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dc.contributor.authorZervakis, M.en
dc.contributor.authorGkoumplias, V.en
dc.contributor.authorTzaphlidou, M.en
dc.date.accessioned2015-11-24T19:36:22Z-
dc.date.available2015-11-24T19:36:22Z-
dc.identifier.issn1350-4533-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/23862-
dc.rightsDefault Licence-
dc.subjectAlgorithmsen
dc.subjectAnimalsen
dc.subjectCollagen/chemistry/*ultrastructureen
dc.subjectFemaleen
dc.subjectFibrillar Collagens/*chemistryen
dc.subjectImage Processing, Computer-Assisted/methodsen
dc.subjectMaleen
dc.subjectMiceen
dc.subjectMicroscopy, Electron/*methodsen
dc.subjectModels, Statisticalen
dc.subjectRabbitsen
dc.subjectRatsen
dc.subjectRats, Wistaren
dc.titleAnalysis of fibrous proteins from electron microscopy imagesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1016/j.medengphy.2005.02.006-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/15893951-
heal.identifier.secondaryhttp://ac.els-cdn.com/S1350453305000421/1-s2.0-S1350453305000421-main.pdf?_tid=9f91905393ec22b7b48724ce741ef85c&acdnat=1333106379_7effbf0a78cbea20a1c70744c225fae7-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2005-
heal.abstractThis paper considers an approach for analyzing fibrillar collagen structures from electron microscopy images. It enables the quantitative comparison between collagen structural data (electron-optical data) and chemical data. The particular objectives of the paper are to model the electron microscopy images according to the periodic structure of collagen, provide methods for extracting periodic features directly from the experimental data and propose schemes for comparing these features with the theoretical amino-acid distributions of the examined collagen tissue. Theoretical models in the form of sequence-generated histograms are used as reference for extracting and analyzing the structural unit in images from collagen fibrils. In this respect, collagen provides a valuable model system for studying the chemical basis of ultra-structure and the mechanisms of various treatments on a protein, as well as detecting the alterations in collagen fibril structure produced by a disorder. The algorithms developed in this study can be applied to any fibrous protein, provided that its amino acid sequences and structural properties are known. Several application examples are presented. The algorithmic results are compared with clinical studies as to verify the applicability and potential of the proposed methodology.en
heal.journalNameMed Eng Physen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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