Cited by 429Genetic Neurodegenerative DiseasesParkinson's Disease Mechanisms and TreatmentsAlzheimer's disease research and treatments

The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.

Yeast Genes That Enhance the Toxicity of a Mutant Huntingtin Fragment or α-Synuclein

Willingham, Stephen, Outeiro, Tiago Fleming, DeVit, Michael J., Lindquist, Susan L., Muchowski, Paul J.·2003·Science

DOI 10.1126/science.1090389

Open this paper in CoChat — free account

Abstract

Genome-wide screens were performed in yeast to identify genes that enhance the toxicity of a mutant huntingtin fragment or of α-synuclein. Of 4850 haploid mutants containing deletions of nonessential genes, 52 were identified that were sensitive to a mutant huntingtin fragment, 86 that were sensitive to α-synuclein, and only one mutant that was sensitive to both. Genes that enhanced toxicity of the mutant huntingtin fragment clustered in the functionally related cellular processes of response to stress, protein folding, and ubiquitin-dependent protein catabolism, whereas genes that modified α-synuclein toxicity clustered in the processes of lipid metabolism and vesicle-mediated transport. Genes with human orthologs were overrepresented in our screens, suggesting that we may have discovered conserved and nonoverlapping sets of cell-autonomous genes and pathways that are relevant to Huntington's disease and Parkinson's disease.

Integrity signals

Registry

Crossref · 10.1126/science.1090389

Cites

31 of 31 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
Functional profiling of the Saccharomyces cerevisiae genome
Giaever, G., Chu, A. M., Ni, L., Connelly, C., Riles, L., Véronneau, S., Dow, S., Lucau-Danila, A., Anderson, K., André, B., et al. (2002) · Nature · doi:10.1038/nature00935 · Cited by 4,316
Functional Characterization of the S. cerevisiae Genome by Gene Deletion and Parallel Analysis
Winzeler, E. A., Shoemaker, D. D., Astromoff, A., Liang, H., Anderson, K., Andre, B., Bangham, R., Benito, R., Boeke, J. D., Bussey, H., et al. (1999) · Science · doi:10.1126/science.285.5429.901 · Cited by 3,953
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group.
Shah, M. A., Datson, N. A., Srinidhi, L., Stanton, V. P., MacDonald, M. E., Allard, M. W., Youngman, S., Am, F., Mott, R., Draths, K., et al. (1993) · Cell · Cited by 3,055
Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes
Davidson, W. S., Jonas, A., Clayton, D. F., & George, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9443 · Cited by 1,622
Alpha-synuclein and neurodegenerative diseases
Goedert, M. (2001) · Nature reviews. Neuroscience · doi:10.1038/35081564 · Cited by 1,428
Pathogenesis of parkinson's disease: dopamine, vesicles and α-synuclein
Lotharius, J., & Brundin, P. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn983 · Cited by 1,319
Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In Vivo
Scherzinger, E., Lurz, R., Turmaine, M., Mangiarini, L., Hollenbach, B., Hasenbank, R., Bates, G. P., Davies, S. W., Lehrach, H., & Wanker, E. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80514-0 · Cited by 1,291

Show all 31 references

Sorted by citations

-Synuclein in Parkinson's Disease
Stefanis, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009399 · Cited by 1,446
Increased Expression of α-Synuclein Reduces Neurotransmitter Release by Inhibiting Synaptic Vesicle Reclustering after Endocytosis
Nemani, V. M., Lü, W., Berge‐Seidl, V., Nakamura, K., Onoa, B., Lee, M. K., Chaudhry, F. A., Nicoll, R. A., & Edwards, R. H. (2010) · Neuron · doi:10.1016/j.neuron.2009.12.023 · Cited by 1,089
Modulation of neurodegeneration by molecular chaperones
Muchowski, P. J., & Wacker, J. L. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1587 · Cited by 1,043
Self-citation
The function of α-synuclein
Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825
Yeast Cells Provide Insight into Alpha-Synuclein Biology and Pathobiology
Outeiro, T. F., & Lindquist, S. L. (2003) · Science · doi:10.1126/science.1090439 · Cited by 811
Self-citation
Parkinson’s disease: genetics and pathogenesis
Shulman, J. M., De Jager, P. L., & Feany, M. B. (2011) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130242 · Cited by 801
Intravesicular Localization and Exocytosis of α-Synuclein and its Aggregates
Lee, H.-J., Patel, S. S., & Lee, S. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0692-05.2005 · Cited by 826
THE BIOCHEMISTRY OF PARKINSON'S DISEASE
Cookson, M. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133400 · Cited by 666
Anti-apoptosis and cell survival: A review
Portt, L., Norman, G., Clapp, C., Greenwood, M., & Greenwood, M. T. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.10.010 · Cited by 661
What Genetics Tells us About the Causes and Mechanisms of Parkinson's Disease
Corti, O., Lesage, S., & Brice, A. (2011) · Physiological Reviews · doi:10.1152/physrev.00022.2010 · Cited by 652
Direct Membrane Association Drives Mitochondrial Fission by the Parkinson Disease-associated Protein α-Synuclein
Nakamura, K., Nemani, V. M., Azarbal, F., Skibinski, G., Levy, J. M., Egami, K., Munishkina, L. A., Zhang, J., Gardner, B. M., Wakabayashi, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213538 · Cited by 624
Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation
Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 593
Cellular Strategies of Protein Quality ControlPreprint
Chen, B., Retzlaff, M., Roos, T. R., & Frydman, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004374 · Cited by 515
Gene Overexpression: Uses, Mechanisms, and Interpretation
Prelich, G. (2012) · Genetics · doi:10.1534/genetics.111.136911 · Cited by 480
The Yeast Deletion Collection: A Decade of Functional Genomics
Giaever, G. N., & Nislow, C. (2014) · Genetics · doi:10.1534/genetics.114.161620 · Cited by 500
Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS
Sun, Z., Diaz, Z., Fang, X., Hart, M. P., Chesi, A., Shorter, J., & Gitler, A. D. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000614 · Cited by 461
C. elegans Model Identifies Genetic Modifiers of α-Synuclein Inclusion Formation During Aging
van Ham, T. J., Thijssen, K. L., Breitling, R., Hofstra, R. M. W., Plasterk, R. H. A., & Nollen, E. A. A. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000027 · Cited by 437
Increased glutathione S -transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease
Whitworth, A. J., Theodore, D. A., Greene, J. C., Beneš, H., Wes, P. D., & Pallanck, L. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501078102 · Cited by 421
α-Synuclein and neuronal cell death
Cookson, M. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-9 · Cited by 440
Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation
Nollen, E. A. A., Garcia, S. M., van Haaften, G., Kim, S., Chavez, A., Morimoto, R. I., & Plasterk, R. H. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307697101 · Cited by 416
A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
Johnson, B. S., McCaffery, J. M., Lindquist, S. L., & Gitler, A. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802082105 · Cited by 416
Self-citation
Huntington's disease: from pathology and genetics to potential therapies
Imarisio, S., Carmichael, J., Korolchuk, V., Chen, C.-W., Saiki, S., Rose, C., Krishna, G., Davies, J. E., Ttofi, E., Underwood, B. R., et al. (2008) · Biochemical Journal · doi:10.1042/bj20071619 · Cited by 409
Heat Shock Proteins 70 and 90 Inhibit Early Stages of Amyloid β-(1–42) Aggregation in Vitro
Evans, C. G., Wisén, S., & Gestwicki, J. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606192200 · Cited by 396
Cell type-specific gene expression of midbrain dopaminergic neurons reveals molecules involved in their vulnerability and protection
Chung, C. Y., Seo, H., Sonntag, K. C., Brooks, A., Lin, L., & Isacson, O. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi178 · Cited by 361
A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease
Giorgini, F., Guidetti, P., Nguyen, Q., Bennett, S. C., & Muchowski, P. J. (2005) · Nature Genetics · doi:10.1038/ng1542 · Cited by 331
Self-citation
Membrane Curvature Induction and Tubulation Are Common Features of Synucleins and Apolipoproteins
Varkey, J., Isas, J. M., Mizuno, N., Jensen, M. B., Bhatia, V. K., Jao, C. C., Petrlová, J., Voss, J. C., Stamou, D. G., Steven, A. C., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.139576 · Cited by 333
Genetics of Parkinson's disease and parkinsonism
Hardy, J., Cai, H., Cookson, M., Gwinn, K. A., & Singleton, A. (2006) · Annals of Neurology · doi:10.1002/ana.21022 · Cited by 312
Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity
Yeger‐Lotem, E., Riva, L., Su, L. J., Gitler, A. D., Cashikar, A. G., King, O. D., Auluck, P. K., Geddie, M. L., Valastyan, J. S., Karger, D. R., et al. (2009) · Nature Genetics · doi:10.1038/ng.337 · Cited by 287
Self-citation
Hypothesis-based RNAi screening identifies neuroprotective genes in a Parkinson's disease model
Hamamichi, S., Rivas, R. N., Knight, A. L., Cao, S., Caldwell, K. A., & Caldwell, G. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711018105 · Cited by 268
Replicative Aging in Yeast: The Means to the End
Steinkraus, K. A., Kaeberlein, M. R., & Kennedy, B. K. (2008) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123509 · Cited by 282
Chaperonin TRiC Promotes the Assembly of polyQ Expansion Proteins into Nontoxic Oligomers
Behrends, C., Langer, C. A., Boteva, R. N., Böttcher, U. M. K., Stemp, M. J., Schaffar, G., Rao, B. V., Giese, A., Kretzschmar, H. A., Siegers, K., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.017 · Cited by 278
Ubiquitin ligase Nedd4 promotes α-synuclein degradation by the endosomal–lysosomal pathway
Tofaris, G. K., Kim, H. T., Hourez, R., Jung, J.-W., Kim, K. P., & Goldberg, A. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109356108 · Cited by 271
TOR-Mediated Cell-Cycle Activation Causes Neurodegeneration in a Drosophila Tauopathy Model
Khurana, V., Lu, Y., Steinhilb, M. L., Oldham, S., Shulman, J. M., & Feany, M. B. (2006) · Current Biology · doi:10.1016/j.cub.2005.12.042 · Cited by 266
The ubiquitin–proteasome pathway in Parkinson's disease and other neurodegenerative diseases
Ross, C. A., & Pickart, C. M. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.10.006 · Cited by 261
Huntington's DiseasePreprint
Finkbeiner, S. M. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007476 · Cited by 274
Dysregulated Lipid Metabolism and Its Role in α-Synucleinopathy in Parkinson’s Disease
Alecu, I., & Bennett, S. A. L. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00328 · Cited by 266
Dietary fatty acids and the risk of Parkinson disease
de Lau, L. M. L., Bornebroek, M., Witteman, J. C. M., Albert Hofman, D., Koudstaal, P. J., & Breteler, M. M. B. (2005) · Neurology · doi:10.1212/01.wnl.0000166038.67153.9f · Cited by 260
Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease models
Armakola, M., Higgins, M., Figley, M. D., Barmada, S. J., Scarborough, E. A., Diaz, Z., Fang, X., Shorter, J., Krogan, N. J., Finkbeiner, S. M., et al. (2012) · Nature Genetics · doi:10.1038/ng.2434 · Cited by 253
Relationships between the Sequence of α-Synuclein and its Membrane Affinity, Fibrillization Propensity, and Yeast Toxicity
Volles, M. J., & Lansbury, P. T. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.044 · Cited by 250
α-Synuclein Inhibits Intersynaptic Vesicle Mobility and Maintains Recycling-Pool Homeostasis
Scott, D. A., & Roy, S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0535-12.2012 · Cited by 243
The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of -synuclein, and enhances its secretion and nuclear localization in cells
Fares, M.-B., Ait‐Bouziad, N., Dikiy, I., Mbefo, M. K., Jovi, A., Kiely, A. P., Holton, J. L., Lee, S., Gitler, A. D., Eliezer, D., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu165 · Cited by 251
Heat Shock Prevents Alpha-synuclein-induced Apoptosis in a Yeast Model of Parkinson's Disease
Flower, T. R., Chesnokova, L. S., Froelich, C. A., Dixon, C., & Witt, S. N. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.06.060 · Cited by 239
Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?
Khurana, V., & Lindquist, S. L. (2010) · Nature reviews. Neuroscience · doi:10.1038/nrn2809 · Cited by 245
Self-citation
CHIP Suppresses Polyglutamine Aggregation and ToxicityIn VitroandIn Vivo
Miller, V. M., Nelson, R. F., Gouvion, C. M., Williams, A. J., Rodríguez-Lebrón, E., Harper, S. Q., Davidson, B. L., Rebagliati, M. R., & Paulson, H. L. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3001-05.2005 · Cited by 240
Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies
Miranda, H. V., Szegő, É. M., Oliveira, L. M. A., Breda, C., Darendelioğlu, E., de Oliveira, R. M., Ferreira, D. G., Gomes, M. A., Rott, R., de Oliveira, M. S. D., et al. (2017) · Brain · doi:10.1093/brain/awx056 · Cited by 234
Self-citation
Yeast as a model for medical and medicinal research
Mager, W. H., & Winderickx, J. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2005.03.004 · Cited by 217
Yeast genome-wide screen reveals dissimilar sets of host genes affecting replication of RNA viruses
Panavas, T., Servienė, E., Brasher, J., & Nagy, P. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502604102 · Cited by 219
Ubiquitin–proteasome system and Parkinson's disease
Olanow, C. W., & McNaught, K. S. P. (2006) · Movement Disorders · doi:10.1002/mds.21013 · Cited by 219
Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells
Kim, K., Stevens, M. V., Akter, M. H., Rusk, S. E., Huang, R. J., Cohen, A., Noguchi, A. C., Springer, D., Bocharov, A. V., Eggerman, T. L., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44736 · Cited by 210
Optical Reporters for the Conformation of α-Synuclein Reveal a Specific Interaction with Mitochondria
Nakamura, K., Nemani, V. M., Wallender, E. K., Kaehlcke, K., Ott, M., & Edwards, R. H. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3088-08.2008 · Cited by 217
A Yeast Model of FUS/TLS-Dependent Cytotoxicity
Ju, S., Tardiff, D. F., Han, H., Divya, K., Zhong, Q., Maquat, L. E., Bosco, D. A., Hayward, L. J., Brown, R. H., Lindquist, S. L., et al. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001052 · Cited by 208
Self-citation
Protein interactions and disease: computational approaches to uncover the etiology of diseases
Kann, M. G. (2007) · Briefings in Bioinformatics · doi:10.1093/bib/bbm031 · Cited by 202
Genome-Wide Screen for Modifiers of Ataxin-3 Neurodegeneration in Drosophila
Bilen, J., & Bonini, N. M. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030177 · Cited by 199
GTPase Activity Plays a Key Role in the Pathobiology of LRRK2
Xiong, Y., Coombes, C. E., Kilaru, A. S., Li, X., Gitler, A. D., Bowers, W. J., Dawson, V. L., Dawson, T. M., & Moore, D. J. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000902 · Cited by 201
The molecular genetics of Huntington disease — a history
Bates, G. P. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1686 · Cited by 201
Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis
Greene, J. C., Whitworth, A. J., Andrews, L. A., Parker, T. J., & Pallanck, L. J. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi074 · Cited by 194
Alpha-Synuclein Physiology and Pathology: A Perspective on Cellular Structures and Organelles
Bernal-Conde, L. D., Ramos-Acevedo, R., Reyes-Hernández, M. A., Balbuena-Olvera, A. J., Morales-Moreno, I. D., Argüero‐Sánchez, R., Schüle, B., & Guerra‐Crespo, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01399 · Cited by 197
Protein Homeostasis in Models of Aging and Age-Related Conformational Disease
Kikis, E. A., Gidalevitz, T., & Morimoto, R. I. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_11 · Cited by 193
α-Synuclein and astrocytes: tracing the pathways from homeostasis to neurodegeneration in Lewy body disease
Sorrentino, Z. A., Giasson, B. I., & Chakrabarty, P. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01977-2 · Cited by 179
Cell systems and the toxic mechanism(s) of α-synuclein
Cookson, M., & van der Brug, M. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.05.022 · Cited by 177
Machado–Joseph disease/spinocerebellar ataxia type 3
Paulson, H. L. (2011) · Handbook of clinical neurology · doi:10.1016/b978-0-444-51892-7.00027-9 · Cited by 180
Alpha-synuclein research: defining strategic moves in the battle against Parkinson’s disease
Oliveira, L. M. A., Gasser, T., Edwards, R. H., Zweckstetter, M., Melki, R., Stefanis, L., Lashuel, H. A., Sulzer, D., Vekrellis, K., Halliday, G. M., et al. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-021-00203-9 · Cited by 174
Self-citation
Distinct Roles for the Hsp40 and Hsp90 Molecular Chaperones during Cystic Fibrosis Transmembrane Conductance Regulator Degradation in Yeast
Youker, R. T., Walsh, P., Beilharz, T. H., Lithgow, T. J., & Brodsky, J. L. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0584 · Cited by 167
Protein aggregation in the pathogenesis of familial and sporadic Parkinson's disease
McNaught, K. S. P., & Olanow, C. W. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.08.012 · Cited by 166
RNA-binding proteins with prion-like domains in ALS and FTLD-U
Gitler, A. D., & Shorter, J. (2011) · Prion · doi:10.4161/pri.5.3.17230 · Cited by 167
Expression Profiling of Substantia Nigra in Parkinson Disease, Progressive Supranuclear Palsy, and Frontotemporal Dementia With Parkinsonism
Hauser, M. A., Li, Y., Xu, H., Noureddine, M., Shao, Y. S., Gullans, S. R., Scherzer, C. R., Jensen, R. V., McLaurin, A. C., Gibson, J., et al. (2005) · Archives of Neurology · doi:10.1001/archneur.62.6.917 · Cited by 158
A network of protein interactions determines polyglutamine toxicity
Duennwald, M. L., Jagadish, S., Giorgini, F., Muchowski, P. J., & Lindquist, S. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604548103 · Cited by 155
Self-citation
Induction of the Phase II Detoxification Pathway Suppresses Neuron Loss in Drosophila Models of Parkinson's Disease
Trinh, K., Moore, K., Wes, P. D., Muchowski, P. J., Dey, J., Andrews, L. A., & Pallanck, L. J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4778-07.2008 · Cited by 151
Self-citation
Oxidative and nitrative alpha‐synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies
Schildknecht, S., Gerding, H. R., Karreman, C., Drescher, M., Lashuel, H. A., Outeiro, T. F., Di Monte, D. A., & Leist, M. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12226 · Cited by 148
Self-citation
Molecular pathways that influence human tau-induced pathology in Caenorhabditis elegans
Kraemer, B. C., Burgess, J. K., Chen, J. H., Thomas, J. H., & Schellenberg, G. D. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl067 · Cited by 150
Rapid selection of cyclic peptides that reduce α-synuclein toxicity in yeast and animal models
Kritzer, J. A., Hamamichi, S., McCaffery, J. M., Santagata, S., Naumann, T. A., Caldwell, K. A., Caldwell, G. A., & Lindquist, S. L. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.193 · Cited by 140
Self-citation
Glutathione peroxidase activity is neuroprotective in models of Huntington's disease
Mason, R. P., Casu, M., Butler, N. J., Breda, C., Campesan, S., Clapp, J., Green, E. W., Dhulkhed, D., Kyriacou, C. P., & Giorgini, F. (2013) · Nature Genetics · doi:10.1038/ng.2732 · Cited by 138
Structural insights on physiological functions and pathological effects of ±‐synuclein
Bisaglia, M., Mammi, S., & Bubacco, L. (2008) · The FASEB Journal · doi:10.1096/fj.08-119784 · Cited by 143
Cytotoxicity of a mutant huntingtin fragment in yeast involves early alterations in mitochondrial OXPHOS complexes II and III
Solans, A., Zambrano, A., Rodríguez, M., & Barrientos, A. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl248 · Cited by 142
Critical Role of the Proline-rich Region in Huntingtin for Aggregation and Cytotoxicity in Yeast
Dehay, B., & Bertolotti, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605558200 · Cited by 136
Protein misfolding in neurodegenerative diseases
Agorogiannis, E. I., Agorogiannis, G. I., Papadimitriou, A., & Hadjigeorgiou, G. M. (2004) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00558.x · Cited by 127
Amino acid sequence motifs and mechanistic features of the membrane translocation of α‐synuclein
Ahn, K. J., Paik, S. R., Chung, K. C., & Kim, J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03731.x · Cited by 123
Phosphorylated tau and the neurodegenerative foldopathies
Kosik, K. S., & Shimura, H. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.10.011 · Cited by 124
Effects of mitochondrial dysfunction on the immunological properties of microglia
Ferger, A. I., Campanelli, L., Reimer, V., Muth, K. N., Merdian, I., Ludolph, A. C., & Witting, A. (2010) · Journal of Neuroinflammation · doi:10.1186/1742-2094-7-45 · Cited by 122
A Genetic Screening Strategy Identifies Novel Regulators of the Proteostasis Network
Silva, M. C., Fox, S. G., Beam, M., Thakkar, H., Amaral, M. D., & Morimoto, R. I. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002438 · Cited by 119
A Mitochondria-Associated Oxidative Stress Perspective on Huntington’s Disease
Zheng, J., Winderickx, J., Franssens, V., & Liu, B. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00329 · Cited by 122
Inhibition of α-Synuclein Fibrillization by Dopamine Is Mediated by Interactions with Five C-Terminal Residues and with E83 in the NAC Region
Herrera, F. E., Chesi, A., Paleologou, K. E., Schmid, A. W., Munoz, A., Vendruscolo, M., Gustincich, S., Lashuel, H. A., & Carloni, P. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003394 · Cited by 118
Chapter 6 Molecular and Cellular Biology of Synucleins
Surguchov, A. P. (2008) · International review of cytology · doi:10.1016/s1937-6448(08)01406-8 · Cited by 123
The uses of genome-wide yeast mutant collections.
Scherens, B., & Goffeau, A. (2004) · Genome biology · doi:10.1186/gb-2004-5-7-229 · Cited by 118
Cellular models of alpha‐synuclein toxicity and aggregation
Delenclos, M., Burgess, J. D., Lamprokostopoulou, A., Outeiro, T. F., Vekrellis, K., & McLean, P. J. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14806 · Cited by 120
Self-citation
Characterization of α‐synuclein aggregation and synergistic toxicity with protein tau in yeast
Zabrocki, P., Pellens, K., Vanhelmont, T., Vandebroek, T., Griffioen, G., Wera, S., LEUVEN, F. V., & Winderickx, J. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04571.x · Cited by 111
Phosphorylation, lipid raft interaction and traffic of α-synuclein in a yeast model for Parkinson
Zabrocki, P., Bastiaens, I., Delay, C., Bammens, T., Ghillebert, R., Pellens, K., VIRGILIO, C. D., LEUVEN, F. V., & Winderickx, J. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.06.010 · Cited by 109
Protein aggregation as a paradigm of aging
Lindner, A. B., & Démarez, A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.06.005 · Cited by 111
Molecular Chaperones: A Double-Edged Sword in Neurodegenerative Diseases
Tittelmeier, J., Nachman, E., & Nussbaum-Krammer, C. I. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.581374 · Cited by 114
Polyunsaturated Fatty Acids Induce α-Synuclein-Related Pathogenic Changes in Neuronal Cells
Assayag, K., Yakunin, E., Loeb, V., Selkoe, D. J., & Sharon, R. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070373 · Cited by 109
Accumulation of aberrant ubiquitin induces aggregate formation and cell death in polyglutamine diseases
de Pril, R. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh188 · Cited by 107
Drosophila Models of Parkinson's Disease
Whitworth, A. J. (2011) · Advances in genetics · doi:10.1016/b978-0-12-380860-8.00001-x · Cited by 110
Loss of Hsp70 Exacerbates Pathogenesis But Not Levels of Fibrillar Aggregates in a Mouse Model of Huntington's Disease
Wacker, J. L., Huang, S., Steele, A. D., Aron, R., Lotz, G. P., Nguyen, Q., Giorgini, F., Roberson, E. D., Lindquist, S., Masliah, E., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2250-09.2009 · Cited by 105
Self-citation
Protein folding diseases and neurodegeneration: Lessons learned from yeast
Winderickx, J., Delay, C., Vos, A. D., Klinger, H., Pellens, K., Vanhelmont, T., LEUVEN, F. V., & Zabrocki, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.020 · Cited by 108
Phosphatidylethanolamine deficiency disrupts α-synuclein homeostasis in yeast and worm models of Parkinson disease
Wang, S., Zhang, S., Liou, L.-C., Ren, Q., Zhang, Z., Caldwell, G. A., Caldwell, K. A., & Witt, S. N. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411694111 · Cited by 102
Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways
Ralser, M., Nonhoff, U., Albrecht, M., Lengauer, T., Wanker, E. E., Lehrach, H. R., & Krobitsch, S. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi321 · Cited by 101
Drosophila Models of Parkinson's Disease: Discovering Relevant Pathways and Novel Therapeutic Strategies
Muñoz, V. F. L., & Paricio, N. (2011) · Parkinson s Disease · doi:10.4061/2011/520640 · Cited by 104
Simple is good: yeast models of neurodegeneration
Tenreiro, S., & Outeiro, T. F. (2010) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2010.00649.x · Cited by 102
Self-citation
The Princeton Protein Orthology Database (P-POD): A Comparative Genomics Analysis Tool for Biologists
Heinicke, S., Livstone, M. S., Lu, C., Oughtred, R., Kang, F., Angiuoli, S. V., White, O. R., Botstein, D., & Dolinski, K. J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000766 · Cited by 98
Histone Deacetylase Inhibition Modulates Kynurenine Pathway Activation in Yeast, Microglia, and Mice Expressing a Mutant Huntingtin Fragment
Giorgini, F., Möller, T., Kwan, W., Zwilling, D., Wacker, J. L., Hong, S. Y., Tsai, L. L., Cheah, C. S., Schwarcz, R. M., Guidetti, P., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708192200 · Cited by 97
Self-citation

Authors: Willingham, S., Outeiro, T. F., DeVit, M. J., Lindquist, S. L., & Muchowski, P. J.
Affiliations: Howard Hughes Medical Institute (US)
Corresponding author: Muchowski, Paul J.
ORCID: Outeiro, Tiago Fleming
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2003-12-05
Volume: 302
Issue: 5651
Pages: 1769-1772
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1090389
OpenAlex: W2013754033
Cited by: 422
References: 31
Citations by year: 2026: 5 · 2025: 4 · 2024: 6 · 2023: 10 · 2022: 5 · 2021: 12 · 2020: 19 · 2019: 14 · 2018: 20 · 2017: 15 · 2016: 9 · 2015: 12 · 2014: 18 · 2013: 18 · 2012: 26
FWCI: 9.12
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Keywords: huntingtin, alpha-synuclein, Huntington's disease, Parkinson's disease, yeast genetic screen, stress response, protein folding, ubiquitin-dependent protein degradation, lipid metabolism, vesicle trafficking, human orthologs, neurodegeneration
MeSH terms: Huntingtin Protein, Biological Transport, Genes, Fungal, Humans, Mutation, Nerve Tissue Proteins, Nuclear Proteins, Osmotic Pressure, Proteins, Saccharomyces cerevisiae, Transformation, Genetic, Nitrosation, Gene Deletion, Protein Folding, Oxidative Stress, Ubiquitin, Lipid Metabolism, Synucleins, alpha-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

Yeast Genes That Enhance the Toxicity of a Mutant Huntingtin Fragment or α-Synuclein

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks