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Choi, Jang Hyun
Lab of Diabetes and Metabolism Lab.
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dc.citation.endPage 204 -
dc.citation.number 2 -
dc.citation.startPage 199 -
dc.citation.title JOURNAL OF NEUROSCIENCE METHODS -
dc.citation.volume 161 -
dc.contributor.author Kim, Sung-Kuk -
dc.contributor.author Cho, Sang-Min -
dc.contributor.author Lee, In-Bum -
dc.contributor.author Lee, Young Han -
dc.contributor.author Kang, Jung Hoon -
dc.contributor.author Choi, Jang Hyun -
dc.contributor.author Suh, Pann-Ghill -
dc.contributor.author Chang, Jong-Soo -
dc.date.accessioned 2023-12-22T09:36:13Z -
dc.date.available 2023-12-22T09:36:13Z -
dc.date.created 2014-09-02 -
dc.date.issued 2007-04 -
dc.description.abstract Neurofilaments (NFs) are heteropolymers composed of light (NF-L), middle (NF-M), and heavy (NF-H) subunits, present in most neurons. NF-L polymerizes on its own to provide a scaffold on which regular NFs form via the cross-bridging of NF-M or NF-H. To clarify the mechanism of regulation of NF-L self-assembly, we developed an assay using truncated mutant NF-L fused to glutathione-S transferase (GST). Western immunoblotting data show that the GST-fused head-rod domains of NF-L are necessary and sufficient for detecting assembled NF-L. The levels of self-assembled NF-L subunits detected using GST fusion proteins were consistent with those detected by electron microscopy and turbidity assay. Our results collectively imply that GST-fused head-rod domains of NF-L are critical tools for analyzing NF-L self-assembly in vitro. -
dc.identifier.bibliographicCitation JOURNAL OF NEUROSCIENCE METHODS, v.161, no.2, pp.199 - 204 -
dc.identifier.doi 10.1016/j.jneumeth.2006.10.022 -
dc.identifier.issn 0165-0270 -
dc.identifier.scopusid 2-s2.0-33947521347 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/5662 -
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33947521347 -
dc.identifier.wosid 000246095200002 -
dc.language 영어 -
dc.publisher ELSEVIER SCIENCE BV -
dc.title In vitro assay of neurofilament light chain self-assembly using truncated mutants -
dc.type Article -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor neurofilament light chain -
dc.subject.keywordAuthor self-assembly assay -
dc.subject.keywordAuthor GST pull-down -
dc.subject.keywordAuthor turbidity -
dc.subject.keywordAuthor electron microscopy -
dc.subject.keywordAuthor Western blotting -
dc.subject.keywordAuthor PC12 cells -
dc.subject.keywordAuthor SW13 cells -
dc.subject.keywordPlus AMYOTROPHIC-LATERAL-SCLEROSIS -
dc.subject.keywordPlus PROTEIN-KINASE -
dc.subject.keywordPlus INTERMEDIATE-FILAMENTS -
dc.subject.keywordPlus AXONAL-TRANSPORT -
dc.subject.keywordPlus END DOMAINS -
dc.subject.keywordPlus ROD DOMAIN -
dc.subject.keywordPlus NF-M -
dc.subject.keywordPlus DISEASE -
dc.subject.keywordPlus PHOSPHORYLATION -
dc.subject.keywordPlus CELLS -

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