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dc.contributor.author Nath, Krishna -
dc.contributor.author Jajoo, Anjana -
dc.contributor.author Poudyal, Roshan Sharma -
dc.contributor.author Timilsina, Rupak -
dc.contributor.author Park, Yu Shin -
dc.contributor.author Aro, Eva-Mari -
dc.contributor.author Nam, Hong Gil -
dc.contributor.author Lee, C. -H. -
dc.date.available 2017-05-11T01:55:43Z -
dc.date.created 2017-04-10 -
dc.date.issued 2013-11 -
dc.identifier.issn 0014-5793 -
dc.identifier.uri http://hdl.handle.net/20.500.11750/1691 -
dc.description.abstract Photosystem II (PSII) is vulnerable to high light (HL) illumination resulting in photoinhibition. In addition to photoprotection mechanisms, plants have developed an efficient PSII repair mechanism to save themselves from irreversible damage to PSII under abiotic stresses including HL illumination. The phosphorylation/dephosphorylation cycle along with subsequent degradation of photodamaged D1 protein to be replaced by the insertion of a newly synthesized copy of D1 into the PSII complex, is the core function of the PSII repair cycle. The exact mechanism of this process is still under discussion. We describe the recent progress in identifying the kinases, phosphatases and proteases, and in understanding their involvement in the maintenance of thylakoid structure and the quality control of proteins by PSII repair cycle during photoinhibition. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. -
dc.language English -
dc.publisher WILEY-BLACKWELL -
dc.title Towards a critical understanding of the photosystem II repair mechanism and its regulation during stress conditions -
dc.type Article -
dc.identifier.doi 10.1016/j.febslet.2013.09.015 -
dc.identifier.scopusid 2-s2.0-84886283430 -
dc.identifier.bibliographicCitation FEBS Letters, v.587, no.21, pp.3372 - 3381 -
dc.subject.keywordAuthor Photodamage and PSII repair cycle -
dc.subject.keywordAuthor STN8 kinase and PSII core proteins phosphorylation -
dc.subject.keywordAuthor Proteases and D1 protein degradation -
dc.subject.keywordAuthor Reactive oxygen species (ROS) -
dc.subject.keywordAuthor Ultra-violet radiation -
dc.subject.keywordPlus CENTER D1 PROTEIN -
dc.subject.keywordPlus QUALITY-CONTROL -
dc.subject.keywordPlus ARABIDOPSIS-THALIANA -
dc.subject.keywordPlus FTSH PROTEASE -
dc.subject.keywordPlus SINGLET OXYGEN -
dc.subject.keywordPlus DEG PROTEASES -
dc.subject.keywordPlus HEAT-STRESS -
dc.subject.keywordPlus PHOTOSYNTHETIC MEMBRANES -
dc.subject.keywordPlus THYLAKOID MEMBRANES -
dc.subject.keywordPlus ELECTRON-TRANSPORT -
dc.citation.endPage 3381 -
dc.citation.number 21 -
dc.citation.startPage 3372 -
dc.citation.title FEBS Letters -
dc.citation.volume 587 -
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Department of New Biology CBRG(Complex Biology Research Group) 1. Journal Articles

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