Alpha-Synuclein

Name: Alpha-Synuclein
SKU: S-1001-1
Price: 300.00 USD
Availability: InStock

Product background: Alpha-Synuclein (α-Synuclein) is a presynaptic protein found to be a major component of Parkinson’s Disease (PD) aggregates and is implicated in the pathogenesis of PD and related neurodegenerative disorders.

About the product: Expressed recombinantly in E. coli, human Alpha-Synuclein is purified to our highest standards to ensure batch to batch consistency in both purity and quality.

Applications: The Alpha-Synuclein is sold in 20mM Tris, 100mM NaCl, pH 7.4 to ensure a highly monomeric starting material that could be suited to aggregation studies, seeding experiments, molecular standards, and more.

Catalog ID: S-1001-1

$300.00

Download Specs Download Datasheet

Product Details
- Size: 0.5 mg
- Physical State: White lyophilized powder
- Temperature Storage: -20°C
- Temperature Shipping: Ambient
- Sequence:
  MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
- Source: Recombinant. A DNA sequence encoding the human alpha-synuclein (1-140) sequence was expressed in E. coli.
- Purity: >95% by SDS-PAGE and Mass Spec.
- Molecular Mass: 14,460 Da theoretical
References

1. Conway, K., et al., (2000) Biochemistry, 39 : 2552
2. Jakes, R., et al., (1994) FEBS Letters, 345 : 27
3. Masliah, E., et al., (2001) Proc. Natl. Acad. Sci., USA, 98 : 12245
4. Ueda, K., et al., (1993) Proc. Natl. Acad. Sci., USA, 90 : 11282
5. Grozdanov, V., et al., (2019) Ann Neurol, 86(4) : 593-606
Publications

Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein.

Journal of the American Society for Mass Spectrometry; doi: 10.1007/s13361-018-2002-2.

Piriya Wongkongkathep, Jong Yoon Han, Tae Su Choi, Sheng Yin, Hugh I. Kim, Joseph A. Loo

Extending the functional characteristics of naturally occurring autoantibodies against β-Amyloid, Prion Protein and α-Synuclein.

journals.plos.org; https://doi.org/10.1371/journal.pone.0202954.

Albus, A., Gold, M., Bach, J.P., Burg-Roderfield, M., Jordens, M.,…Dodel,R.

The involvement of dityrosine crosslinking in α-synuclein assembly and deposition in Lewy Bodies in Parkinson’s disease

Nature.com Scientific Reports; 10.1038/srep39171.

Youssra K. Al-Hilaly, Luca Biasetti, Ben J. F. Blakeman, Saskia J. Pollack, Shahin Zibaee, Alaa Abdul-Sada, Julian R. Thorpe, Wei-Feng Xue & Louise C. Serpell

Broad neutralization of calcium-permeable amyloid pore channels with a chimeric Alzheimer/Parkinson peptide targeting brain gangliosides.

Science Direct; doi:10.1016/j.bbadis.2015.11.012.

Coralie Di Scala, Nouara Yahia, Alessandra Flores, Sonia Boutemeur, Nazim Kourdougli, Henri Chahinian, Jacques Fantini

NLRP3 Inflammasome Is Expressed and Functional in Mouse Brain Microglia but Not in Astrocytes.

PLOS ONE; DOI: 10.1371/journal.pone.0130624.

Audrey Gustin, Mélanie Kirchmeyer, Eric Koncina, Paul Felten, Sophie Losciuto, Tony Heurtaux, Aubry Tardivel, Paul Heuschling, Catherine Dostert

CSF beta-amyloid 1–42 – what are we measuring in Alzheimer’s disease?

Wiley Online Library; DOI: 10.1002/acn3.160.

William T. Hu, Kelly D. Watts, Leslie M. Shaw, Jennifer C. Howell, John Q. Trojanowski, Sundeep Basra, Jonathan D. Glass, James J. Lah and Allan I. Levey

Reduced Vascular Endothelial Growth Factor and Capillary Density in the Occipital Cortex in Dementia with Lewy Bodies

Brain Pathology; DOI: 10.1111/bpa.12130.

Scott Miners, Hayley Moulding, Rohan de Silva, andSeth Love

α-Synuclein promotes IAPP fibril formation in vitro and β-cell amyloid formation in vivo in mice.

Scientific Reports; https://doi.org/10.1038/s41598-020-77409-z.

Mucibabic,M., Steneberg,P., Lidh, E., Straseviciene,J., Ziolkowska,A., Dahl,U., Lindahl,E., Edlund,H.

Criticality as a measure of developing proteinopathy in engineered human neural networks.

bioRxiv; doi: https://doi.org/10.1101/2020.05.03.074666.

Valderhaug, V., Heiney, K., Ramstad, O., Bråthen, G., Kuan, W., Nichele, S., Sandvig, A., Sandvig, J

Gut Microbiome-Modified Polyphenolic Compounds Inhibit α-Synuclein Seeding and Spreading in α-Synucleinopathies.

Frontiers in Neuroscience; https://doi.org/10.3389/fnins.2020.00398.

Yamasaki,T., Ono, K., Ho,L., Pasinetti, G.,

Antioxidant Nanoparticles for Concerted Inhibition of α-Synuclein Fibrillization, and Attenuation of Microglial Intracellular Aggregation and Activation.

Frontiers Bioengineering and Biotechnology; https://doi.org/10.3389/fbioe.2020.00112.

Zhao, N., Yang, X., Calvelli, H., Cao, Y., Francis, N., Chmielowski, R., Joseph, L., Pang, Z., Uhrich, K., Baum,J., Moghe, P.

RT-QuIC-based detection of alpha-synuclein seeding activity in brains of dementia with Lewy Body patients and of a transgenic mouse model of synucleinopathy.

Prion; doi: 10.1080/19336896.2020.1724608.

Han, J., Jang, H., Green, A., Choi, Y.

Hsc70 Ameliorates the Vesicle Recycling Defects Caused by Excess α-Synuclein at Synapses.

ENEURO; DOI: https://doi.org/10.1523/ENEURO.0448-19.2020.

Banks,S., Medeiros, A., McQuillan, M., Busch, D., Ibarraran-Viniegra, A., Sousa, R., Lafer, E., Morgan, J.,

Effects of single and combined immunotherapy approach targeting amyloid β protein and α-synuclein in a dementia with Lewy bodies-like model..

Alzheimers Dement.; doi: 10.1016/j.jalz.2019.02.002.

Markus Mandler, Edward Rockenstein, Cassia Overk, Michael Mante, Jazmin Florio, Anthony Adame, Changyoun Kim, Radmila Santic, Achim Schneeberger, Frank Mattner, Sabine Schmidhuber, Gergan Galabova, Brian Spencer, Eliezer Masliah, Robert A.Rissman

TREM2 deficiency aggravates α-synuclein–induced neurodegeneration and neuroinflammation in Parkinson’s disease models..

FASEB J.; DOI: 10.1096/fj.201900992R.

Ying Guo, Xinbing Wei, Hua Yan, Yue Qin, Shaoqi Yan, Jia Liu, Yong Zhao, Fan Jiang, and Haiyan Lou

Functionalization of the TMEM175 p.M393T Variant as a risk factor for Parkinson Disease..

Hum Mol Genet.; DOI: 10.1093/hmg/ddz136.

Sarah Jinn, Cornelis Blauwendraat, Dawn Toolan, Cheryl A Gretzula, Robert E Drolet, Sean Smith, Mike A Nalls, Jacob Marcus, Andrew B Singleton, David J Stone

Increased Immune Activation by Pathologic α‐Synuclein in Parkinson’s Disease.

Annals of Neurology; https://doi.org/10.1002/ana.25557.

Veselin Grozdanov, Luc Bousset, Meike Hoffmeister, Corinna Bliederhaeuser, Christoph Meier, Karine Madiona, Laura Pieri, Martin Kiechle, Pamela J. McLean, Jan Kassubek, Christian Behrends, Albert C Ludolph, Jochen H Weishaupt, Ronald Melki, Karin M Danzer

Novel Mannitol-Based Small Molecules for Inhibiting Aggregation of α-Synuclein Amyloids in Parkinson’s Disease.

Frontiers; https://doi.org/10.3389/fmolb.2019.00016.

Ashim Paul, Bo-Dou Zhang, Satabdee Mohapatra, Gao Li, Yan-Mei Li, Ehud azit, and Daniel Segal

Protein Damage in Aging and Age-Related Diseases.

Open Biology; https://doi.org/10.1098/rsob.180249.

Miroslav Radman, Anita Krisko

Alpha-synuclein suppresses mitochondrial protease ClpP to trigger mitochondrial oxidative damage and neurotoxicity.

Springer Berlin Heidelberg; https://doi.org/10.1007/s00401-019-01993-2.

Di Hu, Xiaoyan Sun, Xudong Liao, Xinwen Zhang, Sara Zarabi,..Xin Qi

Heterogeneity in gut microbiota drive polyphenol metabolism that influences α-synuclein misfolding and toxicity.

The Journal of Nutritional Biochemistry; https://doi.org/10.1016/j.jnutbio.2018.10.019.

Lap Ho, Danyue Zhao, Kenjiro Ono, Kai Ruan, Ilaria Mogno, Mayumi Tsuji, Eileen Carry, Justin Brathwaite, Steven Sims, Tal Frolinger, Susan Westfall, Paolo Mazzola, Qingli Wu, Ke Hao, Thomas E. Lloyd, James E. Simon, Jeremiah Faith, Giulio M. Pasinetti

Extracellular Alpha-Synuclein Oligomers Induce Parkin S-Nitrosylation: Relevance to Sporadic Parkinson’s Disease Etiopathology.

Springer; https://doi.org/10.1007/s12035-018-1082-0.

Anna Wilkaniec, Anna M. Lenkiewicz, Grzegorz A. Czapski, Henryk M. Jęśko, Wojciech Hilgier, Robert Brodzik, Magdalena Gąssowska-Dobrowolska, Carsten Culmsee, Agata Adamczyk

Monitoring α-synuclein multimerization in vivo..

FASEB Journal; https://doi.org/10.1096/fj.201800148RRR.

Vibha Prasad, Yasmine Wasser, Friederike Hans, Anand Goswami, Istvan Katona, Tiago F. Outeiro, Philipp J. Kahle, Jörg B. Schulz, and Aaron Voigt

Extending the functional characteristics of naturally occurring autoantibodies against β-Amyloid, Prion Protein and α-Synuclein.

PLOS ONE; https://doi.org/10.1371/journal.pone.0202954.

Alexandra Albus, Maike Gold, Jan-Philipp Bach, Monika Burg-Roderfeld, Marit Jördens, Yvonne Kirchhein, Yannick Kronimus, David Mengel, Inga Zerr, Richard Dodel

α‐Synuclein activates innate immunity but suppresses interferon‐γ expression in murine astrocytes..

Eur J Neurosci.; https://doi.org/10.1111/ejn.13956.

Jintang Wang Zheng Chen Jeremy D. Walston Peisong Gao Maolong Gao Sean X. Leng

Extracellular Alpha-Synuclein Oligomers Induce Parkin S-Nitrosylation: Relevance to Sporadic Parkinson’s Disease Etiopathology.

link.springer.com; 10.1007/s12035-018-1082-0.

Anna Wilkaniec, Anna M. Lenkiewicz, Grzegorz A. Czapski, Henryk M. Jęśko, Wojciech Hilgier, Robert Brodzik, Magdalena Gąssowska-Dobrowolska, Carsten Culmsee, Agata Adamczyk

Integrin CD11b mediates α-synuclein-induced activation of NADPH oxidase through a Rho-dependent pathway.

Science Direct; https://doi.org/10.1016/j.redox.2017.11.010.

Liyan Hou, Xiuqi Bao, Caixia Zang, Hanyu Yang, Fuqiang Sun, Yuning Che, Xuefei Wu, Shao Li, Dan Zhang, Qingshan Wang

Alpha-synuclein alters differently gene expression of Sirts, PARPs and other stress response proteins: implications for neurodegenerative disorders..

link.springer.com; https://doi.org/10.1007/s12035-016-0317-1.

Motyl, J., Wencel, P.L., Cieślik, M. Strosznajder,R.P., Strosznajder,J.B.

Cerebrospinal fluid, plasma, and saliva in the BioFIND study: Relationships among biomarkers and Parkinson’s disease Features..

onlinelibrary.wiley.com; https://doi.org/10.1002/mds.27232.

Goldman, J.G., Andrews, H., Amara, A., Naito, A., Alcalay, R.N.,…Kang, U.K.

Transmission of α-synuclein-containing erythrocyte-derived extracellular vesicles across the blood-brain barrier via adsorptive mediated transcytosis: another mechanism for initiation and progression of Parkinson’s disease?.

actaneurocomms.biomedcentral.com; 10.1186/s40478-017-0470-4.

Junichi Matsumoto, Tessandra Stewart, Lifu Sheng, Na Li, Kristin Bullock, Ning Song, Min Shi, William A Banks, Jing ZhangEmail

Chromatin-Bound Oxidized α-Synuclein Causes Strand Breaks in Neuronal Genomes in in vitro Models of Parkinson’s Disease..

Journal of Alzheimer’s Disease; doi: 10.3233/JAD-170342..

Vasquez Velmarinia, Mitra Joya, Hegde Pavana M., Pandey Arvinda, Sengupta Shiladityaa, Mitra Sankara, Rao K.S., Hegde Muralidhar L

Endothelin‐converting enzymes degrade α‐synuclein and are reduced in dementia with Lewy bodies.

Online Library; https://doi.org/10.1111/jnc.13974.

James Scott Miners; Seth Love

Autoimmune antibody decline in Parkinson’s disease and Multiple System Atrophy; a step towards immunotherapeutic strategies.

BioMedCentral; https://doi.org/10.1186/s13024-017-0187-7.

Tomasz Brudek, Kristian Winge, Jonas Folke, Søren Christensen, Karina Fog, Bente Pakkenberg and Lars Østergaard Pedersen

Recommendations for cerebrospinal fluid collection for the analysis by ELISA of neurogranin trunc P75, α-synuclein, and total tau in combination with Aβ(1–42)/Aβ(1–40)..

Alzheimer’s Research & Therapy; https://doi.org/10.1186/s13195-017-0265-7.

Hugo Vanderstichele, Leentje Demeyer, Shorena Janelidze, Els Coart, Erik Stoops, Kimberley Mauroo, Victor Herbst, Cindy François and Oskar Hansson

P2X7 receptor-pannexin 1 interaction mediates extracellular alpha-synuclein-induced ATP release in neuroblastoma SH-SY5Y cells.

Springer Link Purinergic Signalling; DOI: 10.1007/s11302-017-9567-2.

Anna Wilkaniec, Magdalena Gąssowska, Grzegorz A. Czapski, Magdalena Cieślik, Grzegorz Sulkowski, Agata Adamczyk

An extract of the marine alga Alaria esculenta modulates -synuclein folding and amyloid formation.

Elsevier; http://dx.doi.org/10.1016/j.neulet.2017.02.055.

James C. Giffina, Robert C. Richardsb, Cheryl Craftc, Nusrat Jahanc, 1, Cindy Leggiadrob, Thierry Chopind, Michael Szemerdae, Shawna L. MacKinnonc, K.Vanya Ewart

The involvement of dityrosine crosslinking in synuclein assembly and deposition in Lewy Bodies in Parkinson’s disease..

Scientific Reports; http://doi.org/10.1038/srep39171.

Al-Hilaly, Youssra K and Biasetti, Luca and Blakeman, Ben J F and Pollack, Saskia J and Zibaee, Shahin and Abdul-Sada, Alaa and Thorpe, Julian R and Xue, Wei-Feng and Serpell, Louise C

Anti-Inflammatory and Neuroprotective Effects of PGE2 EP4 Signaling in Models of Parkinson’s Disease..

Journal of Neuroimmune Pharmocology; doi: 10.1007/s11481-016-9713-6..

Suraj S. Pradhan, Kirstie Salinas, Alexis C. Garduno, Jenny U. Johansson, Qian Wang, Amy Manning-Bog

5-HT2A Receptor Binding in the Frontal Cortex of Parkinson’s Disease Patients and Alpha-Synuclein Overexpressing Mice: A Postmortem Study.

Parkinson’s Disease; http://dx.doi.org/10.1155/2016/3682936.

Nadja Bredo Rasmussen, Mikkel Vestergaard Olesen, Tomasz Brudek, Per Plenge, Anders Bue Klein, Jenny E. Westin, Karina Fog, Gitta Wörtwein, Susana Aznar

Protein Kinase Cδ Upregulation in Microglia Drives Neuroinflammatory Responses and Dopaminergic Neurodegeneration in Experimental Models of Parkinson’s Disease.

NCBI; doi: 10.1016/j.nbd.2016.04.008.

Richard Gordon, Neeraj Singh, Vivek Lawana, Anamitra Ghosh, Dilshan S. Harischandra, Huajun Jin, Colleen Hogan, Souvarish Sarkar, Dharmin Rokad, Nikhil Panicker, Vellareddy Anantharam, Anumantha G. Kanthasamy, Arthi Kanthasamy

Identification of a specific α-synuclein peptide (α-Syn 29-40) capable of eliciting microglial superoxide production to damage dopaminergic neurons.

BioMed Central; DOI: 10.1186/s12974-016-0606-7.

Shijun Wang, Chun-Hsien Chu, Mingri Guo, Lulu Jiang, Hui Nie, Wei Zhang, Belinda Wilson, Li Yang, Tessandra Stewart, Jau-Shyong HongEmail author and Jing Zhang

Altered Alpha-Synuclein, Parkin, and Synphilin Isoform Levels in Multiple System Atrophy Brains.

Wiley Online Library; DOI: 10.1111/jnc.13392.

Tomasz Brudek, Kristian Winge, Nadja Bredo Rasmussen, Justyna Maria Bahl Czarna, Julia Tanassi, Tina Klitmøller Agander, Thomas M. Hyde, and Bente Pakkenberg

Glucocerebrosidase deficiency accelerates the accumulation of proteinase K-resistant α-synuclein and aggravates neurodegeneration in a Drosophila model of Parkinson’s disease.

Oxford Journals; doi: 10.1093/hmg/ddv372.

Mari Suzuki, Nobuhiro Fujikake, Toshihide Takeuchi, Ayako Kohyama-Koganeya, Kazuki Nakajima, Yoshio Hirabayashi, Keiji Wada and Yoshitaka Nagai

Generation of human pluripotent stem cell reporter lines for the isolation of and reporting on astrocytes generated from ventral midbrain and ventral spinal cord neural progenitors.

ScienceDirect; doi:10.1016/j.scr.2015.05.014.

Staffan Holmqvista, Marinka Brouwer, Mehdi Djelloul, Alejandro Garcia Diaz, Michael J. Devine, Anna Hammarbergf, Karina Fog, Tilo Kunath, Laurent Roybon

Phenolic compounds prevent the oligomerization of α-synuclein and reduce synaptic toxicity.

JNC Journal of Neurochemistry; DOI: 10.1111/jnc.13180.

Ryoichi Takahashi, Kenjiro Ono, Yusaku Takamura, Mineyuki Mizuguchi, Tokuhei Ikeda, Hisao Nishijo andMasahito Yamada

Accumulation of α-synuclein in dementia with Lewy bodies is associated with decline in the α-synuclein-degrading enzymes kallikrein-6 and calpain-1..

Acta Neuropathol Commun.; doi: 10.1186/s40478-014-0164-0..

Scott Miners, Ruth Renfrew, Marta Swirski, Seth Love

Naturally Occurring Alpha-Synuclein Autoantibodies in Parkinson’s Disease: Sources of (Error) Variance in Biomarker Assays..

PLoS One; https://doi.org/10.1371/journal.pone.0114566.

Sebastian Heinzel , Maike Gold, Christian Deuschle, Felix Bernhard, Walter Maetzler, Daniela Berg, Richard Dodel

Plasma exosomal α-synuclein is likely CNS-derived and increased in Parkinson’s disease..

Acta Neurolpathol.; doi: 10.1007/s00401-014-1314-y.

Min Shi, Changqin Liu, Travis J. Cook, Kristin M. Bullock, Yanchun Zhao, Carmen Ginghina, Yanfei Li, Patrick Aro, Romel Dator, Chunmei He, Michael J. Hipp, Cyrus P. Zabetian, Elaine R. Peskind, Shu-Ching Hu, Joseph F. Quinn, Douglas R. Galasko, William A. Banks, Jing Zhang

Quantitative Measurement of Intact Alpha-Synuclein Proteoforms from Post-Mortem Control and Parkinson’s Disease Brain Tissue by Intact Protein Mass Spectrometry.

Scientific Reports; doi:10.1038/srep05797.

John F. Kellie, Richard E. Higgs, John W. Ryder, Anthony Major, Thomas G. Beach, Charles H. Adler, Kalpana Merchant, & Michael D. Knierman

Multifunctional D2/D3 Agonist D-520 with High in Vivo Efficacy: Modulator of Toxicity of Alpha-Synuclein Aggregates.

ACS Publications; DOI: 10.1021/cn500084x.

Gyan Modi, Chandrashekhar Voshavar, Sanjib Gogoi, Mrudang Shah, Tamara Antonio, Maarten E. A. Reith, and Aloke K. Dutta

Aldehyde dehydrogenase 1 defines and protects a nigrostriatal dopaminergic neuron subpopulation.

JCI: The Journal of Clinical Investigation; doi:10.1172/JCI72176..

Guoxiang Liu, Jia Yu, Jinhui Ding, Chengsong Xie, Lixin Sun, Iakov Rudenko, Wang Zheng, Namratha Sastry, Jing Luo, Gay Rudow, Juan C. Troncoso, and Huaibin Cai

Extracellular α-Synuclein Leads to Microtubule Destabilization via GSK-3β-Dependent Tau Phosphorylation in PC12 Cells.

PLOS One; DOI: 10.1371/journal.pone.0094259.

Magdalena Gąssowska, Grzegorz A. Czapski, Beata Pająk, Magdalena Cieślik, Anna M. Lenkiewicz, Agata Adamczyk

Molecular Basis for Preventing α-Synuclein Aggregation by a Molecular Tweezer.

The Journal of Biological Chemistry; doi: 10.1074/jbc.M113.524520.

Srabasti Acharya, Brian M. Safaie, Piriya Wongkongkathep, Magdalena I. Ivanova, Aida Attar, Frank-Gerrit Klärner, Thomas Schrader, Joseph A. Loo, Gal Bitan, and Lisa J. Lapidus

Reduced vascular endothelial growth factor and capillary density in the occipital cortex in dementia with Lewy bodies.

DOI: 10.1111/bpa.12130; Accepted manuscript online: 13 FEB 2014 01:41AM EST Manuscript Accepted: 2 FEB 2014.

Scott Miners, Hayley Moulding, Rohan de Silva, Seth Love

Alpha-Synuclein Aggregates Activate the Nlrp3Inflammasome Following Vesicle Rupture.

Loyola eCommons;. Master’s Theses. Paper 1859.

Rudy Orlando Cedillos

Extracellular alpha-synuclein induces calpain-dependent overactivation of cyclin-dependent kinase 5 in vitro.

Elsevier B.V.; http://dx.doi.org/10.1016/j.febslet.2013.07.053 (Pay to view).

Grzegorz A. Czapski, Magdalena Gąssowska, Anna Wilkaniec, Magdalena Cieślik, and Agata Adamczyk

Alpha-Synuclein Induces Lysosomal Rupture and Cathepsin Dependent Reactive Oxygen Species Following Endocytosis.

PLOS One; DOI: 10.1371/journal.pone.0062143.

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

Inflammation induces multinucleation of Microglia via PKC inhibition of cytokinesis, generating highly phagocytic multinucleated giant cells.

J Neurochem.; doi: 10.1111/jnc.12477.

Tamara C. Hornik, Urte Neniskyte, Guy C. BrownInf

Methamphetamine binds to α-synuclein and causes a conformational change which can be detected by nanopore analysis.

FEBS Letters; In Press, Uncorrected proof (5 July 2012), doi:10.1016/j.febslet.2012.06.040.

Tavassoly, O., Lee, J.S.

A Novel “Molecular Tweezer” Inhibitor of α-Synuclein Neurotoxicity in Vitro and in Vivo.

Neurotherapeutics; Volume 9, Number 2, 464-476, DOI: 10.1007/s13311-012-0105-1.

Prabhudesai, S., Sinha, S., Attar, A., Kotagiri, A., Fitzmaurice, AG, Lakshmanan, R., Ivanova, MI, Loo, JA, Klärner, FG and Schrader, T., et al.

New evidence on α-synuclein and Tau binding to conformation and sequence specific GC* rich DNA: Relevance to neurological disorders.

J Pharm Bioallied Sci.; 2012 Apr-Jun; 4(2): 112–117. doi: 10.4103/0975-7406.9481; PMCID: PMC3341714.

Vasudevaraju, P., Guerrero, E., Hegde, ML, Collen, TB, Britton, GB, and Rao, KS

α-Synuclein oligomers oppose long-term potentiation and impair memory through a calcineurin-dependent mechanism: relevance to human synucleopathic diseases..

Journal of Neurochemistry; 120: 440–452. 2012 Feb; doi: 10.1111/j.1471-4159.2011.07576.x.

Martin, Z. S., Neugebauer, V., Dineley, K. T., Kayed, R., Zhang, W., Reese, L. C. and Taglialatela, G.,

α-Synuclein potentiates interleukin-1β-induced CXCL10 expression in human A172 astrocytoma cells.

Neuroscience Letters; Volume 507, Issue 2, 24 January 2012, Pages 133–136 DOI /10.1016/j.neulet.2011.12.001.

Tousi, A.S., Buck, D.J., Curtis, T., Davis, R.L.

The acute inflammatory response to intranigral a-synuclein differs significantly from intranigral lipopolysaccharide and is exacerbated by peripheral inflammation.

Journal of Neuroinflammation; 2011, 8:166.

Couch, Y, Alvarez-Erviti, L., Sibson, NR, Wood, M and Anthony, D.

The fusogenic tilted peptide (67–78) of α-synuclein is a cholesterol binding domain.

Biochimica et Biophysica Acta (BBA) – Biomembranes; Volume 1808, Issue 10, 2011 October, Pages 2343–2351.

Fantini, J., Carlus, D., Yahi, N.

Role of Matrix Metalloproteinase 3-mediated α-Synuclein Cleavage in Dopaminergic Cell Death.

J Biol Chem.; 2011 Apr 22;286(16):14168-77. Epub 2011 Feb 17..

Choi DH, Kim YJ, Kim YG, Joh TH, Beal MF, Kim YS.

Single Vesicle Observations of the Cardiolipin−Cytochrome c Interaction: Induction of Membrane Morphology Changes.

Langmuir; 2011 April 19, 27 (10), pp 6107–6115 DOI: 10.1021/la104924c.

Beales, PA, Bergstrom, CL, Geerts, N., Groves, JT, and Vanderlick, K.

Ubiquitinylation of α-Synuclein by Carboxyl Terminus Hsp70-Interacting Protein (CHIP) Is Regulated by Bcl-2-Associated Athanogene 5 (BAG5).

PLoS ONE; 6(2): e14695. 2011 Feb 16; doi:10.1371/journal.pone.0014695.

Kalia LV, Kalia SK, Chau H, Lozano AM, Hyman BT, et al.

SNCA variant associated with Parkinson disease and plasma alpha-synuclein level.

Arch Neurol; 2010 Nov; 67 (11) :1350-6. PubMed PMID:21060011; PubMed Central PMCID: PMC3010848..

Mata IF, Shi M, Agarwal P, Chung KA, Edwards KL, Factor SA, Galasko DR, Ginghina C, Griffith A, Higgins DS, Kay DM, Kim H, Leverenz JB, Quinn JF, Roberts JW, Samii A, Snapinn KW, Tsuang DW, Yearout D, Zhang J, Payami H, Zabetian CP.

On-line bioaffinity-electrospray mass spectrometry for simultaneous detection, identification, and quantification of protein-ligand interactions.

J Am Soc Mass Spectrom; 2010 Oct; 21 (10) :1643-8. PubMed PMID:20692851..

Dragusanu M, Petre BA, Slamnoiu S, Vlad C, Tu T, Przybylski M.

Specific antibodies to soluble alpha-synuclein conformations in intravenous immunoglobulin preparations.

Clinical & Experimental Immunology; Volume 161, Issue 3, pages 527–535, September 2010 DOI: 10.1111/j.1365-2249.2010.04214.x.

Patrias L. M., Klaver A. C., Coffey M.P., Loeffler D.A.

Alpha-synuclein activates microglia by inducing the expressions of matrix metalloproteinases and the subsequent activation of protease-activated receptor-1.

J Immunol; 2010 Jul 1; 185 (1) :615-23. PubMed PMID:20511551..

Lee EJ, Woo MS, Moon PG, Baek MC, Choi IY, Kim WK, Junn E, Kim HS.

DJ-1 and α-synuclein in human cerebrospinal fluid as biomarkers of Parkinson’s disease.

Brain; 133 (3): 713-726. doi: 10.1093/brain/awq008.

Hong, Z., Shi, M., Chung, K.A., Quinn, J.F., Peskind, E.R., Galasko, D., Jankovic, J., Zabetian, C.P., Leverenz, J.B., Baird, G., Montine, T.J., Hancock, A.M., Hwang, H., Pan, C., Bradner, J., Kang, U.J., Jensen, P.H., Zhang, J.

Alpha-synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells.

Int J Biochem Cell Biol; 2009 Oct;41(10):2015-24. Epub 2009 May 19. PubMed PMID: 19460457..

Parihar MS, Parihar A, Fujita M, Hashimoto M, Ghafourifar P.

Potential role of alpha-synuclein and metallothionein in lead-induced inclusion body formation.

Toxicol Sci; 2009 Sep;111(1):100-8. Epub 2009 Jun 19. PubMed PMID: 19542206; PubMed Central PMCID: PMC2726298..

Zuo P, Qu W, Cooper RN, Goyer RA, Diwan BA, Waalkes MP.

Charge State Dependent Fragmentation of Gaseous alpha-Synuclein Cations via Ion Trap and Beam-Type Collisional Activation.

Int J Mass Spectrom; 2009 Jun 1;283(1-3):9-16. PubMed PMID: 20160958; PubMed Central PMCID: PMC2759116..

Chanthamontri C, Liu J, McLuckey SA.

Alpha-synuclein inhibits poly (ADP-ribose) polymerase-1 (PARP-1) activity via NO-dependent pathway..

Folia Neuropathol; 2009;47(3):247-51. PubMed PMID: 19813144..

Adamczyk A, Kamierczak A.

Protein–Metal Interactions of Calmodulin and α-Synuclein Monitored by Selective Noncovalent Adduct Protein Probing Mass Spectrometry.

Journal of the American Society for Mass Spectrometry; 19(11): 1663-1672..

Lya, T., Julian, R.R.

The effect of α-synuclein on phospholipid vesicle integrity: a study using 31P NMR and electron mircroscopy.

Moleculalr Membrane Biology; Vol. 25, No.6-7, Pages 518-527 DOI abs/10.1080/09687680802467977.

Madine, J., Hughes, E., Doig, AJ., Middleton, DA.

Length Requirements for Membrane Fusion of Influenza Virus Hemagglutinin Peptide Linkers to Transmembrane or Fusion Peptide Domains {triangledown}.

Journal of Virology; 82(13): 6337-6348..

Li, Z.N., Lee, B.J., Langley, W.A., Bradley, K.C., Russell, R.J., Steinhauer, D.A.

Mitochondrial association of alpha-synuclein causes oxidative stress.

Journal of the Cellular and Molecular Life Sciences; 65(7-8): 1272-1284..

Parihar, M.S., Parihar, A.,Fujita, M., Hashimoto, M., Ghafourifar, P.

A more efficient enzyme-linked immunosorbent assay for measurement of α-synuclein in cerebrospinal fluid.

Journal of Neuroscience Methods; 168(1): 182-185..

Wieneke J.A., Abdo, W.F., Melis, R., Williams, S., Bloem, B.R., Verbeek, M.M.

Interactive sequences in the molecular chaperone, human αB crystallin modulate the fibrillation of amyloidogenic proteins.

The International Journal of Biochemistry & Cell Biology; 40(5): 954-967..

Ghosha, J.G., Houcka, S.A., Clarka, J.I.

Local and Nonlocal Environments around Cis Peptides.

J. Proteome Res; 7(01): 145-153..

Wathen, B., Jia, Z.

Alpha-Synuclein

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