Structural disorder of monomeric α-synuclein persists in mammalian cells

By François-Xavier Theillet, A. Binolfi, Beata Bekei, A. Martorana, H. Rose, M. Stuiver, S. Verzini, D. Lorenz, Marleen van Rossum, D. Goldfarb and 1 more. Nature, 2016

771 citations recorded by the source corpus.

Subfields: Biophysics, Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/f1dca1c81b1f604986c82dcf15b204803f781609

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In Neurology

1. Michele Vendruscolo

In Physiology

1. Michele Vendruscolo
2. Peter Tompa
3. Carlo Camilloni
4. Zsuzsanna Dosztányi
5. Pietro Sormanni

Citations in the corpus

• Tardigrades use intrinsically disordered proteins to survive desiccation (2018, positive): “Importantly, a-synuclein, a protein that exists as a disordered monomer in cells (Fauvet et al., 2012; Theillet et al., 2016) and has no known connection to stress tolerance (Drescher et al., 2012; Theillet et al., 2014), did not increase survival under drying conditions (Figure 6B), demonstrating…”
• MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins (2017, background): “Techniques such as in-cell Nuclear magnetic resonance (NMR) spectroscopy (32,33) and single-molecule fluorescence (34) will soon help study these structures in the physiological state.”