Biosensing strategies for amyloid‐like protein aggregates

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576 · see citing works

The amyloid hypothesis of Alzheimer's disease at 25 years

Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164 · see citing works

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 · see citing works

Gut microbiota regulate motor deficits and neuroinflammation in a model of Parkinson's disease

Sampson, T. R., Debelius, J. W., Thron, T., Janssen, S., Shastri, G. G., Ilhan, Z. E., Challis, C., Schretter, C. E., Rocha, S., Gradinaru, V., et al. (2016) · Cell · doi:10.1016/j.cell.2016.11.018 · Cited by 3,622 · see citing works

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927 · see citing works

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 · see citing works

Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

Cohen, S. I. A., Linse, S. S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218402110 · Cited by 1,410 · see citing works

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 · see citing works

Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response

Riback, J. A., Katanski, C. D., Kear‐Scott, J. L., Pilipenko, E. V., Rojek, A. E., Sosnick, T. R., & Drummond, D. A. (2017) · Cell · doi:10.1016/j.cell.2017.02.027 · Cited by 913 · see citing works

Detection of oligomeric forms of α‐synuclein protein in human plasma as a potential biomarker for Parkinson's disease

El‐Agnaf, O. M. A., Salem, S. A., Paleologou, K. E., Curran, M. D., Gibson, M. J., Court, J. A., Schlossmacher, M. G., & Allsop, D. (2006) · The FASEB Journal · doi:10.1096/fj.03-1449com · Cited by 715 · see citing works

Ultrasensitive human prion detection in cerebrospinal fluid by real-time quaking-induced conversion

Atarashi, R., Satoh, K., Sano, K., Fuse, T., Yamaguchi, N., Ishibashi, D., Matsubara, T., Nakagaki, T., Yamanaka, H., Shirabe, S., et al. (2011) · Nature Medicine · doi:10.1038/nm.2294 · Cited by 655 · see citing works

Antifouling Strategies for Selective In Vitro and In Vivo Sensing

Jiang, C., Wang, G., Hein, R., Liu, N., Luo, X., & Davis, J. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00739 · Cited by 601 · see citing works

Probing cellular protein complexes using single-molecule pull-down

Jain, A., Liu, R., Ramani, B., Arauz, E. J., Ishitsuka, Y., Ragunathan, K., Park, J., Chen, J., Xiang, Y. K., & Ha, T. (2011) · Nature · doi:10.1038/nature10016 · Cited by 429 · see citing works

Eukaryotic Proteasomes Cannot Digest Polyglutamine Sequences and Release Them during Degradation of Polyglutamine-Containing Proteins

Venkatraman, P., Wetzel, R. B., Tanaka, M., Nukina, N., & Goldberg, A. L. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00151-0 · Cited by 424 · see citing works

Senile Systemic Amyloidosis: Clinical Features at Presentation and Outcome

Pinney, J. H., Whelan, C. J., Petrie, A., Dungu, J. N., Banypersad, S. M., Sattianayagam, P. T., Wechalekar, A. D., Gibbs, S. D., Venner, C. P., Wassef, N., et al. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000098 · Cited by 372 · see citing works

Alpha-synuclein oligomers: a new hope

Bengoa‐Vergniory, N., Roberts, R. F., Wade‐Martins, R., & Alegre‐Abarrategui, J. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1755-1 · Cited by 335 · see citing works

Detection of α-synuclein in CSF by RT-QuIC in patients with isolated rapid-eye-movement sleep behaviour disorder: a longitudinal observational study

Iranzo, Á., Fairfoul, G., Ayudhaya, A. C. N., Serradell, M., Gelpí, E., Vilaseca, I., Sánchez‐Valle, R., Gaig, C., Santamaría, J., Tolosa, E. S., et al. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30449-x · Cited by 335 · see citing works

Interrogating Amyloid Aggregates using Fluorescent Probes

Aliyan, A., Cook, N. P., & Martı́, A. A. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00404 · Cited by 295 · see citing works

Oligomeric and phosphorylated alpha-synuclein as potential CSF biomarkers for Parkinson’s disease

Majbour, N. K., Vaikath, N. N., van Dijk, K. D., Ardah, M. T., Varghese, S., Vesterager, L. B., Montezinho, L. P., Poole, S., Safieh‐Garabedian, B., Tokuda, T., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0072-9 · Cited by 279 · see citing works

Serum neuronal exosomes predict and differentiate Parkinson’s disease from atypical parkinsonism

Jiang, C., Hopfner, F., Katsikoudi, A., Hein, R., Catli, C., Evetts, S. G., Huang, Y., Wang, H., Ryder, J. W., Kuhlenbäeumer, G., et al. (2020) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2019-322588 · Cited by 279 · see citing works

Impact of Anti-amyloid-β Monoclonal Antibodies on the Pathology and Clinical Profile of Alzheimer’s Disease: A Focus on Aducanumab and Lecanemab

Shi, M., Chu, F., Zhu, F., & Zhu, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.870517 · Cited by 275 · see citing works

Molecular biomarkers of Alzheimer's disease: progress and prospects

Lashley, T., Schott, J. M., Weston, P. S. J., Murray, C. E., Wellington, H., Keshavan, A., Foti, S. C., Foiani, M. S., Toombs, J., Rohrer, J. D., et al. (2018) · Disease Models & Mechanisms · doi:10.1242/dmm.031781 · Cited by 233 · see citing works

Presymptomatic Detection of Prions in Blood

Saá, P., Castilla, J., & Soto, C. A. (2006) · Science · doi:10.1126/science.1129051 · Cited by 231 · see citing works

Microfluidic Distance Readout Sweet Hydrogel Integrated Paper-Based Analytical Device (μDiSH-PAD) for Visual Quantitative Point-of-Care Testing

Wei, X., Tian, T., Jia, S., Zhu, Z., Ma, Y., Sun, J., Lin, Z., & Yang, C. J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04294 · Cited by 210 · see citing works

A label-free electrical impedimetric biosensor for the specific detection of Alzheimer's amyloid-beta oligomers

Rushworth, J. V., Ahmed, A., Jarosz-Griffiths, H., Pollock, N. M., Hooper, N. M., & Millner, P. A. (2013) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2013.12.036 · Cited by 196 · see citing works

Cyclic amplification of protein misfolding: application to prion-related disorders and beyond

Soto, C. A., Saborı́o, G. P., & Anderes, L. (2002) · Trends in Neurosciences · doi:10.1016/s0166-2236(02)02195-1 · Cited by 189 · see citing works

Amyloid formation as a protein phase transition

Michaels, T. C. T., Qian, D., Šarić, A., Vendruscolo, M., Linse, S. S., & Knowles, T. P. J. (2023) · Nature Reviews Physics · doi:10.1038/s42254-023-00598-9 · Cited by 163 · see citing works

Oligomeric forms of amyloid-β protein in plasma as a potential blood-based biomarker for Alzheimer’s disease

Wang, M. J., Yi, S., Han, J.-Y., Park, Y. H., Jang, J., Chun, I. K., Kim, S. E., Lee, B. S., Kim, G. J., Yu, J. S., et al. (2017) · Alzheimer s Research & Therapy · doi:10.1186/s13195-017-0324-0 · Cited by 152 · see citing works

Detection of α-synuclein oligomers in red blood cells as a potential biomarker of Parkinson’s disease

Wang, X., Yu, S., Li, F., & Feng, T. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.05.030 · Cited by 148 · see citing works

Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins

Sormanni, P., Aprile, F. A., & Vendruscolo, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422401112 · Cited by 145 · see citing works

Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method

Aprile, F. A., Sormanni, P., Perni, M., Arosio, P., Linse, S. S., Knowles, T. P. J., Dobson, C. M., & Vendruscolo, M. (2017) · Science Advances · doi:10.1126/sciadv.1700488 · Cited by 140 · see citing works

Exosomal DNA Aptamer Targeting α-Synuclein Aggregates Reduced Neuropathological Deficits in a Mouse Parkinson’s Disease Model

Ren, X., Zhao, Y., Xue, F., Zheng, Y., Huang, H., Wang, W., Chang, Y., Yang, H., & Zhang, J. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.07.008 · Cited by 139 · see citing works

p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis

Ghosh, S., Salot, S., Sengupta, S., Navalkar, A., Ghosh, D., Jacob, R. S., Das, S., Kumar, R., Jha, N. N., Sahay, S., et al. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.105 · Cited by 136 · see citing works

Third generation antibody discovery methods: in silico rational design

Sormanni, P., Aprile, F. A., & Vendruscolo, M. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00523k · Cited by 136 · see citing works

Tau Oligomers Neurotoxicity

Niewiadomska, G., Niewiadomski, W., Steczkowska, M., & Gąsiorowska, A. (2021) · Life · doi:10.3390/life11010028 · Cited by 132 · see citing works

Liquid-liquid Phase Separation of α-Synuclein: A New Mechanistic Insight for α-Synuclein Aggregation Associated with Parkinson's Disease Pathogenesis

Mukherjee, S., Sakunthala, A., Gadhe, L. G., Poudyal, M., Sawner, A. S., Kadu, P., & Maji, S. K. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167713 · Cited by 129 · see citing works

Photomodulating Carbon Dots for Spatiotemporal Suppression of Alzheimer’s β-Amyloid Aggregation

Chung, Y. J., Lee, C. H., Lim, J., Jang, J., Kang, H., & Park, C. B. (2020) · ACS Nano · doi:10.1021/acsnano.0c06078 · Cited by 125 · see citing works

Validation of α‐Synuclein in L1CAM ‐Immunocaptured Exosomes as a Biomarker for the Stratification of Parkinsonian Syndromes

Jiang, C., Hopfner, F., Berg, D., Hu, M. T., Pilotto, A., Borroni, B., Davis, J. J., & Tofaris, G. K. (2021) · Movement Disorders · doi:10.1002/mds.28591 · Cited by 124 · see citing works

Visual and fluorescent assays for selective detection of beta-amyloid oligomers based on the inner filter effect of gold nanoparticles on the fluorescence of CdTe quantum dots

Xia, N., Zhou, B., Huang, N., Jiang, M., Zhang, J., & Liu, L. (2016) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2016.05.066 · Cited by 118 · see citing works

Ferrocene-Encapsulated Zn Zeolitic Imidazole Framework (ZIF-8) for Optical and Electrochemical Sensing of Amyloid-β Oligomers and for the Early Diagnosis of Alzheimer’s Disease

Qin, J., Cho, M., & Lee, Y. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.8b21425 · Cited by 114 · see citing works

Fabrication of an antibody-aptamer sandwich assay for electrochemical evaluation of levels of β-amyloid oligomers

Zhou, Y., Zhang, H., Liu, L., Li, C., Chang, Z., Zhu, X., Ye, B., & Xu, M. (2016) · Scientific Reports · doi:10.1038/srep35186 · Cited by 106 · see citing works

Aptasensors for the selective detection of alpha-synuclein oligomer by colorimetry, surface plasmon resonance and electrochemical impedance spectroscopy

Sun, K., Xia, N., Zhao, L., Liu, K., Hou, W., & Liu, L. (2017) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2017.01.171 · Cited by 104 · see citing works

A novel electrochemical aptasensor based on nontarget-induced high accumulation of methylene blue on the surface of electrode for sensing of α-synuclein oligomer

Taghdisi, S. M., Danesh, N. M., Nameghi, M. A., Ramezani, M., Alibolandi, M., Hassanzadeh-Khayat, M., Emrani, A. S., & Abnous, K. (2018) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2018.09.081 · Cited by 102 · see citing works

Preparation of near-infrared AIEgen-active fluorescent probes for mapping amyloid-β plaques in brain tissues and living mice

Yan, C., Dai, J., Yao, Y., Fu, W., Tian, H., Zhu, W., & Guo, Z. (2023) · Nature Protocols · doi:10.1038/s41596-022-00789-1 · Cited by 100 · see citing works

A General Way to Assay Protein by Coupling Peptide with Signal Reporter via Supermolecule Formation

Li, H., Xie, H., Cao, Y., Ding, X., Yin, Y., & Li, G. (2012) · Analytical Chemistry · doi:10.1021/ac302906c · Cited by 98 · see citing works

Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at neutral pH

Dada, S., Hardenberg, M. C., Toprakcioglu, Z., Mrugalla, L. K., Cali, M. P., McKeon, M. O., Klimont, E., Michaels, T. C. T., Knowles, T. P. J., & Vendruscolo, M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208792120 · Cited by 95 · see citing works

Small molecule probes of protein aggregation

Young, L. M., Ashcroft, A. E., & Radford, S. E. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.06.008 · Cited by 93 · see citing works

Multiplexed Profiling of Extracellular Vesicles for Biomarker Development

Jiang, C., Fu, Y., Liu, G., Shu, B., Davis, J. J., & Tofaris, G. K. (2021) · Nano-Micro Letters · doi:10.1007/s40820-021-00753-w · Cited by 92 · see citing works

Artificial intelligence–coupled plasmonic infrared sensor for detection of structural protein biomarkers in neurodegenerative diseases

Kavungal, D., Magalhães, P., Kumar, S. T., Rajasekhar, K., Lashuel, H. A., & Altug, H. (2023) · Science Advances · doi:10.1126/sciadv.adg9644 · Cited by 91 · see citing works

Are We Ready for Detecting α-Synuclein Prone to Aggregation in Patients? The Case of “Protein-Misfolding Cyclic Amplification” and “Real-Time Quaking-Induced Conversion” as Diagnostic Tools

Paciotti, S., Bellomo, G., Gatticchi, L., & Parnetti, L. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00415 · Cited by 89 · see citing works

Quartz Crystal Microbalance With Dissipation Monitoring: A Powerful Method to Predict the in vivo Behavior of Bioengineered Surfaces

Tonda‐Turo, C., Carmagnola, I., & Ciardelli, G. (2018) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2018.00158 · Cited by 88 · see citing works

Detection of oligomers and fibrils of α-synuclein by AIEgen with strong fluorescence

Leung, C. W. T., Guo, F., Hong, Y., Zhao, E., Kwok, R. T. K., Leung, N. L. C., Chen, S., Vaikath, N. N., El‐Agnaf, O. M. A., Tang, Y., et al. (2014) · Chemical Communications · doi:10.1039/c4cc07911f · Cited by 83 · see citing works

Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein Aggregates

Flagmeier, P., De, S., Wirthensohn, D. C., Lee, S. F., Vincke, C., Muyldermans, S., Knowles, T. P. J., Gandhi, S., Dobson, C. M., & Klenerman, D. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201700966 · Cited by 79 · see citing works

Cofilin 1 promotes the pathogenicity and transmission of pathological α-synuclein in mouse models of Parkinson’s disease

Yan, M., Xiong, M., Dai, L., Zhang, X., Zha, Y., Deng, X., Yu, Z., & Zhang, Z. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-021-00272-w · Cited by 78 · see citing works

Small Molecule Fluorescent Probes for the Detection of Amyloid Self-Assembly In Vitro and In Vivo

Bertoncini, C. W., & Celej, M. S. (2011) · Current Protein and Peptide Science · doi:10.2174/138920311795860151 · Cited by 77 · see citing works

Tau oligomers in cerebrospinal fluid in Alzheimer's disease

Sengupta, U., Portelius, E., Hansson, O., Farmer, K., Castillo‐Carranza, D., Woltjer, R., Zetterberg, H., Galasko, D., Blennow, K., & Kayed, R. (2017) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.382 · Cited by 77 · see citing works

ELISA method to detect α-synuclein oligomers in cell and animal models

Lassen, L. B., Gregersen, E., Isager, A. K., Betzer, C., Kofoed, R. H., & Jensen, P. H. (2018) · PLoS ONE · doi:10.1371/journal.pone.0196056 · Cited by 75 · see citing works

Facile Impedimetric Analysis of Neuronal Exosome Markers in Parkinson’s Disease Diagnostics

Fu, Y., Jiang, C., Tofaris, G. K., & Davis, J. J. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c03092 · Cited by 74 · see citing works

Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer’s disease

Sideris, D. I., Danial, J. S. H., Emin, D., Ruggeri, F. S., Xia, Z., Zhang, Y. P., Lobanova, E., Dakin, H., De, S., Miller, A., et al. (2021) · Brain Communications · doi:10.1093/braincomms/fcab147 · Cited by 71 · see citing works

C/EBPβ/AEP is age-dependently activated in Parkinson’s disease and mediates α-synuclein in the gut and brain

Wang, H., Chen, G., Ahn, E. H., Xia, Y., Kang, S. S., Liu, X., Liu, C., Han, M.-H., Chen, S., & Ye, K. (2023) · npj Parkinson's Disease · doi:10.1038/s41531-022-00430-8 · Cited by 71 · see citing works

Determination of β-amyloid oligomer using electrochemiluminescent aptasensor with signal enhancement by AuNP/MOF nanocomposite

Yin, L., Wang, Y., Tan, R., Li, H., & Tu, Y. (2021) · Microchimica Acta · doi:10.1007/s00604-021-04710-7 · Cited by 70 · see citing works

Strategic Design of Amyloid-β Species Fluorescent Probes for Alzheimer’s Disease

Su, D., Diao, W., Li, J., Pan, L., Zhang, X., Wu, X., & Mao, W. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00810 · Cited by 63 · see citing works

An electrochemical aptasensor based on AuPt alloy nanoparticles for ultrasensitive detection of amyloid-β oligomers

Liu, Y., Xu, Q., Zhang, Y., Ren, B., Huang, L., Cai, H., Xu, T., Liu, Q., & Zhang, X. (2021) · Talanta · doi:10.1016/j.talanta.2021.122360 · Cited by 59 · see citing works

Self-Assembling NanoLuc Luciferase Fragments as Probes for Protein Aggregation in Living Cells

Zhao, J., Nelson, T. J., Vu, Q. V., Truong, T. A., & Stains, C. I. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00758 · Cited by 58 · see citing works

Protein amyloid aggregate: Structure and function

Xu, Q., Ma, Y., Sun, Y., Li, D., Zhang, X., & Liu, C. (2023) · Aggregate · doi:10.1002/agt2.333 · Cited by 56 · see citing works

Integrating terahertz metamaterial and water nanodroplets for ultrasensitive detection of amyloid β aggregates in liquids

Tang, C., Yang, J., Wang, Y., Cheng, J., Li, X., Chang, C., Hu, J., & Lü, J. (2020) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2020.129113 · Cited by 55 · see citing works

Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution

Awasthi, S., Ying, C., Li, J., & Mayer, M. (2023) · ACS Nano · doi:10.1021/acsnano.3c01393 · Cited by 54 · see citing works

Plasma alpha‐synuclein detected by single molecule array is increased in <scp>PD</scp>

Ng, A. S. L., Tan, Y. J., Lu, Z., Ng, E. Y. L., Ng, S. Y. E., Chia, N. S. Y., Setiawan, F., Xu, Z., Tay, K. Y., Prakash, K. M., et al. (2019) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.729 · Cited by 53 · see citing works

Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells

Whiten, D. R., Zuo, Y., Calò, L., Choi, M. L., De, S., Flagmeier, P., Wirthensohn, D. C., Kundel, F., Ranasinghe, R. T., Sanchez, S. E., et al. (2018) · ChemBioChem · doi:10.1002/cbic.201800209 · Cited by 50 · see citing works

An Electrochemical Immunosensor Based on a Self-Assembled Monolayer Modified Electrode for Label-Free Detection of α-Synuclein

Ge, C., Rahman, M. M., Zhang, W., Lopa, N. S., Jin, L., Yoon, S., Jang, H., Xu, G., & Kim, W. (2020) · Sensors · doi:10.3390/s20030617 · Cited by 47 · see citing works

A Maleimide‐functionalized Tetraphenylethene for Measuring and Imaging Unfolded Proteins in Cells

Zhang, S., Liu, M., Tan, L. Y. F., Hong, Q., Pow, Z. L., Owyong, T. C., Ding, S., Wong, W. W. H., & Hong, Y. (2019) · Chemistry - An Asian Journal · doi:10.1002/asia.201900150 · Cited by 45 · see citing works

Strategies To Achieve Control over the Surface Ratio of Two Different Components on Modified Electrodes Using Aryldiazonium Salts

Jiang, C., Alam, M. T., Parker, S. G., Darwish, N. A., & Gooding, J. J. (2016) · Langmuir · doi:10.1021/acs.langmuir.5b04550 · Cited by 43 · see citing works

Cerebrospinal α‐Synuclein Oligomers Reflect Disease Motor Severity in DeNoPa Longitudinal Cohort

Majbour, N. K., Abdi, I. Y., Dakna, M., Wicke, T., Lang, E., Moussa, H. Y. A., Thomas, M. A., Trenkwalder, C., Safieh‐Garabedian, B., Tokuda, T., et al. (2021) · Movement Disorders · doi:10.1002/mds.28611 · Cited by 43 · see citing works

Biofunctionalized Silica Nanoparticles: Standards in Amyloid-β Oligomer-Based Diagnosis of Alzheimer’s Disease

Hülsemann, M., Zafiu, C., Kühbach, K., Lühmann, N., Herrmann, Y., Peters, L., Linnartz, C., Willbold, J., Kravchenko, K., Kulawik, A., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160253 · Cited by 43 · see citing works

EGFR detection in extracellular vesicles of breast cancer patients through immunosensor based on silica-chitosan nanoplatform

Ortega, F. G., Piguillem, S. V., Messina, G. A., Tortella, G., Rubilar, O., Castillo, M. I. J., Lorente, J. A., Serrano, M. J., Raba, J., & Fernández‐Baldo, M. A. (2018) · Talanta · doi:10.1016/j.talanta.2018.10.016 · Cited by 42 · see citing works

SARS‐CoV‐2 nucleocapsid protein interacts with immunoregulators and stress granules and phase separates to form liquid droplets

Somasekharan, S. P., & Gleave, M. E. (2021) · FEBS Letters · doi:10.1002/1873-3468.14229 · Cited by 41 · see citing works

Fibrinogen alpha amyloidosis: insights from proteomics

Chapman, J. R., & Doǧan, A. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1659137 · Cited by 40 · see citing works

Alternating Magnetic Field-Promoted Nanoparticle Mixing: The On-Chip Immunocapture of Serum Neuronal Exosomes for Parkinson’s Disease Diagnostics

Sharafeldin, M., Yan, S., Jiang, C., Tofaris, G. K., & Davis, J. J. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c00357 · Cited by 40 · see citing works

Detection of Prion Protein Particles in Blood Plasma of Scrapie Infected Sheep

Bannach, O., Birkmann, E., Reinartz, E., Jaeger, K., Langeveld, J., Rohwer, R. G., Gregori, L. L., Terry, L. A., Willbold, D., & Riesner, D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036620 · Cited by 40 · see citing works

Exploring Interactions of Aptamers with Aβ40 Amyloid Aggregates and Its Application: Detection of Amyloid Aggregates

Zheng, Y., Geng, X., Yang, X., Li, S., Liu, Y., Liu, X., Wang, Q., Wang, K., Jia, R., & Yao, X. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05493 · Cited by 40 · see citing works

Progranulin in neurodegenerative dementia

Wang, X., Zeng, P. H., Fang, Y., Zhang, T., & Tian, Q. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15378 · Cited by 38 · see citing works

Ultrasensitive assay of amyloid-beta oligomers using Au-vertical graphene/carbon cloth electrode based on poly(thymine)-templated copper nanoparticles as probes

Zhou, Y., Lv, Y., Dong, H. Y., Liu, L., Mao, G., Zhang, Y., & Xu, M. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2020.129429 · Cited by 37 · see citing works

Counting of single prion particles bound to a capture-antibody surface (surface-FIDA)

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Nanopore Technology for the Application of Protein Detection

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Protein misfolding cyclic amplification (PMCA): Current status and future directions

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Monitoring α-synuclein ubiquitination dynamics reveals key endosomal effectors mediating its trafficking and degradation

Zenko, D., Marsh, J., Castle, A. R., Lewin, R., Fischer, R., & Tofaris, G. K. (2023) · Science Advances · doi:10.1126/sciadv.add8910 · Cited by 33 · see citing works

Adsorption and Disruption of Lipid Bilayers by Nanoscale Protein Aggregates

Hirano, A., Yoshikawa, H., Matsushita, S., Yamada, Y., & Shiraki, K. (2012) · Langmuir · doi:10.1021/la204717c · Cited by 32 · see citing works

Dual‐Functional, Multi‐Targeting GNNQQNY‐AIE Conjugates as Amyloid Probes and Amyloid Modulators via Amyloid Cross‐Seeding Principle

Tang, Y., Zhang, D., Gong, X., & Zheng, J. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202208022 · Cited by 32 · see citing works

Electrochemical analysis of the fibrillation of Parkinson's disease α-synuclein

Lopes, P., Dyrnesli, H., Lorenzen, N., Otzen, D. E., & Ferapontova, E. E. (2013) · The Analyst · doi:10.1039/c3an01616a · Cited by 32 · see citing works

A dual-screening electrochemiluminescent aptasensor based on a mesoporous silica nano-sieve for specific detection of amyloid-β monomer

Tan, R., Wang, Y., Mi, X., Li, H., & Tu, Y. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2021.131065 · Cited by 31 · see citing works

Application of an Amyloid Beta Oligomer Standard in the sFIDA Assay

Kühbach, K., Hülsemann, M., Herrmann, Y., Kravchenko, K., Kulawik, A., Linnartz, C., Peters, L., Wang, K., Willbold, J., Willbold, D., et al. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00008 · Cited by 29 · see citing works

DNAzyme-driven tripedal DNA walker mediated signal-on and label-free for electrochemical detection of α-synuclein oligomers

Gong, Y., Fu, M., Li, L., Yin, Y., Tang, Q., Zhou, W., Zhang, G., Liao, X., & Gao, F. (2022) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2022.133150 · Cited by 28 · see citing works

Single‐Molecule Counting Coupled to Rapid Amplification Enables Detection of α‐Synuclein Aggregates in Cerebrospinal Fluid of Parkinson's Disease Patients

Bhumkar, A., Magnan, C., Lau, D., Jun, E. S. W., Dzamko, N. L., Gambin, Y., & Sierecki, E. (2021) · Angewandte Chemie · doi:10.1002/ange.202014898 · Cited by 24 · see citing works

Design strategies, current applications and future perspective of aptasensors for neurological disease biomarkers

Erkmen, C., Tığ, G. A., Marrazza, G., & Uslu, B. (2022) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2022.116675 · Cited by 22 · see citing works

Investigation of α‐Synuclein and Amyloid‐β(42)‐E22Δ Oligomers Using SiN Nanopore Functionalized with L‐Dopa

Nemeir, I. A., Bentin, J., Meyer, N., Janot, J., Torrent, J., Picaud, F., & Balme, S. (2022) · Chemistry - An Asian Journal · doi:10.1002/asia.202200726 · Cited by 21 · see citing works

Alpha-synuclein as a biomarker in Parkinson’s disease: focus on neural derived extracelluar vesicles

Agliardi, C., Guerini, F. R., Meloni, M., & Clerici, M. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.330604 · Cited by 20 · see citing works

Patterning amyloid-β aggregation under the effect of acetylcholinesterase using a biological nanopore - an in vitro study

Subramanian, N., Watson, B. E., Li, C., Moss, M. A., & Liu, C. (2023) · Sensors and Actuators Reports · doi:10.1016/j.snr.2023.100170 · Cited by 20 · see citing works

Copper oxide nanoparticles promote α-synuclein oligomerization and underlying neurotoxicity as a model of Parkinson's disease

Lyu, J., Long, X., Xie, T., Jiang, G., Jiang, J., Ye, L., & Li, Q. (2020) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2020.115051 · Cited by 18 · see citing works

Single-Particle Detection System for Aβ Aggregates: Adaptation of Surface-Fluorescence Intensity Distribution Analysis to Laser Scanning Microscopy

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Unpacking the aggregation-oligomerization-fibrillization process of naturally-occurring hIAPP amyloid oligomers isolated directly from sera of children with obesity or diabetes mellitus

Altamirano‐Bustamante, M. M., Altamirano-Bustamante, N. F., Larralde-Laborde, M., Lara‐Martínez, R., Leyva-García, E., Garrido-Magaña, E. P., Rojas, G., Jiménez‐García, L. F., Revilla, M., Altamirano, P., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-54570-8 · Cited by 17 · see citing works

An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients

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Developing an Affinity-Based Chemical Proteomics Method to In Situ Capture Amorphous Aggregated Proteome and Profile Its Heterogeneity in Stressed Cells

Shen, D., Zhao, Q., Wang, M., Zhong, B., Jin, W., Huang, Y., Jin, H., Jing, B., Wan, W., Zhang, X., et al. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.2c05689 · Cited by 17 · see citing works

Discrimination between Alpha-Synuclein Protein Variants with a Single Nanometer-Scale Pore

Bakshloo, M. A., Yahiaoui, S., Bourderioux, M., Daniel, R., Pastoriza‐Gallego, M., Kasianowicz, J. J., & Oukhaled, A. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00164 · Cited by 16 · see citing works

Direct Demonstration of Seed Size-Dependent α-Synuclein Amyloid Amplification

Sakunthala, A., Datta, D., Navalkar, A., Gadhe, L., Kadu, P., Patel, K., Mehra, S., Kumar, R., Chatterjee, D., Devi, J., et al. (2022) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.2c01650 · Cited by 16 · see citing works

α-Synuclein–Confocal Nanoscanning (ASYN-CONA), a Bead-Based Assay for Detecting Early-Stage α-Synuclein Aggregation

Pérez‐Pi, I., Evans, D. A., Horrocks, M. H., Pham, N. T., Dolt, K. S., Koszela, J., Kunath, T., & Auer, M. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b03842 · Cited by 16 · see citing works

Biosensors for α-synuclein detection: Towards an improved diagnosis of Parkinson's disease

Carneiro, P., Morais, S., & Pereira, M. D. C. (2023) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2023.117150 · Cited by 15 · see citing works

Confinement-guided ultrasensitive optical assay with artificial intelligence for disease diagnostics

Zhang, W., Lu, Y., Su, C., Wang, Y., Wang, Y., Zhang, B., Jiang, C., Guo, K., & Xu, C. S. (2023) · The Innovation Medicine · doi:10.59717/j.xinn-med.2023.100023 · Cited by 15 · see citing works

Separation and determination of alpha‐synuclein monomeric and oligomeric species using two electrophoretic approaches

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Pathogenesis of experimental amyloid protein A amyloidosis in sore hocks-affected rabbits

Murakami, T., Inoshima, Y., Watanabe, K., KOBAYASHI, Y., MATSUI, T., Kurazono, H., & Ishiguro, N. (2011) · Amyloid · doi:10.3109/13506129.2011.582901 · Cited by 14 · see citing works

A computational suite for the structural and functional characterization of amyloid aggregates

Xia, Z., Wu, Y., Lam, J. Y. L., Zhang, Z., Burke, M., Fertan, E., Ranasinghe, R. T., Hidari, E., Danial, J. S. H., & Klenerman, D. (2023) · Cell Reports Methods · doi:10.1016/j.crmeth.2023.100499 · Cited by 13 · see citing works

Fibril-directed Therapies in Systemic Light Chain AL Amyloidosis

Bhutani, D., Leng, S., & Lentzsch, S. (2019) · Clinical Lymphoma Myeloma & Leukemia · doi:10.1016/j.clml.2019.03.029 · Cited by 12 · see citing works

RT-QuIC for detection of prodromal α-synucleinopathies

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Liposome Enhanced Detection of Amyloid Protein Aggregates

Kocsis, I., Sanna, E., & Hunter, C. A. (2021) · Organic Letters · doi:10.1021/acs.orglett.0c03597 · Cited by 10 · see citing works

Boosting the specific molecular recognition of β-amyloid oligomer by constructing of antibody-mimic Y probe

Zheng, Y., Zhao, J., Zhang, L., & Wang, W.-Z. (2023) · Sensors and actuators. B, Chemical · doi:10.1016/j.snb.2023.133418 · Cited by 10 · see citing works

Ultrastiff Amyloid-Fibril Network of α-Synuclein Formed by Surface Seeding Reaction Confirmed by Multichannel Electrodeless Quartz-Crystal-Microbalance Biosensor

Zhou, L., Hajiri, T., Nakajima, K., Aguirre, C., Ikenaka, K., Mochizuki, H., Yamaguchi, K., Goto, Y., & Ogi, H. (2023) · ACS Sensors · doi:10.1021/acssensors.3c00331 · Cited by 10 · see citing works

Dual functional amphiphilic sugar-coated AIE-active fluorescent organic nanoparticles for the monitoring and inhibition of insulin amyloid fibrillation based on carbohydrate–protein interactions

Ji, Y., Zhang, W., Zhang, J., Li, X.-F., Yu, F., Li, C., Liu, G., & Xing, G. (2022) · Journal of Materials Chemistry B · doi:10.1039/d2tb01070d · Cited by 9 · see citing works

Rational Design of Crystallization‐Induced‐Emission Probes To Detect Amorphous Protein Aggregation in Live Cells

Shen, D., Jin, W., Bai, Y., Huang, Y., Lyu, H., Zeng, L., Wang, M., Tang, Y., Wan, W., Dong, X., et al. (2021) · Angewandte Chemie · doi:10.1002/ange.202103674 · Cited by 9 · see citing works

Protein-conformational diseases in childhood: Naturally-occurring hIAPP amyloid-oligomers and early β-cell damage in obesity and diabetes

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Protein aggregation detection with fluorescent macromolecular and nanostructured probes: challenges and opportunities

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Extracellular vesicles and seeding amplification: a step closer to a Parkinson’s disease blood test

Martínez-Valbuena, I., Kovács, G. G., & Lang, A. E. (2022) · Brain · doi:10.1093/brain/awac292 · Cited by 7 · see citing works

A Rapid, Sensitive, and Specific Detection of Aggregated α-Synuclein by a Liposome-Immobilized Cantilever Sensor

Kobayashi, R., Kamitani, K., Sawamura, M., Yamakado, H., Takahashi, R., Sohgawa, M., & Noda, M. (2023) · IEEE Sensors Journal · doi:10.1109/jsen.2023.3272659 · Cited by 5 · see citing works

Electrochemical Analysis in Studying β-Amyloid Aggregation

Suprun, E. V., Radko, S. P., Kozin, S. A., Mitkevich, V. A., & Makarov, A. А. (2023) · Biochemistry (Moscow) · doi:10.1134/s0006297923140067 · Cited by 3 · see citing works

A Signal-Enhanced Regenerative Electrochemical Aptasensor for Amyloid-β Oligomers Based on Triple-Helix Aptamer Probe

Hu, J., Chen, X., Xu, J., & Wang, X. (2023) · Journal of The Electrochemical Society · doi:10.1149/1945-7111/acb5c5 · Cited by 2 · see citing works

Electrochemical detection of extracellular vesicles for early diagnosis: a focus on disease biomarker analysis

Zheng, J., Zhou, R., Wang, B., He, C., Bai, S., Yan, H., Yu, J., Li, H., Peng, B., Gao, Z., et al. (2024) · Extracellular Vesicles and Circulating Nucleic Acids · doi:10.20517/evcna.2023.72 · Cited by 37 · see citing works

Extracellular vesicles as nanotheranostic platforms for targeted neurological disorder interventions

Choi, H. K., Chen, M., Goldston, L. L., & Lee, K.-B. (2024) · Nano Convergence · doi:10.1186/s40580-024-00426-5 · Cited by 26 · see citing works

Real-Time Intracellular Monitoring of miRNA Dynamics during Induced Pluripotent Stem Cell Neuronal Differentiation via Plasmon-Enhanced Nanobiosensing

Hou, Y., Chen, M., Yang, L., & Lee, K. (2025) · Nano Letters · doi:10.1021/acs.nanolett.5c01840 · Cited by 8 · see citing works

The L1CAM‐positive extracellular vesicle‐based biomarker as a promising predictor of Parkinson's disease

Lai, M., Guo, K., Huang, Y., Wang, D., Duo, Y., Yuan, J., & Shu, B. (2024) · Brain‐X · doi:10.1002/brx2.66 · Cited by 3 · see citing works

High-Throughput Fluorescence Profiling of Remodeling Dynamics at Surface-Deposited Amyloid Interfaces

Lee, T., Seo, Y., Hwang, W., Choi, S., Bae, M., Kang, D., Roh, S., Lee, H., Kim, S., & Lee, G. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c02272 · Cited by 2 · see citing works

Highly sensitive detection of different aggregation stages of Aβ1-42 -amyloid peptide in urine-like samples by auto-fluorescence

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Digital Dual‐Dimensional α‐Synuclein Aggregate Decoding Sensor for Parkinson's Disease Diagnostics

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Quantifying protein aggregate concentration through electrochemical oxidation of thioflavin T

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Study of the Aggregation Behavior of Proteins Related to Neurodegenerative Diseases Based on the Photoluminescence of Perovskite Nanocrystals

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Patterning technologies in bioanalysis: From sensing surface construction to detection applications

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Recent Advances in Protein Nanopore‐Based Analysis for Molecules Related to Cellular Metabolism

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Trends and Perspectives in Biosensing and Diagnosis

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Highly Sensitive and Robust Detection of Human Telomerase Based on Strand-Displacement Cascade Amplification

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Deep Learning‐Powered Plasmonic Platform for Decoding Dynamic Protein Aggregation Landscapes in Parkinson's Disease Progression

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Recent Research on Biosensors for Biomarker Detection Related to Neurological Disorders Utilizing Surface Engineering Strategies

이예진, Seo, M., Pyo, S., Kim, Y., Choi, H. K., Shin, M., & Yoon, J. (2026) · Biosensors · doi:10.3390/bios16100541

Electronic profiling of neuronal extracellular vesicles enables early prediction of Parkinson’s disease

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A Universal Method for Detection of Amyloidogenic Misfolded Proteins

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Advances in methods to detect and study protein aggregation

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Assessing amyloid fibrils and amorphous aggregates: A review

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Million-fold sensitivity enhancement in proteopathic seed amplification assays for biospecimens by Hofmeister ion comparisons

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Application of biomaterials for the detection of amyloid aggregates

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