Please use this identifier to cite or link to this item: http://223.31.159.10:8080/jspui/handle/123456789/644
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dc.contributor.authorBarua, Pragya-
dc.contributor.authorSubba, Pratigya-
dc.contributor.authorLande, Nilesh Vikram-
dc.contributor.authorMangalaparthi, Kiran K.-
dc.contributor.authorPrasad, T.S. Keshava-
dc.contributor.authorChakraborty, Subhra-
dc.contributor.authorChakraborty, Niranjan-
dc.date.accessioned2016-05-03T07:07:29Z-
dc.date.available2016-05-03T07:07:29Z-
dc.date.issued2016-
dc.identifier.citationJ. Proteomics, 143: 199-208en_US
dc.identifier.issn1874-3919-
dc.identifier.urihttp://172.16.0.77:8080/jspui/handle/123456789/644-
dc.descriptionAccepted date: 18 April 2016en_US
dc.description.abstractPlasma membrane (PM) encompasses total cellular contents, serving as semi-porous barrier to cell exterior. This living barrier regulates all cellular exchanges in a spatio-temporal fashion. Most of the essential tasks of PMs including molecular transport, cell-cell interaction and signal transduction are carried out by their proteinaceous components, which make the PM protein repertoire to be diverse and dynamic. Here, we report the systematic analysis of PM proteome of a food legume, chickpea and develop a PM proteome reference map. Proteins were extracted from highly enriched PM fraction of four-week-old seedlings using aqueous two-phase partitioning. To address a population of PM proteins that is as comprehensive as possible, both gel-based and gel-free approaches were employed, which led to the identification of a set of 2732 non-redundant proteins. These included both integral proteins having bilayer spanning domains as well as peripheral proteins associated with PMs through posttranslational modifications or protein-protein interactions. Further, the proteins were subjected to various in-silico analyses and functionally classified based on their gene ontology. Finally an inventory of the complete set of PM proteins, identified in several monocot and dicot species, was created for comparative study with the generated PM protein dataset of chickpea.en_US
dc.description.sponsorshipThis work was supported by a grant [BT/AGR/CG-Phase-II] from the Department of Biotechnology (DBT), Govt. of India. The authors thank DBT and Council of Scientific and Industrial Research (CSIR) for providing research fellowship to PB and NVL, respectively. The authors gratefully acknowledge International Crops Research Institute for the Semi-Arid Tropics (ICRISAT), Hyderabad, India for providing chickpea seeds. Mr. Jasbeer Singh is thanked for manuscript layout and format, and the artwork.en_US
dc.language.isoen_USen_US
dc.publisherElsevier B.V.en_US
dc.subjectFood legumeen_US
dc.subjectHydropathy indicesen_US
dc.subjectLC-MS/MS analysisen_US
dc.subjectPlasma membrane proteomeen_US
dc.subjectPosttranslational modificationsen_US
dc.subjectTrans-membrane domainen_US
dc.titleGel-based and gel-free search for plasma membrane proteins in chickpea (Cicer arietinum L.) augments the comprehensive data sets of membrane protein repertoireen_US
dc.typeArticleen_US
dc.identifier.officialurlhttp://www.sciencedirect.com/science/article/pii/S1874391916301373en_US
dc.identifier.doi10.1016/j.jprot.2016.04.015en_US
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