Please use this identifier to cite or link to this item: https://cris.library.msu.ac.zw//handle/11408/5038
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dc.contributor.authorMuleya, Victor-
dc.contributor.authorLois, L. Maria-
dc.contributor.authorChahtane, Hicham-
dc.contributor.authorThomas, Ludivine-
dc.contributor.authorChiapello, Marco-
dc.contributor.authorMarondedze, Claudius-
dc.date.accessioned2022-08-02T18:34:43Z-
dc.date.available2022-08-02T18:34:43Z-
dc.date.issued2022-02-21-
dc.identifier.citationMuleya, V.; Lois, L.M.; Chahtane, H.; Thomas, L.; Chiapello, M.; Marondedze, C. (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants. Life 2022, 12, 324. https://doi.org/ 10.3390/life12020324en_US
dc.identifier.issn2075-1729-
dc.identifier.urihttps://doi.org/ 10.3390/life12020324-
dc.identifier.urihttp://hdl.handle.net/11408/5038-
dc.description.abstractThe increasing dynamic functions of post-translational modifications (PTMs) within protein molecules present outstanding challenges for plant biology even at this present day. Protein PTMs are among the first and fastest plant responses to changes in the environment, indicating that the mechanisms and dynamics of PTMs are an essential area of plant biology. Besides being key players in signaling, PTMs play vital roles in gene expression, gene, and protein localization, protein stability and interactions, as well as enzyme kinetics. In this review, we take a broader but concise approach to capture the current state of events in the field of plant PTMs. We discuss protein modifications including citrullination, glycosylation, phosphorylation, oxidation and disulfide bridges, N-terminal, SUMOylation, and ubiquitination. Further, we outline the complexity of studying PTMs in relation to compartmentalization and function. We conclude by challenging the proteomics community to engage in holistic approaches towards identification and characterizing multiple PTMs on the same protein, their interaction, and mechanism of regulation to bring a deeper understanding of protein function and regulation in plants.en_US
dc.language.isoenen_US
dc.publisherMDPIen_US
dc.relation.ispartofseriesLife;Vol. 12, Issue 2, No. 324.-
dc.subjectplant post-translational modificationsen_US
dc.subjectphosphorylationen_US
dc.subjectN-glycosylationen_US
dc.subjectmethionine oxidationen_US
dc.subjectN-terminal acetylationen_US
dc.title(De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plantsen_US
dc.typeArticleen_US
item.languageiso639-1en-
item.cerifentitytypePublications-
item.fulltextWith Fulltext-
item.grantfulltextopen-
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
Appears in Collections:Research Papers
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