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Amytracker - References

2024

  • Pinzi, Luca, Christian Conze, Nicolo Bisi, Gabriele Dalla Torre, Ahmed Soliman, Nanci Monteiro-Abreu, Nataliya I. Trushina, et al. 2024. “Quantitative Live Cell Imaging of a Tauopathy Model Enables the Identification of a Polypharmacological Drug Candidate That Restores Physiological Microtubule Interaction.” Nature Communications 15 (February): 1679. https://doi.org/10.1038/s41467-024-45851-6.

2023

  • Arad, Elad, Nimrod Golan, Hanna Rapaport, Meytal Landau, and Raz Jelinek. 2023. “Staphylococcus Aureus Functional Amyloids Catalyze Degradation of β-Lactam Antibiotics.” BioRxiv. https://doi.org/10.1101/2023.02.01.526669
  • Balana, Aaron T., Anne-Laure Mahul-Mellier, Binh A Nguyen, Mian Horvath, Afraah Javed, Eldon R. Hard, Yllza Jasiqi, et al. 2023. “O-GlcNAc Modification Forces the Formation of an α-Synuclein Amyloid-Strain with Notably Diminished Seeding Activity and Pathology.” BioRxiv, March, 2023.03.07.531573. https://doi.org/10.1101/2023.03.07.531573.
  • Chandhok, Sahil, Lionel Pereira, Evgenia A Momchilova, Dane Marijan, Richard Zapf, Emma Lacroix, Avneet Kaur, Shayan Keymanesh, Charles Krieger, and Timothy E Audas. 2023. “Stress-Mediated Aggregation of Disease-Associated Proteins in Amyloid Bodies.” Scientific Reports 13: 14471. https://doi.org/10.1038/s41598-023-41712-2.
  • Chia, Sean, Z Faidon Brotzakis, Robert I Horne, Andrea Possenti, Benedetta Mannini, Rodrigo Cataldi, Magdalena Nowinska, et al. 2023. “Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates.” Mol. Pharmaceutics 20: 183–93. https://doi.org/10.1021/acs.molpharmaceut.2c00548.
  • Frenkel, Alona, Eli Zecharia, Daniel Gómez-Pérez, Eleonora Sendersky, Yevgeni Yegorov, Avi Jacob, Jennifer I. C. Benichou, et al. 2023. “Cell Specialization in Cyanobacterial Biofilm Development Revealed by Expression of a Cell-Surface and Extracellular Matrix Protein.” Npj Biofilms and Microbiomes 2023 9:1 9 (March): 1–10. https://doi.org/10.1038/s41522-023-00376-6.
  • Gvazava, Nika, Sabine Konings, Efrain Cepeda-Prado, Valeriia Skoryk, Chimezie H Umeano, Jiao Dong, Iran A N Silva, et al. 2023. “Label-Free High-Resolution Infrared Spectroscopy for Spatiotemporal Analysis of Complex Living Systems.” BioRxiv. https://doi.org/10.1101/2023.01.05.522847.
  • Amaral, Mariana Juliani Do, Aline Ribeiro Passos, Satabdee Mohapatra, Taiana Sousa Lopes Da Silva, Renato Sampaio Carvalho, Marcius Da, Silva Almeida, Anderson De Sá Pinheiro, Susanne Wegmann, and Yraima Cordeiro. 2023. “Copper Drives Prion Protein Phase Separation and Modulates Aggregation.” BioRxiv. https://doi.org/10.1101/2023.02.15.528739.
  • Kreutzer, Adam G., Chelsea Marie T. Parrocha, Sepehr Haerianardakani, Gretchen Guaglianone, Jennifer T. Nguyen, Michelle N. Diab, William Yong, Mari Perez-Rosendahl, Elizabeth Head, and James S. Nowick. 2023. “Antibodies Raised Against an Aβ Oligomer Mimic Recognize Pathological Features in Alzheimer’s Disease and Associated Amyloid-Disease Brain Tissue.” BioRxiv, May, 2023.05.11.540404. https://doi.org/10.1101/2023.05.11.540404.
  • Kommaddi, Reddy Peera, Aditi Verma, Graciela Muniz-Terrera, Vivek Tiwari, Keerthana Chithanathan, Latha Diwakar, Ruturaj Gowaikar, et al. 2023. “Sex Difference in Evolution of Cognitive Decline: Studies on Mouse Model and the Dominantly Inherited Alzheimer Network Cohort.” Translational Psychiatry 13 (April): 1–12. https://doi.org/10.1038/s41398-023-02411-8.
  • Ornithopoulou, Eirini, Carolina Åstrand, Linnea Gustafsson, Thomas Crouzier, and My Hedhammar. 2023. “Self-Assembly of RGD-Functionalized Recombinant Spider Silk Protein into Microspheres in Physiological Buffer and in the Presence of Hyaluronic Acid.” ACS Applied Bio Materials, August. https://doi.org/10.1021/ACSABM.3C00373.
  • Petrlova, Jitka, Erik Hartman, Ganna Petruk, Jeremy Chun, Hwee Lim, Sunil Shankar Adav, Sven Kjellström, Manoj Puthia, and Artur Schmidtchen. 2023. “Protein Aggregation in Wound Fluid Confines Bacterial Lipopolysaccharide and Reduces in-Flammation.” BioRxiv. https://doi.org/10.1101/2023.01.27.525825.
  • Piroska, Leonard, Alexis Fenyi, Scott Thomas, Marie Aude Plamont, Virginie Redeker, Ronald Melki, and Zoher Gueroui. 2023. “Α-Synuclein Liquid Condensates Fuel Fibrillar α-Synuclein Growth.” Science Advances 9 (August): eadg5663. https://doi.org/10.1126/SCIADV.ADG5663.
  • Prater, Craig, Yeran Bai, Sabine C. Konings, Isak Martinsson, Vinay S. Swaminathan, Pontus Nordenfelt, Gunnar Gouras, Ferenc Borondics, and Oxana Klementieva. 2023. “Fluorescently Guided Optical Photothermal Infrared Microspectroscopy for Protein-Specific Bioimaging at Subcellular Level.” Journal of Medicinal Chemistry 66 (February): 2542–49. https://doi.org/10.1021/ACS.JMEDCHEM.2C01359/SUPPL_FILE/JM2C01359_SI_001.PDF.
  • Šulskis, Darius, and Andrius Sakalauskas. 2023. “Formation of Amyloid Fibrils by the Regulatory 14-3-3ζ Protein.” BioRxiv. https://doi.org/10.1101/2023.05.31.543065.

2022

  • Cascella, Roberta, Martina Banchelli, Seyyed Abolghasem Ghadami, Diletta Ami, Maria Cristina Gagliani, Alessandra Bigi, Tommaso Staderini, et al. 2022. “An in Situ and in Vitro Investigation of Cytoplasmic TDP-43 Inclusions Reveals the Absence of a Clear Amyloid Signature.” Annals of Medicine 55: 72–88. https://doi.org/10.1080/07853890.2022.2148734.
  • Choi, Minee L, Alexandre Chappard, Bhanu P Singh, Catherine Maclachlan, Andrey Y ✉ Abramov, Mathew H ✉ Horrocks, and Sonia ✉ Gandhi. 2022. “Pathological Structural Conversion of α-Synuclein at the Mitochondria Induces Neuronal Toxicity.” Nature Neuroscience.
  • Luca, Chiara Maria Giulia De, Alessandra Consonni, Federico Angelo Cazzaniga, Edoardo Bistaffa, Giuseppe Bufano, Giorgia Quitarrini, Luigi Celauro, et al. 2022. “The Alpha-Synuclein RT-QuIC Products Generated by the Olfactory Mucosa of Patients with Parkinson’s Disease and Multiple System Atrophy Induce Inflammatory Responses in SH-SY5Y Cells.” Cells 11 (January). https://doi.org/10.3390/cells11010087.
  • Wood, Jack I, Eugenia Wong, Damian M Cummings, John Hardy, Frances A Edwards Correspondence, Ridwaan Joghee, Aya Balbaa, et al. 2022. “Plaque Contact and Unimpaired Trem2 Is Required for the Microglial Response to Amyloid Pathology.” Cell Reports. https://doi.org/10.1016/j.celrep.2022.111686.
  • Pinzi, Luca, Christian Conze, Nicolo Bisi, Gabriele Dalla Torre, Nanci Monteiro-Abreu, Nataliya I Trushina, Ahmed Soliman, et al. 2022. “Quantitative Live Cell Imaging of a Tauopathy Model Enables the Identification of a Polypharmacological Drug Candidate That Restores Physiological Microtubule Regulation.” BioRxiv. https://doi.org/10.1101/2022.10.31.514565.
  • Petrlova, Jitka, Firdaus Samsudin, Peter J Bond, and Artur Schmidtchen. 2022. “SARS-CoV-2 Spike Protein Aggregation Is Triggered by Bacterial Lipopolysaccharide.” FEBS Letters. https://doi.org/10.1002/1873-3468.14490.
  • Morten, Michael J, Liina Sirvio, Huzefa Rupawala, Emma Mee Hayes, Aitor Franco, Carola Radulescu, Liming Ying, Samuel J Barnes, Arturo Muga, and Yu Ye. 2022. “Quantitative Super-Resolution Imaging of Pathological Aggregates Reveals Distinct Toxicity Profiles in Different Synucleinopathies.” PNAS. https://doi.org/10.1073/pnas.
  • Hochmair, Janine, Christian Exner, Maximilian Franck, Alvaro Dominguez‐Baquero, Lisa Diez, Hévila Brognaro, Matthew L Kraushar, et al. 2022. “Molecular Crowding and RNA Synergize to Promote Phase Separation, Microtubule Interaction, and Seeding of Tau Condensates.” The EMBO Journal 41 (June). https://doi.org/10.15252/EMBJ.2021108882.
  • Kitamura, Akira, Ai Fujimoto, Rei Kawashima, Yidan Lyu, Kanami Moriya, Ayumi Kurata, Kazuho Takahashi, et al. 2022. “Hetero-Oligomerization of TDP-43 Carboxy-Terminal Fragments with Cellular Proteins Contributes to Proteotoxicity.” BioRxiv, May. https://doi.org/10.1101/2022.05.22.493003.
  • Kumar, Senthil T., Anne Laure Mahul-Mellier, Ramanath Narayana Hegde, Gwladys Rivière, Rani Moons, Alain Ibáñez de Opakua, Pedro Magalhães, et al. 2022. “A NAC Domain Mutation (E83Q) Unlocks the Pathogenicity of Human Alpha-Synuclein and Recapitulates Its Pathological Diversity.” Science Advances 8 (April): 44. https://doi.org/10.1126/SCIADV.ABN0044.
  • Lackie, Rachel E., Aline S. de Miranda, Mei Peng Lim, Vladislav Novikov, Nimrod Madrer, Nadun C. Karunatilleke, Benjamin S. Rutledge, et al. 2022. “Stress-Inducible Phosphoprotein 1 (HOP/STI1/STIP1) Regulates the Accumulation and Toxicity of α-Synuclein in Vivo.” Acta Neuropathologica, November. https://doi.org/10.1007/s00401-022-02491-8.

2021

  • Aubi, Oscar, Karina S. Prestegård, Kunwar Jung-KC, Tie Jun Sten Shi, Ming Ying, Ann Kari Grindheim, Tanja Scherer, et al. 2021. “The Pah-R261Q Mouse Reveals Oxidative Stress Associated with Amyloid-Like Hepatic Aggregation of Mutant Phenylalanine Hydroxylase.” Nature Communications 2021 12:1 12 (April): 1–16. https://doi.org/10.1038/s41467-021-22107-1.
  • Frey, Bryan, Abdelrahman AlOkda, Matthew P. Jackson, Nathan Riguet, James A. Duce, and Hilal A. Lashuel. 2021. “Monitoring Alpha-Synuclein Oligomerization and Aggregation Using Bimolecular Fluorescence Complementation Assays: What You See Is Not Always What You Get.” Journal of Neurochemistry 157: 872–88. https://doi.org/10.1111/jnc.15147.
  • Frottin, Frédéric, Manuela Pérez-Berlanga, F Ulrich Hartl, and Mark S Hipp. 2021. “Multiple Pathways of Toxicity Induced by C9orf72 Dipeptide Repeat Aggregates and G4C2 RNA in a Cellular Model.” eLife 10 (June). https://doi.org/10.7554/eLife.62718.
  • Rimal, Suman, Yu Li, Rasika Vartak, Ji Geng, Ishaq Tantray, Shuangxi Li, Sungun Huh, et al. 2021. “Inefficient Quality Control of Ribosome Stalling During APP Synthesis Generates CAT-Tailed Species That Precipitate Hallmarks of Alzheimer’s Disease.” Acta Neuropathologica Communications 9 (December): 1–24. https://doi.org/10.1186/S40478-021-01268-6/FIGURES/7.
  • Hofbauer, Daniel, Dimitrios Mougiakakos, Andreas Mackensen, Stefano Ricagno, and Heiko Bruns Correspondence. 2021. “B2-Microglobulin Triggers NLRP3 Inflammasome Activation in Tumor-Associated Macrophages to Promote Multiple Myeloma Progression.” Immunity. https://doi.org/10.1016/j.immuni.2021.07.002.
  • Johari, Mridul, Jaakko Sarparanta, Anna Vihola, Per Harald Jonson, Marco Savarese, Manu Jokela, Annalaura Torella, et al. 2021. “Missense Mutations in Small Muscle Protein x-Linked (SMPX) Cause Distal Myopathy with Protein Inclusions.” Acta Neuropathologica. https://doi.org/10.1007/s00401-021-02319-x.

2020

  • Mahul-Mellier, Anne Laure, Johannes Burtscher, Niran Maharjan, Laura Weerens, Marie Croisier, Fabien Kuttler, Marion Leleu, Graham W. Knott, and Hilal A. Lashuel. 2020. “The Process of Lewy Body Formation, Rather Than Simply α-Synuclein Fibrillization, Is One of the Major Drivers of Neurodegeneration.” Proceedings of the National Academy of Sciences of the United States of America 117: 4971–82. https://doi.org/10.1073/pnas.1913904117.
  • Ghosh, Anshua, Keiko Mizuno, Sachin S. Tiwari, Petroula Proitsi, Beatriz Gomez Perez-Nievas, Elizabeth Glennon, Rocio T. Martinez-Nunez, and K. Peter Giese. 2020. “Alzheimer’s Disease-Related Dysregulation of mRNA Translation Causes Key Pathological Features with Ageing.” Translational Psychiatry 10: 1–18. https://doi.org/10.1038/s41398-020-00882-7.
  • Louros, Nikolaos, Gabriele Orlando, Matthias De Vleeschouwer, Frederic Rousseau, and Joost Schymkowitz. 2020. “Structure-Based Machine-Guided Mapping of Amyloid Sequence Space Reveals Uncharted Sequence Clusters with Higher Solubilities.” Nature Communications 11: 1–13. https://doi.org/10.1038/s41467-020-17207-3.

2019

  • Page, Martin J., Greig J. A. Thomson, J. Massimo Nunes, Anna Mart Engelbrecht, Theo A. Nell, Willem J. S. de Villiers, Maria C. de Beer, Lize Engelbrecht, Douglas B. Kell, and Etheresia Pretorius. 2019. “Serum Amyloid a Binds to Fibrin(ogen), Promoting Fibrin Amyloid Formation.” Scientific Reports 9: 1–14. https://doi.org/10.1038/s41598-019-39056-x.
  • Adams, Büin, J. Massimo Nunes, Martin J. Page, Timothy Roberts, Jonathan Carr, Theo A. Nell, Douglas B. Kell, and Etheresia Pretorius. 2019. “Parkinson’s Disease: A Systemic Inflammatory Disease Accompanied by Bacterial Inflammagens.” Frontiers in Aging Neuroscience 10: 1–17. https://doi.org/10.3389/fnagi.2019.00210.
  • Frottin, F., F. Schueder, S. Tiwary, R. Gupta, R. Körner, T. Schlichthaerle, J. Cox, R. Jungmann, F. U. Hartl, and M. S. Hipp. 2019. “The Nucleolus Functions as a Phase-Separated Protein Quality Control Compartment.” Science 365: 342–47. https://doi.org/10.1126/science.aaw9157.

2018

  • Waal, Greta M. de, Lize Engelbrecht, Tanja Davis, Willem J. S. de Villiers, Douglas B. Kell, and Etheresia Pretorius. 2018. “Correlative Light-Electron Microscopy Detects Lipopolysaccharide and Its Association with Fibrin Fibres in Parkinson’s Disease, Alzheimer’s Disease and Type 2 Diabetes Mellitus.” Scientific Reports 8: 1–12. https://doi.org/10.1038/s41598-018-35009-y.
  • Pretorius, Etheresia, Martin J. Page, Lisa Hendricks, Nondumiso B. Nkosi, Sven R. Benson, and Douglas B. Kell. 2018. “Both Lipopolysaccharide and Lipoteichoic Acids Potently Induce Anomalous Fibrin Amyloid Formation: Assessment with Novel Amytracker TM Stains.” Journal of the Royal Society Interface 15. https://doi.org/10.1098/rsif.2017.0941.

2017

  • Sehlin, Dag, Xiaotian T. Fang, Silvio R. Meier, Malin Jansson, and Stina Syvänen. 2017. “Pharmacokinetics, Biodistribution and Brain Retention of a Bispecific Antibody-Based PET Radioligand for Imaging of Amyloid-β.” Scientific Reports 7: 1–9. https://doi.org/10.1038/s41598-017-17358-2.
  • Pretorius, Etheresia, Martin J. Page, Lize Engelbrecht, Graham C. Ellis, and Douglas B. Kell. 2017. “Substantial Fibrin Amyloidogenesis in Type 2 Diabetes Assessed Using Amyloid-Selective Fluorescent Stains.” Cardiovascular Diabetology 16: 1–14. https://doi.org/10.1186/s12933-017-0624-5.