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권태준

Kwon, Taejoon
TaejoonLab
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dc.citation.endPage 474.e14 -
dc.citation.number 2 -
dc.citation.startPage 460 -
dc.citation.title CELL -
dc.citation.volume 181 -
dc.contributor.author McWhite, Claire D. -
dc.contributor.author Papoulas, Ophelia -
dc.contributor.author Drew, Kevin -
dc.contributor.author Cox, Rachael M. -
dc.contributor.author June, Viviana -
dc.contributor.author Dong, Oliver Xiaoou -
dc.contributor.author Kwon, Taejoon -
dc.contributor.author Wan, Cuihong -
dc.contributor.author Salmi, Mari L. -
dc.contributor.author Roux, Stanley J. -
dc.contributor.author Browning, Karen S. -
dc.contributor.author Chen, Z. Jeffrey -
dc.contributor.author Ronald, Pamela C. -
dc.contributor.author Marcotte, Edward M. -
dc.date.accessioned 2023-12-21T17:42:31Z -
dc.date.available 2023-12-21T17:42:31Z -
dc.date.created 2020-05-01 -
dc.date.issued 2020-04 -
dc.description.abstract Plants are foundational for global ecological and economic systems, but most plant proteins remain uncharacterized. Protein interaction networks often suggest protein functions and open new avenues to characterize genes and proteins. We therefore systematically determined protein complexes from 13 plant species of scientific and agricultural importance, greatly expanding the known repertoire of stable protein complexes in plants. By using co-fractionation mass spectrometry, we recovered known complexes, confirmed complexes predicted to occur in plants, and identified previously unknown interactions conserved over 1.1 billion years of green plant evolution. Several novel complexes are involved in vernalization and pathogen defense, traits critical for agriculture. We also observed plant analogs of animal complexes with distinct molecular assemblies, including a megadalton-scale tRNA multi-synthetase complex. The resulting map offers a cross-species view of conserved, stable protein assemblies shared across plant cells and provides a mechanistic, biochemical framework for interpreting plant genetics and mutant phenotypes. -
dc.identifier.bibliographicCitation CELL, v.181, no.2, pp.460 - 474.e14 -
dc.identifier.doi 10.1016/j.cell.2020.02.049 -
dc.identifier.issn 0092-8674 -
dc.identifier.scopusid 2-s2.0-85083051606 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/32048 -
dc.identifier.url https://www.sciencedirect.com/science/article/pii/S0092867420302269?dgcid=rss_sd_all -
dc.identifier.wosid 000526184900023 -
dc.language 영어 -
dc.publisher CELL PRESS -
dc.title A Pan-plant Protein Complex Map Reveals Deep Conservation and Novel Assemblies -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.relation.journalWebOfScienceCategory Biochemistry & Molecular Biology; Cell Biology -
dc.relation.journalResearchArea Biochemistry & Molecular Biology; Cell Biology -
dc.type.docType Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor plantsprotein interactionsevolutionprotein complexesco-fractionation mass spectrometry (CF-MS)comparative proteomicscross-linking mass spectrometry (CL-MS)interaction-to-phenotypepathogen defense -
dc.subject.keywordPlus SCALE GENE NETWORK -
dc.subject.keywordPlus HUMAN INTERACTOME -
dc.subject.keywordPlus ANION CHANNEL -
dc.subject.keywordPlus GENOME -
dc.subject.keywordPlus MULTIPLE -
dc.subject.keywordPlus EVOLUTION -
dc.subject.keywordPlus SIZE -
dc.subject.keywordPlus TRANSCRIPTION -
dc.subject.keywordPlus PURIFICATION -
dc.subject.keywordPlus ASSOCIATION -

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