MobiDB 3.0: More annotations for intrinsic disorder, conformational diversity and interactions in proteins

التفاصيل البيبلوغرافية
العنوان: MobiDB 3.0: More annotations for intrinsic disorder, conformational diversity and interactions in proteins
المؤلفون: Eva Schad, Silvio C. E. Tosatto, Alexander Miguel Monzon, Zsuzsanna Dosztányi, Ivan Mičetić, Damiano Piovesan, Pietro Sormanni, Lisanna Paladin, Francesco Tabaro, Bálint Mészáros, Gustavo Parisi, Michele Vendruscolo, Carlo Camilloni, Peter Tompa, Marco Necci, Wim F. Vranken, Norman E. Davey
المساهمون: Lääketieteen ja biotieteiden tiedekunta - Faculty of Medicine and Life Sciences, University of Tampere, Structural Biology Brussels, Department of Bio-engineering Sciences, Informatics and Applied Informatics, Chemistry, Basic (bio-) Medical Sciences
المصدر: Nucleic acids research, 46 (D1
Nucleic Acids Research
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
بيانات النشر: Oxford University Press, 2018.
سنة النشر: 2018
مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Protein Folding, DATABASE, Protein Data Bank (RCSB PDB), Datasets as Topic, Information layer, Roentgen rays, Computational biology, Biology, Indirect evidence, Biokemia, solu- ja molekyylibiologia - Biochemistry, cell and molecular biology, purl.org/becyt/ford/1 [https], 03 medical and health sciences, Annotation, Journal Article, Genetics, Database Issue, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, Databases, Protein, Protein secondary structure, Search function, Internet, Binding Sites, PROTEIN DISORDER, Molecular Sequence Annotation, purl.org/becyt/ford/1.2 [https], Intrinsically Disordered Proteins, Gene Ontology, 030104 developmental biology, Ciencias de la Computación e Información, INTRINSIC DISORDER, UniProt, Sequence Alignment, Biologie, Ciencias de la Información y Bioinformática, Software, CIENCIAS NATURALES Y EXACTAS, Protein Binding
الوصف: The MobiDB (URL: mobidb.bio.unipd.it) database of protein disorder and mobility annotations has been significantly updated and upgraded since its last major renewal in 2014. Several curated datasets for intrinsic disorder and folding upon binding have been integrated from specialized databases. The indirect evidence has also been expanded to better capture information available in the PDB, such as high temperature residues in X-ray structures and overall conformational diversity. Novel nuclear magnetic resonance chemical shift data provides an additional experimental information layer on conformational dynamics. Predictions have been expanded to provide new types of annotation on backbone rigidity, secondary structure preference and disordered binding regions. MobiDB 3.0 contains information for the complete UniProt protein set and synchronization has been improved by covering all UniParc sequences. An advanced search function allows the creation of a wide array of custom-made datasets for download and further analysis. A large amount of information and cross-links to more specialized databases are intended to make MobiDB the central resource for the scientific community working on protein intrinsic disorder and mobility.
SCOPUS: ar.j
info:eu-repo/semantics/published
وصف الملف: application/pdf; fulltext; D471-D476; 1 full-text file(s): application/pdf
اللغة: English
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2a173b8e499eafa1f22f66340d235ae
https://academic.oup.com/nar/article/46/D1/D471/4612964
Rights: OPEN
رقم الانضمام: edsair.doi.dedup.....f2a173b8e499eafa1f22f66340d235ae
قاعدة البيانات: OpenAIRE