Assessing protein disorder and induced folding

By V. Receveur-Bréchot, J. Bourhis, Vladimir N Uversky, Bruno Canard, Sonia Longhi. 2005

458 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

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. Lukasz Kurgan
3. Burkhard Rost
4. A. Keith Dunker
5. Zsuzsanna Dosztányi
6. Avner Schlessinger
7. Christopher J. Oldfield
8. Yaoqi Zhou

In Molecular Biology

1. Vladimir N Uversky
2. Lukasz Kurgan
3. Burkhard Rost
4. A. Keith Dunker
5. Zsuzsanna Dosztányi
6. Yaoqi Zhou
7. Avner Schlessinger
8. Zhenling Peng

In Spectroscopy

1. Vladimir N Uversky
2. Zsuzsanna Dosztányi
3. A. Keith Dunker
4. Burkhard Rost
5. Avner Schlessinger
6. Marco Punta
7. Christopher J. Oldfield
8. Peter Tompa

Citations in the corpus

• SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, background): “Due to the extensive monetary and time cost of experimental procedures, such as nuclear magnetic resonance (NMR), Xray crystallography, and circular dichroism (CD) [12,13], many computational methods have been designed to bridge the growing gap between unannotated and annotated protein structures an”
• DisProt 7.0: a major update of the database of disordered proteins (2016, positive): “Therefore, beyond X-ray crystallography and NMR, a plethora of alternative biochemical and bio-physical approaches (termed ‘secondary techniques’) provide orthogonal information on protein disorder in DisProt (4,22).”
• How Random are Intrinsically Disordered Proteins? A Small Angle Scattering Perspective (2012, background): “Only a strategic combination of complementary structural and biophysical techniques would allow one to decipher their mode of action at the structural level [12].”
• MetaDisorder: a meta-server for the prediction of intrinsic disorder in proteins (2012, background): “Intrinsically unfolded proteins, once purified, can be identified by various experimental methods [6-9].”
• Length-dependent prediction of protein intrinsic disorder (2006, background): “On the other hand, in comparison to the random coil-like form, the pre-molten globule form is less extended, contains more (usually transient) secondary structure and also exhibits more evidence for hydrophobic clusters [11].”
• Improved Disorder Prediction by Combination of Orthogonal Approaches (2009, methodology): “Thus, there is no single gold standard for order/disorder assignment; instead, we need to use several experimental methods in concert [5,12,13,14,15,16,17].”