Protein Misfolding, Functional Amyloid, and Human Disease

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

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434

Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease

Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227

The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation

Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209

Rationalization of the effects of mutations on peptide andprotein aggregation rates

Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072

Amyloid β-Protein Fibrillogenesis

Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046

Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein

Giasson, B. I., Forman, M. S., Higuchi, M., Golbe, L. I., Graves, C. L., Kotzbauer, P. T., Trojanowski, J. Q., & Lee, V. M.-Y. (2003) · Science · doi:10.1126/science.1082324 · Cited by 879

Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model

Dodart, J.-C., Bales, K. R., Gannon, K. S., Greene, S. J., DeMattos, R. B., Mathis, C., DeLong, C. A., Wu, S., Wu, X., Holtzman, D. M., et al. (2002) · Nature Neuroscience · doi:10.1038/nn842 · Cited by 858

FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils

Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725

Molecular chaperones in protein folding and proteostasis

Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381

Inflammasomes: mechanism of action, role in disease, and therapeutics

Guo, H., Callaway, J. B., & Ting, J. P.-Y. (2015) · Nature Medicine · doi:10.1038/nm.3893 · Cited by 3,340

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629

The amyloid state and its association with protein misfolding diseases.

Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382

Cryo-EM structures of tau filaments from Alzheimer’s disease

Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061

Self-propagation of pathogenic protein aggregates in neurodegenerative diseases

Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663

The proteostasis network and its decline in ageing

Hipp, M. S., Kasturi, P., & Hartl, F. U. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0101-y · Cited by 1,642

The Biology of Proteostasis in Aging and Disease

Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472

The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis

Li, J., McQuade, T., Siemer, A. B., Napetschnig, J., Moriwaki, K., Hsiao, Y.-S., Damko, E., Moquin, D., Walz, T., McDermott, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.019 · Cited by 1,222

Superoxide dismutases and superoxide reductases

Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S. (2014) · Chemical Reviews · doi:10.1021/cr4005296 · Cited by 1,081

Misfolded proteins partition between two distinct quality control compartments

Kaganovich, D., Kopito, R., & Frydman, J. (2008) · Nature · doi:10.1038/nature07195 · Cited by 932

Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, A., Sandal, M., Clarke, R. W., Dunne, P., Aprile, F. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.037 · Cited by 911

Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging

Morimoto, R. I. (2008) · Genes & Development · doi:10.1101/gad.1657108 · Cited by 872

The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy

Sengupta, U., Nilson, A. N., & Kayed, R. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.03.035 · Cited by 740

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1750 · Cited by 661

Widespread protein aggregation as an inherent part of aging in C. elegans

David, D. C., Ollikainen, N., Trinidad, J. C., Cary, M. P., Burlingame, A. L., & Kenyon, C. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000450 · Cited by 627

Triggering of inflammasome by aggregated α-synuclein, an inflammatory response in synucleinopathies

Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., & de Bernard, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055375 · Cited by 585

Towards an understanding of amyloid-β oligomers: characterization, toxicity mechanisms, and inhibitors

Lee, S. J. C., Nam, E., Lee, H. J., Savelieff, M. G., & Lim, M. H. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00731g · Cited by 576

Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide

Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530

Modulators of Protein–Protein Interactions

Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497

The Transcellular Spread of Cytosolic Amyloids, Prions, and Prionoids

Aguzzi, A., & Rajendran, L. (2009) · Neuron · doi:10.1016/j.neuron.2009.12.016 · Cited by 473

Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation

Gsponer, J., Futschik, M. E., Teichmann, S. A., & Babu, M. M. (2008) · Science · doi:10.1126/science.1163581 · Cited by 466

The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system

Tai, H.-C., Serrano-Pozo, A., Hashimoto, T., Frosch, M. P., Spires-Jones, T. L., & Hyman, B. T. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.06.033 · Cited by 443

Fluorescence Correlation Spectroscopy: Past, Present, Future

Elson, E. L. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.11.012 · Cited by 438

Alpha-synuclein structure and Parkinson’s disease – lessons and emerging principles

Meade, R. M., Fairlie, D. P., & Mason, J. M. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0329-1 · Cited by 404

Neurodegenerative Diseases: Expanding the Prion Concept

Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361

Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering

Sandberg, A., Luheshi, L. M., Söllvander, S., Pereira de Barros, T., Macao, B., Knowles, T. P. J., Biverstål, H., Lendel, C., Ekholm-Petterson, F., Dubnovitsky, A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001740107 · Cited by 358

Prebiotic Peptides: Molecular Hubs in the Origin of Life

Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354

TopologyNet: Topology based deep convolutional and multi-task neural networks for biomolecular property predictions

Cang, Z., & Wei, G.-W. (2017) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1005690 · Cited by 330

Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

Escusa-Toret, S., Vonk, W. I. M., & Frydman, J. (2013) · Nature Cell Biology · doi:10.1038/ncb2838 · Cited by 321

Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins

Niwa, T., Ying, B.-W., Saito, K., Jin, W., Takada, S., Ueda, T., & Taguchi, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811922106 · Cited by 321

Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity

Friedrich, R. P., Tepper, K., Rönicke, R., Soom, M., Westermann, M., Reymann, K., Kaether, C., & Fändrich, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904532106 · Cited by 303

Activation of Microglia by Amyloid β Requires P2X7 Receptor Expression

Sanz, J. M., Chiozzi, P., Ferrari, D., Colaianna, M., Idzko, M., Falzoni, S., Fellin, R., Trabace, L., & Di Virgilio, F. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803612 · Cited by 293

The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments

Jeganathan, S., von Bergen, M., Mandelkow, E.-M., & Mandelkow, E. (2008) · Biochemistry · doi:10.1021/bi800783d · Cited by 286

Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins

Ciryam, P., Tartaglia, G. G., Morimoto, R. I., Dobson, C. M., & Vendruscolo, M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.043 · Cited by 270

Fuzzy Complexes: A More Stochastic View of Protein Function

Fuxreiter, M., & Tompa, P. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4614-0659-4_1 · Cited by 240

Phycobiliproteins: Structural aspects, functional characteristics, and biotechnological perspectives

Dagnino-Leone, J., Figueroa, C. P., Castañeda, M. L., Youlton, A. D., Vallejos-Almirall, A., Agurto-Muñoz, A., Pavón Pérez, J., & Agurto-Muñoz, C. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.02.016 · Cited by 234

The Amyloid Formation Mechanism in Human IAPP: Dimers Have β-Strand Monomer−Monomer Interfaces

Dupuis, N. F., Wu, C., Shea, J.-E., & Bowers, M. T. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1081537 · Cited by 216

Emerging New Concepts of Degrader Technologies

Ding, Y., Fei, Y., & Lu, B. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.04.005 · Cited by 204

Prediction of aggregation prone regions of therapeutic proteins

Chennamsetty, N., Voynov, V., Kayser, V., Helk, B., & Trout, B. L. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp911706q · Cited by 200

Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies

Wang, X., Das, T. K., Singh, S. K., & Kumar, S. (2009) · mAbs · doi:10.4161/mabs.1.3.8035 · Cited by 198

Tau Oligomers Impair Artificial Membrane Integrity and Cellular Viability

Flach, K., Hilbrich, I., Schiffmann, A., Gärtner, U., Krüger, M., Leonhardt, M., Waschipky, H., Wick, L., Arendt, T., & Holzer, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.396176 · Cited by 188

Insulin-Degrading Enzyme in the Fight against Alzheimer's Disease

Kurochkin, I. V., Guarnera, E., & Berezovsky, I. N. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.10.008 · Cited by 185

Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein

Pirchi, M., Ziv, G., Riven, I., Cohen, S. S., Zohar, N., Barak, Y., & Haran, G. (2011) · Nature Communications · doi:10.1038/ncomms1504 · Cited by 179

Nonhuman Primate Models of Alzheimer-Like Cerebral Proteopathy

Heuer, E., F. Rosen, R., Cintron, A., & C. Walker, L. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799315885 · Cited by 169

Aggregation of Copper–Zinc Superoxide Dismutase in Familial and Sporadic ALS

Chattopadhyay, M., & Valentine, J. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2536 · Cited by 163

Identification of Oxa1 homologs operating in the eukaryotic endoplasmic reticulum.

Anghel, S. A., McGilvray, P. T., Hegde, R. S., & Keenan, R. J. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.12.006 · Cited by 150

Phycocyanin: Anti-inflammatory effect and mechanism

Liu, R., Qin, S., & Li, W. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113362 · Cited by 157

Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson’s Disease

Tóth, G., Gardai, S. J., Zago, W., Bertoncini, C. W., Cremades, N., Roy, S. L., Tambe, M. A., Rochet, J.-C., Galvagnion, C., Skibinski, G., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087133 · Cited by 151

Identification of an Aggregation-Prone Structure of Tau

Elbaum-Garfinkle, S., & Rhoades, E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305206m · Cited by 149

Islet amyloid polypeptide toxicity and membrane interactions

Cao, P., Abedini, A., Wang, H., Tu, L.-H., Zhang, X., Schmidt, A. M., & Raleigh, D. P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305517110 · Cited by 146

Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity

Wilson, M. R., Yerbury, J. J., & Poon, S. (2007) · Molecular BioSystems · doi:10.1039/b712728f · Cited by 142

Identification of MOAG-4/SERF as a regulator of age-related proteotoxicity

van Ham, T. J., Holmberg, M. A., van der Goot, A. T., Teuling, E., Garcia-Arencibia, M., Kim, H.-E., Du, D., Thijssen, K. L., Wiersma, M., Burggraaff, R., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.020 · Cited by 133

Biophysical Insights into How Surfaces, Including Lipid Membranes, Modulate Protein Aggregation Related to Neurodegeneration

Burke, K. A., Yates, E. A., & Legleiter, J. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00017 · Cited by 127

In vivo rate-determining steps of tau seed accumulation in Alzheimer’s disease

Meisl, G., Hidari, E., Allinson, K., Rittman, T., DeVos, S. L., Sanchez, J. S., Xu, C. K., Duff, K. E., Johnson, K. A., Rowe, J. B., et al. (2021) · Science Advances · doi:10.1126/sciadv.abh1448 · Cited by 127

The potential therapeutic effects of THC on Alzheimer’s disease

Cao, C., Li, Y., Liu, H., Bai, G., Mayl, J., Lin, X., Sutherland, K., Nabar, N., & Cai, J. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140093 · Cited by 121

Thermodynamic forces from protein and water govern condensate formation of an intrinsically disordered protein domain

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Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters

Xue, W.-F., Hellewell, A. L., Hewitt, E. W., & Radford, S. E. (2010) · Prion · doi:10.4161/pri.4.1.11378 · Cited by 117

Multiscale multiphysics and multidomain models—Flexibility and rigidity

Xia, K., Opron, K., & Wei, G.-W. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4830404 · Cited by 88

Functional amyloids in Streptococcus mutans, their use as targets of biofilm inhibition and initial characterization of SMU_63c

Besingi, R. N., Wenderska, I. B., Senadheera, D. B., Cvitkovitch, D. G., Long, J. R., Wen, Z. T., & Brady, L. J. (2017) · Microbiology · doi:10.1099/mic.0.000443 · Cited by 99

Age-Related Oxidative Stress Compromises Endosomal Proteostasis

Cannizzo, E. S., Clement, C. C., Morozova, K., Valdor, R., Kaushik, S., Almeida, L. N., Follo, C., Sahu, R., Cuervo, A. M., Macian, F., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.06.005 · Cited by 95

Concerted Perturbation Observed in a Hub Network in Alzheimer’s Disease

Liang, D., Han, G., Feng, X., Sun, J., Duan, Y., & Lei, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040498 · Cited by 93

Extensive accumulation of misfolded protein aggregates during natural aging and senescence

Cuanalo-Contreras, K., Schulz, J., Mukherjee, A., Park, K.-W., Armijo, E., & Soto, C. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1090109 · Cited by 92

Pathogenic mechanisms of prion protein, amyloid-β and α-synuclein misfolding: the prion concept and neurotoxicity of protein oligomers

Ugalde, C. L., Finkelstein, D. I., Lawson, V. A., & Hill, A. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13772 · Cited by 92

SOLart: a structure-based method to predict protein solubility and aggregation

Hou, Q., Kwasigroch, J. M., Rooman, M., & Pucci, F. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btz773 · Cited by 86

Amyloid β: one of three danger‐associated molecules that are secondary inducers of the proinflammatory cytokines that mediate Alzheimer's disease

Clark, I. A., & Vissel, B. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13181 · Cited by 84

Microbial functional amyloids serve diverse purposes for structure, adhesion and defence

Shanmugam, N., Baker, M. O. D. G., Ball, S. R., Steain, M., Pham, C. L. L., & Sunde, M. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00526-1 · Cited by 75

Liquid-liquid phase transitions and amyloid aggregation in proteins related to cancer and neurodegenerative diseases

(2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.08.002 · Cited by 78

Proteins behaving badly: emerging technologies in profiling biopharmaceutical aggregation

Hamrang, Z., Rattray, N. J. W., & Pluen, A. (2013) · Trends in Biotechnology · doi:10.1016/j.tibtech.2013.05.004 · Cited by 75

A relationship between mRNA expression levels and protein solubility in E. coli

Tartaglia, G. G., Pechmann, S., Dobson, C. M., & Vendruscolo, M. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.03.002 · Cited by 63

The A53T Mutation is Key in Defining the Differences in the Aggregation Kinetics of Human and Mouse α-Synuclein

Kang, L., Wu, K.-P., Vendruscolo, M., & Baum, J. (2011) · Journal of the American Chemical Society · doi:10.1021/ja203979j · Cited by 65

Reversible and irreversible unfolding of multi-domain proteins

Strucksberg, K. H., Rosenkranz, T., & Fitter, J. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.09.005 · Cited by 55

Evolutionarily conserved regulators of tau identify targets for new therapies

Kim, J., de Haro, M., Al-Ramahi, I., Garaicoechea, L. L., Jeong, H.-H., Sonn, J. Y., Tadros, B., Liu, Z., Botas, J., & Zoghbi, H. Y. (2023) · Neuron · doi:10.1016/j.neuron.2022.12.012 · Cited by 50

Order, Disorder, and Reorder State of Lysozyme: Aggregation Mechanism by Raman Spectroscopy

Dolui, S., Mondal, A., Roy, A., Pal, U., Das, S., Saha, A., & Maiti, N. C. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b09139 · Cited by 48

Design of amyloidogenic peptide traps

Sahtoe, D. D., Andrzejewska, E. A., Han, H. L., Rennella, E., Schneider, M. M., Meisl, G., Ahlrichs, M., Decarreau, J., Nguyen, H., Kang, A., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01578-5 · Cited by 48

Production of lysozyme nanofibers using deep eutectic solvent aqueous solutions

Silva, N. H. C. S., Pinto, R. J. B., Freire, C. S. R., & Marrucho, I. M. (2016) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2016.07.005 · Cited by 47

Seizures are a druggable mechanistic link between TBI and subsequent tauopathy.

Alyenbaawi, H., Kanyo, R., Locskai, L. F., Kamali-Jamil, R., DuVal, M. G., Bai, Q., Wille, H., Burton, E. A., & Allison, W. T. (2021) · eLife · doi:10.7554/elife.58744 · Cited by 40

Nanotechnological approaches for targeting amyloid-β aggregation with potential for neurodegenerative disease therapy and diagnosis

Shukla, R., Singh, A., Handa, M., Flora, S. J. S., & Kesharwani, P. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.04.011 · Cited by 40

C-Phycocyanin from Spirulina Inhibits α-Synuclein and Amyloid-β Fibril Formation but Not Amorphous Aggregation

Liu, Y., Jovcevski, B., & Pukala, T. L. (2019) · Journal of Natural Products · doi:10.1021/acs.jnatprod.8b00610 · Cited by 39

C1R mutations trigger constitutive complement 1 activation in periodontal Ehlers-Danlos syndrome

Gröbner, R., Kapferer-Seebacher, I., Amberger, A., Redolfi, R., Dalonneau, F., Björck, E., Milnes, D., Bally, I., Rossi, V., Thielens, N., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02537 · Cited by 35

Does Intrinsic Disorder in Proteins Favor Their Interaction with Lipids?

Deryusheva, E., Nemashkalova, E., Galloux, M., Richard, C., Eléouët, J., Kovacs, D., Van Belle, K., Tompa, P., Uversky, V., & Permyakov, S. (2019) · PROTEOMICS · doi:10.1002/pmic.201800098 · Cited by 34

Heterogeneity in α-synuclein fibril activity correlates to disease phenotypes in Lewy body dementia

Sokratian, A., Ziaee, J., Kelly, K., Chang, A., Bryant, N., Wang, S., Xu, E., Li, J. Y., Wang, S.-H., Ervin, J., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02288-1 · Cited by 34

The Cytotoxicity and Clearance of Mutant Huntingtin and Other Misfolded Proteins

Folger, A., & Wang, Y. (2021) · Cells · doi:10.3390/cells10112835 · Cited by 32

Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A

Göbl, C., Morris, V. K., van Dam, L., Visscher, M., Polderman, P. E., Hartlmüller, C., de Ruiter, H., Hora, M., Liesinger, L., Birner-Gruenberger, R., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2019.101316 · Cited by 29

Evaluation of capillary electrophoresis-mass spectrometry for the analysis of the conformational heterogeneity of intact proteins using beta2-microglobulin as model compound

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EMBER multidimensional spectral microscopy enables quantitative determination of disease- and cell-specific amyloid strains

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