There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
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 | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.