دورية أكاديمية

DisProt 7.0: a major update of the database of disordered proteins

التفاصيل البيبلوغرافية
العنوان: DisProt 7.0: a major update of the database of disordered proteins
المؤلفون: Piovesan, Damiano, Tabaro, Francesco, Micetic, Ivan, Necci, Marco, Quaglia, Federica, Oldfield, Christopher J., Aspromonte, Maria Cristina, Davey, Norman E., Davidović, Radoslav S., Dosztanyi, Zsuzsanna, Elofsson, Arne, Gasparini, Alessandra, Hatos, Andras, 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 V., Ventura, Salvador, Vranken, Wim, Warholm, Per, Uversky, Vladimir N., Dunker, A. Keith, Longhi, Sonia, Tompa, Peter, Tosatto, Silvio C. E.
المصدر: Nucleic Acids Research
سنة النشر: 2017
المجموعة: VinaR Repository (Vinča Institute of Nuclear Sciences / University of Belgrade)
الوصف: 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.
نوع الوثيقة: article in journal/newspaper
اللغة: unknown
تدمد: 0305-1048
1362-4962
العلاقة: info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/173001/RS//; info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/173049/RS//; COST Action BM1405 NGP-net, ELIXIR-IIB, Hungarian Academy of Sciences [LP2014-16], Hungarian Scientific Research Fund [OTKA K 108798], AIRC Research Fellowship, Spanish Ministerio de Educacion Cultura i Deporte PhD Fellowship, Mexican National Council for Science and Technology (CONACYT) [215503], Grant PortoNeuroDRIve'i3S - Norte Portugal Regional Operational Programme (NORTE), under the PORTUGAL Partnership Agreement, through the European Regional Development Fund (ERDF), Direction Generale des Armees, Aix-Marseille University PhD Fellowship, OTKA Grant [PD-OTKA 108772], French Ministry of National Education, Research and Technology PhD Fellowship, ICREAAcademia Award, Odysseus Grant from Research Foundation Flanders (FWO) [G.0029.12], AIRC IG Grant [17753], Italian Ministry of Health [GR-2011-02347754, GR-2011-02346845], Swedish Research Council Grant [VR-NT 2012-5046]; https://vinar.vin.bg.ac.rs/handle/123456789/1464Test; 000396575500033; 2-s2.0-85016112986; https://vinar.vin.bg.ac.rs//bitstream/id/11836/1460.pdfTest
DOI: 10.1093/nar/gkw1056
الإتاحة: https://doi.org/10.1093/nar/gkw1056Test
https://vinar.vin.bg.ac.rs/handle/123456789/1464Test
https://vinar.vin.bg.ac.rs//bitstream/id/11836/1460.pdfTest
حقوق: openAccess ; https://creativecommons.org/licenses/by-nc/4.0Test/ ; BY-NC
رقم الانضمام: edsbas.73455B9E
قاعدة البيانات: BASE
الوصف
تدمد:03051048
13624962
DOI:10.1093/nar/gkw1056