Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillation

By Joseph A. Marsh, Vinay Singh, Z. Jia, Julie D. Forman-Kay. 2006

678 citations recorded by the source corpus.

Subfields: Molecular Biology, Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/e11017fe8981adf6f0574d6cf4adef3a9bafafd6

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Gül H. Zerze
2. Jeetain Mittal
3. Nicolas L. Fawzi
4. Alexander E. Conicella

Citations in the corpus

• Residue-by-residue view of in vitro FUS granules that bind the C-terminal domain of RNA polymerase II (2015, positive): “These data can be combined with chemical shift values for backbone amide and carbonyl positions to generate residue-by-residue predictions of local secondary structure population using secondary structure propensity (SSP) (Marsh et al., 2006) and d2D algorithms (Camilloni et al., 2012).”
• ALS mutations disrupt phase separation mediated by -helical structure in the TDP-43 low complexity C-terminal domain (2016, result): “The chemical shift index(Wishart et al., 1992), secondary structure propensity (SSP) scores (Marsh et al., 2006), and δ2D population predictions (Sormanni et al., 2015) are also consistent with partial helical structure in the region 321–330 (Figure S1C–”