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

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

Identification of common genetic modifiers of neurodegenerative diseases from an integrative analysis of diverse genetic screens in model organisms

Chen, X., & Burgoyne, R. D. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-71 · Cited by 34

? - synuclein and Parkinson's disease: the first roadblock

Chua, C. E. L., & Tang, B. L. (2006) · Journal of Cellular and Molecular Medicine · doi:10.2755/jcmm010.004.04 · Cited by 34

The wtf4 meiotic driver utilizes controlled protein aggregation to generate selective cell death

Nuckolls, N. L., Mok, A. C., Lange, J. J., Yi, K., Kandola, T. S., Hunn, A. M., McCroskey, S., Snyder, J. L., Núñez, M. A. B., McClain, M. L., et al. (2020) · eLife · doi:10.7554/elife.55694 · Cited by 33

Yeast Screens Identify the RNA Polymerase II CTD and SPT5 as Relevant Targets of BRCA1 Interaction

Bennett, C. B., Westmoreland, T. J., Verrier, C. S., Blanchette, C., Winsor, T. S., Phatnani, H. P., Mishina, Y. V., Hüper, G., Selim, A. L., Madison, E. R., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001448 · Cited by 33

Alpha‐synuclein in Parkinson's disease: Light from two new angles

Golbe, L. I., & Mouradian, M. M. (2004) · Annals of Neurology · doi:10.1002/ana.20036 · Cited by 33

Genome-wide analysis ofSaccharomyces cerevisiaeidentifies cellular processes affecting intracellular aggregation of Alzheimer's amyloid-β42: importance of lipid homeostasis

Nair, S., Traini, M. D., Dawes, I. W., & Perrone, G. G. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-04-0216 · Cited by 32

Contribution of Alanine-76 and Serine Phosphorylation inα-Synuclein Membrane Association and Aggregation in Yeasts

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

Cytosolic aggregates perturb the degradation of nontranslocated secretory and membrane proteins

Chakrabarti, O., Rane, N. S., & Hegde, R. S. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-07-0638 · Cited by 31

ERAD defects and the HFE-H63D variant are associated with increased risk of liver damages in Alpha 1-Antitrypsin Deficiency

Joly, P., Vignaud, H., Martino, J. S. D., Ruiz, M., Garin, R., Restier, L., Belmalih, A., Marchal, C., Cullin, C., Arveiler, B., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0179369 · Cited by 29

How to bake a brain: yeast as a model neuron

Sarto‐Jackson, I., & Tomáška, Ľ. (2016) · Current Genetics · doi:10.1007/s00294-015-0554-2 · Cited by 29

New Therapeutic Strategies for Cancer and Neurodegeneration Emerging from Yeast Cell-based Systems

Pereira, C., Leao, M., Soares, J., Bessa, C., & Saraiva, L. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212802430422 · Cited by 28

Modifiers and mechanisms of multi-system polyglutamine neurodegenerative disorders: lessons from fly models

Mallik, M., & Lakhotia, S. C. (2010) · Journal of Genetics · doi:10.1007/s12041-010-0072-4 · Cited by 27

Connecting environmental exposure and neurodegeneration using cheminformatics and high resolution mass spectrometry: potential and challenges

Schymanski, E., Baker, N., Williams, A. J., Singh, R. R., Trezzi, J., Wilmes, P., Kolber, P. L., Krüger, R., Paczia, N., Linster, C. L., et al. (2019) · Environmental Science Processes & Impacts · doi:10.1039/c9em00068b · Cited by 27

Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones

Gillies, A. T., Taylor, R. J., & Gestwicki, J. E. (2012) · Molecular BioSystems · doi:10.1039/c2mb25248a · Cited by 27

Linking amyloidprotein aggregation and yeast survival

Morell, M., de Groot, N. S., Vendrell, J., Avilés, F. X., & Ventura, S. (2011) · Molecular BioSystems · doi:10.1039/c0mb00297f · Cited by 27

Oxidative stress and neurodegeneration: the yeast model system

Breitenbach, M. (2013) · Frontiers in bioscience · doi:10.2741/4171 · Cited by 27

Evolution of Neurodegeneration

Cookson, M. (2012) · Current Biology · doi:10.1016/j.cub.2012.07.008 · Cited by 27

α - synuclein and Parkinson's disease: the first roadblock

Chua, C. E. L., & Tang, B. L. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00528.x · Cited by 27

Mechanisms of Disease II: Cellular Protein Quality Control

Outeiro, T. F., & Tetzlaff, J. E. (2007) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.11.005 · Cited by 27

Yeast genetic screen reveals novel therapeutic strategy for ALS

Figley, M. D., & Gitler, A. D. (2013) · Rare Diseases · doi:10.4161/rdis.24420 · Cited by 27

Ubiquitin-dependent proteolysis in yeast cells expressing neurotoxic proteins

Braun, R. J. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00008 · Cited by 26

DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization

Popova, B., Wang, D., Pätz, C., Akkermann, D., Lázaro, D. F., Gałka, D., Gulko, M. K., Bohnsack, M. T., Möbius, W., Bohnsack, K. E., et al. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009407 · Cited by 26

Yeast as a model to study protein misfolding in aged cells

Gregorio, S. E. D., & Duennwald, M. L. (2018) · FEMS Yeast Research · doi:10.1093/femsyr/foy054 · Cited by 25

Polyglutamine-Rich Suppressors of Huntingtin Toxicity Act Upstream of Hsp70 and Sti1 in Spatial Quality Control of Amyloid-Like Proteins

Wolfe, K. J., Ren, H. Y., Trepte, P., & Cyr, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095914 · Cited by 25

Ordered Assembly of Heat Shock Proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on Expanded Polyglutamine Fragments Revealed by Chemical Probes

Walter, G. M., Smith, M. C. P., Wisén, S., Basrur, V., Elenitoba‐Johnson, K. S. J., Duennwald, M. L., Kumar, A., & Gestwicki, J. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.284448 · Cited by 25

How Surrogate and Chemical Genetics in Model Organisms Can Suggest Therapies for Human Genetic Diseases

Strynatka, K. A., Gurrola-Gal, M. C., Berman, J. N., & McMaster, C. R. (2018) · Genetics · doi:10.1534/genetics.117.300124 · Cited by 25

Ca2+ homeostasis in the budding yeast Saccharomyces cerevisiae: Impact of ER/Golgi Ca2+ storage

D’hooge, P., Coun, C., Eyck, V. V., Faes, L., Ghillebert, R., Mariën, L., Winderickx, J., & Callewaert, G. (2015) · Cell Calcium · doi:10.1016/j.ceca.2015.05.004 · Cited by 25

α-Synuclein Decreases the Abundance of Proteasome Subunits and Alters Ubiquitin Conjugates in Yeast

Popova, B., Gałka, D., Häffner, N., Wang, D., Schmitt, K., Valerius, O., Knop, M., & Braus, G. H. (2021) · Cells · doi:10.3390/cells10092229 · Cited by 24

Protein Aggregation and Polyasparagine-Mediated Cellular Toxicity inSaccharomyces cerevisiae

Peters, T. W., & Huang, M. (2007) · Prion · doi:10.4161/pri.1.2.4630 · Cited by 24

A Saccharomyces cerevisiae strain unable to store neutral lipids is tolerant to oxidative stress induced by α-synuclein

Sere, Y. Y., Régnacq, M., Colas, J., & Bergès, T. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.007 · Cited by 24

Transient expression of human TorsinA enhances secretion of two functionally distinct proteins in cultured Chinese hamster ovary (CHO) cells

Jossé, L., Smales, C. M., & Tuite, M. F. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22572 · Cited by 24

University Licensing: Harnessing or Tarnishing Faculty Research?

Thursby, J. G., & Thursby, M. (2010) · Innovation Policy and the Economy · doi:10.1086/605856 · Cited by 24

Cell Surface Expression of the Prion Protein in Yeast Does Not Alter Copper Utilization Phenotypes

Li, A., Dong, J., & Harris, D. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402517200 · Cited by 24

Variant‐specific and reciprocal Hsp40 functions in Hsp104‐mediated prion elimination

Astor, M. T., Kamiya, E., Sporn, Z. A., Berger, S. E., & Hines, J. K. (2018) · Molecular Microbiology · doi:10.1111/mmi.13966 · Cited by 23

Modeling Parkinson’s Disease: Not Only Rodents?

Shadrina, M. I., & Slominsky, P. A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.695718 · Cited by 23

Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation

Popova, B., Wang, D., Rajavel, A., Dhamotharan, K., Lázaro, D. F., Gerke, J., Uhrig, J. F., Hoppert, M., Outeiro, T. F., & Braus, G. H. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.659926 · Cited by 23

Role of the ribosomal quality control machinery in nucleocytoplasmic translocation of polyQ-expanded huntingtin exon-1

Zheng, J., Yang, J., Choe, Y., Hao, X., Cao, X., Zhao, Q., Zhang, Y., Franssens, V., Hartl, F. U., Nyström, T., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.08.126 · Cited by 22

Proteomics-Based Monitoring of Pathway Activity Reveals that Blocking Diacylglycerol Biosynthesis Rescues from Alpha-Synuclein Toxicity

Soste, M., Charmpi, K., Lampert, F., Gerez, J., van Oostrum, M., Malinovska, L., Boersema, P. J., Prymaczok, N. C., Riek, R., Peter, M., et al. (2019) · Cell Systems · doi:10.1016/j.cels.2019.07.010 · Cited by 22

Screening for Toxic Amyloid in Yeast Exemplifies the Role of Alternative Pathway Responsible for Cytotoxicity

Couthouis, J., Rébora, K., Immel, F., Berthelot, K., Castroviejo, M., & Cullin, C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004539 · Cited by 22

Dual Functions of Heat Shock Proteins: Molecular Chaperones Inside of Cells and Danger Signals Outside of Cells

Ohtsuka, K., KAWASHIMA, D., & Asai, M. (2007) · Thermal Medicine(Japanese Journal of Hyperthermic Oncology) · doi:10.3191/thermalmedicine.23.11 · Cited by 22

Structural and functional properties of lengsin, a pseudo-glutamine synthetase in the transparent human lens

Grassi, F., Moretto, N., Rivetti, C., Cellai, S., Betti, M., Márquez, A. J., Maraini, G., & Ottonello, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.09.062 · Cited by 21

Transmembrane protein 85 from both human (TMEM85) and yeast (YGL231c) inhibit hydrogen peroxide mediated cell death in yeast

Ring, G., Khoury, C. M., Solar, A. J., Yang, Z., Mandato, C. A., & Greenwood, M. T. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.06.042 · Cited by 20

Peroxisomes of the Brain: Distribution, Functions, and Associated Diseases

Deb, R., Joshi, N., & Nagotu, S. (2021) · Neurotoxicity Research · doi:10.1007/s12640-020-00323-9 · Cited by 19

Modeling LRRK2 Pathobiology in Parkinson’s Disease: From Yeast to Rodents

Daniel, G., & Moore, D. J. (2014) · Current topics in behavioral neurosciences · doi:10.1007/7854_2014_311 · Cited by 19

Melatonin improves survival and respiratory activity of yeast cells challenged by alpha‐synuclein and menadione

Zampol, M. A., & de Barros, M. H. (2017) · Yeast · doi:10.1002/yea.3296 · Cited by 19

Modifier pathways in polyglutamine (PolyQ) diseases: from genetic screens to drug targets

Costa, M. D., & Maciel, P. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04280-8 · Cited by 19

Protein aggregation propensity is a crucial determinant of intracellular inclusion formation and quality control degradation

Villar‐Piqué, A., & Ventura, S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.023 · Cited by 19

Choosing and usingDrosophilamodels to characterize modifiers of Huntington's disease

Green, E. W., & Giorgini, F. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120072 · Cited by 19

Aggresome formation and segregation of inclusions influence toxicity of α-synuclein and synphilin-1 in yeast

Swinnen, E., Büttner, S., Outeiro, T. F., Galas, M., Madeo, F., Winderickx, J., & Franssens, V. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391476 · Cited by 19

Identification of Mammalian Protein Quality Control Factors by High-Throughput Cellular Imaging

Pegoraro, G., Voss, T. C., Martin, S. E., Tuzmen, P., Guha, R., & Misteli, T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031684 · Cited by 19

Sneaking Out for Happy Hour: Yeast-Based Approaches to Explore and Modulate Immune Response and Immune Evasion

Angrand, G., Quillévéré, A., Loaëc, N., Daskalogianni, C., Granzhan, A., Teulade‐Fichou, M., Fåhræus, R., Martins, R. P., & Blondel, M. (2019) · Genes · doi:10.3390/genes10090667 · Cited by 19

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species

Zhao, Y., Zurawel, A. A., Jenkins, N. P., Duennwald, M. L., Cheng, C., Kettenbach, A. N., & Supattapone, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-27900-5 · Cited by 18

Exploiting Post-mitotic Yeast Cultures to Model Neurodegeneration

Ruetenik, A., & Barrientos, A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00400 · Cited by 18

Binding between Prion Protein and Aβ Oligomers Contributes to the Pathogenesis of Alzheimer’s Disease

Kong, C., Xie, H., Gao, Z., Shao, M., Li, H., Shi, R., Cai, L., Gao, S., Sun, T., & Li, C. (2019) · Virologica Sinica · doi:10.1007/s12250-019-00124-1 · Cited by 18

Attenuation of polyglutamine-induced toxicity by enhancement of mitochondrial OXPHOS in yeast and fly models of aging

Ruetenik, A., Ocampo, A., Ruan, K., Zhu, Y., Li, C. V., Zhai, R. G., & Barrientos, A. (2016) · Microbial Cell · doi:10.15698/mic2016.08.518 · Cited by 18

Biophysical studies of protein misfolding and aggregation in in vivo models of Alzheimer's and Parkinson's diseases

Sinnige, T., Stroobants, K., Dobson, C. M., & Vendruscolo, M. (2020) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583520000025 · Cited by 18

Barcode technology in yeast: application to pharmacogenomics

Delneri, D. (2010) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2010.00676.x · Cited by 18

How and why do toxic conformers of aberrant proteins accumulate during ageing?

Josefson, R., Andersson, R., & Nyström, T. (2017) · Essays in Biochemistry · doi:10.1042/ebc20160085 · Cited by 17

Screening for Genetic Modifiers of Amyloid Toxicity in Yeast

Giorgini, F., & Muchowski, P. J. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)12013-3 · Cited by 17

New Approaches to the Pathology and Genetics of Neurodegeneration

Feany, M. Β. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.091077 · Cited by 17

Identification of small-molecule HSF1 amplifiers by high content screening in protection of cells from stress induced injury

Zhang, B., Au, Q., Yoon, I. S., Tremblay, M.-H., Yip, G., Zhou, Y., Barber, J. R., & Ng, S. C. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.079 · Cited by 17

1D-myo-inositol 3-phosphate synthase: conservation, regulation, and putative target of mood stabilizers

Ju, S., & Greenberg, M. L. (2004) · Clinical Neuroscience Research · doi:10.1016/j.cnr.2004.09.010 · Cited by 17

Impairment of lipid homeostasis causes lysosomal accumulation of endogenous protein aggregates through ESCRT disruptionPreprint

Yong, J., Villalta, J. E., Vu, N., Kukurugya, M. A., Olsson, N., López, M. P., Lazzari-Dean, J. R., Hake, K., McAllister, F. E., Bennett, B. D., et al. (2023) · eLife · doi:10.7554/elife.86194 · Cited by 17

α-Synuclein in traumatic and vascular diseases of the central nervous system

Zeng, H., Liu, N., Liu, X.-X., Yang, Y., & Zhou, M. (2020) · Aging · doi:10.18632/aging.103675 · Cited by 17

Lipid metabolism in Alzheimer’s and Parkinson’s disease

Xu, Q., & Huang, Y. (2006) · Future Lipidology · doi:10.2217/17460875.1.4.441 · Cited by 16

A central role for TOR signalling in a yeast model for juvenile CLN3 disease

Bond, M., Brown, R. E., Rallis, C., Bähler, J., & Mole, S. (2015) · Microbial Cell · doi:10.15698/mic2015.12.241 · Cited by 16

Genetic Manipulation of Palmitoylethanolamide Production and Inactivation in Saccharomyces cerevisiae

Muccioli, G. G., Sia, A., Muchowski, P. J., & Stella, N. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005942 · Cited by 16

Mechanisms and models of α-synuclein-related neurodegeneration

Springer, W., & Kahle, P. J. (2006) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-996-0025-8 · Cited by 16

Robust Sequence Determinants of α-Synuclein Toxicity in Yeast Implicate Membrane Binding

Newberry, R. W., Arhar, T., Costello, J. M., Hartoularos, G. C., Maxwell, A. M., Naing, Z. Z. C., Pittman, M., Reddy, N. R., Schwarz, D. M. C., Wassarman, D. R., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00339 · Cited by 15

Exploiting Yeast Genetics to Inform Therapeutic Strategies for Huntington’s Disease

Giorgini, F., & Muchowski, P. J. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-540-4_9 · Cited by 15

Mammalian ribosomal and chaperone protein RPS3A counteracts α-synuclein aggregation and toxicity in a yeast model system

Graeve, S. D., Marinelli, S., Stolz, F., Hendrix, J., Vandamme, J., Engelborghs, Y., Dijck, P. V., & Thevelein, J. M. (2013) · Biochemical Journal · doi:10.1042/bj20130417 · Cited by 15

Yeast as a model eukaryote in toxinology: A functional genomics approach to studying the molecular basis of action of pharmacologically active molecules

Ušaj, M. M., Petrovič, U., & Križaj, I. (2012) · Toxicon · doi:10.1016/j.toxicon.2012.03.014 · Cited by 15

Distinct gene expression profiles and reduced JNK signaling in retinitis pigmentosa caused by RP1 mutations

Liu, J., Huang, Q., Higdon, J., Liu, W., Xie, T., Yamashita, T., Cheon, K., Cheng, C., & Zuo, J. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi325 · Cited by 15

Protein aggregation and neurodegeneration

Mayo, K. J., & Cyr, D. (2011) · Methods · doi:10.1016/j.ymeth.2011.02.009 · Cited by 15

Biophysical studies of protein misfolding and aggregation in in vivo models of Alzheimer's and Parkinson's diseases – ERRATUM

Sinnige, T., Stroobants, K., Dobson, C. M., & Vendruscolo, M. (2020) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583520000104 · Cited by 15

Yeast as a Model to Unravel Mechanisms Behind FUS Toxicity in Amyotrophic Lateral Sclerosis

Lindström, M., & Liu, B. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00218 · Cited by 14

The toxicity of an “artificial” amyloid is related to how it interacts with membranes

Couthouis, J., Marchal, C., D’Angelo, F., Berthelot, K., & Cullin, C. (2010) · Prion · doi:10.4161/pri.4.4.13126 · Cited by 14

Modulation of mutant Huntingtin aggregates and toxicity by human myeloid leukemia factors

Banerjee, M., Datta, M., & Bhattacharyya, N. P. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.11.008 · Cited by 14

In the moonlight: non-catalytic functions of ubiquitin and ubiquitin-like proteases

Alonso, M. C., & Knobeloch, K. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1349509 · Cited by 13

α-Synuclein and neuronal membranes: Conformational flexibilities in health and disease

Bozelli, J. C., Kamski‐Hennekam, E. R., Melacini, G., & Epand, R. M. (2021) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2020.105034 · Cited by 13

A novel high-throughput yeast genetic screen for factors modifying protein levels of the Early-Onset Torsion Dystonia-associated variant torsinAΔE

Zacchi, L. F., Dittmar, J. C., Mihalevic, M. J., Shewan, A. M., Schulz, B. L., Brodsky, J. L., & Bernstein, K. A. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.029926 · Cited by 12

Yeast Phenomics: An Experimental Approach for Modeling Gene Interaction Networks that Buffer Disease

Hartman, J. L., Stisher, C., Outlaw, D. A., Guo, J., Shah, N. A., Tian, D., Santos, S. M., Rodgers, J. W., & White, R. (2015) · Genes · doi:10.3390/genes6010024 · Cited by 12

Experimental models of Huntington's disease

Raamsdonk, J. M. V., Hayden, M. R., & Leavitt, B. R. (2005) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2005.11.010 · Cited by 12

α-synuclein inhibits Snx3-retromer retrograde trafficking of the conserved membrane-bound proprotein convertase Kex2 in the secretory pathway of Saccharomyces cerevisiae

Rajasekaran, S., Peterson, P. P., Liu, Z., Robinson, L. C., & Witt, S. N. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab284 · Cited by 11

SUMO-Targeted Ubiquitin Ligases (STUbLs) Reduce the Toxicity and Abnormal Transcriptional Activity Associated With a Mutant, Aggregation-Prone Fragment of Huntingtin

Ohkuni, K., Pasupala, N., Peek, J. L., Holloway, G., Sclar, G. D., Levy-Myers, R., Baker, R. E., Basrai, M. A., & Kerscher, O. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00379 · Cited by 11

Bioprospection of Natural Sources of Polyphenols with Therapeutic Potential for Redox-Related Diseases

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