Molecular principles of the interactions of disordered proteins.
By Bálint Mészáros, Peter Tompa, István Simon, Zsuzsanna Dosztányi. 2007
294 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
- Vladimir N Uversky
- István Simon
- Gábor Erdös
- Peter E. Wright
- H. J. Dyson
- Tomislav Domazet-Lošo
In Molecular Biology
- Zsuzsanna Dosztányi
- Vladimir N Uversky
- Bálint Mészáros
- Gábor Erdös
- István Simon
- Lukasz Kurgan
- Peter E. Wright
- H. J. Dyson
Citations in the corpus
- IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “Such disordered binding regions or MoRFs (molecular recognition features) commonly occur in modular proteins involved in signaling and regulation (3,4).”
- ANCHOR: web server for predicting protein binding regions in disordered proteins (2009, unknown): “Multiple disordered binding regions were predicted, and several of these can be confirmed experimentally [see Mészáros et al. (2009) for more details].”
- The evolutionary origin of orphan genes (2011, background): “There is also an increasing awareness that proteins and protein regions do not have to be structured to be functiona”
- Linking Folding and Binding (2009, background): “A survey of the intermolecular interfaces in IDP complexes indicated that IDPs rely more on hydrophobic interactions than their globular counterparts and form a more intimate fit with their binding partners [24].”
- Prediction of Protein Binding Regions in Disordered Proteins (2009, methodology): “These regions are linear in sequence, unlike in the case of globular proteins, where distinct sites in the amino acid sequence are brought together to form the interface for interaction [43].”
- Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins (2010, background): “Nevertheless, evolutionary conserved IDPs can also be found, especially among those that are involved in complex formation [26, 75].”