DisProt: a database of protein disorder

By Slobodan Vucetic, Zoran Obradovic, Vladimir Vacic, Predrag Radivojac, Kang Peng, Lilia M. Iakoucheva, Marc S. Cortese, J. David Lawson, C. Brown, Jason G. Sikes and 2 more. 2005

237 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. 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. Zsuzsanna Dosztányi
5. A. Keith Dunker
6. Zhenling Peng
7. Yaoqi Zhou
8. Fanchi Meng

Citations in the corpus

• SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, methodology): “To summarize, we obtained 4229 non-redundant, high-resolution protein sequences from the Protein Data Bank (PDB) and Database of Protein Disorder (DisProt) [42].”
• DisProt 7.0: a major update of the database of disordered proteins (2016, positive): “DisProt is the primary repository of disorder-related data on sequence-and functional annotations, focusing on disordered proteins or regions with experimental verification (13,14).”
• Improved Disorder Prediction by Combination of Orthogonal Approaches (2009, background): “. Since different experimental techniques capture different aspects or types of protein disorder, they occasionally do not agree on the assignments of these regions”
• Intrinsically unstructured proteins and their functions (2005, background): “, and a database of protein disorder has recently been establishe”
• Assessing protein disorder and induced folding (2005, background): “org).(25) Furthermore, comprehensive description of the experimental approaches for the study of protein intrinsic disorder is scarce, except for a few examples.”
• Natively Unstructured Loops Differ from Other Loops (2007, background): “]. Thanks to the outstanding data collection by the Dunker group, we could also describe this as regions that are the minimal common denominator between all proteins collected in DisProt [”
• Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling (2005, background): “Nevertheless, various reports have been analyzed and the ID regions that have been adequately characterized have been put into a curated Database of Disordered Proteins (DisProt; Vucetic et al., 2005).”
• Length-dependent prediction of protein intrinsic disorder (2006, background): “2) [45] with 160 long (>30 residues) and 28 short (≤30 residues) disordered regions, 511 PDB chains with 42 long and 929 short disordered regions [39], 290 completely folded PDB chains [39,46], and 373 recent PDB chains (released before June, 2004) with 15 long and 432 short disordered regions.”
• Prediction of intrinsic disorder and its use in functional proteomics. (2007, background): “Although numerous predictors of intrinsic disorder are currently available as web servers (see DisProt website, http://www.disprot.org, for a complete list of such servers), focus will be on utilization of PONDR tools, as they cover a wide range of potential applications of ID concept for structural”
• Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes (2006, methodology): “Here, amino acid compositions of ordered and disordered hubs and ends were compared with the amino acid composition of disordered protein regions extracted from the DisProt database [”
• The interplay between structure and function in intrinsically unstructured proteins (2005, methodology): “For almost 200 proteins and protein domains [18], the lack of a unique 3D structure has been convincingly demonstrated by using three techniques mostly, X-ray crystallography, mul-”
• Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions (2017, background): “Figure 1A shows predictions of disordered protein binding regions from DisoRDPbind and putative MoRF regions generated by MoRFpred, ANCHOR, MFSPSSMpred, and MoRFCHiBiWeb for anophelin protein (DisProt ID: DP00824).”
• Intrinsic disorder and functional proteomics. (2007, background): “This figure compares the compositions of the 460 proteins currently available in the database with the compositions of the 152 proteins present in DisProt in July 2002, with the amino acids arranged in order for the larger database.”