Naiki H - Search Results

1

Reversible heat-induced dissociation of β2-microglobulin amyloid fibrils.

Kardos J, Micsonai A, Pál-Gábor H, Petrik É, Gráf L, Kovács J, Lee YH, Naiki H, Goto Y. Kardos J, et al. Among authors: naiki h. Biochemistry. 2011 Apr 19;50(15):3211-20. doi: 10.1021/bi2000017. Epub 2011 Mar 24. Biochemistry. 2011. PMID: 21388222

2

Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH.

Yamamoto S, Hasegawa K, Yamaguchi I, Tsutsumi S, Kardos J, Goto Y, Gejyo F, Naiki H. Yamamoto S, et al. Among authors: naiki h. Biochemistry. 2004 Aug 31;43(34):11075-82. doi: 10.1021/bi049262u. Biochemistry. 2004. PMID: 15323566

3

Exothermic effects observed upon heating of beta2-microglobulin monomers in the presence of amyloid seeds.

Sasahara K, Naiki H, Goto Y. Sasahara K, et al. Among authors: naiki h. Biochemistry. 2006 Jul 25;45(29):8760-9. doi: 10.1021/bi0606748. Biochemistry. 2006. PMID: 16846219

4

Heat-triggered conversion of protofibrils into mature amyloid fibrils of beta2-microglobulin.

Sasahara K, Yagi H, Naiki H, Goto Y. Sasahara K, et al. Among authors: naiki h. Biochemistry. 2007 Mar 20;46(11):3286-93. doi: 10.1021/bi602403v. Epub 2007 Feb 23. Biochemistry. 2007. PMID: 17316024

5

Mechanism of lysophosphatidic acid-induced amyloid fibril formation of beta(2)-microglobulin in vitro under physiological conditions.

Pál-Gábor H, Gombos L, Micsonai A, Kovács E, Petrik E, Kovács J, Gráf L, Fidy J, Naiki H, Goto Y, Liliom K, Kardos J. Pál-Gábor H, et al. Among authors: naiki h. Biochemistry. 2009 Jun 23;48(24):5689-99. doi: 10.1021/bi900356r. Biochemistry. 2009. PMID: 19432419

6

Heating during agitation of β₂-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH.

Noji M, Sasahara K, Yamaguchi K, So M, Sakurai K, Kardos J, Naiki H, Goto Y. Noji M, et al. Among authors: naiki h. J Biol Chem. 2019 Oct 25;294(43):15826-15835. doi: 10.1074/jbc.RA119.009971. Epub 2019 Sep 8. J Biol Chem. 2019. PMID: 31495783 Free PMC article.

7

Possible mechanisms of polyphosphate-induced amyloid fibril formation of β₂-microglobulin.

Zhang CM, Yamaguchi K, So M, Sasahara K, Ito T, Yamamoto S, Narita I, Kardos J, Naiki H, Goto Y. Zhang CM, et al. Among authors: naiki h. Proc Natl Acad Sci U S A. 2019 Jun 25;116(26):12833-12838. doi: 10.1073/pnas.1819813116. Epub 2019 Jun 10. Proc Natl Acad Sci U S A. 2019. PMID: 31182591 Free PMC article.

8

Amyloid Formation under Complicated Conditions in Which β₂-Microglobulin Coexists with Its Proteolytic Fragments.

Muta H, So M, Sakurai K, Kardos J, Naiki H, Goto Y. Muta H, et al. Among authors: naiki h. Biochemistry. 2019 Dec 10;58(49):4925-4934. doi: 10.1021/acs.biochem.9b00917. Epub 2019 Nov 20. Biochemistry. 2019. PMID: 31724398

9

The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH.

Ohhashi Y, Hagihara Y, Kozhukh G, Hoshino M, Hasegawa K, Yamaguchi I, Naiki H, Goto Y. Ohhashi Y, et al. Among authors: naiki h. J Biochem. 2002 Jan;131(1):45-52. doi: 10.1093/oxfordjournals.jbchem.a003076. J Biochem. 2002. PMID: 11754734 Free article.

10

Conformational dynamics of beta(2)-microglobulin analyzed by reduction and reoxidation of the disulfide bond.

Gozu M, Lee YH, Ohhashi Y, Hoshino M, Naiki H, Goto Y. Gozu M, et al. Among authors: naiki h. J Biochem. 2003 Jun;133(6):731-6. doi: 10.1093/jb/mvg094. J Biochem. 2003. PMID: 12869529 Free article.

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