The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly
Open accessAbstract
Neuronal and oligodendrocytic aggregates of fibrillar alpha-synuclein define several diseases of the nervous system. It is likely that these inclusions impair vital metabolic processes and compromise viability of affected cells. Here, we report that a 12-amino acid stretch ((71)VTGVTAVAQKTV(82)) in the middle of the hydrophobic domain of human alpha-synuclein is necessary and sufficient for its fibrillization based on the following observations: 1) human beta-synuclein is highly homologous to alpha-synuclein but lacks these 12 residues, and it does not assemble into filaments in vitro; 2) the rate of alpha-synuclein polymerization in vitro decreases after the introduction of a single charged amino acid within these 12 residues, and a deletion within this region abrogates assembly; 3) this stretch of 12 amino acids appears to form the core of alpha-synuclein filaments, because it is resistant to proteolytic digestion in alpha-synuclein filaments; and 4) synthetic peptides corresponding to this 12-amino acid stretch self-polymerize to form filaments, and these peptides promote fibrillization of full-length human alpha-synuclein in vitro. Thus, we have identified key sequence elements necessary for the assembly of human alpha-synuclein into filaments, and these elements may be exploited as targets for the design of drugs that inhibit alpha-synuclein fibrillization and might arrest disease progression.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Introducing hydrophilic point mutations within the NAC significantly reduces the oligomerization and fibrillation potential of αSyn”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [116]
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Self-citationSpillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868
(1998) · Europe PMC (PubMed Central) · Cited by 1,594
Self-citationConway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,520
Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.
Uéda, K., Fukushima, H., Masliah, E., Xia, Y., Iwai, A., Yoshimoto, M., Otero, D. A., Kondo, J. D. M., Ihara, Y., & Saitoh, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11282 · Cited by 1,469
Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T. (1995) · Neuron · doi:10.1016/0896-6273(95)90302-x · Cited by 1,316
Identification of two distinct synucleins from human brain
Jakes, R., Spillantini, M. G., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00395-5 · Cited by 1,080
Spillantini, M. G., Crowther, R. A., Jakes, R., Cairns, N. J., Lantos, P. L., & Goedert, M. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00504-7 · Cited by 1,052
George, J. M., Jin, H., Woods, W. S., & Clayton, D. F. (1995) · Neuron · doi:10.1016/0896-6273(95)90040-3 · Cited by 844
Flagged first, then by citations
Research works printed but not linked: 3
- Baba, 1998, Am. J. Pathol., 152, 879
- Takeda, 1998, Am. J. Pathol., 152, 367
- Masliah, 1996, Am. J. Pathol., 148, 201
Cited by
Sorted by citations
Items 501–600 of 1,000
Ray, C., & Akhremitchev, B. B. (2005) · Journal of the American Chemical Society · doi:10.1021/ja052932e · Cited by 34
α-Synuclein-mediated neurodegeneration in Dementia with Lewy bodies: the pathobiology of a paradox
Simon, C. A., Soga, T., Okano, H. J., & Parhar, I. S. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00709-y · Cited by 35
Autophagy in α-Synucleinopathies—An Overstrained System
Fellner, L., Gabassi, E., Haybaeck, J., & Edenhofer, F. (2021) · Cells · doi:10.3390/cells10113143 · Cited by 36
Immunolocalization of alpha-synuclein in the rat spinal cord by two novel monoclonal antibodies
Vivacqua, G., Yin, J.-J., Casini, A., Li, X., Li, Y.-H., D’Este, L., Chan, P., Renda, T. G., & Yu, S. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.12.001 · Cited by 33
Impairment of microtubule system increases α-synuclein aggregation and toxicity
Kim, M., Jung, W.-S., Lee, I., Bhak, G., Paik, S. R., & Hahn, J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.11.020 · Cited by 33
Masliah, E., & Hashimoto, M. (2002) · NeuroToxicology · doi:10.1016/s0161-813x(02)00029-3 · Cited by 33
Taking a Bite Out of Amyloid: Mechanistic Insights into α-Synuclein Degradation by Cathepsin L
McGlinchey, R. P., Dominah, G. A., & Lee, J. C. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00360 · Cited by 33
Rutherford, N. J., Dhillon, J.-K. S., Riffe, C. J., Howard, J. K., Brooks, M., & Giasson, B. I. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx371 · Cited by 33
Self-citationThe Appendix in Parkinson’s Disease: From Vestigial Remnant to Vital Organ?
Killinger, B. A., & Labrie, V. (2019) · Journal of Parkinson s Disease · doi:10.3233/jpd-191703 · Cited by 36
Anderson, E. N., Hirpa, D., Zheng, K. H., Banerjee, R., & Gunawardena, S. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00540 · Cited by 32
A unifying framework for amyloid-mediated membrane damage: The lipid-chaperone hypothesis
Tempra, C., Scollo, F., Pannuzzo, M., Lolicato, F., & Rosa, C. L. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2022.140767 · Cited by 32
Truncation or proteolysis of α-synuclein in Parkinsonism
Suthar, S. K., & Lee, S. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101978 · Cited by 34
Jose, J. C., Chatterjee, P., & Sengupta, N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106883 · Cited by 32
Shigemitsu, Y., & Hiroaki, H. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx056 · Cited by 34
Chiti, F. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_3 · Cited by 33
McLean, P. J., & Hyman, B. T. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00154-4 · Cited by 32
β‐Synuclein exhibits chaperone activity more efficiently than α‐synuclein
Lee, D., Paik, S. R., & Choi, K. Y. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.08.075 · Cited by 32
α-Synuclein: Experimental PathologyPreprint
Hasegawa, M., Nonaka, T., & Masuda‐Suzukake, M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024273 · Cited by 33
Siwecka, N., Saramowicz, K., Galita, G., Rozpędek‐Kamińska, W., & Majsterek, I. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15082051 · Cited by 33
Chen, S., Puri, A., Bell, B., Fritsche, J., Palacios, H. H., Balch, M., Sprunger, M. L., Howard, M. K., Ryan, J. J., Haines, J. N., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46538-8 · Cited by 32
Familial Mutations May Switch Conformational Preferences in α-Synuclein Fibrils
Xu, L., Ma, B., Nussinov, R., & Thompson, D. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00406 · Cited by 31
Crosstalk between presynaptic trafficking and autophagy in Parkinson's disease
Pan, P., Zhu, Y., Shen, Y., & Yue, Z. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.04.020 · Cited by 33
Late-stage peptide and protein modifications through phospha-Michael addition reaction
He, P., Chen, H., Hu, H., Hu, J., Lim, Y., & Li, Y. (2020) · Chemical Communications · doi:10.1039/d0cc04969g · Cited by 31
A SUMO1-Derived Peptide Targeting SUMO-Interacting Motif Inhibits α-Synuclein Aggregation
Liang, Z., Chan, H. Y. E., Lee, M. M., & Chan, M. K. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2020.12.010 · Cited by 31
A glutaminyl cyclase-catalyzed α-synuclein modification identified in human synucleinopathies
Hartlage‐Rübsamen, M., Bluhm, A., Moceri, S., Machner, L., Köppen, J., Schenk, M., Hilbrich, I., Holzer, M., Weidenfeller, M., Richter, F., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02349-5 · Cited by 31
Parkinson's disease as a member of Prion-like disorders
Herva, M. E., & Spillantini, M. G. (2014) · Virus Research · doi:10.1016/j.virusres.2014.10.016 · Cited by 33
Fiske, M., Valtierra, S., Solvang, K., Zorniak, M., White, M., Herrera, S., Konnikova, A., Brezinsky, R., & DebBurman, S. K. (2011) · Parkinson s Disease · doi:10.4061/2011/392180 · Cited by 32
Developing intrabodies for the therapeutic suppression of neurodegenerative pathology
Messer, A. C., Lynch, S. M., & Butler, D. C. (2009) · Expert Opinion on Biological Therapy · doi:10.1517/14712590903176387 · Cited by 32
Crowet, J., Lins, L., Dupiereux-Fettweis, I., Elmoualija, B., Lorin, A., Charloteaux, B., Stroobant, V., Heinen, E., & Brasseur, R. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21483 · Cited by 30
Hydralazine Modifies Aβ Fibril Formation and Prevents Modification by Lipids in Vitro
Maheshwari, M., Roberts, J. K., DeSutter, B., Duong, K. T., Tingling, J. D., Fawver, J. N., Schall, H. E., Kahle, M., & Murray, I. V. J. (2010) · Biochemistry · doi:10.1021/bi101249p · Cited by 32
Self-citationMorgan, S., Lavenir, I., Fan, J., Masuda‐Suzukake, M., Passarella, D., Deture, M. A., Dickson, D. W., Ghetti, B. F., & Goedert, M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012179 · Cited by 31
α-Synuclein Aggregation and Modulating Factors
Paleologou, K. E., & El‐Agnaf, O. M. A. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5416-4_6 · Cited by 33
Makwana, P. K., Jethva, P. N., & Roy, I. (2011) · The Analyst · doi:10.1039/c0an00829j · Cited by 32
Zeng, H., Liu, Y., Liu, X., Li, J., Lu, L., Cheng, X., Wu, X., Zhang, X., Zheng, Z., & Lu, G. (2024) · Inflammation · doi:10.1007/s10753-024-02156-6 · Cited by 31
Dopamine promotes the neurodegenerative potential of β‐synuclein
Raina, A., Leite, K., Darvas, S. G., Mahajani, S. U., Chakrabarti, K. S., Voll, D., Becker, S., Griesinger, C., Bähr, M., & Kügler, S. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15134 · Cited by 29
Unraveling the NaCl Concentration Effect on the First Stages of α-Synuclein Aggregation
Ramis, R., Ortega‐Castro, J., Vilanova, B., Adrover, M., & Frau, J. (2020) · Biomacromolecules · doi:10.1021/acs.biomac.0c01292 · Cited by 30
Collusion of α-Synuclein and Aβ aggravating co-morbidities in a novel prion-type mouse model
Lloyd, G. M., Dhillon, J.-K. S., Gorion, K.-M. M., Riffe, C. J., Fromholt, S., Xia, Y., Giasson, B. I., & Borchelt, D. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00486-9 · Cited by 29
Self-citationThe amyloid state of proteins: A boon or bane?
Hassan, M. N., Nabi, F., Khan, A. N., Hussain, M. S., Siddiqui, W. A., Uversky, V. N., & Khan, R. H. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.01.115 · Cited by 30
The Role of NEDD4 E3 Ubiquitin–Protein Ligases in Parkinson’s Disease
Conway, J. A., Kinsman, G., & Kramer, E. R. (2022) · Genes · doi:10.3390/genes13030513 · Cited by 30
Sivakumar, P., Nagashanmugam, K. B., Priyatharshni, S., Lavanya, R., Prabhu, N., & Ponnusamy, S. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105461 · Cited by 29
Suk, J.-E., Lokappa, S. B., & Ulmer, T. S. (2010) · Biochemistry · doi:10.1021/bi901753h · Cited by 29
Kamiyoshihara, T., Kojima, M., Uéda, K., Tashiro, M., & Shimotakahara, S. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.01.162 · Cited by 29
Structural Role of Compensatory Amino Acid Replacements in the α-Synuclein Protein
Losasso, V., Pietropaolo, A., Claudio Zannoni, A., Gustincich, S., & Carloni, P. (2011) · Biochemistry · doi:10.1021/bi2007564 · Cited by 29
Membrane-Bound Alpha Synuclein Clusters Induce Impaired Lipid Diffusion and Increased Lipid Packing
Iyer, A., Schilderink, N., Claessens, M. M. A. E., & Subramaniam, V. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.10.016 · Cited by 29
Xu, L., Bhattacharya, S., & Thompson, D. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp08321a · Cited by 29
Mechanistic Insights into Polyphenols’ Aggregation Inhibition of α-Synuclein and Related Peptides
Martins, G. F., Nascimento, C., & Galamba, N. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00162 · Cited by 28
Synaptic sabotage: How Tau and α-Synuclein undermine synaptic health
Uytterhoeven, V., Verstreken, P., & Nachman, E. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202409104 · Cited by 29
Saffari, B., & Amininasab, M. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00379 · Cited by 28
Second Sphere Interactions in Amyloidogenic Diseases
Roy, M., Nath, A. K., Pal, I., & Dey, S. G. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00941 · Cited by 29
Single-domain antibody–based noninvasive in vivo imaging of α-synuclein or tau pathology
Jiang, Y., Lin, Y., Krishnaswamy, S., Pan, R., Wu, Q., Sandusky‐Beltran, L. A., Liu, M., Kuo, M., Kong, X., Congdon, E. E., et al. (2023) · Science Advances · doi:10.1126/sciadv.adf3775 · Cited by 29
Rabs, SNAREs and α-synuclein — Membrane trafficking defects in synucleinopathies
Chua, C. E. L., & Tang, B. L. (2011) · Brain Research Reviews · doi:10.1016/j.brainresrev.2011.03.002 · Cited by 28
Wang, S., Chu, C., Guo, M., Jiang, L., Nie, H., Zhang, W., Wilson, B. C., Li, Y., Stewart, T., Hong, J., et al. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0606-7 · Cited by 28
Synucleinopathies: a pathological and molecular review
Murray, I. V. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2001) · Clinical Neuroscience Research · doi:10.1016/s1566-2772(01)00023-8 · Cited by 28
Self-citationFibril fuzzy coat is important for α-synuclein pathological transmission activity
Han, Y., Li, J., Xia, W., Li, Q., Sun, Z., Zeng, W., Hu, Y., Luk, K. C., Liu, C., Xiang, S., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.03.019 · Cited by 28
Lloyd, G. M., Sorrentino, Z. A., Quintin, S. S., Gorion, K.-M. M., Bell, B. M., Paterno, G., Long, B., Prokop, S., & Giasson, B. I. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02425-4 · Cited by 28
Self-citationSeetaloo, N., Zacharopoulou, M., Stephens, A. D., Schierle, G. S. K., & Phillips, J. J. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c03183 · Cited by 27
Henrı́quez, G., & Narayan, M. (2023) · Exploration of Neuroprotective Therapy · doi:10.37349/ent.2023.00048 · Cited by 27
Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein
Williams, J. K., Yang, X., Atieh, T. B., Olson, M. P., Khare, S. D., & Baum, J. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.024 · Cited by 27
In‐Cell NMR Spectroscopy of Intrinsically Disordered Proteins
Sciolino, N., Burz, D. S., & Shekhtman, A. G. (2018) · PROTEOMICS · doi:10.1002/pmic.201800055 · Cited by 27
Gotte, G., Donadelli, M., Laurents, D. V., Vottariello, F., Morbio, M., & Libonati, M. (2006) · Biochemistry · doi:10.1021/bi060933t · Cited by 27
In Search of Effective Treatments Targeting α-Synuclein Toxicity in Synucleinopathies: Pros and Cons
Fouka, M., Mavroeidi, P., Tsaka, G., & Xilouri, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.559791 · Cited by 27
The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Aggregates
Creekmore, B. C., Chang, Y., & Lee, E. B. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab039 · Cited by 28
Dou, T., Matveyenka, M., & Kurouski, D. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00314 · Cited by 26
Can Intrabodies Serve as Neuroprotective Therapies for Parkinson's Disease? Beginning Thoughts
Bhatt, M. A., Messer, A. C., & Kordower, J. H. (2013) · Journal of Parkinson s Disease · doi:10.3233/jpd-130252 · Cited by 26
Identification of an amyloid fibril forming peptide comprising residues 46–59 of apolipoprotein A‐I
Wong, Y. Q., Binger, K. J., Howlett, G. J., & Griffin, M. D. W. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.05.007 · Cited by 26
Intrabody and Parkinson's disease
Zhou, C. H., & Przedborski, S. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.09.001 · Cited by 28
Photo‐activity induced by amyloidogenesis
Tcherkasskaya, O. (2007) · Protein Science · doi:10.1110/ps.062578307 · Cited by 28
The inhibitory effects of biomimetically designed peptides on α-synuclein aggregation
Rezaeian, N., Shirvanizadeh, N., Mohammadi, S., Nikkhah, M., & Arab, S. S. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.09.015 · Cited by 26
Ranjan, P., Ghosh, D., Yarramala, D. S., Das, S., Maji, S. K., & Kumar, A. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.11.043 · Cited by 25
A subset of calcium‐binding S100 proteins show preferential heterodimerization
Spratt, D. E., Barber, K. R., Marlatt, N. M., Ngo, V., Macklin, J. A., Xiao, Y., Konermann, L., Duennwald, M. L., & Shaw, G. S. (2019) · FEBS Journal · doi:10.1111/febs.14775 · Cited by 25
Harada, R., Kobayashi, N., Kim, J., Nakamura, C., Han, S.-W., Ikebukuro, K., & Sode, K. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.06.010 · Cited by 27
Synuclein Proteins of the Pufferfish Fugu rubripes: Sequences and Functional Characterization
Yoshida, H., Craxton, M., Jakes, R., Zibaee, S., Tavaré, R., Fraser, G. M., Serpell, L. C., Davletov, B. A., Crowther, R. A., & Goedert, M. (2006) · Biochemistry · doi:10.1021/bi051993m · Cited by 25
Drobny, A., Ngo, P. A., Neurath, M. F., Zunke, F., & López-Posadas, R. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.655123 · Cited by 24
Navale, G. R., Ahmed, I., Lim, M. H., & Ghosh, K. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202401991 · Cited by 24
Sizes, conformational fluctuations, and SAXS profiles for intrinsically disordered proteins
Mugnai, M. L., Chakraborty, D., Nguyen, H. T., Maksudov, F., Kumar, A., Zeno, W. F., Stachowiak, J. C., Straub, J. E., & Thirumalai, D. (2025) · Protein Science · doi:10.1002/pro.70067 · Cited by 24
Aggregation of α-synuclein splice isoforms through a phase separation pathway
Röntgen, A., Toprakcioglu, Z., Dada, S., Morris, O. M., Knowles, T. P. J., & Vendruscolo, M. (2025) · Science Advances · doi:10.1126/sciadv.adq5396 · Cited by 25
Choudhary, S., Save, S. N., & Vavilala, S. L. (2018) · Scientific Reports · doi:10.1038/s41598-018-24079-7 · Cited by 25
Re-designing the α-synuclein tetramer
Xu, L., Bhattacharya, S., & Thompson, D. (2018) · Chemical Communications · doi:10.1039/c8cc04054k · Cited by 24
Hmila, I., Vaikath, N. N., Majbour, N. K., Erskine, D., Sudhakaran, I. P., Gupta, V. R., Ghanem, S. S., Islam, Z., Emara, M. M., Abdesselem, H., et al. (2022) · FEBS Journal · doi:10.1111/febs.16376 · Cited by 24
Patrias, L. M., Klaver, A. C., Coffey, M. P., & Loeffler, D. A. (2010) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2010.04214.x · Cited by 24
Molecular Mechanisms of the Bindings between Non-Amyloid β Component Oligomers and Amylin Oligomers
Atsmon‐Raz, Y., & Miller, Y. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b07731 · Cited by 24
The ER retention protein RER1 promotes alpha-synuclein degradation via the proteasome
Park, H., Ryu, D. H., Parmar, M. S., Giasson, B. I., & McFarland, N. R. (2017) · PLoS ONE · doi:10.1371/journal.pone.0184262 · Cited by 24
Self-citationNanomaterial synthesis, an enabler of amyloidosis inhibition against human diseases
Andrikopoulos, N., Li, Y., Cecchetto, L., Nandakumar, A., Ros, T. D., Davis, T. P., Velonia, K., & Ke, P. C. (2020) · Nanoscale · doi:10.1039/d0nr04273k · Cited by 24
Moussa, C., Mahmoodian, F., Tomita, Y. A., & Sidhu, A. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.11.075 · Cited by 24
Ubiquitination of alpha-synuclein filaments by Nedd4 ligases
Mund, T., Masuda‐Suzukake, M., Goedert, M., & Pelham, H. R. B. (2018) · PLoS ONE · doi:10.1371/journal.pone.0200763 · Cited by 25
The Role of α-Synuclein in Methamphetamine-Induced Neurotoxicity
Wu, M., Su, H., & Zhao, M. (2021) · Neurotoxicity Research · doi:10.1007/s12640-021-00332-2 · Cited by 23
Passive Immunization in Alpha-Synuclein Preclinical Animal Models
Folke, J., Ferreira, N., Brudek, T., Borghammer, P., & Berge, N. V. D. (2022) · Biomolecules · doi:10.3390/biom12020168 · Cited by 23
Chung, C. W., Stephens, A. D., Ward, E., Feng, Y., Davis, M. J., Kaminski, C. F., & Schierle, G. S. K. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.1c05651 · Cited by 23
Jiang, B., Han, F., Lü, M.-H., Wang, Z., Liu, W., Zhang, Y., Xu, J. P., & Li, R.-J. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114529 · Cited by 23
Residue Glu83 plays a major role in negatively regulating α-synuclein amyloid formation
Waxman, E. A., Emmer, K. L., & Giasson, B. I. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.12.079 · Cited by 23
Self-citationInvestigational α-synuclein aggregation inhibitors: hope for Parkinson’s disease
Török, N., Majláth, Z., Szalárdy, L., & Vécsei, L. (2016) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2016.1237501 · Cited by 23
DT-diaphorase Protects Against Autophagy Induced by Aminochrome-Dependent Alpha-Synuclein Oligomers
Muñoz, P., & Segura‐Aguilar, J. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9747-4 · Cited by 23
Kiely, A. P., Miners, J. S., Courtney, R. J., Strand, C., Love, S., & Holton, J. L. (2018) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12512 · Cited by 23
Segmental 13C‐Labeling and Raman Microspectroscopy of α‐Synuclein Amyloid Formation
Flynn, J. D., Jiang, Z., & Lee, J. C. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201809865 · Cited by 23
Amyloids and their untapped potential as hydrogelators
Belwal, V. K., & Chaudhary, N. (2020) · Soft Matter · doi:10.1039/d0sm01578d · Cited by 23
Aggregation and phase separation of α-synuclein in Parkinson's disease
Han, W., Wei, M., Xu, F., & Niu, Z. (2024) · Chemical Communications · doi:10.1039/d4cc01591f · Cited by 22
Cu2+, Ca2+, and methionine oxidation expose the hydrophobic α-synuclein NAC domain
Ramis, R., Ortega‐Castro, J., Vilanova, B., Adrover, M., & Frau, J. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.12.018 · Cited by 22
Chetty, D., Abrahams, S., van Coller, R., Carr, J. A., Kenyon, C. P., & Bardien, S. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15324 · Cited by 22
Interplay between α-synuclein and parkin genes: Insights of Parkinson’s disease
Sharma, K., Chib, S., Gupta, A., Singh, R., & Chalotra, R. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09520-7 · Cited by 22
Folding and amyloid‐fibril formation for a series of human stefins' chimeras: Any correlation?
Kenig, M., Kokalj, S. J., Žnidarič, M. T., Pompe‐Novak, M., Gunčar, G., Türk, V., Waltho, J. P., Staniforth, R. A., Avbelj, F., & Žerovnik, E. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20812 · Cited by 22
Metadata
- Authors
- Giasson, B. I., Murray, I. V. J., Trojanowski, J. Q., & Lee, V. M.-Y.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Lee, Virginia M.-Y.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-01
- Volume
- 276
- Issue
- 4
- Pages
- 2380-2386
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2166789153
- Cited by
- 1,080
- References
- 36
- Citations by year
- 2026: 33 · 2025: 60 · 2024: 77 · 2023: 58 · 2022: 78 · 2021: 59 · 2020: 65 · 2019: 51 · 2018: 57 · 2017: 51 · 2016: 36 · 2015: 36 · 2014: 39 · 2013: 32 · 2012: 36
- FWCI
- 21.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- alpha-synuclein, fibrillization, filament assembly, hydrophobic domains, beta-synuclein, protease resistance, amyloid fibrils, neurodegenerative diseases
- MeSH terms
- Amino Acid Sequence, Humans, Molecular Sequence Data, Nerve Tissue Proteins, Nervous System Diseases, Peptide Fragments, Protein Binding, Protein Conformation, Recombinant Proteins, Synucleins, alpha-Synuclein, beta-Synuclein
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review