Bibliography
Selected
publications
S. Endo, F. Shutoh, T. L.
Dinh, T. Okamoto, T.
Ikeda, M. Suzuki, S. Kawahara, Dai Yanagihara, K. Yamada, Y. Kirino, T.
Sakamoto, S Itohara, A. Nairn, P Greengard, S. Nagao, and M. Ito. Dual
involvement of G-substrate in motor learning revealed by gene deletion.
Proc. Natl. Acad. Sci. USA. 106,
3525-3530, 2009.
N. Kojima, G. Borlikova, T.
Sakamoto, K.
Yamada, T. Ikeda, S. Itohara, H. Niki, and S. Endo. Inducible cAMP
early repressor acts as a negative regulator for kindling
epileptogenesis and long-term fear memory. J. Neurosci.
28, 6459-6472, 2008.
T. Launey, S. Endo, R.
Sakai, J. Harano, and M. Ito.
Protein phosphatase -2A regulates cerebellar long-term depression and
declustering of synaptic AMPA receptor.
Proc. Natl. Acad. Sci. USA. 101, 676-681, 2004.
S. Endo and T. Launey.
ERKs regulate PKC-dependent synaptic depression and declustering of
glutamate receptors in cerebellar Purkinje cells.
Neuropharmacol. 45, 863-872, 2003.
S. Endo, M. Suzuki, M. Sumi, A.C. Nairn, R. Morita, K. Yamakawa, P.
Greengard, and M. Ito.
Molecular identification of human G-substrate, a possible downstream
component of cGMP-dependent protein kinase cascade.
Proc. Natl. Acad. Sci. USA 96, 2467-2472, 1999.
Q.R. Liu. S. Hattar, S. Endo, K. MacPhee, H. Zhang, L.J. Cleary, J.H.
Byrne, and A. Eskin.
A developmental Gene (Tolloid/BMP-1) is regulated in Aplysia neurons by
treatments that induce long-term sensitization.
J. Neurosci. 17, 755-764, 1997.
F. Zhang, S. Endo, L.J. Cleary, A. Eskin, and J.H. Byrne.
Role of transforming growth factor-β in long-term synaptic
facilitation in Aplysia.
Science 275, 1318-1320, 1997.
S. Endo, S.D. Critz, J.H. Byrne, and S. Shenolikar.
Protein phosphatase-1 regulates K+ currents in
the sensory neurons of Aplysia californica.
J. Neurochem. 64, 1833-1840, 1995.
R.M. Mulkey, S. Endo, S. Shenolikar, and R.C. Malenka.
Involvement of a calcineurin/inhibitor-1 phosphatase cascade in
hippocampal long-term depression.
Nature 369, 486-488, 1994.
Full
publications
Y. Uechi, M. Bayarjargal,
M. Umikawa, M.
Oshiro, K. Takei, Y. Yamashiro, T. Asato, S. Endo, R. Misaki, T.
Taguchi, K. Kariya. Rap2 function requires palmitoylation and recycling
endosome localization. Biochem.Biophys.Res. Commu.
378, 732-737, 2009.
S. Endo, F. Shutoh, T. L.
Dinh, T. Okamoto, T.
Ikeda, M. Suzuki, S. Kawahara, Dai Yanagihara, K. Yamada, Y. Kirino, T.
Sakamoto, S Itohara, A. Nairn, P Greengard, S. Nagao, and M. Ito. Dual
involvement of G-substrate in motor learning revealed by gene deletion.
Proc. Natl. Acad. Sci. USA. 106,
3525-3530, 2009.
G. Borlikova and S. Endo.
Inducible cAMP early repressor (ICER) and Brain Functions. Mol.
Neurobiol. 40, 73-86, 2009.
T. Nakazawa, M. Shimura, M.
Ryu, K. Nishida,
G. Pagès, J. Pouyssègur, and S. Endo. ERK1 plays
a
critical protective role against N-methyl-D-aspartate-induced retinal
injury. J. Neurosci. Res. 86(1),
136-144, 2008
T. Suzuki, F. Du, QB. Tian,
J. Zhang, and S.
Endo. Ca2+/calmodulin-dependent protein kinase IIα clusters
are
associated with stable lipid rafts and their formation traps PSD-95. J.
Neurochem. 104(3), 596-610,
2008
N. Kojima, G. Borlikova, T.
Sakamoto, K.
Yamada, T. Ikeda, S. Itohara, H. Niki, and S. Endo. Inducible cAMP
early repressor acts as a negative regulator for kindling
epileptogenesis and long-term fear memory. J. Neurosci.
28, 6459-6472, 2008.
T. Sakamoto, and S. Endo.
GABAA receptors in deep cerebellar nuclei play important roles in mouse
eyeblink conditioning. Brain Res. 1230,
125-137, 2008.
T. Nakazawa, M. Shimura, M.
Kondo, S.
Yokokura, M. Tamai, K. Nishida, and S. Endo. The neuroprotective role
of G-substrate in N-methyl-D-aspartate-induced amacrine cell death. J.
Neurosci. Res. 86,
136-144, 2008.
T. Nakazawa, M. Shimura, R.
Mourin, M Kondo,
S. Yokokura, T.C. Saido, K. Nishida, and S. Endo. Calpain-mediated
degradation of G-substrate plays a critical role in retinal
excitotoxicity for amacrine cells. J Neurosci. Res. 87,
1412-1423.
H. Nonaka, K. Takei, M.
Umikawa, M, Oshiro, K.
Kuninaka, M. Bayarjargal, T. Asato, Y. Yamashiro, Y. Uechi, S. Endo,
Tatsuo Suzuki. MINK is a Rap2 effector for phosphorylation of
the
postsynaptic scaffold protein TANC1. Biochem. Biophys. Res.
Comm. 377, 573-578, 2008.
O. Imamura, Y. Satoh, S.
Endo, and K.
Takishima. Analysis of extracellular signal-regulated kinase 2 function
in neural stem.progenitor cells via nervous system-specific gene
disruption. Stem cells, 26, 3247-3256, 2008.
T. Suzuki, Q.B. Tian, J.
Kuromitsu, T. Kawai,
and S. Endo. Characterization of mRNA species that are associated with
postsynaptic density fraction by gene chip microarray analysis.
Neurosci. Res. 57(1), 61-85, 2007
E. Maruyama, K. Ogawa, S.
Endo, M. Tsujimoto,
T. Hashikawa, T. Nabetani, and A. Tsugita. Brain-derived neurotrophic
factor induces cell surface expression of short-form tenascin R complex
in hippocampal presynapses. Int. J. Biochem. Cell. Biol. 39(10),
1930-1942, 2007.
Y. Lu, QB. Tian, S. Endo,
and T. Suzuki A role
for LRP4 in neuronal cell viability is related to apoE-binding. Brain
Res. 1177, 19-28, 2007.
C.Y. Chung, J. B. Koprich,
S. Endo, and O.
Isacson. An endogenous Ser/Thr protein phosphatase inhibitor,
G-substrate, reduces vulnerability in models of Parkinson’s
disease. J. Neurosci. 27(31), 8314-8323, 2007.
Y. Satoh, S. Endo, T.
Ikeda, K. Yamada, M.
Ito, M. Kuroki, T. Hiramoto, O. Imamura, Y. Kobayashi, Y. Watanabe, S.
Itohara, and K. Takishima. ERK2 knockdown mice show deficit in
long-term memory; ERK2 has a specific function in learning and memory.
J. Neurosci. 27(40), 10765-10776, 2007
S. Endo, Y. Satoh, K. Shah,
and K. Takishima A
single amino-acid change in ERK1/2 makes the enzyme susceptible to PP1
derivatives. Biochem. Biophys. Res. Commun. 341, 261-265, 2006.
Q.B. Tian, T. Suzuki, T.
Yamauchi, H.
Sakagami, Y. Yoshimura, S. Miyazawa, K. Nakayama, F. Saitoh, J.P.
Zhang, Y. Lu, H. Kondo, and S. Endo. Interaction of LDL
receptor-related protein 4 (LRP4) with postsynaptic scaffold proteins
via its C-terminal PDZ domain-binding motif, and its regulation by
Ca2+/calmodulin-dependent protein kinase II. Eur. J. Neurosci. 23,
2864-2876, 2006
F. Du, F. Saitoh, Q.B.
Tian, S. Miyazawa, S.
Endo, and T. Suzuki Mechanisms for association of
Ca2+/calmodulin-dependent protein kinase II with lipid rafts. Biochem.
Biophys. Res. Commun. 347, 814-820, 2006.
T. Suzuki, W. Li, J.P. Zhang, Q.B. Tian, H. Sakagami, N. Usada, H.
Kondo, T. Fujii, and S. Endo. A novel scaffold protein, TANC, possibly
a rat homolog of Drosophila rolling pebbles
(rols), forms a multiprotein complex with various postsynaptic density
proteins.
Eur. J. Neurosci. 21,
339-350, 2005
X. Wang, Q.B. Tian, A.
Okano, H. Sakagami,
I.S. Moon, H. Kondo, S. Endo, and T. Suzuki. BAALC 1-6-8 protein is
targeted to postsynaptic lipid rafts by its N-terminal myristoylation
and palmitoylation, and interacts with α, but not β,
subunit
of Ca2+/calmodulin-dependent protein kinase II.
J. Neurochem. 92,
647-659, 2005
N. Kojima, T. Sakamoto, S.
Endo, and H. Niki.
Impairment of conditioned freezing to tone, but not to context, in
Fyn-transgenic mice: Relationship to NMDA receptor subunit 2B function.
Eur. J. Neurosci. 21,
1359-1369, 2005
J.P. Zhang, Q.B. Tian, H.
Sakagami, H. Kondo,
S. Endo, and T. Suzuki. p55 protein is a member of PSD scaffold
proteins in the rat brain and interacts with various PSD proteins.
Brain Res. Mol. Brain Res. 135,
204-216, 2005
JS. Bae, S. Furuya, Y.
Shinoda, S. Endo, EH.
Schuchman, Y. Hirabayashi and HK. Jin. Neurodegeneration augments the
ability of bone marrow-derived mesenchymal stem cells to fuse with
Purkinje neurons in Niemann-Pick type C Mice.
Hum. Gene, Ther. 16,
1006-1011, 2005.
T. Nakazawa, S. Endo, M.
Shimura, M. Kondo, S.
Ueno, and M. Tamai. Retinal G-substrate, potential downstream component
of NO/cGMP/PKG pathway, is located in subtype of retinal ganglion cells
and amacrine cells with protein phosphatases.
Brain Res. Mol. Brain Res. 135,
58-68, 2005
T. Nakazawa, M. Shimura, S.
Endo, H.
Takahashi, N. Mori, and M. Tamai. N-Methyl-D-Aspartate suppresses Akt
activity through protein phosphatase in the retinal ganglion cells.
Mol. Vision. 11,
1173-1182, 2005
Y. Satoh, Y. Kanda, M.
Terakawa, M. Obara, K.
Mizuno, Y. Watanabe, S. Endo, H. Ooigawa, H. Nawashiro, S. Sato, and K.
Takishima. Targeted DNA transfection into the mouse central nervous
system using laser-induced stress waves. J. Biomed. Opt.
10, 060501, 2005
Q.B. Tian, T. Suzuki, T. Yamauchi, H. Sakagami, Y. Yoshimura, S.
Miyazawa, K. Nakayama, F. Saitoh, J.P. Zhang, Y. Lu, H. Kondo and S.
Endo.
Interaction of LDL receptor-related protein 4 (LRP4) with postsynaptic
scaffold proteins via its C-terminal PDZ domain-binding motif, and its
regulation by Ca2+/calmodulin-dependent protein kinase II.
Eur. J. Neurosci.23, 2864-2876, 2006
S. Endo, Y. Satoh, K. Shah,
and K. Takishima
A single amino-acid change in ERK1/2 makes the enzyme susceptible to
PP1 derivatives.
Biochem. Biophys. Res. Commun. 341, 261-265, 2006.
T. Suzuki, W. Li, J.P.
Zhang, Q.B. Tian, H. Sakagami, N. Usada, H. Kondo, T. Fujii, and S.
Endo.
A novel scaffold protein, TANC, possibly a rat homolog of Drosophila
rolling pebbles (rols), forms a multiprotein complex with various
postsynaptic density proteins.
Eur. J. Neurosci. 21, 339-350, 2005
X. Wang, Q.B. Tian, A. Okano, H. Sakagami, I.S. Moon, H. Kondo, S.
Endo, and T. Suzuki.
BAALC 1-6-8 protein is targeted to postsynaptic lipid rafts by its
N-terminal miristoylation and palmitoylation, and interacts with
α, but not β, subunit of Ca2+/calmodulin-dependent
protein kinase II.
J. Neurochem. 92, 647-659, 2005
N. Kojima, T. Sakamoto, S. Endo, and H. Niki.
Impairment of conditioned freezing to tone, but not to context, in
Fyn-transgenic mice: Relationship to NMDA receptor subunit 2B function.
Eur. J. Neurosci. 21, 1359-1369, 2005
J.P. Zhang, Q.B. Tian, H. Sakagami, H. Kondo, S. Endo, and T. Suzuki.
p55 protein is a member of PSD scaffold proteins in the rat brain and
interacts with various PSD proteins.
Brain Res Mol Brain Res. 135, 204-216, 2005
JS. Bae, S. Furuya, Y. Shinoda, S. Endo, EH. Schuchman, Y. Hirabayashi
and HK. Jin.
Neurodegeneration Augments the Ability of Bone Marrow-Derived
Mesenchymal Stem Cells to Fuse with Purkinje Neurons in Niemann-Pick
Type C Mice.
Hum. Gene, Ther. 16, 1006-1011, 2005.
T. Nakazawa, S. Endo, M. Shimura, M. Kondo, S. Ueno, and M. Tamai.
Retinal G-substrate, potential downstream component of NO/cGMP/PKG
pathway, is located in subtype of retinal ganglion cells and amacrine
cells with protein phosphatases.
Brain Res Mol Brain Res. 135, 58-68, 2005
T. Nakazawa, M. Shimura, S. Endo, H. Takahashi, N. Mori, and M. Tamai.
N-Methyl-D-Aspartate suppresses Akt activity through protein
phosphatase in the retinal ganglion cells.
Mol. Vision. 11, 1173-1182, 2005
Y. Satoh, Y. Kanda, M. Terakawa, M. Obara, K. Mizuno, Y. Watanabe, S.
Endo, H. Ooigawa, H. Nawashiro, S. Sato, and K. Takishima.
Targeted DNA transfection into the mouse central nervous system using
laser-induced stress waves.
J. Biomed. Opt. 10, 060501, 2005
T. Launey, S. Endo, R. Sakai, J. Harano, and M. Ito.
Protein phosphatase -2A regulates cerebellar long-term depression and
declustering of synaptic AMPA receptor.
Proc. Natl. Acad. Sci. USA. 101, 676-681, 2004.
M. Michishita, T. Ikeda, T. Nakashiba, M. Ogawa, K. Tashiro, T. Honjo,
K. Doi, S. Itohara, and S. Endo.
Expression of Btcl2, a novel member of Btcl gene family, during
development of the central nervous system.
Developmental Brain Res, 153, 135-142, 2004.
S. Endo, A.C. Nairn, P. Greengard, and M. Ito.
Thr123 of rat G-substrate contributes to its action as a protein
phosphatase inhibitor.
Neuroscience Research. 45, 79-89, 2003.
M. Michishita, T. Ikeda, T. Nakashiba, M. Ogawa, K. Tashiro, T. Honjo,
K. Doi, S. Itohara, and S. Endo.
A novel gene, Btcl1, encoding CUB and LDLa domains is expressed in
restricted areas of mouse brain.
Biochem. Biophys. Res. Commun. 306, 680-686, 2003.
S. Endo and T. Launey.
ERKs regulate PKC-dependent synaptic depression and declustering of
glutamate receptors in cerebellar Purkinje cells.
Neuropharmacol. 45, 863-872, 2003.
S. Endo and T. Launey.
Nitric oxide activates ERK1/2 and enhances declustering of GluR2/3 in
cerebellar Purkinje cells.
Neurosci. Lett. 350, 122-126, 2003.
Q.B. Tian, A. Okano, K. Nakayama, S. Miyazawa, S. Endo, and T. Suzuki.
A novel ubiquitin-specific protease, synUSP, is localized at the
postsynaptic density and postsynaptic lipid raft.
J. Neurochem. 87, 665-675, 2003.
H. Nishiyama, T. Knopfel, S. Endo, and S. Itohara.
Glial protein S100B modulates long term neuronal synaptic plasticity.
Proc. Natl. Acad. Sci. USA 99, 4037-4042, 2002.
J. Levenson, S. Endo, J.H. Byrne, and A. Eskin.
Long-term regulation of neuronal high-affinity glutamate uptake in
Aplysia.
Proc. Natl. Acad. Sci. USA 97, 12858-12863, 2000.
S. Endo, M. Suzuki, M. Sumi, A.C. Nairn, R. Morita, K. Yamakawa, P.
Greengard, and M. Ito.
Molecular identification of human G-substrate, a possible downstream
component of cGMP-dependent protein kinase cascade.
Proc. Natl. Acad. Sci. USA 96, 2467-2472, 1999.
Q.R. Liu. S. Hattar, S. Endo, K. MacPhee, H. Zhang, L.J. Cleary, J.H.
Byrne, and A. Eskin.
A developmental Gene (Tolloid/BMP-1) is regulated in Aplysia neurons by
treatments that induce long-term sensitization.
J. Neurosci. 17, 755-764, 1997.
F. Zhang, S. Endo, L.J. Cleary, A. Eskin, and J.H. Byrne.
Role of transforming growth factor-β in long-term synaptic
facilitation in Aplysia.
Science 275, 1318-1320, 1997.
S. Endo, J.H. Connor, B. Forney, L. Zhang, T.S. Ingebritsen, E.Y.C.
Lee, and S. Shenolikar.
Conversion of protein phosphatase 1 catalytic subunit to a Mn2+-dependent
enzyme impairs its regulation by inhibitor 1.
Biochemistry 36, 6986-6992, 1997.
S. Endo, X. Zhou, J. Connor, B. Wang, and S. Shenolikar.
Multiple structural elements defines the specificity of recombinant
human inhibitor-1 as a protein phosphatase-1 inhibitor.
Biochemistry 35, 5220-5228, 1996.
S. Endo, S.D. Critz, J.H. Byrne, and S. Shenolikar.
Protein phosphatase-1 regulates K+ currents in
the sensory neurons of Aplysia californica.
J. Neurochem. 64, 1833-1840, 1995.
S. Endo.
Neuronal membrane Protein Phosphatases.
Neuroprotocols 6, 29-34, 1995.
R.M. Mulkey, S. Endo, S. Shenolikar, and R.C. Malenka.
Involvement of a calcineurin/inhibitor-1 phosphatase cascade in
hippocampal long-term depression.
Nature 369, 486-488, 1994.
S. Endo and S. Shenolikar.
Protein phosphatases and memory currents.
Neurosci. Facts 4, 11-12, 1993.
S. Endo, R.E. Zwartjes, A. Eskin, S. Shenolikar, and J.H. Byrne.
Characterization of protein phosphatases in Aplysia californica.
J. Neurochem. 58, 975-982, 1992.
S. Endo, M. Ichinose, S.D. Critz, A. Eskin, J.H. Byrne, and S.
Shenolikar.
Protein phosphatases and their role in control of membrane currents in
Aplysia neurons.
Adv. Protein Phosphatase, 6, 411-432, 1991.
M. Ichinose, S. Endo, S.D. Critz, S. Shenolikar, and J.H. Byrne.
MCYST-LR, a potent protein phosphatase inhibitor, prolongs the
serotonin- and cAMP-induced currents in sensory neurons of Aplysia
californica.
Brain Research 533, 137-140, 1990.
S. Endo, H. Yokosawa, and S. Ishii.
Degradation of substance P by neuronal and glial cells cultured from
rat fetal brain and their membrane.
Neuropeptides 14, 31-37, 1989.
S. Endo, H. Yokosawa, and S. Ishii.
Involvement of endopeptidase-24.11 in degradation of substance P by
glioma cells.
Neuropeptides 14, 177-184, 1989.
S. Endo, H. Yokosawa, and S. Ishii. Purification and
characterization of a substance P-degrading endopeptidase from rat
brain. J. Biochem. 104, 999-1006, 1988.
H. Yokosawa, S. Endo, Y. Ohgaki, J. Maeyama, and S. Ishii.
Hydrolysis of substance P and its analogues by angiotensin-converting
enzyme from rat lung. Characterization of endopeptidase
activity of the enzyme. J. Biochem. 98, 1293-1299, 1985.
S. Endo, H. Yokosawa, and S. Ishii. Degradation of substance
P by neuroblastoma cells and their membrane. Biochem.
Biophys. Res. Commun. 129, 694-700, 1985.
H. Yokosawa, S. Endo, Y. Ogura and S. Ishii. New feature of
angiotensin-converting enzyme in the brain : Hydrolysis of substance
P. Biochem. Biophys. Res. Commun. 116, 735-742, 1983.
Reviews
S. Endo.
Mechanisms of Memory.
Vol1, pp254-264, Neurosurgery Guide Book, A. Yamaura, ed., Nakayama
Shoten Co., Tokyo, Japan.
S. Endo.
Learning and Memory.
pp 247-256, Neuroscience Illustrated, Mori et al ed., Yodosha, Tokyo,
Japan
S. Endo.
An efficient animal facility for he study of learning and memory study
using genetically modified animals.
LABBIO21. 24, 18-24, 2006
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