Akimasa Matsugami
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Explore the profile of Akimasa Matsugami including associated specialties, affiliations and a list of published articles.
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44
Citations
430
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Recent Articles
1.
Oktaviani N, Malay A, Matsugami A, Hayashi F, Numata K
Biomacromolecules
. 2023 Mar;
24(4):1604-1616.
PMID: 36990448
Spider dragline silk is a remarkably tough biomaterial and composed primarily of spidroins MaSp1 and MaSp2. During fiber self-assembly, the spidroin N-terminal domains (NTDs) undergo rapid dimerization in response to...
2.
Mizuno F, Aoki S, Matsugami A, Hayashi F, Nishimura C
Protein Pept Lett
. 2023 Jan;
30(2):103-107.
PMID: 36600624
Introduction: Sensitive methods are necessary to identify the residual structure in an unfolded protein, which may be similar to the functionally native structure. Signal intensity in NMR experiments is useful...
3.
Sato Y, Matsugami A, Watanabe S, Hayashi F, Arai M, Kigawa T, et al.
Protein Sci
. 2021 Sep;
30(11):2233-2245.
PMID: 34523753
HIV-1 capsid is comprised of over a hundred p24 protein molecules, arranged as either pentamers or hexamers. Three p24 mutants with amino acid substitutions in capsid N-terminal domain protein were...
4.
Tsukakoshi K, Yamagishi Y, Kanazashi M, Nakama K, Oshikawa D, Savory N, et al.
Nucleic Acids Res
. 2021 Jun;
49(11):6069-6081.
PMID: 34095949
Aptamers can control the biological functions of enzymes, thereby facilitating the development of novel biosensors. While aptamers that inhibit catalytic reactions of enzymes were found and used as signal transducers...
5.
Hatanaka T, Kikkawa N, Matsugami A, Hosokawa Y, Hayashi F, Ishida N
Sci Rep
. 2020 Nov;
10(1):19468.
PMID: 33173124
Lanthanide ions (Ln) show similar physicochemical properties in aqueous solutions, wherein they exist as + 3 cations and exhibit ionic radii differences of less than 0.26 Å. A flexible linear...
6.
Oktaviani N, Malay A, Matsugami A, Hayashi F, Numata K
Biomol NMR Assign
. 2020 Aug;
14(2):335-338.
PMID: 32767002
Spider dragline silk is well recognized due to its excellent mechanical properties. Dragline silk protein mainly consists of two proteins, namely, major ampullate spidroin 1 (MaSp1) and major ampullate spidroin...
7.
Okuwaki R, Shinmura I, Morita S, Matsugami A, Hayashi F, Goto Y, et al.
Biochim Biophys Acta Proteins Proteom
. 2020 Jun;
1868(9):140464.
PMID: 32497661
The residual solution structures of two alpha-synuclein mutants, A30P and A53T, observed in family members of patients with Parkinson's disease were compared with that of wild-type by NMR. The A53T...
8.
Oktaviani N, Matsugami A, Hayashi F, Numata K
Chem Commun (Camb)
. 2019 Jul;
55(66):9761-9764.
PMID: 31355386
The effect of ions on the structure and dynamics of a spider silk protein is elucidated. Chaotropic ions prevent intra- and inter-molecular interactions on the repetitive domain, which are required...
9.
Nonsuwan P, Matsugami A, Hayashi F, Hyon S, Matsumura K
Carbohydr Polym
. 2018 Oct;
204:131-141.
PMID: 30366524
The objective of this study is to control and elucidate the mechanism of molecular degradation in a polysaccharide hydrogel. Glycidyl methacrylate (GMA) immobilized dextran (Dex-GMA) was oxidized by periodate to...
10.
Oktaviani N, Matsugami A, Malay A, Hayashi F, Kaplan D, Numata K
Nat Commun
. 2018 May;
9(1):2121.
PMID: 29844575
The β-sheet is the key structure underlying the excellent mechanical properties of spider silk. However, the comprehensive mechanism underlying β-sheet formation from soluble silk proteins during the transition into insoluble...