Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation

Search Page

My NCBI Filters
Text availability
Article attribute
Article type
Publication date

Search Results

259 results
Filters applied: . Clear all Results are displayed in a computed author sort order. Results by year timeline is unavailable
Page 1
Phosphorylation states of microtubule-associated protein 2 (MAP2) determine the regulatory role of MAP2 in microtubule dynamics.
Itoh TJ, Hisanaga S, Hosoi T, Kishimoto T, Hotani H. Itoh TJ, et al. Among authors: hisanaga s. Biochemistry. 1997 Oct 14;36(41):12574-82. doi: 10.1021/bi962606z. Biochemistry. 1997. PMID: 9376363
Ser787 in the proline-rich region of human MAP4 is a critical phosphorylation site that reduces its activity to promote tubulin polymerization.
Kitazawa H, Iida J, Uchida A, Haino-Fukushima K, Itoh TJ, Hotani H, Ookata K, Murofushi H, Bulinski JC, Kishimoto T, Hisanaga S. Kitazawa H, et al. Among authors: hisanaga s. Cell Struct Funct. 2000 Feb;25(1):33-9. doi: 10.1247/csf.25.33. Cell Struct Funct. 2000. PMID: 10791892
Mutation of Ser787 to Glu strikingly reduced the MAP4's MT-polymerization activity, while Glu-mutation at Ser696 did not. These results suggest that Ser787 could be the critical phosphorylation site causing MTs to be dynamic at mitosis....
Mutation of Ser787 to Glu strikingly reduced the MAP4's MT-polymerization activity, while Glu-mutation at Ser696 did not. These resul …
Role of the pyrrolidine ring of proline in determining the substrate specificity of cdc2 kinase or cdk5.
Ando S, Ikuhara T, Kamata T, Sasaki Y, Hisanaga S, Kishimoto T, Ito H, Inagaki M. Ando S, et al. Among authors: hisanaga s. J Biochem. 1997 Aug;122(2):409-14. doi: 10.1093/oxfordjournals.jbchem.a021768. J Biochem. 1997. PMID: 9378721
MAP4 is the in vivo substrate for CDC2 kinase in HeLa cells: identification of an M-phase specific and a cell cycle-independent phosphorylation site in MAP4.
Ookata K, Hisanaga S, Sugita M, Okuyama A, Murofushi H, Kitazawa H, Chari S, Bulinski JC, Kishimoto T. Ookata K, et al. Among authors: hisanaga s. Biochemistry. 1997 Dec 16;36(50):15873-83. doi: 10.1021/bi971251w. Biochemistry. 1997. PMID: 9398320
Limited chymotryptic digestion of bovine adrenal 190,000-Mr microtubule-associated protein and preparation of a 27,000-Mr fragment which stimulates microtubule assembly.
Aizawa H, Murofushi H, Kotani S, Hisanaga S, Hirokawa N, Sakai H. Aizawa H, et al. Among authors: hisanaga s. J Biol Chem. 1987 Mar 15;262(8):3782-7. J Biol Chem. 1987. PMID: 3818666
., Kotani, S., Aizawa, H., Hisanaga, S., Hirokawa, N., and Sakai, H. (1986) J. Cell Biol. 103, 1911-1919). Limited chymotryptic digestion of 190-kDa MAP produced a fragment of Mr 27,000 (27-kDa fragment), which bound to microtubules reconstituted in the prese …
., Kotani, S., Aizawa, H., Hisanaga, S., Hirokawa, N., and Sakai, H. (1986) J. Cell Biol. 103, 1911-1919). Limited chym …
Purification and characterization of a 190-kD microtubule-associated protein from bovine adrenal cortex.
Murofushi H, Kotani S, Aizawa H, Hisanaga S, Hirokawa N, Sakai H. Murofushi H, et al. Among authors: hisanaga s. J Cell Biol. 1986 Nov;103(5):1911-9. doi: 10.1083/jcb.103.5.1911. J Cell Biol. 1986. PMID: 3782289 Free PMC article.
At maximum 1 mol of 190-kD MAP could bind to 2.3 mol of tubulin. 190-kD MAP was phosphorylated by a cAMP-dependent protein kinase prepared from sea urchin spermatozoa and by protein kinase(s) present in the microtubule protein fraction prepared from mammalian brains. ...Th …
At maximum 1 mol of 190-kD MAP could bind to 2.3 mol of tubulin. 190-kD MAP was phosphorylated by a cAMP-dependent protein kinase prepared f …
Dephosphorylation of microtubule-binding sites at the neurofilament-H tail domain by alkaline, acid, and protein phosphatases.
Hisanaga S, Yasugawa S, Yamakawa T, Miyamoto E, Ikebe M, Uchiyama M, Kishimoto T. Hisanaga S, et al. J Biochem. 1993 Jun;113(6):705-9. doi: 10.1093/oxfordjournals.jbchem.a124107. J Biochem. 1993. PMID: 8396571
Phosphorylation of native and reassembled neurofilaments composed of NF-L, NF-M, and NF-H by the catalytic subunit of cAMP-dependent protein kinase.
Hisanaga S, Matsuoka Y, Nishizawa K, Saito T, Inagaki M, Hirokawa N. Hisanaga S, et al. Mol Biol Cell. 1994 Feb;5(2):161-72. doi: 10.1091/mbc.5.2.161. Mol Biol Cell. 1994. PMID: 8019002 Free PMC article.
Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics.
Ookata K, Hisanaga S, Bulinski JC, Murofushi H, Aizawa H, Itoh TJ, Hotani H, Okumura E, Tachibana K, Kishimoto T. Ookata K, et al. Among authors: hisanaga s. J Cell Biol. 1995 Mar;128(5):849-62. doi: 10.1083/jcb.128.5.849. J Cell Biol. 1995. PMID: 7876309 Free PMC article.
Neurofilament-associated protein phosphatase 2A: its possible role in preserving neurofilaments in filamentous states.
Saito T, Shima H, Osawa Y, Nagao M, Hemmings BA, Kishimoto T, Hisanaga S. Saito T, et al. Among authors: hisanaga s. Biochemistry. 1995 Jun 6;34(22):7376-84. doi: 10.1021/bi00022a010. Biochemistry. 1995. PMID: 7779779
259 results
Jump to page
Feedback