Y. Matsuoka

发表

Adducin Regulation

C. Hughes, V. Bennett, Y. Matsuoka, 1996, The Journal of Biological Chemistry.

Regulation of the Association of Adducin with Actin Filaments by Rho-associated Kinase (Rho-kinase) and Myosin Phosphatase*

K. Kaibuchi, A. Iwamatsu, Y. Fukata, 1998, The Journal of Biological Chemistry.

Synthetic linear and cyclic peptides corresponding to the sites phosphorylated in histone H1 and vimentin as substrates of cdc2 kinase

M. Inagaki, N. Nishino, S. Ando, 1993 .

Two different protein kinases act on a different time schedule as glial filament kinases during mitosis.

M. Inagaki, T. Yano, M. Shibata, 1992, The EMBO journal.

α-Adducin dissociates from F-actin and spectrin during platelet activation

J. Hartwig, V. Bennett, J. Italiano, 2003, The Journal of cell biology.

Phosphorylation of native and reassembled neurofilaments composed of NF-L, NF-M, and NF-H by the catalytic subunit of cAMP-dependent protein kinase.

N. Hirokawa, M. Inagaki, S. Hisanaga, 1994, Molecular biology of the cell.

Phosphorylation of Adducin by Rho-Kinase Plays a Crucial Role in Cell Motility

K. Kaibuchi, N. Oshiro, Y. Fukata, 1999, The Journal of cell biology.

Dynamic property of intermediate filaments: Regulation by phosphorylation

M. Inagaki, N. Inagaki, Toshitada Takahashi, 1996 .

Adducin Is an In Vivo Substrate for Protein Kinase C: Phosphorylation in the MARCKS-related Domain Inhibits Activity in Promoting Spectrin–Actin Complexes and Occurs in Many Cells, Including Dendritic Spines of Neurons

V. Bennett, Xiaolin Li, Y. Matsuoka, 1998, The Journal of cell biology.

Adducin: structure, function and regulation

Y. Matsuoka, V. Bennett, X. Li, 2000, Cellular and Molecular Life Sciences CMLS.

Identification of phosphorylation sites on glial fibrillary acidic protein for cdc2 kinase and Ca(2+)-calmodulin-dependent protein kinase II.

M. Inagaki, M. Kusubata, H. Sugiura, 1994, Journal of biochemistry.

Adducin Preferentially Recruits Spectrin to the Fast Growing Ends of Actin Filaments in a Complex Requiring the MARCKS-related Domain and a Newly Defined Oligomerization Domain*

V. Bennett, Xiaolin Li, Y. Matsuoka, 1998, The Journal of Biological Chemistry.

p13suc1 suppresses the catalytic function of p34cdc2 kinase for intermediate filament proteins, in vitro.

H. Yasuda, T. Kishimoto, M. Kusubata, 1992, The Journal of biological chemistry.

Rho-kinase induces association of adducin with the cytoskeleton in platelet activation.

K. Kaibuchi, H. Shiku, M. Nishikawa, 2005, Biochemical and biophysical research communications.

Phosphorylation ofNative andReassembled Neurofilaments Composed ofNF-L,NF-M,and NF-HbytheCatalytic Subunit ofcAMP-dependent

S. Hisanaga, Y. Matsuoka, 1994 .

Phosphorylation of Adducin by Rho-Kinase Plays a Crucial Role in Cell Motility

K. Kaibuchi, N. Oshiro, Y. Fukata, 1999, The Journal of cell biology.

Phosphorylation of synthetic vimentin peptides by cdc2 kinase.

M. Inagaki, H. Yasuda, T. Kishimoto, 1993, Biochemical and biophysical research communications.

cdc2 kinase phosphorylation of desmin at three serine/threonine residues in the amino-terminal head domain.

M. Inagaki, H. Yasuda, T. Kishimoto, 1993, Biochemical and biophysical research communications.

Mediation of the physiological response of platelets by interactions of spectrin and protein 4.1 with the cytoskeleton.

T. Yano, R. Yatani, S. Ando, 1994, Biochemical and biophysical research communications.