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  1. Article

    Open Access

    Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response

    Age-related changes in cellular metabolism can affect brain homeostasis, creating conditions that are permissive to the onset and progression of neurodegenerative disorders such as Alzheimer’s and Parkinson’s ...

    Priyanka Joshi, Michele Perni, Ryan Limbocker, Benedetta Mannini in Communications Biology (2021)

  2. No Access

    Article

    Generic nature of the condensed states of proteins

    Proteins undergoing liquid–liquid phase separation are being discovered at an increasing rate. Since at the high concentrations present in the cell most proteins would be expected to form a liquid condensed st...

    Monika Fuxreiter, Michele Vendruscolo in Nature Cell Biology (2021)

  3. No Access

    Article

    Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases

    Protein misfolding and aggregation are characteristic of a wide range of neurodegenerative disorders, including Alzheimer and Parkinson diseases. A hallmark of these diseases is the aggregation of otherwise so...

    Klara Kulenkampff, Adriana-M. Wolf Perez, Pietro Sormanni in Nature Reviews Chemistry (2021)

  4. Article

    Open Access

    The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition

    α-Synuclein (αS) is a presynaptic disordered protein whose aberrant aggregation is associated with Parkinson’s disease. The functional role of αS is still debated, although it has been involved in the regulati...

    Wing K. Man, Bogachan Tahirbegi, Michail D. Vrettas, Swapan Preet in Nature Communications (2021)

  5. Article

    Open Access

    Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers

    Significant efforts have been devoted in the last twenty years to develo** compounds that can interfere with the aggregation pathways of proteins related to misfolding disorders, including Alzheimer’s and Pa...

    Francesco Simone Ruggeri, Johnny Habchi, Sean Chia in Nature Communications (2021)

  6. Article

    Open Access

    Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers

    A Correction to this paper has been published: https://doi.org/10.1038/s42003-021-01680-7.

    Rodrigo Cataldi, Sean Chia, Katarina Pisani, Francesco S. Ruggeri in Communications Biology (2021)

  7. Article

    Open Access

    A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers

    Aberrant soluble oligomers formed by the amyloid-β peptide (Aβ) are major pathogenic agents in the onset and progression of Alzheimer’s disease. A variety of biomolecules can influence the formation of these o...

    Rodrigo Cataldi, Sean Chia, Katarina Pisani, Francesco S. Ruggeri in Communications Biology (2021)

  8. No Access

    Article

    A kinetic ensemble of the Alzheimer’s Aβ peptide

    The conformational and thermodynamic properties of disordered proteins are commonly described in terms of structural ensembles and free energy landscapes. To provide information on the transition rates between...

    Thomas Löhr, Kai Kohlhoff, Gabriella T. Heller in Nature Computational Science (2021)

  9. Article

    Open Access

    Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter

    The aggregation of α-synuclein is a central event in Parkinsons’s disease and related synucleinopathies. Since pharmacologically targeting this process, however, has not yet resulted in approved disease-modify...

    Roxine Staats, Thomas C. T. Michaels, Patrick Flagmeier in Communications Chemistry (2020)

  10. No Access

    Article

    Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies

    The amyloid cascade hypothesis, according to which the self-assembly of amyloid-β peptide (Aβ) is a causative process in Alzheimer’s disease, has driven many therapeutic efforts for the past 20 years. Failures...

    Sara Linse, Tom Scheidt, Katja Bernfur in Nature Structural & Molecular Biology (2020)

  11. No Access

    Article

    Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation

    The formation of amyloid deposits in human tissues is a defining feature of more than 50 medical disorders, including Alzheimer’s disease. Strong genetic and histological evidence links these conditions to the...

    Patrick Flagmeier, Suman De, Thomas C. T. Michaels in Nature Structural & Molecular Biology (2020)

  12. Article

    Open Access

    A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer’s disease

    Bicyclic peptides have great therapeutic potential since they can bridge the gap between small molecules and antibodies by combining a low molecular weight of about 2 kDa with an antibody-like binding specific...

    Tatsuya Ikenoue, Francesco A. Aprile, Pietro Sormanni in Scientific Reports (2020)

  13. Article

    Open Access

    Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism

    The onset and progression of numerous protein misfolding diseases are associated with the presence of oligomers formed during the aberrant aggregation of several different proteins, including amyloid-β (Aβ) in...

    Ryan Limbocker, Benedetta Mannini, Francesco S. Ruggeri in Communications Biology (2020)

  14. Article

    Open Access

    Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy

    The chemical and structural properties of biomolecules determine their interactions, and thus their functions, in a wide variety of biochemical processes. Innovative imaging methods have been developed to char...

    Francesco Simone Ruggeri, Benedetta Mannini, Roman Schmid in Nature Communications (2020)

  15. No Access

    Article

    Assessing motor-related phenotypes of Caenorhabditis elegans with the wide field-of-view nematode tracking platform

    Caenorhabditis elegans is a valuable model organism in biomedical research that has led to major discoveries in the fields of neurodegeneration, cancer and aging. Because movement phenotypes are commonly used and...

    Mandy Koopman, Quentin Peter, Renée I. Seinstra, Michele Perni in Nature Protocols (2020)

  16. Article

    Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide

    An amendment to this paper has been published and can be accessed via a link at the top of the paper.

    Thomas C. T. Michaels, Andela Šarić, Samo Curk, Katja Bernfur in Nature Chemistry (2020)

  17. No Access

    Article

    Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide

    Oligomeric species populated during the aggregation of the Aβ42 peptide have been identified as potent cytotoxins linked to Alzheimer’s disease, but the fundamental molecular pathways that control their dynami...

    Thomas C. T. Michaels, Andela Šarić, Samo Curk, Katja Bernfur in Nature Chemistry (2020)

  18. Article

    Open Access

    A single ultrasensitive assay for detection and discrimination of tau aggregates of Alzheimer and Pick diseases

    Multiple neurodegenerative diseases are characterized by aggregation of tau molecules. Adult humans express six isoforms of tau that contain either 3 or 4 microtubule binding repeats (3R or 4R tau). Different ...

    Michael A. Metrick II, Natália do Carmo Ferreira in Acta Neuropathologica Communications (2020)

  19. Article

    Chris Dobson (1949–2019)

    Chris Dobson passed away on September 8th, leaving a wide-reaching legacy. He is best known for revealing the generality of the phenomenon of protein misfolding and aggregation and has provided inspiration for...

    Tuomas P. J. Knowles, Michele Vendruscolo in Nature Chemical Biology (2020)

  20. Article

    Open Access

    The N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State

    The aggregation of α-synuclein (αS), a protein abundant at presynaptic terminals, is associated with a range of highly debilitating neurodegenerative conditions, including Parkinson’s disease (PD), dementia wi...

    Matteo Runfola, Alfonso De Simone, Michele Vendruscolo in Scientific Reports (2020)

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