Simultaneous quantification of protein order and disorder.
By Pietro Sormanni, Damiano Piovesan, Gabriella T. Heller, Massimiliano Bonomi, Predrag Kukic, Carlo Camilloni, Mónika Fuxreiter, Zsuzsanna Dosztányi, Rohit V. Pappu, M. Babu and 6 more. 2017
113 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
- Zsuzsanna Dosztányi
- Bálint Mészáros
- Damiano Piovesan
- Michele Vendruscolo
- Silvio C. E. Tosatto
- Vladimir N Uversky
- Peter Tompa
- Carlo Camilloni
In Molecular Biology
- Zsuzsanna Dosztányi
- Bálint Mészáros
- Vladimir N Uversky
- Michele Vendruscolo
- Damiano Piovesan
- Silvio C. E. Tosatto
- Lukasz Kurgan
- Peter Tompa
Citations in the corpus
- MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins (2017, background): “0 better exploits the power of NMR spectroscopy to probe the structural properties of proteins in solution, as well as their dynamics on a wide range of timescales (44).”
- Intrinsic protein disorder and conditional folding in AlphaFoldDB (2022, background): “21 As AlphaFold leverages large sequence alignments to generate its models, 3 it is implicitly encoding sequence conservation in its predictions and this is reflected in the pLDDT score.”
- Prediction of protein disorder based on IUPred (2018, background): “76 Another frontier is the prediction of functionally important regions located within IDRs.”