Okamoto K - Search Results

1

A small nuclear acidic protein (MTI-II, Zn²⁺-binding protein, parathymosin) attenuates TNF-α inhibition of BMP-induced osteogenesis by enhancing accessibility of the Smad4-NF-κB p65 complex to Smad binding element.

Hirata-Tsuchiya S, Suzuki S, Okamoto K, Saito N, Yuan H, Yamada S, Jimi E, Shiba H, Kitamura C. Hirata-Tsuchiya S, et al. Among authors: okamoto k. Mol Cell Biochem. 2020 Jun;469(1-2):133-142. doi: 10.1007/s11010-020-03734-6. Epub 2020 Apr 18. Mol Cell Biochem. 2020. PMID: 32304006

2

A Small Nuclear Acidic Protein (MTI-II, Zn²⁺ Binding Protein, Parathymosin) That Inhibits Transcriptional Activity of NF-κB and Its Potential Application to Antiinflammatory Drugs.

Okamoto K, Hirata-Tsuchiya S, Kitamura C, Omoteyama K, Sato T, Arito M, Kurokawa MS, Suematsu N, Kato T. Okamoto K, et al. Endocrinology. 2016 Dec;157(12):4973-4986. doi: 10.1210/en.2016-1746. Epub 2016 Oct 14. Endocrinology. 2016. PMID: 27740872

3

The Novel NF-κB Inhibitor, MTI-II Peptide Anti-Inflammatory Drug, Suppresses Inflammatory Responses in Odontoblast-Like Cells.

Nakayama K, Hirata-Tsuchiya S, Okamoto K, Morotomi T, Jimi E, Kitamura C. Nakayama K, et al. Among authors: okamoto k. J Cell Biochem. 2016 Nov;117(11):2552-8. doi: 10.1002/jcb.25548. Epub 2016 Apr 4. J Cell Biochem. 2016. PMID: 27012464

4

Purification and primary structure of a macromolecular-translocation inhibitor II of glucocorticoid-receptor binding to nuclei from rat liver. Inhibitor II is the 11.5-kDa Zn2+-binding protein (parathymosin).

Okamoto K, Isohashi F. Okamoto K, et al. Eur J Biochem. 2000 Jan;267(1):155-62. doi: 10.1046/j.1432-1327.2000.00987.x. Eur J Biochem. 2000. PMID: 10601862 Free article.

5

Subcellular distribution of ATP-stimulated and ADP-inhibited acetyl-CoA hydrolase in livers from control and clofibrate-treated rats: comparison of the cytosolic and peroxisomal enzyme.

Nakanishi Y, Okamoto K, Isohashi F. Nakanishi Y, et al. Among authors: okamoto k. J Biochem. 1994 Feb;115(2):328-32. doi: 10.1093/oxfordjournals.jbchem.a124337. J Biochem. 1994. PMID: 7911463 Free article.

6

Macromolecular translocation inhibitor II (Zn(2+)-binding protein, parathymosin) interacts with the glucocorticoid receptor and enhances transcription in vivo.

Okamoto K, Isohashi F. Okamoto K, et al. J Biol Chem. 2005 Nov 4;280(44):36986-93. doi: 10.1074/jbc.M506056200. Epub 2005 Sep 2. J Biol Chem. 2005. PMID: 16150697 Free article.

7

Purification and characterization of a macromolecular-translocation inhibitor III of activated glucocorticoid-receptor-complex binding to nuclei from rat liver.

Liu G, Okamoto K, Isohashi F. Liu G, et al. Among authors: okamoto k. Eur J Biochem. 1993 Dec 1;218(2):679-87. doi: 10.1111/j.1432-1033.1993.tb18422.x. Eur J Biochem. 1993. PMID: 8269959 Free article.

Macromolecular-translocation inhibitors (MTI) of binding of the activated glucocorticoid-receptor complex (GRC) to nuclei from rat liver are separated into at least three components (MTI-I-III) by DEAE-cellulose column chromatography [Okamoto, K., Isohashi, F., Hori …

Macromolecular-translocation inhibitors (MTI) of binding of the activated glucocorticoid-receptor complex (GRC) to nuclei from rat liver are …

8

Inhibition of weak-base amine-induced lysis of lysosomes by cytosol.

Arai K, Yasuda N, Isohashi F, Okamoto K, Ohkuma S. Arai K, et al. Among authors: okamoto k. J Biochem. 2002 Oct;132(4):529-34. doi: 10.1093/oxfordjournals.jbchem.a003253. J Biochem. 2002. PMID: 12359066 Free article.

9

ATP-stimulated translocation promoter that enhances the nuclear binding of activated glucocorticoid receptor complex. Biochemical properties and its function (mini-review).

Isohashi F, Okamoto K. Isohashi F, et al. Among authors: okamoto k. Receptor. 1993 Summer;3(2):113-24. Receptor. 1993. PMID: 8251951 Review.

10

Properties of an adenosine triphosphate-stimulated factor that enhances the nuclear binding of activated glucocorticoid-receptor complex: binding to histone-agarose.

Okamoto K, Isohashi F, Ueda K, Sakamoto Y. Okamoto K, et al. Endocrinology. 1989 Feb;124(2):675-80. doi: 10.1210/endo-124-2-675. Endocrinology. 1989. PMID: 2912694

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