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Protein condensation diseases: therapeutic opportunities

Author

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  • Michele Vendruscolo

    (University of Cambridge)

  • Monika Fuxreiter

    (University of Padova)

Abstract

Condensed states of proteins, including liquid-like membraneless organelles and solid-like aggregates, contribute in fundamental ways to the organisation and function of the cell. Perturbations of these states can lead to a variety of diseases through mechanisms that we are now beginning to understand. We define protein condensation diseases as conditions caused by the disruption of the normal behaviour of the condensed states of proteins. We analyze the problem of the identification of targets for pharmacological interventions for these diseases and explore opportunities for the regulation of the formation and organisation of aberrant condensed states of proteins.

Suggested Citation

  • Michele Vendruscolo & Monika Fuxreiter, 2022. "Protein condensation diseases: therapeutic opportunities," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32940-7
    DOI: 10.1038/s41467-022-32940-7
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    Cited by:

    1. Samuel T. Dada & Zenon Toprakcioglu & Mariana P. Cali & Alexander Röntgen & Maarten C. Hardenberg & Owen M. Morris & Lena K. Mrugalla & Tuomas P. J. Knowles & Michele Vendruscolo, 2024. "Pharmacological inhibition of α-synuclein aggregation within liquid condensates," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Ashish Joshi & Anuja Walimbe & Anamika Avni & Sandeep K. Rai & Lisha Arora & Snehasis Sarkar & Samrat Mukhopadhyay, 2023. "Single-molecule FRET unmasks structural subpopulations and crucial molecular events during FUS low-complexity domain phase separation," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    3. Steen W. B. Bender & Marcus W. Dreisler & Min Zhang & Jacob Kæstel-Hansen & Nikos S. Hatzakis, 2024. "SEMORE: SEgmentation and MORphological fingErprinting by machine learning automates super-resolution data analysis," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    4. Mónika Gönczi & João M. C. Teixeira & Susana Barrera-Vilarmau & Laura Mediani & Francesco Antoniani & Tamás Milán Nagy & Krisztina Fehér & Zsolt Ráduly & Viktor Ambrus & József Tőzsér & Endre Barta & , 2023. "Alternatively spliced exon regulates context-dependent MEF2D higher-order assembly during myogenesis," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    5. Jing Tao & Yanping Zeng & Bin Dai & Yin Liu & Xiaohan Pan & Li-Qiang Wang & Jie Chen & Yu Zhou & Zuneng Lu & Liwei Xie & Yi Liang, 2023. "Excess PrPC inhibits muscle cell differentiation via miRNA-enhanced liquid–liquid phase separation implicated in myopathy," Nature Communications, Nature, vol. 14(1), pages 1-22, December.

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