DisProt: intrinsic protein disorder annotation in 2020
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Silvio C. E. Tosatto | Arne Elofsson | Marco Necci | Damiano Piovesan | Nevena Veljkovic | Patrick Ruch | Cristina Marino Buslje | Julien Gobeill | Emilie Pasche | Giovanni Minervini | Christos A. Ouzounis | Matteo Lambrughi | Elena Papaleo | Vasilis J. Promponas | Zsuzsanna Dosztányi | Bálint Mészáros | Lisanna Paladin | Valentin Iglesias | Salvador Ventura | Peter Tompa | A. Keith Dunker | Wim F. Vranken | Claudio Bassot | Tamás Horváth | Agnes Tantos | Beata Szabo | Ivan Micetic | Norman E. Davey | Alexander Miguel Monzon | Gustavo D. Parisi | Eva Schad | Emanuela Leonardi | Federica Quaglia | Elizabeth Martínez-Pérez | Rita Pancsa | Anastasia Chasapi | Tamas Lazar | Mainak Guharoy | Andrey V. Kajava | Sandra Macedo-Ribeiro | Jordi Pujols | John Lamb | Stella Tamana | Borbála Hajdu-Soltész | András Hatos | Lucía B. Chemes | Tamás Szaniszló | Radoslav Davidovic | Nicolas Palopoli | José A. Manso | Martina Bevilacqua | C. Ouzounis | Damiano Piovesan | E. Papaleo | A. Dunker | C. M. Buslje | N. Davey | P. Ruch | P. Tompa | A. Elofsson | Z. Dosztányi | W. Vranken | M. Guharoy | V. Promponas | M. Lambrughi | A. M. Monzon | S. Tosatto | G. Parisi | G. Sudha | Nicolás Palopoli | B. Szabó | R. Pancsa | S. Ventura | É. Schád | Valentín Iglesias | L. Paladin | Bálint Mészáros | Burcu Aykaç Fas | Emiliano Maiani | S. Macedo-Ribeiro | M. Salvatore | J. Manso | N. Veljkovic | A. Chasapi | G. Minervini | Federica Quaglia | A. Kajava | E. Pasche | J. Gobeill | Tamas Lazar | Elizabeth Martínez-Pérez | András Hatos | Tamás Szaniszló | E. Leonardi | P. Pereira | Jordi Pujols | I. Mičetić | M. Necci | R. Davidović | Mauricio Macossay-Castillo | Nikoletta Murvai | Á. Tantos | Borbála Hajdu-Soltész | Lucía Álvarez | Claudio Bassot | Guillermo I. Benítez | Martina Bevilacqua | N. S. G. Foutel | Tamás Horváth | Orsolya P Kovács | J. Lamb | Jeremy Y. Leclercq | Mátyás Pajkos | S. Tamana | Emiliano Maiani | Govindarajan Sudha | Lucía Álvarez | Nicolás S. González Foutel | Orsolya P. Kovacs | Mauricio Macossay-Castillo | Nikoletta Murvai | Mátyás Pajkos | Pedro J. Barbosa Pereira | Marco Salvatore | Patrick Ruch | L. Chemes | R. Davidovic | F. Quaglia | Orsolya P. Kovács | Sandra Macedo-Ribeiro | Elena Papaleo | Anastasia Chasapi | Rita Pancsa | Beáta Szabó | Govindarajan Sudha
[1] Alexander Sczyrba,et al. Common ELIXIR Service for Researcher Authentication and Authorisation , 2018, F1000Research.
[2] Vijay S Pande,et al. Finding Our Way in the Dark Proteome. , 2016, Journal of the American Chemical Society.
[3] A. Reményi,et al. Systematic analysis of somatic mutations driving cancer: Uncovering functional protein regions in disease development , 2016 .
[4] Silvio C. E. Tosatto,et al. The Pfam protein families database in 2019 , 2018, Nucleic Acids Res..
[5] Weilin Zhang,et al. Targeting intrinsically disordered proteins at the edge of chaos. , 2019, Drug discovery today.
[6] Sonia Longhi,et al. DisProt 7.0: a major update of the database of disordered proteins , 2016, Nucleic Acids Res..
[7] Christopher J. Oldfield,et al. Classification of Intrinsically Disordered Regions and Proteins , 2014, Chemical reviews.
[8] Erzsébet Fichó,et al. MFIB: a repository of protein complexes with mutual folding induced by binding , 2017, Bioinform..
[9] E. Myers,et al. Basic local alignment search tool. , 1990, Journal of molecular biology.
[10] Silvio C. E. Tosatto,et al. A comprehensive assessment of long intrinsic protein disorder from the DisProt database , 2018, Bioinform..
[11] Robert D. Finn,et al. The challenge of increasing Pfam coverage of the human proteome , 2013, Database J. Biol. Databases Curation.
[12] Sophia Ananiadou,et al. Europe PMC: a full-text literature database for the life sciences and platform for innovation , 2014, Nucleic Acids Res..
[13] Katrine Bugge,et al. Extreme disorder in an ultrahigh-affinity protein complex , 2018, Nature.
[14] H. Dyson,et al. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. , 1999, Journal of molecular biology.
[15] C. Brangwynne,et al. Liquid phase condensation in cell physiology and disease , 2017, Science.
[16] Lukasz Kurgan,et al. Untapped Potential of Disordered Proteins in Current Druggable Human Proteome. , 2016, Current drug targets.
[17] M. Madan Babu,et al. The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease , 2016, Biochemical Society transactions.
[18] Norman E. Davey,et al. The functional importance of structure in unstructured protein regions. , 2019, Current opinion in structural biology.
[19] P. Tompa. The interplay between structure and function in intrinsically unstructured proteins , 2005, FEBS letters.
[20] A. Mapp,et al. From Fuzzy to Function: The New Frontier of Protein-Protein Interactions. , 2017, Accounts of chemical research.
[21] B. Rost,et al. Unexpected features of the dark proteome , 2015, Proceedings of the National Academy of Sciences.
[22] K. Kavanagh,et al. Structure and Mechanism of Human UDP-glucose 6-Dehydrogenase , 2011, The Journal of Biological Chemistry.
[23] Anna Tramontano,et al. Assessment of protein disorder region predictions in CASP10 , 2014, Proteins.
[24] Silvio C. E. Tosatto,et al. MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins , 2017, Nucleic Acids Res..
[25] Philipp Selenko,et al. Structural disorder of monomeric α-synuclein persists in mammalian cells , 2016, Nature.
[26] Zsuzsanna Dosztányi,et al. DIBS: a repository of disordered binding sites mediating interactions with ordered proteins , 2017, Bioinform..
[27] M. Franzblau,et al. Conflict of Interest Statement , 2004 .
[28] M. Ashburner,et al. The OBO Foundry: coordinated evolution of ontologies to support biomedical data integration , 2007, Nature Biotechnology.
[29] Patrick Ruch,et al. neXtA5: accelerating annotation of articles via automated approaches in neXtProt , 2016, Database J. Biol. Databases Curation.
[30] The UniProt Consortium,et al. UniProt: a worldwide hub of protein knowledge , 2018, Nucleic Acids Res..
[31] S. Harvey,et al. The entropic force generated by intrinsically disordered segments tunes protein function , 2018, Nature.
[32] A K Dunker,et al. Thousands of proteins likely to have long disordered regions. , 1998, Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing.
[33] Yongqi Huang,et al. Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding , 2019, Protein science : a publication of the Protein Society.
[34] Silvio C. E. Tosatto,et al. Where differences resemble: sequence-feature analysis in curated databases of intrinsically disordered proteins , 2018, Database J. Biol. Databases Curation.
[35] Dragan Ivanovic,et al. Towards the Information System for Research Programmes of the Ministry of Education, Science and Technological Development of the Republic of Serbia , 2017, CRIS.
[36] David A. Lee,et al. Gene3D: Extensive prediction of globular domains in proteins , 2017, Nucleic Acids Res..
[37] Silvio C. E. Tosatto,et al. Large‐scale analysis of intrinsic disorder flavors and associated functions in the protein sequence universe , 2016, Protein science : a publication of the Protein Society.
[38] Toby J. Gibson,et al. The eukaryotic linear motif resource – 2018 update , 2017, Nucleic Acids Res..
[39] Damiano Piovesan,et al. INGA 2.0: improving protein function prediction for the dark proteome , 2019, Nucleic Acids Res..
[40] D. Selkoe,et al. α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation , 2011, Nature.