PubMed (cited) for id: 607809

Year	Number of Results
1973	1
1982	1
1990	1
1991	2
1992	4
1993	1
1994	1
1996	1
1998	2
2002	1
2003	1
2007	1
2016	1
2020	2
2024	0

1

Structural basis for catalysis and substrate specificity of human ACAT1.

Qian H, Zhao X, Yan R, Yao X, Gao S, Sun X, Du X, Yang H, Wong CCL, Yan N. Qian H, et al. Nature. 2020 May;581(7808):333-338. doi: 10.1038/s41586-020-2290-0. Epub 2020 May 13. Nature. 2020. PMID: 32433614

2

Structure of nevanimibe-bound tetrameric human ACAT1.

Long T, Sun Y, Hassan A, Qi X, Li X. Long T, et al. Nature. 2020 May;581(7808):339-343. doi: 10.1038/s41586-020-2295-8. Epub 2020 May 13. Nature. 2020. PMID: 32433613 Free PMC article.

3

Potentiating the antitumour response of CD8(+) T cells by modulating cholesterol metabolism.

Yang W, Bai Y, Xiong Y, Zhang J, Chen S, Zheng X, Meng X, Li L, Wang J, Xu C, Yan C, Wang L, Chang CC, Chang TY, Zhang T, Zhou P, Song BL, Liu W, Sun SC, Liu X, Li BL, Xu C. Yang W, et al. Nature. 2016 Mar 31;531(7596):651-5. doi: 10.1038/nature17412. Epub 2016 Mar 16. Nature. 2016. PMID: 26982734 Free PMC article.

4

Kinetic and expression analyses of seven novel mutations in mitochondrial acetoacetyl-CoA thiolase (T2): identification of a Km mutant and an analysis of the mutational sites in the structure.

Sakurai S, Fukao T, Haapalainen AM, Zhang G, Yamada K, Lilliu F, Yano S, Robinson P, Gibson MK, Wanders RJ, Mitchell GA, Wierenga RK, Kondo N. Sakurai S, et al. Mol Genet Metab. 2007 Apr;90(4):370-8. doi: 10.1016/j.ymgme.2006.12.002. Epub 2007 Jan 22. Mol Genet Metab. 2007. PMID: 17236799

5

Single base substitutions at the initiator codon in the mitochondrial acetoacetyl-CoA thiolase (ACAT1/T2) gene result in production of varying amounts of wild-type T2 polypeptide.

Fukao T, Matsuo N, Zhang GX, Urasawa R, Kubo T, Kohno Y, Kondo N. Fukao T, et al. Hum Mutat. 2003 Jun;21(6):587-92. doi: 10.1002/humu.10209. Hum Mutat. 2003. PMID: 12754704

6

Characterization of six mutations in five Spanish patients with mitochondrial acetoacetyl-CoA thiolase deficiency: effects of amino acid substitutions on tertiary structure.

Fukao T, Nakamura H, Nakamura K, Perez-Cerda C, Baldellou A, Barrionuevo CR, Castello FG, Kohno Y, Ugarte M, Kondo N. Fukao T, et al. Mol Genet Metab. 2002 Mar;75(3):235-43. doi: 10.1006/mgme.2001.3288. Mol Genet Metab. 2002. PMID: 11914035

7

Characterization of N93S, I312T, and A333P missense mutations in two Japanese families with mitochondrial acetoacetyl-CoA thiolase deficiency.

Fukao T, Nakamura H, Song XQ, Nakamura K, Orii KE, Kohno Y, Kano M, Yamaguchi S, Hashimoto T, Orii T, Kondo N. Fukao T, et al. Hum Mutat. 1998;12(4):245-54. doi: 10.1002/(SICI)1098-1004(1998)12:4<245::AID-HUMU5>3.0.CO;2-E. Hum Mutat. 1998. PMID: 9744475

8

Mitochondrial acetoacetyl-CoA thiolase (beta-ketothiolase) deficiency and pregnancy.

Sewell AC, Herwig J, Wiegratz I, Lehnert W, Niederhoff H, Song XQ, Kondo N, Fukao T. Sewell AC, et al. J Inherit Metab Dis. 1998 Jun;21(4):441-2. doi: 10.1023/a:1005335515166. J Inherit Metab Dis. 1998. PMID: 9700610 No abstract available.

9

Comparative genome mapping of the ataxia-telangiectasia region in mouse, rat, and Syrian hamster.

Matsuda Y, Imai T, Shiomi T, Saito T, Yamauchi M, Fukao T, Akao Y, Seki N, Ito H, Hori TA. Matsuda Y, et al. Genomics. 1996 Jun 15;34(3):347-52. doi: 10.1006/geno.1996.0297. Genomics. 1996. PMID: 8786135

10

Molecular studies of mitochondrial acetoacetyl-coenzyme A thiolase deficiency in the two original families.

Fukao T, Yamaguchi S, Scriver CR, Dunbar G, Wakazono A, Kano M, Orii T, Hashimoto T. Fukao T, et al. Hum Mutat. 1993;2(3):214-20. doi: 10.1002/humu.1380020310. Hum Mutat. 1993. PMID: 8103405

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