To be folded or to be unfolded?
By Sergiy O. Garbuzynskiy, Michail Yu. Lobanov, Oxana V. Galzitskaya. 2004
74 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
- Vladimir N Uversky
- Zsuzsanna Dosztányi
- Lukasz Kurgan
- Burkhard Rost
- A. Keith Dunker
- Avner Schlessinger
- Bálint Mészáros
- István Simon
In Molecular Biology
- Vladimir N Uversky
- Lukasz Kurgan
- Zsuzsanna Dosztányi
- Burkhard Rost
- A. Keith Dunker
- Zhenling Peng
- Bálint Mészáros
- Avner Schlessinger
Citations in the corpus
- IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “The basic assumption of this method is that intrinsically disordered proteins have a specific amino acid composition that does not allow the formation of enough favorable inter-residue interactions to stabilize a well-defined structural state (20,21).”
- Improved Disorder Prediction by Combination of Orthogonal Approaches (2009, unknown): “Some methods focus on the fact that unstructured regions tend to have low hydrophobicity/high net-charge [3,36], high loop content [37], and few stable intra-chain contacts [38,39].”
- Intrinsic disorder and functional proteomics. (2007, background): “, hydropathy scale only (74) or expected number of contacts per residue (75), to predict disordered regions without significant loss of accuracy.”
- Natively Unstructured Loops Differ from Other Loops (2007, methodology): “Furthermore, methods using pairwise energy potentials, such as IUPred, to predict unstructured regions are also likely to miss these regions, as many cysteines typically coincide with many paired cysteine bonds that significantly contribute to protein stability [40,41].”
- The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. (2005, methodology): “This idea of the importance of interaction capacity has also been raised recently by work in which the average number of contacts per residue was used as an indicator of disorder.(46) Our quadratic formula combined with the energy predictor matrix captures the energetic aspect of this observation.”
- Natively unstructured regions in proteins identified from contact predictions (2007, background): “1) than wellstructured regions and can therefore be identified by average contact propensities (Dosztanyi, et al., 2005a; Dosztanyi, et al., 2005b; Garbuzynskiy, et al., 2004).”