenstein, Birgit ; Madiona, Karine ; Olieric, Vincent ; Böckmann, Anja ; Meier, Beat H ; Melki, Ronald

Nature communications, 2013-10, Vol.4 (1), p.2575-2575, Article 2575 [Periódico revisado por pares]

England: Nature Publishing Group

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4
α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, and Escherichia coli Exists Predominantly as Disordered Monomer
α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, and Escherichia coli Exists Predominantly as Disordered Monomer
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α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, and Escherichia coli Exists Predominantly as Disordered Monomer

Fauvet, Bruno ; Mbefo, Martial K. ; Fares, Mohamed-Bilal ; Desobry, Carole ; Michael, Sarah ; Ardah, Mustafa T. ; Tsika, Elpida ; Coune, Philippe ; Prudent, Michel ; Lion, Niels ; Eliezer, David ; Moore, Darren J. ; Schneider, Bernard ; Aebischer, Patrick ; El-Agnaf, Omar M. ; Masliah, Eliezer ; Lashuel, Hilal A.

The Journal of biological chemistry, 2012-05, Vol.287 (19), p.15345-15364 [Periódico revisado por pares]

United States: Elsevier Inc

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5
Alpha synuclein, the culprit in Parkinson disease, is required for normal immune function
Alpha synuclein, the culprit in Parkinson disease, is required for normal immune function
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Alpha synuclein, the culprit in Parkinson disease, is required for normal immune function

Alam, Md Masud ; Yang, De ; Li, Xiao-Qing ; Liu, Jia ; Back, Timothy Carrel ; Trivett, Anna ; Karim, Baktiar ; Barbut, Denise ; Zasloff, Michael ; Oppenheim, Joost J.

Cell reports (Cambridge), 2022-01, Vol.38 (2), p.110090-110090, Article 110090 [Periódico revisado por pares]

United States: Elsevier Inc

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6
Structural basis of synaptic vesicle assembly promoted by α-synuclein
Structural basis of synaptic vesicle assembly promoted by α-synuclein
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Structural basis of synaptic vesicle assembly promoted by α-synuclein

Fusco, Giuliana ; Pape, Tillmann ; Stephens, Amberley D ; Mahou, Pierre ; Costa, Ana Rita ; Kaminski, Clemens F ; Kaminski Schierle, Gabriele S ; Vendruscolo, Michele ; Veglia, Gianluigi ; Dobson, Christopher M ; De Simone, Alfonso

Nature communications, 2016-09, Vol.7 (1), p.12563-12563, Article 12563 [Periódico revisado por pares]

England: Nature Publishing Group

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7
Phosphorylation of Ser-129 Is the Dominant Pathological Modification of α-Synuclein in Familial and Sporadic Lewy Body Disease
Phosphorylation of Ser-129 Is the Dominant Pathological Modification of α-Synuclein in Familial and Sporadic Lewy Body Disease
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Phosphorylation of Ser-129 Is the Dominant Pathological Modification of α-Synuclein in Familial and Sporadic Lewy Body Disease

Anderson, John P. ; Walker, Donald E. ; Goldstein, Jason M. ; de Laat, Rian ; Banducci, Kelly ; Caccavello, Russell J. ; Barbour, Robin ; Huang, Jiping ; Kling, Kristin ; Lee, Michael ; Diep, Linnea ; Keim, Pamela S. ; Shen, Xiaofeng ; Chataway, Tim ; Schlossmacher, Michael G. ; Seubert, Peter ; Schenk, Dale ; Sinha, Sukanto ; Gai, Wei Ping ; Chilcote, Tamie J.

The Journal of biological chemistry, 2006-10, Vol.281 (40), p.29739-29752 [Periódico revisado por pares]

United States: Elsevier Inc

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8
C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction
C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction
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C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction

Lautenschläger, Janin ; Stephens, Amberley D ; Fusco, Giuliana ; Ströhl, Florian ; Curry, Nathan ; Zacharopoulou, Maria ; Michel, Claire H ; Laine, Romain ; Nespovitaya, Nadezhda ; Fantham, Marcus ; Pinotsi, Dorothea ; Zago, Wagner ; Fraser, Paul ; Tandon, Anurag ; St George-Hyslop, Peter ; Rees, Eric ; Phillips, Jonathan J ; De Simone, Alfonso ; Kaminski, Clemens F ; Schierle, Gabriele S Kaminski

Nature communications, 2018-02, Vol.9 (1), p.712-13, Article 712 [Periódico revisado por pares]

England: Nature Publishing Group

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9
Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies
Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies
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Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies

Karpowicz, Richard J. ; Haney, Conor M. ; Mihaila, Tiberiu S. ; Sandler, Raizel M. ; Petersson, E. James ; Lee, Virginia M.-Y.

The Journal of biological chemistry, 2017-08, Vol.292 (32), p.13482-13497 [Periódico revisado por pares]

United States: Elsevier Inc

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10
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
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Alpha-synuclein induces lysosomal rupture and cathepsin dependent reactive oxygen species following endocytosis

Freeman, David ; Cedillos, Rudy ; Choyke, Samantha ; Lukic, Zana ; McGuire, Kathleen ; Marvin, Shauna ; Burrage, Andrew M ; Sudholt, Stacey ; Rana, Ajay ; O'Connor, Christopher ; Wiethoff, Christopher M ; Campbell, Edward M Kahle, Philipp J.

PloS one, 2013-04, Vol.8 (4), p.e62143-e62143 [Periódico revisado por pares]

United States: Public Library of Science

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