D2P2: database of disordered protein predictions
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Lukasz A. Kurgan | Mohamed F. Ghalwash | Zoran Obradovic | Takashi Ishida | Bin Xue | Zsuzsanna Dosztányi | A. Keith Dunker | Pedro Romero | Julian Gough | Vladimir N. Uversky | Matt E. Oates | Marcin J. Mizianty | J. Gough | P. Romero | Z. Obradovic | A. Dunker | Lukasz Kurgan | T. Ishida | V. Uversky | Z. Dosztányi | B. Xue | M. Mizianty
[1] G. Hong,et al. Nucleic Acids Research , 2015, Nucleic Acids Research.
[2] Zoran Obradovic,et al. DisProt: the Database of Disordered Proteins , 2006, Nucleic Acids Res..
[3] M. Bolognesi,et al. Function and Structure of Inherently Disordered Proteins This Review Comes from a Themed Issue on Proteins Edited Prediction of Non-folding Proteins and Regions Frequency of Disordered Regions Protein Evolution Partitioning Unstructured Proteins and Regions into Groups Involvement of Inherently Diso , 2022 .
[4] Janusz M. Bujnicki,et al. MetaDisorder: a meta-server for the prediction of intrinsic disorder in proteins , 2012, BMC Bioinformatics.
[5] Cyrus Chothia,et al. SUPERFAMILY 1.75 including a domain-centric gene ontology method , 2010, Nucleic Acids Res..
[6] A. Dunker,et al. Predicting intrinsic disorder in proteins: an overview , 2009, Cell Research.
[7] Tim J. P. Hubbard,et al. SCOP database in 2004: refinements integrate structure and sequence family data , 2004, Nucleic Acids Res..
[8] Motonori Ota,et al. IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature , 2011, Nucleic Acids Res..
[9] John L Markley,et al. Micelle-induced folding of spinach thylakoid soluble phosphoprotein of 9 kDa and its functional implications. , 2006, Biochemistry.
[10] Silvio C. E. Tosatto,et al. ESpritz: accurate and fast prediction of protein disorder , 2012, Bioinform..
[11] A G Murzin,et al. SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.
[12] Anna Tramontano,et al. Evaluation of disorder predictions in CASP9 , 2011, Proteins.
[13] Kengo Kinoshita,et al. PrDOS: prediction of disordered protein regions from amino acid sequence , 2007, Nucleic Acids Res..
[14] A Keith Dunker,et al. Conservation of intrinsic disorder in protein domains and families: II. functions of conserved disorder. , 2006, Journal of proteome research.
[15] Zsuzsanna Dosztányi,et al. Prediction of Protein Binding Regions in Disordered Proteins , 2009, PLoS Comput. Biol..
[16] Xinchen Wang,et al. Tissue-specific alternative splicing remodels protein-protein interaction networks. , 2012, Molecular cell.
[17] C. Chothia,et al. Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. , 2001, Journal of molecular biology.
[18] L. Iakoucheva,et al. The importance of intrinsic disorder for protein phosphorylation. , 2004, Nucleic acids research.
[19] Lukasz Kurgan,et al. Comprehensive comparative assessment of in-silico predictors of disordered regions. , 2012, Current protein & peptide science.
[20] P. Romero,et al. Sequence complexity of disordered protein , 2001, Proteins.
[21] A.K. Dunker,et al. Identifying disordered regions in proteins from amino acid sequence , 1997, Proceedings of International Conference on Neural Networks (ICNN'97).
[22] Bin Zhang,et al. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse , 2011, Nucleic Acids Res..
[23] BMC Bioinformatics , 2005 .
[24] Zoran Obradovic,et al. Length-dependent prediction of protein intrinsic disorder , 2006, BMC Bioinformatics.
[25] H. Dyson,et al. Intrinsically unstructured proteins and their functions , 2005, Nature Reviews Molecular Cell Biology.
[26] D T Jones,et al. Protein secondary structure prediction based on position-specific scoring matrices. , 1999, Journal of molecular biology.
[27] Takashi Gojobori,et al. Development of an accurate classification system of proteins into structured and unstructured regions that uncovers novel structural domains: its application to human transcription factors , 2009, BMC Structural Biology.
[28] Jessica W. Chen. Conversation of Intrinsic Disorder in Protein Domains and Families , 2005 .
[29] David S. Goodsell,et al. The RCSB Protein Data Bank: redesigned web site and web services , 2010, Nucleic Acids Res..
[30] Silvio C. E. Tosatto,et al. MobiDB: a comprehensive database of intrinsic protein disorder annotations , 2012, Bioinform..
[31] Takashi Gojobori,et al. Binary classification of protein molecules into intrinsically disordered and ordered segments , 2011, BMC Structural Biology.
[32] Joshua L. Phillips,et al. A Bimodal Distribution of Two Distinct Categories of Intrinsically Disordered Structures with Separate Functions in FG Nucleoporins* , 2010, Molecular & Cellular Proteomics.
[33] J. S. Sodhi,et al. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. , 2004, Journal of molecular biology.
[34] Obradovic,et al. Predicting Protein Disorder for N-, C-, and Internal Regions. , 1999, Genome informatics. Workshop on Genome Informatics.
[35] Silvio C. E. Tosatto,et al. MOBI: a web server to define and visualize structural mobility in NMR protein ensembles , 2010, Bioinform..
[36] Mohamed F Ghalwash,et al. Uncertainty analysis in protein disorder prediction. , 2012, Molecular bioSystems.
[37] V. Uversky. Natively unfolded proteins: A point where biology waits for physics , 2002, Protein science : a publication of the Protein Society.
[38] Lukasz A. Kurgan,et al. On the Complementarity of the Consensus-Based Disorder Prediction , 2011, Pacific Symposium on Biocomputing.
[39] P. Romero,et al. Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions. , 2006, Journal of Proteome Research.
[40] Burkhard Rost,et al. PHD - an automatic mail server for protein secondary structure prediction , 1994, Comput. Appl. Biosci..
[41] P. Tompa,et al. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. , 2005, Journal of molecular biology.
[42] Roland L. Dunbrack,et al. PONDR-FIT: a meta-predictor of intrinsically disordered amino acids. , 2010, Biochimica et biophysica acta.
[43] A. Biegert,et al. Sequence context-specific profiles for homology searching , 2009, Proceedings of the National Academy of Sciences.
[44] V. Uversky,et al. Why are “natively unfolded” proteins unstructured under physiologic conditions? , 2000, Proteins.