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@ARTICLE{Rai:155725,
      author       = {Rai, Sandeep K and Savastano, Adriana and Singh, Priyanka
                      and Mukhopadhyay, Samrat and Zweckstetter, Markus},
      title        = {{L}iquid-liquid phase separation of tau: {F}rom molecular
                      biophysics to physiology and disease.},
      journal      = {Protein science},
      volume       = {30},
      number       = {7},
      issn         = {1469-896X},
      address      = {Bethesda, Md.},
      publisher    = {Protein Society},
      reportid     = {DZNE-2021-00893},
      pages        = {1294 - 1314},
      year         = {2021},
      abstract     = {Biomolecular condensation via liquid-liquid phase
                      separation (LLPS) of intrinsically disordered
                      proteins/regions (IDPs/IDRs), with and without nucleic
                      acids, has drawn widespread interest due to the rapidly
                      unfolding role of phase-separated condensates in a diverse
                      range of cellular functions and human diseases. Biomolecular
                      condensates form via transient and multivalent
                      intermolecular forces that sequester proteins and nucleic
                      acids into liquid-like membrane-less compartments. However,
                      aberrant phase transitions into gel-like or solid-like
                      aggregates might play an important role in neurodegenerative
                      and other diseases. Tau, a microtubule-associated neuronal
                      IDP, is involved in microtubule stabilization, regulates
                      axonal outgrowth and transport in neurons. A growing body of
                      evidence indicates that tau can accomplish some of its
                      cellular activities via LLPS. However, liquid-to-solid
                      transition resulting in the abnormal aggregation of tau is
                      associated with neurodegenerative diseases. The physical
                      chemistry of tau is crucial for governing its propensity for
                      biomolecular condensation which is governed by various
                      intermolecular and intramolecular interactions leading to
                      simple one-component and complex multi-component
                      condensates. In this review, we aim at capturing the current
                      scientific state in unveiling the intriguing molecular
                      mechanism of phase separation of tau. We particularly focus
                      on the amalgamation of existing and emerging biophysical
                      tools that offer unique spatiotemporal resolutions on a wide
                      range of length- and time-scales. We also discuss the link
                      between quantitative biophysical measurements and novel
                      biological insights into biomolecular condensation of tau.
                      We believe that this account will provide a broad and
                      multidisciplinary view of phase separation of tau and its
                      association with physiology and disease.},
      subtyp        = {Review Article},
      keywords     = {Biomolecular Condensates: chemistry / Humans /
                      Intrinsically Disordered Proteins: chemistry / Intrinsically
                      Disordered Proteins: isolation $\&$ purification /
                      Intrinsically Disordered Proteins: metabolism /
                      Neurodegenerative Diseases: metabolism / tau Proteins:
                      chemistry / tau Proteins: isolation $\&$ purification / tau
                      Proteins: metabolism},
      cin          = {AG Zweckstetter},
      ddc          = {610},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33930220},
      pmc          = {pmc:PMC8197432},
      doi          = {10.1002/pro.4093},
      url          = {https://pub.dzne.de/record/155725},
}