Comprehensive large-scale assessment of intrinsic protein disorder

By Ian Walsh, Manuel Giollo, Tomás Di Domenico, Carlo Ferrari, O. Zimmermann, Silvio C. E. Tosatto. 2015

140 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

1. Vladimir N Uversky
2. Silvio C. E. Tosatto
3. Ian Walsh
4. Emilio Potenza
5. Tomás Di Domenico
6. Zsuzsanna Dosztányi
7. A. Keith Dunker
8. Lukasz Kurgan

In Molecular Biology

1. Vladimir N Uversky
2. Silvio C. E. Tosatto
3. Ian Walsh
4. Tomás Di Domenico
5. Emilio Potenza
6. Lukasz Kurgan
7. Zsuzsanna Dosztányi
8. Yaoqi Zhou

Citations in the corpus

• MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins (2014, background): “Missing residues in x-ray crystallographic structures in particular have become the de facto standard proxy to infer disorder (1,6,9–10).”
• Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “The natural abundance of intrinsic disorder was later supported by multiple comprehensive computational studies [3, 6, 17, 24, 44, 45], which are illustrated by Figure 1, where the correlation between the intrinsic disorder content and proteome size is shown for 3,484 viral, archaeal, bacterial, and”