25 results on '"Naiki, Hironobu"'
Search Results
2. 2P069 The mechanism of ultrasonication-induced amyloid fibril formation(01C. Protein: Property)
3. 2P067 Effects of various fatty acids on the amyloid fibrillation of β_2-microglobulin(01C. Protein: Property)
4. 2P068 The properties of the residual structure of amyloid precursor state of β2-microglobulin(01C. Protein: Property)
5. 1E1436 Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation(Proteins: Property I,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan)
6. 1PT145 Correlation of the dynamics of β_2-microglobulin fragments with their amyloidogenicity(The 50th Annual Meeting of the Biophysical Society of Japan)
7. 2P051 High Speed Amyloid Fibrilization Induced by Ultrasonication(The 48th Annual Meeting of the Biophysical Society of Japan)
8. 1P064 Analysis of the intermediate state of the formation of the β2-microglobulin amyloid fibril using paramagnetic relaxation enhancement(Protein:Property,The 48th Annual Meeting of the Biophysical Society of Japan)
9. 1P063 1YA0930 Identification of transient intermediates of the formation of the β2-microglobulin amyloid fibril by heteronuclear NMR techniques.(Protein:Property,Early Research in Biophysics Award Candidate Presentations,Early Research in Biophysics Award,The 48th Annual Meeting of the Biophysical Society of Japan)
10. 2P-052 Site directed spin labeling - electron spin resonance analysis of the structure of amyloid fibrils(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan)
11. 2P-048 Analysis of the mechanism of the amyloid fiber extension using H/D exchange(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan)
12. 2P-038 Direct Observation of β_2-microglubulin amyloid fibrils using solution NMR(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan)
13. 1P-087 Structural analysis of the amyloid fibril formed by the fragment of β2-microglobulin(The 46th Annual Meeting of the Biophysical Society of Japan)
14. 3P-008 The ability of fibril formation of the constant domain of immunoglobulin light chain in comparison with β2-microglobulin(The 46th Annual Meeting of the Biophysical Society of Japan)
15. 2P-083 Monitoring the fibrillation intermediate of β2-microglobulin by Trp fluorescence and H/D exchange-NMR(The 46th Annual Meeting of the Biophysical Society of Japan)
16. 3P-010 Analysis of the amyloid fiber extension mechanism using H/D exchange(The 46th Annual Meeting of the Biophysical Society of Japan)
17. 2P-008 Structural Analysis of Amyloid Fibrils of β2-Microglobulin by Solid-State NMR(The 46th Annual Meeting of the Biophysical Society of Japan)
18. 3P052 The effects of reductant on the amyloid fibril formation of β2-microglobulin(Proteins-stability, folding, and other physicochemical properties,Poster Presentations)
19. 3P048 Packing density of amiloid-like and amyloid fibrils(Proteins-stability, folding, and other physicochemical properties,Poster Presentations)
20. 3P055 Uniforming the Molecular Weigh of Amyloid Fibrils by Ultrasonication(Proteins-stability, folding, and other physicochemical properties,Oral Presentations)
21. 2P105 Structural polymorphism of β_2-microglobulin amyloid fibrils induced by the addition of trifluoroethanol(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
22. 2P119 Reduction of disulfide bridge inhibits the amyloid fibril formation of β2-microglobulin(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
23. 2P109 Folding and Unfolding Kinetics of β2-Microglobulin as Probed by Tryptophan Fluorescence(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
24. 2P106 Orientation of amyloid fibrils formed by β2-microglobulin and its peptide fragment in a flow(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
25. 2P112 Heat Capacity Change Associated with Structural Conversion into Amyloid Fibril(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
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