Effects of lysine residues on structural characteristics and stability of tau proteins
DC Field | Value | Language |
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dc.contributor.author | Lee, Myeongsang | - |
dc.contributor.author | Baek, Inchul | - |
dc.contributor.author | Choi, Hyunsung | - |
dc.contributor.author | Kim, Jae In | - |
dc.contributor.author | Na, Sungsoo | - |
dc.date.accessioned | 2021-09-04T11:20:23Z | - |
dc.date.available | 2021-09-04T11:20:23Z | - |
dc.date.created | 2021-06-10 | - |
dc.date.issued | 2015-10-23 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/92168 | - |
dc.description.abstract | Pathological amyloid proteins have been implicated in neuro-degenerative diseases, specifically Alzheimer's, Parkinson's, Lewy-body diseases and prion related diseases. In prion related diseases, functional tau proteins can be transformed into pathological agents by environmental factors, including oxidative stress, inflammation, A beta-mediated toxicity and covalent modification. These pathological agents are stable under physiological conditions and are not easily degraded. This un-degradable characteristic of tau proteins enables their utilization as functional materials to capturing the carbon dioxides. For the proper utilization of amyloid proteins as functional materials efficiently, a basic study regarding their structural characteristic is necessary. Here, we investigated the basic tau protein structure of wild-type (WT) and tau proteins with lysine residues mutation at glutamic residue (Q2K) on tau protein at atomistic scale. We also reported the size effect of both the WT and Q2K structures, which allowed us to identify the stability of those amyloid structures. (C) 2015 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | PARTICLE MESH EWALD | - |
dc.subject | MOLECULAR-DYNAMICS | - |
dc.subject | NEURODEGENERATIVE DISEASES | - |
dc.subject | AMYLOID FIBERS | - |
dc.subject | BETA STRUCTURE | - |
dc.subject | OLIGOMERS | - |
dc.subject | SIMULATIONS | - |
dc.subject | EFFICIENT | - |
dc.subject | FILAMENTS | - |
dc.subject | SYSTEMS | - |
dc.title | Effects of lysine residues on structural characteristics and stability of tau proteins | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Na, Sungsoo | - |
dc.identifier.doi | 10.1016/j.bbrc.2015.09.056 | - |
dc.identifier.scopusid | 2-s2.0-84943352514 | - |
dc.identifier.wosid | 000363094400034 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.466, no.3, pp.486 - 492 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 466 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 486 | - |
dc.citation.endPage | 492 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | PARTICLE MESH EWALD | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS | - |
dc.subject.keywordPlus | NEURODEGENERATIVE DISEASES | - |
dc.subject.keywordPlus | AMYLOID FIBERS | - |
dc.subject.keywordPlus | BETA STRUCTURE | - |
dc.subject.keywordPlus | OLIGOMERS | - |
dc.subject.keywordPlus | SIMULATIONS | - |
dc.subject.keywordPlus | EFFICIENT | - |
dc.subject.keywordPlus | FILAMENTS | - |
dc.subject.keywordPlus | SYSTEMS | - |
dc.subject.keywordAuthor | Amyloid proteins | - |
dc.subject.keywordAuthor | Tau protein | - |
dc.subject.keywordAuthor | Lysine mutation | - |
dc.subject.keywordAuthor | Molecular dynamics | - |
dc.subject.keywordAuthor | Size effects | - |
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