DisProt 7.0: a major update of the database of disordered proteins
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DisProt 7.0 : a major update of the database of disordered proteins. / Piovesan, Damiano; Tabaro, Francesco; Mičetić, Ivan; Necci, Marco; Quaglia, Federica; Oldfield, Christopher J; Aspromonte, Maria Cristina; Davey, Norman E.; Davidović, Radoslav; Dosztányi, Zsuzsanna; Elofsson, Arne; Gasparini, Alessandra; Hatos, András; Kajava, Andrey V.; Kalmar, Lajos; Leonardi, Emanuela; Lazar, Tamas; Macedo-Ribeiro, Sandra; Macossay-Castillo, Mauricio; Meszaros, Attila; Minervini, Giovanni; Murvai, Nikoletta; Pujols, Jordi; Roche, Daniel B; Salladini, Edoardo; Schad, Eva; Schramm, Antoine; Szabo, Beata; Tantos, Agnes; Tonello, Fiorella; Tsirigos, Konstantinos D.; Veljković, Nevena; Ventura, Salvador; Vranken, Wim; Warholm, Per; Uversky, Vladimir N; Dunker, A Keith; Longhi, Sonia; Tompa, Peter; Tosatto, Silvio C E.
In: Nucleic Acids Research, Vol. 45, No. D1, 2017, p. D219-D227.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - DisProt 7.0
T2 - a major update of the database of disordered proteins
AU - Piovesan, Damiano
AU - Tabaro, Francesco
AU - Mičetić, Ivan
AU - Necci, Marco
AU - Quaglia, Federica
AU - Oldfield, Christopher J
AU - Aspromonte, Maria Cristina
AU - Davey, Norman E.
AU - Davidović, Radoslav
AU - Dosztányi, Zsuzsanna
AU - Elofsson, Arne
AU - Gasparini, Alessandra
AU - Hatos, András
AU - Kajava, Andrey V.
AU - Kalmar, Lajos
AU - Leonardi, Emanuela
AU - Lazar, Tamas
AU - Macedo-Ribeiro, Sandra
AU - Macossay-Castillo, Mauricio
AU - Meszaros, Attila
AU - Minervini, Giovanni
AU - Murvai, Nikoletta
AU - Pujols, Jordi
AU - Roche, Daniel B
AU - Salladini, Edoardo
AU - Schad, Eva
AU - Schramm, Antoine
AU - Szabo, Beata
AU - Tantos, Agnes
AU - Tonello, Fiorella
AU - Tsirigos, Konstantinos D.
AU - Veljković, Nevena
AU - Ventura, Salvador
AU - Vranken, Wim
AU - Warholm, Per
AU - Uversky, Vladimir N
AU - Dunker, A Keith
AU - Longhi, Sonia
AU - Tompa, Peter
AU - Tosatto, Silvio C E
N1 - © The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.
PY - 2017
Y1 - 2017
N2 - The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance (primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.
AB - The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance (primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.
KW - Animals
KW - Crystallography, X-Ray
KW - Databases, Protein
KW - Fluorescence Resonance Energy Transfer
KW - Forecasting
KW - Forms and Records Control
KW - Humans
KW - Intrinsically Disordered Proteins/classification
KW - Nuclear Magnetic Resonance, Biomolecular
KW - Protein Conformation
U2 - 10.1093/nar/gkw1056
DO - 10.1093/nar/gkw1056
M3 - Journal article
C2 - 27899601
VL - 45
SP - D219-D227
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - D1
ER -
ID: 238682431