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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
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“all known autosomal dominant point mutations that cause PD reside within these repeat motifs, specifically A30P[120], E46K[121], A53T[122], G51D[123], and H50Q[124]”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [120]
Citations
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Genetic complexity and Parkinson's disease.
Gasser, T., Müller‐Myhsok, B., Wszołek, Z. K., Dürr, A., Vaughan, J. R., Bonifati, V., Meco, G., Bereznai, B., Oehlmann, R., Agid, Y., et al. (1997) · PubMed · Cited by 50
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APOE4 exacerbates α-synuclein pathology and related toxicity independent of amyloid
Zhao, N., Attrebi, O. N., Ren, Y., Qiao, W., Sonustun, B., Martens, Y. A., Meneses, A. D., Li, F., Shue, F., Zheng, J., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aay1809 · Cited by 156
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A molecular pathway of neurodegeneration linking α-synuclein to ApoE and Aβ peptides
Gallardo, G., Schlüter, O. M., & Südhof, T. C. (2008) · Nature Neuroscience · doi:10.1038/nn2058 · Cited by 145
Mutant α-Synuclein Overexpression Mediates Early Proinflammatory Activity
Su, X., Federoff, H. J., & Maguire-Zeiss, K. A. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9053-x · Cited by 145
Ahmed, I., Liang, Y., Schools, S., Dawson, V. L., Dawson, T. M., & Savitt, J. M. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0209-12.2012 · Cited by 144
Cellular Mechanisms of Melatonin: Insight from Neurodegenerative Diseases
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Alpha-Synuclein: Mechanisms of Release and Pathology Progression in Synucleinopathies
Brás, I. C., & Outeiro, T. F. (2021) · Cells · doi:10.3390/cells10020375 · Cited by 136
Could a loss of α‐synuclein function put dopaminergic neurons at risk?
Perez, R. G., & Hastings, T. G. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02423.x · Cited by 133
Healy-Stoffel, M., & Levant, B. (2018) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527317666180412153612 · Cited by 133
Does cellular iron dysregulation play a causative role in Parkinson’s disease?
Kaur, D., & Andersen, J. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2004.01.003 · Cited by 123
Role of Matrix Metalloproteinase 3-mediated α-Synuclein Cleavage in Dopaminergic Cell Death
Choi, D.-H., Kim, Y.-J., Kim, Y.-G., Joh, T. H., Beal, M. F., & Kim, Y.-S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.222430 · Cited by 123
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Pathogenic Mechanisms of Neurodegeneration in Parkinson Disease
Mullin, S., & Schapira, A. H. V. (2015) · Neurologic Clinics · doi:10.1016/j.ncl.2014.09.010 · Cited by 108
Expression of mutant alpha-synuclein modulates microglial phenotype in vitro
Rojanathammanee, L., Murphy, E. J., & Combs, C. K. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-44 · Cited by 106
Fluoxetine rescues impaired hippocampal neurogenesis in a transgenic A53T synuclein mouse model
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Parkinsons Disease and other α-Synucleinopathies
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Neuroinflammation in Multiple System Atrophy: Response to and Cause of α-Synuclein Aggregation
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“…α-synucleinopathies (mostly PD), but where G51D and A53E α-syn mutations have been described in patients with atypical parkinsonism and may overlap with MSA (Polymeropoulos et al., 1997; Krüger et al., 1998; Zarranz et al., 2004; Lesage et al., 2013; Proukakis et al., 2013; Pasanen et al., 2014).”
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Fatty Acid Binding Protein 3 Enhances the Spreading and Toxicity of α-Synuclein in Mouse Brain
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Relevance of chronic stress and the two faces of microglia in Parkinson's disease
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Dose- and time-dependent α-synuclein aggregation induced by ferric iron in SK-N-SH cells
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Paraquat and iron exposure as possible synergistic environmental risk factors in Parkinson’s disease
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Wahl, C., Kautzmann, S., Krebiehl, G., Strauss, K., Woitalla, D., Müller, T., Bauer, P., Riess, O., & Krüger, R. (2008) · Journal of Neural Transmission · doi:10.1007/s00702-008-0054-3 · Cited by 22
Self-citationAlpha-synuclein aggresomes inhibit ciliogenesis and multiple functions of the centrosome
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Cspg4 high microglia contribute to microgliosis during neurodegeneration
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Metadata
- Authors
- Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O.
- Affiliations
- Ruhr University Bochum (DE)
- Max Planck Society (DE)
- Corresponding author
- Riess, Olaf
- Venue
- Nature Genetics
- Published
- 1998-02
- Volume
- 18
- Issue
- 2
- Pages
- 106-108
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- OpenAlex
- W2091265794
- Cited by
- 3,836
- References
- 10
- Citations by year
- 2026: 56 · 2025: 64 · 2024: 102 · 2023: 109 · 2022: 115 · 2021: 118 · 2020: 122 · 2019: 134 · 2018: 140 · 2017: 140 · 2016: 117 · 2015: 129 · 2014: 155 · 2013: 169 · 2012: 155
- FWCI
- 92.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- Open Repository and Bibliography (University of Luxembourg) (submittedVersion)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- alpha-synuclein, Parkinson's disease, synucleinopathies, protein misfolding, UBQLN2, genetic mutations
- MeSH terms
- Alanine, Amino Acid Sequence, Base Sequence, Female, Humans, Male, Nerve Tissue Proteins, Parkinson Disease, Pedigree, Proline, Point Mutation, Polymorphism, Single-Stranded Conformational, Synucleins, alpha-Synuclein
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