Ihara Y - Search Results

1

Potent amyloidogenicity and pathogenicity of Aβ43.

Saito T, Suemoto T, Brouwers N, Sleegers K, Funamoto S, Mihira N, Matsuba Y, Yamada K, Nilsson P, Takano J, Nishimura M, Iwata N, Van Broeckhoven C, Ihara Y, Saido TC. Saito T, et al. Among authors: ihara y. Nat Neurosci. 2011 Jul 3;14(8):1023-32. doi: 10.1038/nn.2858. Nat Neurosci. 2011. PMID: 21725313

2

Enzymatic characteristics of I213T mutant presenilin-1/gamma-secretase in cell models and knock-in mouse brains: familial Alzheimer disease-linked mutation impairs gamma-site cleavage of amyloid precursor protein C-terminal fragment beta.

Shimojo M, Sahara N, Mizoroki T, Funamoto S, Morishima-Kawashima M, Kudo T, Takeda M, Ihara Y, Ichinose H, Takashima A. Shimojo M, et al. Among authors: ihara y. J Biol Chem. 2008 Jun 13;283(24):16488-96. doi: 10.1074/jbc.M801279200. Epub 2008 Apr 21. J Biol Chem. 2008. PMID: 18430735 Free article.

3

Substrate ectodomain is critical for substrate preference and inhibition of γ-secretase.

Funamoto S, Sasaki T, Ishihara S, Nobuhara M, Nakano M, Watanabe-Takahashi M, Saito T, Kakuda N, Miyasaka T, Nishikawa K, Saido TC, Ihara Y. Funamoto S, et al. Among authors: ihara y. Nat Commun. 2013;4:2529. doi: 10.1038/ncomms3529. Nat Commun. 2013. PMID: 24108142 Free PMC article.

4

Truncated carboxyl-terminal fragments of beta-amyloid precursor protein are processed to amyloid beta-proteins 40 and 42.

Funamoto S, Morishima-Kawashima M, Tanimura Y, Hirotani N, Saido TC, Ihara Y. Funamoto S, et al. Among authors: ihara y. Biochemistry. 2004 Oct 26;43(42):13532-40. doi: 10.1021/bi049399k. Biochemistry. 2004. PMID: 15491160

5

Longer forms of amyloid beta protein: implications for the mechanism of intramembrane cleavage by gamma-secretase.

Qi-Takahara Y, Morishima-Kawashima M, Tanimura Y, Dolios G, Hirotani N, Horikoshi Y, Kametani F, Maeda M, Saido TC, Wang R, Ihara Y. Qi-Takahara Y, et al. Among authors: ihara y. J Neurosci. 2005 Jan 12;25(2):436-45. doi: 10.1523/JNEUROSCI.1575-04.2005. J Neurosci. 2005. PMID: 15647487 Free PMC article.

6

Alanine substitutions in the GXXXG motif alter C99 cleavage by γ-secretase but not its dimerization.

Higashide H, Ishihara S, Nobuhara M, Ihara Y, Funamoto S. Higashide H, et al. Among authors: ihara y. J Neurochem. 2017 Mar;140(6):955-962. doi: 10.1111/jnc.13942. Epub 2017 Jan 30. J Neurochem. 2017. PMID: 28032911 Free article.

7

gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment.

Takami M, Nagashima Y, Sano Y, Ishihara S, Morishima-Kawashima M, Funamoto S, Ihara Y. Takami M, et al. Among authors: ihara y. J Neurosci. 2009 Oct 14;29(41):13042-52. doi: 10.1523/JNEUROSCI.2362-09.2009. J Neurosci. 2009. PMID: 19828817 Free PMC article.

8

The A673T mutation in the amyloid precursor protein reduces the production of β-amyloid protein from its β-carboxyl terminal fragment in cells.

Kokawa A, Ishihara S, Fujiwara H, Nobuhara M, Iwata M, Ihara Y, Funamoto S. Kokawa A, et al. Among authors: ihara y. Acta Neuropathol Commun. 2015 Nov 4;3:66. doi: 10.1186/s40478-015-0247-6. Acta Neuropathol Commun. 2015. PMID: 26531305 Free PMC article.

9

Equimolar production of amyloid beta-protein and amyloid precursor protein intracellular domain from beta-carboxyl-terminal fragment by gamma-secretase.

Kakuda N, Funamoto S, Yagishita S, Takami M, Osawa S, Dohmae N, Ihara Y. Kakuda N, et al. Among authors: ihara y. J Biol Chem. 2006 May 26;281(21):14776-86. doi: 10.1074/jbc.M513453200. Epub 2006 Apr 4. J Biol Chem. 2006. PMID: 16595682 Free article.

10

Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid beta-peptides.

Nakaya Y, Yamane T, Shiraishi H, Wang HQ, Matsubara E, Sato T, Dolios G, Wang R, De Strooper B, Shoji M, Komano H, Yanagisawa K, Ihara Y, Fraser P, St George-Hyslop P, Nishimura M. Nakaya Y, et al. Among authors: ihara y. J Biol Chem. 2005 May 13;280(19):19070-7. doi: 10.1074/jbc.M501130200. Epub 2005 Mar 10. J Biol Chem. 2005. PMID: 15764596 Free article.

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