Kawata Y - Search Results

1

High-Sensitivity Rheo-NMR Spectroscopy for Protein Studies.

Morimoto D, Walinda E, Iwakawa N, Nishizawa M, Kawata Y, Yamamoto A, Shirakawa M, Scheler U, Sugase K. Morimoto D, et al. Among authors: kawata y. Anal Chem. 2017 Jul 18;89(14):7286-7290. doi: 10.1021/acs.analchem.7b01816. Epub 2017 Jul 5. Anal Chem. 2017. PMID: 28665116 Free article.

2

Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: insight into intrinsically disordered proteins.

Iwasa H, Meshitsuka S, Hongo K, Mizobata T, Kawata Y. Iwasa H, et al. Among authors: kawata y. J Biol Chem. 2011 Jun 17;286(24):21796-805. doi: 10.1074/jbc.M111.228445. Epub 2011 Apr 20. J Biol Chem. 2011. PMID: 21507961 Free PMC article.

3

Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR.

Iwakawa N, Morimoto D, Walinda E, Kawata Y, Shirakawa M, Sugase K. Iwakawa N, et al. Among authors: kawata y. Int J Mol Sci. 2017 Oct 28;18(11):2271. doi: 10.3390/ijms18112271. Int J Mol Sci. 2017. PMID: 29143789 Free PMC article.

4

Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases.

Yagi H, Kusaka E, Hongo K, Mizobata T, Kawata Y. Yagi H, et al. Among authors: kawata y. J Biol Chem. 2005 Nov 18;280(46):38609-16. doi: 10.1074/jbc.M508623200. Epub 2005 Sep 14. J Biol Chem. 2005. PMID: 16162499 Free article.

5

Chaperonin-encapsulation of proteins for NMR.

Tanaka S, Kawata Y, Otting G, Dixon NE, Matsuzaki K, Hoshino M. Tanaka S, et al. Among authors: kawata y. Biochim Biophys Acta. 2010 Apr;1804(4):866-71. doi: 10.1016/j.bbapap.2009.12.016. Epub 2010 Jan 4. Biochim Biophys Acta. 2010. PMID: 20045085 Free article.

6

Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure.

Miyawaki S, Uemura Y, Hongo K, Kawata Y, Mizobata T. Miyawaki S, et al. Among authors: kawata y. J Biol Chem. 2019 Feb 1;294(5):1590-1601. doi: 10.1074/jbc.RA118.005611. Epub 2018 Dec 10. J Biol Chem. 2019. PMID: 30530490 Free PMC article.

7

GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.

Miyazaki T, Yoshimi T, Furutsu Y, Hongo K, Mizobata T, Kanemori M, Kawata Y. Miyazaki T, et al. Among authors: kawata y. J Biol Chem. 2002 Dec 27;277(52):50621-8. doi: 10.1074/jbc.M209183200. Epub 2002 Oct 10. J Biol Chem. 2002. PMID: 12377767 Free article.

8

Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity.

Machida K, Kono-Okada A, Hongo K, Mizobata T, Kawata Y. Machida K, et al. Among authors: kawata y. J Biol Chem. 2008 Mar 14;283(11):6886-96. doi: 10.1074/jbc.M708002200. Epub 2008 Jan 9. J Biol Chem. 2008. PMID: 18184659 Free article.

9

Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein.

Ishino S, Kawata Y, Taguchi H, Kajimura N, Matsuzaki K, Hoshino M. Ishino S, et al. Among authors: kawata y. J Biol Chem. 2015 Jun 12;290(24):15042-51. doi: 10.1074/jbc.M114.633636. Epub 2015 Apr 17. J Biol Chem. 2015. PMID: 25887400 Free PMC article.

10

Modulating the Effects of the Bacterial Chaperonin GroEL on Fibrillogenic Polypeptides through Modification of Domain Hinge Architecture.

Fukui N, Araki K, Hongo K, Mizobata T, Kawata Y. Fukui N, et al. Among authors: kawata y. J Biol Chem. 2016 Nov 25;291(48):25217-25226. doi: 10.1074/jbc.M116.751925. Epub 2016 Oct 14. J Biol Chem. 2016. PMID: 27742838 Free PMC article.

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