There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 336 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 332 | - |
dc.citation.title | JOURNAL OF STRUCTURAL BIOLOGY | - |
dc.citation.volume | 168 | - |
dc.contributor.author | Youn, Hwa Shik | - |
dc.contributor.author | Shin, Tae Joo | - |
dc.date.accessioned | 2023-12-22T07:37:44Z | - |
dc.date.available | 2023-12-22T07:37:44Z | - |
dc.date.created | 2020-01-23 | - |
dc.date.issued | 2009-11 | - |
dc.description.abstract | Supramolecular assembly of collagen fibrils into collagen fiber and its distribution in fish scales of red seabream, Pagrus major, were investigated. By virtue of Zernike phase-contrast hard X-ray microscopy, it has been firstly observed that collagen fiber consists of helical substructures of collagen fibrils wrapped with incrustation. As it close to the scalar focus (that is, with aging), loosened- and deteriorated-helical assemblies started to be observed with loosing wrapping incrustation, indicative of the distortion of the basic helical assembly. Various distributions and packing arrangements of collagen fibers were observed dependent on subdivisions of fish scale. Freshly growing edge region of fish scale, embedded into fish skin, showed rarely patched and one directionally arranged collagen fibers, in which specifically triple helical assemblies of collagen fibrils were found. On the contrary, relatively aged region of the rostral field close to the scalar focus displayed randomly directed and densely packed collagen fibers, in which loosened- and deteriorated-helical assemblies of collagen fibrils were mostly found. Our results have demonstrated that hard X-ray microscope can be a powerful tool to study in situ internal structure of biological specimens in an atmospheric pressure. | - |
dc.identifier.bibliographicCitation | JOURNAL OF STRUCTURAL BIOLOGY, v.168, no.2, pp.332 - 336 | - |
dc.identifier.doi | 10.1016/j.jsb.2009.08.001 | - |
dc.identifier.issn | 1047-8477 | - |
dc.identifier.scopusid | 2-s2.0-70349466531 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/30892 | - |
dc.identifier.url | https://www.sciencedirect.com/science/article/pii/S104784770900210X?via%3Dihub | - |
dc.identifier.wosid | 000270865000013 | - |
dc.language | 영어 | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.title | Supramolecular assembly of collagen fibrils into collagen fiber in fish scales of red seabream, Pagrus major | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology; Biophysics; Cell Biology | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology; Biophysics; Cell Biology | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | Supramolecular assembly of collagen fibrils | - |
dc.subject.keywordAuthor | Zernike phase-contrast hard X-ray microscopy | - |
dc.subject.keywordAuthor | Helical substructure | - |
dc.subject.keywordAuthor | Collagen fiber | - |
dc.subject.keywordPlus | ZERNIKE PHASE-CONTRAST | - |
dc.subject.keywordPlus | X-RAY-DIFFRACTION | - |
dc.subject.keywordPlus | I COLLAGEN | - |
dc.subject.keywordPlus | MINERALIZATION | - |
dc.subject.keywordPlus | BONE | - |
dc.subject.keywordPlus | MICROSCOPY | - |
dc.subject.keywordPlus | PACKING | - |
dc.subject.keywordPlus | TENDON | - |
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.