Tomoharu Matsumoto - Search Results

Year	Number of Results
2003	1
2004	1
2007	1
2008	1
2009	1
2011	1
2012	1
2016	1
2019	2
2020	1
2021	1
2023	1
2024	0

1

D-Loop Mutation G42A/G46A Decreases Actin Dynamics.

Matsuzaki M, Fujiwara I, Kashima S, Matsumoto T, Oda T, Hayashi M, Maeda K, Takiguchi K, Maéda Y, Narita A. Matsuzaki M, et al. Among authors: matsumoto t. Biomolecules. 2020 May 8;10(5):736. doi: 10.3390/biom10050736. Biomolecules. 2020. PMID: 32397190 Free PMC article.

2

Mechanical Stress Decreases the Amplitude of Twisting and Bending Fluctuations of Actin Filaments.

Okura K, Matsumoto T, Narita A, Tatsumi H. Okura K, et al. Among authors: matsumoto t. J Mol Biol. 2023 Nov 15;435(22):168295. doi: 10.1016/j.jmb.2023.168295. Epub 2023 Oct 11. J Mol Biol. 2023. PMID: 37783285 Free article.

3

Dynamic Properties of Human α-Synuclein Related to Propensity to Amyloid Fibril Formation.

Fujiwara S, Kono F, Matsuo T, Sugimoto Y, Matsumoto T, Narita A, Shibata K. Fujiwara S, et al. Among authors: matsumoto t. J Mol Biol. 2019 Aug 9;431(17):3229-3245. doi: 10.1016/j.jmb.2019.05.047. Epub 2019 Jun 8. J Mol Biol. 2019. PMID: 31181290

4

A cryo-TSEM with temperature cycling capability allows deep sublimation of ice to uncover fine structures in thick cells.

Usukura J, Narita A, Matsumoto T, Usukura E, Sunaoshi T, Watanabe S, Tamba Y, Nagakubo Y, Mizuo T, Azuma J, Osumi M, Nimura K, Tamochi R, Ose Y. Usukura J, et al. Among authors: matsumoto t. Sci Rep. 2021 Nov 1;11(1):21406. doi: 10.1038/s41598-021-00979-z. Sci Rep. 2021. PMID: 34725450 Free PMC article.

5

Direct observation of the actin filament by tip-scan atomic force microscopy.

Narita A, Usukura E, Yagi A, Tateyama K, Akizuki S, Kikumoto M, Matsumoto T, Maéda Y, Ito S, Usukura J. Narita A, et al. Among authors: matsumoto t. Microscopy (Oxf). 2016 Aug;65(4):370-7. doi: 10.1093/jmicro/dfw017. Epub 2016 May 30. Microscopy (Oxf). 2016. PMID: 27242058 Free PMC article.

6

Hot spots in prion protein for pathogenic conversion.

Kuwata K, Nishida N, Matsumoto T, Kamatari YO, Hosokawa-Muto J, Kodama K, Nakamura HK, Kimura K, Kawasaki M, Takakura Y, Shirabe S, Takata J, Kataoka Y, Katamine S. Kuwata K, et al. Among authors: matsumoto t. Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):11921-6. doi: 10.1073/pnas.0702671104. Epub 2007 Jul 6. Proc Natl Acad Sci U S A. 2007. PMID: 17616582 Free PMC article.

7

Facile preparation of optically active jasmonates and their biological activities in rice.

Miyamoto K, Matsumoto T, Yumoto E, Sakazawa T, Yokota T, Yamane H, Uchida K. Miyamoto K, et al. Among authors: matsumoto t. Biosci Biotechnol Biochem. 2019 May;83(5):876-881. doi: 10.1080/09168451.2019.1569500. Epub 2019 Jan 24. Biosci Biotechnol Biochem. 2019. PMID: 30676297

8

Size-selective olefin hydrogenation by a Pd nanocluster provided in an apo-ferritin cage.

Ueno T, Suzuki M, Goto T, Matsumoto T, Nagayama K, Watanabe Y. Ueno T, et al. Among authors: matsumoto t. Angew Chem Int Ed Engl. 2004 May 3;43(19):2527-30. doi: 10.1002/anie.200353436. Angew Chem Int Ed Engl. 2004. PMID: 15127443 No abstract available.

9

Critical region for amyloid fibril formation of mouse prion protein: unusual amyloidogenic properties of the helix 2 peptide.

Yamaguchi K, Matsumoto T, Kuwata K. Yamaguchi K, et al. Among authors: matsumoto t. Biochemistry. 2008 Dec 16;47(50):13242-51. doi: 10.1021/bi801562w. Biochemistry. 2008. PMID: 19053276

10

Proper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication-induced amyloid formation process.

Yamaguchi K, Matsumoto T, Kuwata K. Yamaguchi K, et al. Among authors: matsumoto t. Protein Sci. 2012 Jan;21(1):38-49. doi: 10.1002/pro.755. Epub 2011 Nov 22. Protein Sci. 2012. PMID: 22095682 Free PMC article.

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