메뉴 건너뛰기




Volumn 287, Issue 4, 2012, Pages 2437-2445

Amyloid precursor protein revisited: Neuron-specific expression and highly stable nature of soluble derivatives

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMYLOID PRECURSOR PROTEINS; CENTRAL NERVOUS SYSTEMS; DEATH-RECEPTOR; FUNDAMENTAL PROPERTIES; GLIAL CELLS; PATHOPHYSIOLOGY; SOLUBLE DERIVATIVES; WILD TYPES;

EID: 84862953172     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.315051     Document Type: Article
Times cited : (73)

References (49)
  • 1
    • 79955128215 scopus 로고    scopus 로고
    • Biology and pathophysiology of the amyloid precursor protein
    • Zheng, H., and Koo, E. H. (2011) Biology and pathophysiology of the amyloid precursor protein. Mol. Neurodegener. 6, 27
    • (2011) Mol. Neurodegener. , vol.6 , pp. 27
    • Zheng, H.1    Koo, E.H.2
  • 2
    • 0031035006 scopus 로고    scopus 로고
    • Mab22C11 antibody to amyloid precursor protein recognizes a protein associated with specific astroglial cells of the rat central nervous system characterized by their capacity to support axonal outgrowth
    • DOI 10.1002/(SICI)1096-9861(19970127)377:4<550::AID-CNE6>3.0.CO;2-1
    • Chauvet, N., Apert, C., Dumoulin, A., Epelbaum, J., and Alonso, G. (1997) Mab22C11 antibody to amyloid precursor protein recognizes a protein associated with specific astroglial cells of the rat central nervous system characterized by their capacity to support axonal outgrowth. J. Comp. Neurol. 377, 550-564 (Pubitemid 27053548)
    • (1997) Journal of Comparative Neurology , vol.377 , Issue.4 , pp. 550-564
    • Chauvet, N.1    Apert, C.2    Dumoulin, A.3    Epelbaum, J.4    Alonso, G.5
  • 4
    • 0009631131 scopus 로고    scopus 로고
    • Cell-specific expression of β-amyloid precursor protein isoform mRNAs and proteins in neurons and astrocytes
    • DOI 10.1016/S0169-328X(97)00045-4, PII S0169328X97000454
    • Rohan de Silva, H. A., Jen, A., Wickenden, C., Jen, L. S., Wilkinson, S. L., and Patel, A. J. (1997) Cell-specific expression of β-amyloid precursor protein isoform mRNAs and proteins in neurons and astrocytes. Brain Res. Mol. Brain Res. 47, 147-156 (Pubitemid 27268270)
    • (1997) Molecular Brain Research , vol.47 , Issue.1-2 , pp. 147-156
    • De Silva, H.A.R.1    Jen, A.2    Wickenden, C.3    Jen, L.-S.4    Wilkinson, S.L.5    Patel, A.J.6
  • 5
    • 78049267204 scopus 로고    scopus 로고
    • Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP
    • Li, H., Wang, B., Wang, Z., Guo, Q., Tabuchi, K., Hammer, R. E., Südhof, T. C., and Zheng, H. (2010) Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP. Proc. Natl. Acad. Sci. U.S.A. 107, 17362-17367
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17362-17367
    • Li, H.1    Wang, B.2    Wang, Z.3    Guo, Q.4    Tabuchi, K.5    Hammer, R.E.6    Südhof, T.C.7    Zheng, H.8
  • 6
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev, A., McLaughlin, T., O'Leary, D. D., and Tessier-Lavigne, M. (2009) APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457, 981-989
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 8
    • 26944435186 scopus 로고    scopus 로고
    • Alzheimer disease-like neuropathology of gene-targeted APP-SLxPS1mut mice expressing the amyloid precursor protein at endogenous levels
    • Köhler, C., Ebert, U., Baumann, K., and Schröder, H. (2005) Alzheimer disease-like neuropathology of gene-targeted APP-SLxPS1mut mice expressing the amyloid precursor protein at endogenous levels. Neurobiol. Dis. 20, 528-540
    • (2005) Neurobiol. Dis. , vol.20 , pp. 528-540
    • Köhler, C.1    Ebert, U.2    Baumann, K.3    Schröder, H.4
  • 9
    • 0033016172 scopus 로고    scopus 로고
    • Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice
    • DOI 10.1038/4789
    • Guo, Q., Fu, W., Sopher, B. L., Miller, M. W., Ware, C. B., Martin, G. M., and Mattson, M. P. (1999) Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice. Nat. Med. 5, 101-106 (Pubitemid 29051006)
    • (1999) Nature Medicine , vol.5 , Issue.1 , pp. 101-106
    • Guo, Q.1    Fu, W.2    Sopher, B.L.3    Miller, M.W.4    Ware, C.B.5    Martin, G.M.6    Mattson, M.P.7
  • 13
    • 80955125227 scopus 로고    scopus 로고
    • Disruption of the NF-κB/IκBα autoinhibitory loop improves cognitive performance and promotes hyperexcitability of hippocampal neurons
    • Shim, D. J., Yang, L., Reed, J. G., Noebels, J. L., Chiao, P. J., and Zheng, H. (2011) Disruption of the NF-κB/IκBα autoinhibitory loop improves cognitive performance and promotes hyperexcitability of hippocampal neurons. Mol. Neurodegener. 6, 42
    • (2011) Mol. Neurodegener. , vol.6 , pp. 42
    • Shim, D.J.1    Yang, L.2    Reed, J.G.3    Noebels, J.L.4    Chiao, P.J.5    Zheng, H.6
  • 14
    • 0026354082 scopus 로고
    • Rapid appearance of β-amyloid precursor protein immunoreactivity in damaged axons and reactive glial cells in rat brain following needle stab injury
    • Otsuka, N., Tomonaga, M., and Ikeda, K. (1991) Rapid appearance of β-amyloid precursor protein immunoreactivity in damaged axons and reactive glial cells in rat brain following needle stab injury. Brain Res. 568, 335-338
    • (1991) Brain Res. , vol.568 , pp. 335-338
    • Otsuka, N.1    Tomonaga, M.2    Ikeda, K.3
  • 15
    • 0030006010 scopus 로고    scopus 로고
    • Immunohistochemical characterization of alterations in the distribution of amyloid precursor proteins and β-amyloid peptide after experimental brain injury in the rat
    • Pierce, J. E., Trojanowski, J. Q., Graham, D. I., Smith, D. H., and McIntosh, T. K. (1996) Immunohistochemical characterization of alterations in the distribution of amyloid precursor proteins and β-amyloid peptide after experimental brain injury in the rat. J. Neurosci. 16, 1083-1090 (Pubitemid 26140865)
    • (1996) Journal of Neuroscience , vol.16 , Issue.3 , pp. 1083-1090
    • Pierce, J.E.S.1    Trojanowski, J.Q.2    Graham, D.I.3    Smith, D.H.4    McIntosh, T.K.5
  • 19
    • 0026501562 scopus 로고
    • Kunitz protease inhibitor-containing amyloid β-protein precursor immunoreactivity in Alzheimer disease
    • Hyman, B. T., Tanzi, R. E., Marzloff, K., Barbour, R., and Schenk, D. (1992) Kunitz protease inhibitor-containing amyloid β-protein precursor immunoreactivity in Alzheimer disease. J. Neuropathol. Exp. Neurol. 51, 76-83
    • (1992) J. Neuropathol. Exp. Neurol. , vol.51 , pp. 76-83
    • Hyman, B.T.1    Tanzi, R.E.2    Marzloff, K.3    Barbour, R.4    Schenk, D.5
  • 20
    • 0024005801 scopus 로고
    • Alzheimer disease amyloidogenic glycoprotein: Expression pattern in rat brain suggests a role in cell contact
    • Shivers, B. D., Hilbich, C., Multhaup, G., Salbaum, M., Beyreuther, K., and Seeburg, P. H. (1988) Alzheimer disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact. EMBO J. 7, 1365-1370
    • (1988) EMBO J. , vol.7 , pp. 1365-1370
    • Shivers, B.D.1    Hilbich, C.2    Multhaup, G.3    Salbaum, M.4    Beyreuther, K.5    Seeburg, P.H.6
  • 21
    • 65249143369 scopus 로고    scopus 로고
    • Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2
    • Kaden, D., Voigt, P., Munter, L. M., Bobowski, K. D., Schaefer, M., and Multhaup, G. (2009) Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2. J. Cell Sci. 122, 368-377
    • (2009) J. Cell Sci. , vol.122 , pp. 368-377
    • Kaden, D.1    Voigt, P.2    Munter, L.M.3    Bobowski, K.D.4    Schaefer, M.5    Multhaup, G.6
  • 22
    • 0026671821 scopus 로고
    • β-amyloid precursor protein localization in the Golgi apparatus in neurons and oligodendrocytes. An immunocytochemical structural and ultrastructural study in normal and axotomized neurons
    • Palacios, G., Palacios, J. M., Mengod, G., and Frey, P. (1992) β-amyloid precursor protein localization in the Golgi apparatus in neurons and oligodendrocytes. An immunocytochemical structural and ultrastructural study in normal and axotomized neurons. Brain Res. Mol. Brain Res. 15, 195-206
    • (1992) Brain Res. Mol. Brain Res. , vol.15 , pp. 195-206
    • Palacios, G.1    Palacios, J.M.2    Mengod, G.3    Frey, P.4
  • 23
    • 0028351791 scopus 로고
    • Morphologic and biochemical analysis of the intracellular trafficking of the Alzheimer β/A4 amyloid precursor protein
    • Caporaso, G. L., Takei, K., Gandy, S. E., Matteoli, M., Mundigl, O., Greengard, P., and De Camilli, P. (1994) Morphologic and biochemical analysis of the intracellular trafficking of the Alzheimer β/A4 amyloid precursor protein. J. Neurosci. 14, 3122-3138
    • (1994) J. Neurosci. , vol.14 , pp. 3122-3138
    • Caporaso, G.L.1    Takei, K.2    Gandy, S.E.3    Matteoli, M.4    Mundigl, O.5    Greengard, P.6    De Camilli, P.7
  • 24
    • 0024815331 scopus 로고
    • The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer's disease subjects
    • DOI 10.1016/0014-4886(89)90156-8
    • Benowitz, L. I., Rodriguez, W., Paskevich, P., Mufson, E. J., Schenk, D., and Neve, R. L. (1989) The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects. Exp. Neurol. 106, 237-250 (Pubitemid 20011225)
    • (1989) Experimental Neurology , vol.106 , Issue.3 , pp. 237-250
    • Benowitz, L.I.1    Rodriguez, W.2    Paskevich, P.3    Mufson, E.J.4    Schenk, D.5    Neve, R.L.6
  • 25
    • 0032475957 scopus 로고    scopus 로고
    • The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Aβ40 and Aβ42 secretion
    • DOI 10.1074/jbc.273.40.25552
    • Yang, Y., Turner, R. S., and Gaut, J. R. (1998) The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Aβ40 and Aβ42 secretion. J. Biol. Chem. 273, 25552-25555 (Pubitemid 28475772)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.40 , pp. 25552-25555
    • Yang, Y.1    Turner, R.S.2    Gaut, J.R.3
  • 27
    • 78449247854 scopus 로고    scopus 로고
    • Identification of NEEP21 as a β-amyloid precursor protein-interacting protein in vivo that modulates amyloidogenic processing in vitro
    • Norstrom, E. M., Zhang, C., Tanzi, R., and Sisodia, S. S. (2010) Identification of NEEP21 as a β-amyloid precursor protein-interacting protein in vivo that modulates amyloidogenic processing in vitro. J. Neurosci. 30, 15677-15685
    • (2010) J. Neurosci. , vol.30 , pp. 15677-15685
    • Norstrom, E.M.1    Zhang, C.2    Tanzi, R.3    Sisodia, S.S.4
  • 28
    • 4444337390 scopus 로고    scopus 로고
    • Expression of amyloid precursor protein-like molecule in astroglial cells of the subventricular zone and rostral migratory stream of the adult rat forebrain
    • DOI 10.1111/j.0021-8782.2004.00320.x
    • Yasuoka, K., Hirata, K., Kuraoka, A., He, J. W., and Kawabuchi, M. (2004) Expression of amyloid precursor protein-like molecule in astroglial cells of the subventricular zone and rostral migratory stream of the adult rat fore-brain. J. Anat. 205, 135-146 (Pubitemid 39199126)
    • (2004) Journal of Anatomy , vol.205 , Issue.2 , pp. 135-146
    • Yasuoka, K.1    Hirata, K.2    Kuraoka, A.3    He, J.-W.4    Kawabuchi, M.5
  • 29
    • 0026452028 scopus 로고
    • Expression of amyloid precursor protein mRNAs in endothelial, neuronal, and glial cells: Modulation by interleukin-1
    • Forloni, G., Demicheli, F., Giorgi, S., Bendotti, C., and Angeretti, N. (1992) Expression of amyloid precursor protein mRNAs in endothelial, neuronal, and glial cells: modulation by interleukin-1. Brain Res. Mol. Brain Res. 16, 128-134
    • (1992) Brain Res. Mol. Brain Res. , vol.16 , pp. 128-134
    • Forloni, G.1    Demicheli, F.2    Giorgi, S.3    Bendotti, C.4    Angeretti, N.5
  • 31
    • 0032857375 scopus 로고    scopus 로고
    • Intracellular and cell-surface distribution of amyloid precursor protein in cortical astrocytes
    • DOI 10.1016/S0361-9230(99)00084-2, PII S0361923099000842
    • Young, M. J., Lee, R. K., Jhaveri, S., and Wurtman, R. J. (1999) Intracellular and cell surface distribution of amyloid precursor protein in cortical astrocytes. Brain Res. Bull. 50, 27-32 (Pubitemid 29424224)
    • (1999) Brain Research Bulletin , vol.50 , Issue.1 , pp. 27-32
    • Young, M.J.1    Lee, R.K.K.2    Jhaveri, S.3    Wurtman, R.J.4
  • 32
    • 79952440163 scopus 로고    scopus 로고
    • P2 receptor stimulation induces amyloid precursor protein production and secretion in rat cortical astrocytes
    • Tran, M. D. (2011) P2 receptor stimulation induces amyloid precursor protein production and secretion in rat cortical astrocytes. Neurosci. Lett. 492, 155-159
    • (2011) Neurosci. Lett. , vol.492 , pp. 155-159
    • Tran, M.D.1
  • 33
    • 0024723475 scopus 로고
    • Expression of β-amyloid precursor protein in reactive astrocytes following neuronal damage
    • Siman, R., Card, J. P., Nelson, R. B., and Davis, L. G. (1989) Expression of β-amyloid precursor protein in reactive astrocytes following neuronal damage. Neuron 3, 275-285
    • (1989) Neuron , vol.3 , pp. 275-285
    • Siman, R.1    Card, J.P.2    Nelson, R.B.3    Davis, L.G.4
  • 34
    • 0028986501 scopus 로고
    • Increased β-amyloid precursor protein expression in astrocytes in the gerbil hippocampus following ischemia: Association with proliferation of astrocytes
    • Palacios, G., Mengod, G., Tortosa, A., Ferrer, I., and Palacios, J. M. (1995) Increased β-amyloid precursor protein expression in astrocytes in the gerbil hippocampus following ischemia: association with proliferation of astrocytes. Eur. J. Neurosci. 7, 501-510
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 501-510
    • Palacios, G.1    Mengod, G.2    Tortosa, A.3    Ferrer, I.4    Palacios, J.M.5
  • 35
    • 0035959993 scopus 로고    scopus 로고
    • Altered expression of apolipoprotein E, amyloid precursor protein and presenilin-1 is associated with chronic reactive gliosis in rat cortical tissue
    • DOI 10.1016/S0306-4522(01)00289-5, PII S0306452201002895
    • Martins, R. N., Taddei, K., Kendall, C., Evin, G., Bates, K. A., and Harvey, A. R. (2001) Altered expression of apolipoprotein E, amyloid precursor protein, and presenilin-1 is associated with chronic reactive gliosis in rat cortical tissue. Neuroscience 106, 557-569 (Pubitemid 32925244)
    • (2001) Neuroscience , vol.106 , Issue.3 , pp. 557-569
    • Martins, R.N.1    Taddei, K.2    Kendall, C.3    Evin, G.4    Bates, K.A.5    Harvey, A.R.6
  • 36
    • 0035070084 scopus 로고    scopus 로고
    • Expression and distribution of beta amyloid precursor protein and beta amyloid peptide in reactive astrocytes after transient middle cerebral artery occlusion
    • DOI 10.1007/s007010170109
    • Nihashi, T., Inao, S., Kajita, Y., Kawai, T., Sugimoto, T., Niwa, M., Kabeya, R., Hata, N., Hayashi, S., and Yoshida, J. (2001) Expression and distribution of β-amyloid precursor protein and β-amyloid peptide in reactive astrocytes after transient middle cerebral artery occlusion. Acta Neurochir. (Wien.) 143, 287-295 (Pubitemid 32268603)
    • (2001) Acta Neurochirurgica , vol.143 , Issue.3 , pp. 287-295
    • Nihashi, T.1    Inao, S.2    Kajita, Y.3    Kawai, T.4    Sugimoto, T.5    Niwa, M.6    Kabeya, R.7    Hata, N.8    Hayashi, S.9    Yoshida, J.10
  • 37
    • 79955855980 scopus 로고    scopus 로고
    • Glial amyloid precursor protein expression is restricted to astrocytes in an experimental toxic model of multiple sclerosis
    • Clarner, T., Buschmann, J. P., Beyer, C., and Kipp, M. (2011) Glial amyloid precursor protein expression is restricted to astrocytes in an experimental toxic model of multiple sclerosis. J. Mol. Neurosci. 43, 268-274
    • (2011) J. Mol. Neurosci. , vol.43 , pp. 268-274
    • Clarner, T.1    Buschmann, J.P.2    Beyer, C.3    Kipp, M.4
  • 38
    • 0027393439 scopus 로고
    • Increased levels of the Kunitz protease inhibitor-containing β-APP mRNAs in rat brain following neurotoxic damage
    • Solà, C., García-Ladona, F. J., Mengod, G., Probst, A., Frey, P., and Palacios, J. M. (1993) Increased levels of the Kunitz protease inhibitor-containing β-APP mRNAs in rat brain following neurotoxic damage. Brain Res. Mol. Brain Res. 17, 41-52
    • (1993) Brain Res. Mol. Brain Res. , vol.17 , pp. 41-52
    • Solà, C.1    García-Ladona, F.J.2    Mengod, G.3    Probst, A.4    Frey, P.5    Palacios, J.M.6
  • 39
    • 0032525329 scopus 로고    scopus 로고
    • βA amyloid peptide (25-35) induced APP expression in cultured astrocytes
    • DOI 10.1002/(SICI)1097-4547(19980615)52:6<661::AID-JNR5>3.0.CO;2-6
    • Moreno-Flores, M. T., Salinero, O., and Wandosell, F. (1998) βA amyloid peptide (25-35) induced APP expression in cultured astrocytes. J. Neurosci. Res. 52, 661-671 (Pubitemid 28300046)
    • (1998) Journal of Neuroscience Research , vol.52 , Issue.6 , pp. 661-671
    • Moreno-Flores, M.T.1    Salinero, O.2    Wandosell, F.3
  • 40
  • 41
    • 27144492610 scopus 로고    scopus 로고
    • Traumatic brain injury: Cause or risk of Alzheimer's disease? A review of experimental studies
    • DOI 10.1007/s00702-005-0326-0
    • Szczygielski, J., Mautes, A., Steudel, W. I., Falkai, P., Bayer, T. A., and Wirths, O. (2005) Traumatic brain injury: cause or risk of Alzheimer disease? A review of experimental studies. J. Neural. Transm. 112, 1547-1564 (Pubitemid 41504269)
    • (2005) Journal of Neural Transmission , vol.112 , Issue.11 , pp. 1547-1564
    • Szczygielski, J.1    Mautes, A.2    Steudel, W.I.3    Falkai, P.4    Bayer, T.A.5    Wirths, O.6
  • 42
    • 79959941349 scopus 로고    scopus 로고
    • Controlled cortical impact traumatic brain injury in 3xTg-AD mice causes acute intra-axonal amyloid-β accumulation and independently accelerates the development of Tau abnormalities
    • Tran, H. T., LaFerla, F. M., Holtzman, D. M., and Brody, D. L. (2011) Controlled cortical impact traumatic brain injury in 3xTg-AD mice causes acute intra-axonal amyloid-β accumulation and independently accelerates the development of Tau abnormalities. J. Neurosci. 31, 9513-9525
    • (2011) J. Neurosci. , vol.31 , pp. 9513-9525
    • Tran, H.T.1    LaFerla, F.M.2    Holtzman, D.M.3    Brody, D.L.4
  • 44
    • 0025312290 scopus 로고
    • Amyloid β-protein precursor accumulates in dystrophic neurites of senile plaques in Alzheimer-type dementia
    • DOI 10.1016/0006-8993(90)91187-L
    • Shoji, M., Hirai, S., Yamaguchi, H., Harigaya, Y., and Kawarabayashi, T. (1990) Amyloid β-protein precursor accumulates in dystrophic neurites of senile plaques in Alzheimer-type dementia. Brain Res. 512, 164-168 (Pubitemid 20103842)
    • (1990) Brain Research , vol.512 , Issue.1 , pp. 164-168
    • Shoji, M.1    Hirai, S.2    Yamaguchi, H.3    Harigaya, Y.4    Kwarabayashi, T.5
  • 46
    • 0026718402 scopus 로고
    • Aggregation of the amyloid precursor protein within degenerating neurons and dystrophic neurites in Alzheimer disease
    • Cummings, B. J., Su, J. H., Geddes, J. W., Van Nostrand, W. E., Wagner, S. L., Cunningham, D. D., and Cotman, C. W. (1992) Aggregation of the amyloid precursor protein within degenerating neurons and dystrophic neurites in Alzheimer disease. Neuroscience 48, 763-777
    • (1992) Neuroscience , vol.48 , pp. 763-777
    • Cummings, B.J.1    Su, J.H.2    Geddes, J.W.3    Van Nostrand, W.E.4    Wagner, S.L.5    Cunningham, D.D.6    Cotman, C.W.7
  • 47
    • 79951537603 scopus 로고    scopus 로고
    • Beyond the endoplasmic reticulum: Atypical GRP78 in cell viability, signaling and therapeutic targeting
    • Ni, M., Zhang, Y., and Lee, A. S. (2011) Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signaling and therapeutic targeting. Biochem. J. 434, 181-188
    • (2011) Biochem. J. , vol.434 , pp. 181-188
    • Ni, M.1    Zhang, Y.2    Lee, A.S.3
  • 48
    • 33947271016 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperones inhibit the production of amyloid-β peptides
    • DOI 10.1042/BJ20061318
    • Hoshino, T., Nakaya, T., Araki, W., Suzuki, K., Suzuki, T., and Mizushima, T. (2007) Endoplasmic reticulum chaperones inhibit the production of amyloid-β-peptides. Biochem. J. 402, 581-589 (Pubitemid 46423895)
    • (2007) Biochemical Journal , vol.402 , Issue.3 , pp. 581-589
    • Hoshino, T.1    Nakaya, T.2    Araki, W.3    Suzuki, K.4    Suzuki, T.5    Mizushima, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.