共 19 条
DisProt 7.0: a major update of the database of disordered proteins (vol 45, pg D219, 2017)
被引:32
作者:
Piovesan, Damiano
[1
]
Tabaro, Francesco
[1
,2
]
Micetic, Ivan
[1
]
Necci, Marco
[1
]
Quaglia, Federica
[1
]
Oldfield, Christopher J.
[3
]
Aspromonte, Maria Cristina
[4
]
Davey, Norman E.
[5
,6
]
Davidovic, Radoslav
[7
]
Dosztanyi, Zsuzsanna
[8
,9
]
Elofsson, Arne
Gasparini, Alessandra
[4
]
Hatos, Andras
[1
,9
]
Kajava, Andrey V.
[11
,12
,13
]
Kalmar, Lajos
[9
,14
]
Leonardi, Emanuela
[4
]
Lazar, Tamas
Macedo-Ribeiro, Sandra
[17
,18
]
Macossay-Castillo, Mauricio
[15
,16
]
Meszaros, Attila
Minervini, Giovanni
[1
]
Murvai, Nikoletta
Pujols, Jordi
Roche, Daniel B.
[12
]
Salladini, Edoardo
Schad, Eva
[9
]
Schramm, Antoine
Szabo, Beata
[9
]
Tantos, Agnes
[9
]
Tonello, Fiorella
[1
,21
]
Tsirigos, Konstantinos D.
[10
]
Veljkovic, Nevena
[7
]
Ventura, Salvador
[19
]
Vranken, Wim
[15
,16
,22
]
Warholm, Per
Uversky, Vladimir N.
[23
,24
,25
]
Dunker, A. Keith
[3
]
Longhi, Sonia
[20
]
Tompa, Peter
[9
,15
,16
]
Tosatto, Silvio C. E.
[1
,21
]
机构:
[1] Univ Padua, Dept Biomed Sci, I-35121 Padua, Italy
[2] Univ Tampere, Inst Biosci & Med Technol, Tampere, Finland
[3] Indiana Univ, Sch Med, Ctr Computat Biol & Bioinformat, Indianapolis, IN 46202 USA
[4] Univ Padua, Dept Woman & Child Hlth, I-35128 Padua, Italy
[5] Univ Coll Dublin, Conway Inst Biomol & Biomed Res, Dublin 4, Ireland
[6] Univ Coll Dublin, Ireland UCD Sch Med Med Sci, Dublin 4, Ireland
[7] Univ Belgrade, Ctr Multidisciplinary Res, Inst Nucl Sci Vinca, Belgrade 11001, Serbia
[8] Eotvos Lorand Univ, Dept Biochem, MTA ELTE Lendulet Bioinformat Res Grp, 1-C Pazmany Peter Setany, H-1117 Budapest, Hungary
[9] Hungarian Acad Sci, Res Ctr Nat Sci, Inst Enzymol, POB 7, H-1518 Budapest, Hungary
[10] Stockholm Univ, Dept Biochem & Biophys, Sci Life Lab, Box 1031, S-17121 Solna, Sweden
[11] Univ Montpellier, Ctr Rech Biol Cellulaire Montpellier CRBM, CNRS, UMR 5237, 1919 Route Mende, F-34293 Montpellier 5, France
[12] Inst Biol Computationnelle IBC, F-34095 Montpellier, France
[13] Univ ITMO, Inst Bioengn, St Petersburg 197101, Russia
[14] Univ Cambridge, Dept Vet Med, Madingley Rd, Cambridge CB3 0ES, England
[15] Vrije Univ Brussel VUB, Struct Biol Brussels, B-1050 Brussels, Belgium
[16] Struct Biol Res Ctr SBRC, Flanders Inst Biotechnol VIB, B-1050 Brussels, Belgium
[17] Univ Porto, Inst Biol Mol Celular IBMC, Biomol Struct & Funct Grp, P-4200135 Oporto, Portugal
[18] Univ Porto, Inst Invest Inovacao Saude i3S, P-4200135 Oporto, Portugal
[19] Autonomous Univ Barcelona, Inst Biotecnol & Biomed, Dept Bioquim & Biol Mol, Bellaterra 08193, Spain
[20] Aix Marseille Univ, CNRS, AFMB, UMR 7257, Marseille, France
[21] CNR, Inst Neurosci, I-35121 Padua, Italy
[22] ULB VUB, Interuniv Inst Bioinformat Brussels IB2, B-1050 Brussels, Belgium
[23] Russian Acad Sci, Inst Cytol, Lab Struct Dynam Stabil & Folding Proteins, St Petersburg 194064, Russia
[24] Univ S Florida, Dept Mol Med, Tampa, FL 33612 USA
[25] Univ S Florida, USF Hlth Byrd Alzheimers Res Inst, Morsani Coll Med, Tampa, FL 33612 USA
基金:
匈牙利科学研究基金会;
瑞典研究理事会;
关键词:
D O I:
10.1093/nar/gkw1279
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
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.
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页码:D1123 / D1124
页数:2
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