dc.contributor.authorAdav, Sunil S.
dc.contributor.authorRavindran, Anita
dc.contributor.authorSze, Siu Kwan
dc.date.accessioned2017-01-19T07:12:25Z
dc.date.available2017-01-19T07:12:25Z
dc.date.issued2015
dc.identifier.citationAdav, S. S., Ravindran, A., & Sze, S. K. (2015). Data for iTRAQ secretomic analysis of Aspergillus fumigatus in response to different carbon sources. Data in Brief, 3, 175-179.en_US
dc.identifier.issn2352-3409en_US
dc.identifier.urihttp://hdl.handle.net/10220/42058
dc.description.abstractHere, we provide data related to the research article entitled “Quantitative proteomics study of Aspergillus fumigatus secretome revealed deamidation of secretory enzymes” by Adav et al. (J. Proteomics (2015) [1]). Aspergillus sp. plays an important role in lignocellulosic biomass recycling. To explore biomass hydrolyzing enzymes of A. fumigatus, we profiled secretome under different carbon sources such as glucose, cellulose, xylan and starch by high throughput quantitative proteomics using isobaric tags for relative and absolute quantification (iTRAQ). The data presented here represents the detailed comparative abundances of diverse groups of biomass hydrolyzing enzymes including cellulases, hemicellulases, lignin degrading enzymes, and peptidases and proteases; and their post translational modification like deamidation.en_US
dc.description.sponsorshipMOE (Min. of Education, S’pore)en_US
dc.format.extent5 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesData in Briefen_US
dc.rights© 2015 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).en_US
dc.subjectAspergillus fumigatesen_US
dc.subjectBioenergyen_US
dc.titleData for iTRAQ secretomic analysis of Aspergillus fumigatus in response to different carbon sourcesen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1016/j.dib.2015.03.001
dc.description.versionPublished versionen_US


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