메뉴 건너뛰기




Volumn 19, Issue 3, 1999, Pages 255-265

Presenilins: Structural aspects and posttranslational events

Author keywords

Alzheimer's disease; Apoptosis; A peptide; Caspases; Development; Embryogenesis; Maturation; Mutations; Presenilins; APP processing

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BETA CATENIN; CALCIUM BINDING PROTEIN; CASEIN KINASE I; CASEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; PRESENILIN 1; PRESENILIN 2; PROTEIN KINASE C;

EID: 0032872131     PISSN: 08937648     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02821716     Document Type: Article
Times cited : (20)

References (90)
  • 1
    • 0025824636 scopus 로고
    • Molecular genetics of Alzheimer disease amyloid
    • 1. Tanzi R. E., St. George-Hyslop P., and Gusella J. F. (1991) Molecular genetics of Alzheimer disease amyloid. J. Biol. Chem. 266, 20579-20582.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20579-20582
    • Tanzi, R.E.1    St. George-Hyslop, P.2    Gusella, J.F.3
  • 3
    • 0027422751 scopus 로고
    • Genetic and molecular advances in Alzheimer's disease
    • 3. Mullan M and Crawford F. (1993) Genetic and molecular advances in Alzheimer's disease. Trends Neurosci. 16, 398-403.
    • (1993) Trends Neurosci. , vol.16 , pp. 398-403
    • Mullan, M.1    Crawford, F.2
  • 4
    • 0029073383 scopus 로고
    • Genetic dissection of Alzheimer disease, a heterogeneous disorder
    • 4. Schellenberg G. D. (1995) Genetic dissection of Alzheimer disease, a heterogeneous disorder. Proc. Natl. Acad. Sci. USA 92, 8552-8559.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8552-8559
    • Schellenberg, G.D.1
  • 7
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • 7. Goldgaber D., Lerman M. I., McBride O. W., Saffiotti U., and Gajdusek D. C. (1987) Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 235, 887-880.
    • (1987) Science , vol.235 , pp. 887-1880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 11
    • 0029115555 scopus 로고    scopus 로고
    • The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset A. D. families
    • 11. Alzheimer's Disease Collaborative Group (1996) The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset A. D. families. Nature Genet. 11, 219-222.
    • (1996) Nature Genet. , vol.11 , pp. 219-222
  • 12
    • 0030816386 scopus 로고    scopus 로고
    • Transcriptional regulation of the mouse presenilin-1 gene
    • 12. Mitsuda N., Roses A. D., and Vitek M. P. (1997) Transcriptional regulation of the mouse presenilin-1 gene. J. Biol. Chem. 272, 23,489-23,497.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23489-23497
    • Mitsuda, N.1    Roses, A.D.2    Vitek, M.P.3
  • 13
    • 0030246887 scopus 로고    scopus 로고
    • Presenilin 1 mRNA expression in hippocampi of sporadic Alzheimer's disease patients
    • 13. Nishiyama K., Murayama S., Suzuki T., Mitsui Y., Sakaki Y., and Kanazawa I. (1996) Presenilin 1 mRNA expression in hippocampi of sporadic Alzheimer's disease patients. Neurosci. Res. 26, 75-78.
    • (1996) Neurosci. Res. , vol.26 , pp. 75-78
    • Nishiyama, K.1    Murayama, S.2    Suzuki, T.3    Mitsui, Y.4    Sakaki, Y.5    Kanazawa, I.6
  • 14
    • 0032973915 scopus 로고    scopus 로고
    • Regional distribution of presenilin-1 messenger RNA in the embryonic rat brain: Comparison with β-amyloid precursor protein messenger RNA localization
    • 14. Tanimukai H., Sato K., Kudo T., Kashiwagi Y., Tohyama M., and Takeda M. (1999) Regional distribution of presenilin-1 messenger RNA in the embryonic rat brain: comparison with β-amyloid precursor protein messenger RNA localization. Neuroscience 90, 27-39.
    • (1999) Neuroscience , vol.90 , pp. 27-39
    • Tanimukai, H.1    Sato, K.2    Kudo, T.3    Kashiwagi, Y.4    Tohyama, M.5    Takeda, M.6
  • 15
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • 15. Hardy J. (1997) Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20, 154-159.
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 19
    • 0029984784 scopus 로고    scopus 로고
    • Genomic structure and expression of STM2, the chromosome 1 familial Alzheimer disease gene
    • 19. Levy-Lahad E., Poorkaj P., Wang K., Fu Y. H., Oshima J., Mulligan J., and Schellenberg G. D. (1996) Genomic structure and expression of STM2, the chromosome 1 familial Alzheimer disease gene. Genomics 34, 198-204.
    • (1996) Genomics , vol.34 , pp. 198-204
    • Levy-Lahad, E.1    Poorkaj, P.2    Wang, K.3    Fu, Y.H.4    Oshima, J.5    Mulligan, J.6    Schellenberg, G.D.7
  • 24
    • 0030922146 scopus 로고    scopus 로고
    • Evidence for a six-transmembrane domain structure of presenilin 1
    • 24. Lehmann S., Chiesa R., and Harris D. A. (1997) Evidence for a six-transmembrane domain structure of presenilin 1. J. Biol. Chem. 272, 12,047-12,051.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12047-12051
    • Lehmann, S.1    Chiesa, R.2    Harris, D.A.3
  • 25
    • 0030293894 scopus 로고    scopus 로고
    • Membrane topology of the C-elegans SEL-12 presenilin
    • 25. Li X. and Greenwald I. (1996) Membrane topology of the C-elegans SEL-12 presenilin. J. Biol. Chem. 17, 1015-1021.
    • (1996) J. Biol. Chem. , vol.17 , pp. 1015-1021
    • Li, X.1    Greenwald, I.2
  • 27
    • 0031442678 scopus 로고    scopus 로고
    • The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells
    • 27. Dewji N. N. and Singer S. J. (1997) The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells. Proc. Natl. Acad. Sci. USA 94, 14,025-14,030.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14025-14030
    • Dewji, N.N.1    Singer, S.J.2
  • 31
    • 0030984042 scopus 로고    scopus 로고
    • Neuronal expresion and intracellular localization of presenilins in normal and Alzheimer's disease
    • 31. Huynh D. P., Vinters H. V., Ho D. H. D., Ho V. V., and Pulst S-M. (1997) Neuronal expresion and intracellular localization of presenilins in normal and Alzheimer's disease. J. Neuropathol. Exp. Neurol. 56, 1009-1017.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 1009-1017
    • Huynh, D.P.1    Vinters, H.V.2    Ho, D.H.D.3    Ho, V.V.4    Pulst, S.-M.5
  • 34
    • 0030657665 scopus 로고    scopus 로고
    • Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation
    • 34. Capell A., Saffrich R., Olivo J-C., Meyn L., Walter J., Grünberg J., Mathews P., Nixon R., Dotti C., and Haass C. (1997) Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation. J. Neurochem. 69, 2432-2440.
    • (1997) J. Neurochem. , vol.69 , pp. 2432-2440
    • Capell, A.1    Saffrich, R.2    Olivo, J.-C.3    Meyn, L.4    Walter, J.5    Grünberg, J.6    Mathews, P.7    Nixon, R.8    Dotti, C.9    Haass, C.10
  • 35
    • 0031006343 scopus 로고    scopus 로고
    • Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease
    • 35. Busciglio J., Hartmann H., Lorenzo A., Wong C., Baumann K., Sommer B., Staufenbiel M., and Yankner B. A. (1997) Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease. J. Neurosci. 17, 5101-5107.
    • (1997) J. Neurosci. , vol.17 , pp. 5101-5107
    • Busciglio, J.1    Hartmann, H.2    Lorenzo, A.3    Wong, C.4    Baumann, K.5    Sommer, B.6    Staufenbiel, M.7    Yankner, B.A.8
  • 37
    • 0030746669 scopus 로고    scopus 로고
    • Immunohistochemical analysis of presenilin 2 expression in the mouse brain: Distribution pattern and co-localization with presenilin 1 protein
    • 37. Blanchard V., Czech C., Bonici B., Clavel N., Gohin M., Dalet K., Revah F., Pradier L., Imperato A., and Moussaoui S. (1997) Immunohistochemical analysis of presenilin 2 expression in the mouse brain: distribution pattern and co-localization with presenilin 1 protein. Brain Res. 758, 209-217.
    • (1997) Brain Res. , vol.758 , pp. 209-217
    • Blanchard, V.1    Czech, C.2    Bonici, B.3    Clavel, N.4    Gohin, M.5    Dalet, K.6    Revah, F.7    Pradier, L.8    Imperato, A.9    Moussaoui, S.10
  • 40
    • 0030924177 scopus 로고    scopus 로고
    • Cell surface expression of the Alzheimer disease-related presenilin proteins
    • 40. Dewji N. N. and Singer S. J. (1997) Cell surface expression of the Alzheimer disease-related presenilin proteins. Proc. Natl. Acad. Sci. USA 94, 9926-9931.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9926-9931
    • Dewji, N.N.1    Singer, S.J.2
  • 41
    • 0032411251 scopus 로고    scopus 로고
    • Specific intercellular binding of the Ξ-amyloid precursor protein to the presenilins induces intercellular signalling: Its significance for Alzheimer's disease
    • 41. Dewji N. N. and Singer S. J. (1998) Specific intercellular binding of the Ξ-amyloid precursor protein to the presenilins induces intercellular signalling: its significance for Alzheimer's disease. Proc. Natl. Acad. Sci. USA 93, 15,055-15,060.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15055-15060
    • Dewji, N.N.1    Singer, S.J.2
  • 42
    • 0030761059 scopus 로고    scopus 로고
    • Alzheimer presenilins in the nuclear membrane, interphase kinetochores, and centrosomes suggest a role in chromosome seggregation
    • 42. Li J., Xu M., Zhou H., and Ma J., Potter H. (1997) Alzheimer presenilins in the nuclear membrane, interphase kinetochores, and centrosomes suggest a role in chromosome seggregation. Cell 90, 917-927.
    • (1997) Cell , vol.90 , pp. 917-927
    • Li, J.1    Xu, M.2    Zhou, H.3    Ma, J.4    Potter, H.5
  • 43
    • 0033573936 scopus 로고    scopus 로고
    • Phosphorylation of presenilin-2 regulates its cleavage by caspases and retards progression of apoptosis
    • 43. Walter J., Schindzielorz A., Grünberg J., and Haass C. (1999) Phosphorylation of presenilin-2 regulates its cleavage by caspases and retards progression of apoptosis. Proc. Natl. Acad. Sci. USA 96, 1391-1396.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1391-1396
    • Walter, J.1    Schindzielorz, A.2    Grünberg, J.3    Haass, C.4
  • 46
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells
    • 46. Kim T. W., Pettingell W. H., Hallmark O. G., Moir R. D., Wasco W., and Tanzi R. E. (1997) Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells. J. Biol. Chem. 272, 11,006-11,010.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11006-11010
    • Kim, T.W.1    Pettingell, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 48
    • 0031587396 scopus 로고    scopus 로고
    • Determination of a cleavage site of presenilin 2 protein in stably transfected SH-SY5Y human neuroblastoma cell lines
    • 48. Shirotani K., Takahashi K., Ozawa K., Kunishita T., and Tabira T. (1997) Determination of a cleavage site of presenilin 2 protein in stably transfected SH-SY5Y human neuroblastoma cell lines. Biochem. Biophys. Res. Commun. 240, 728-731.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 728-731
    • Shirotani, K.1    Takahashi, K.2    Ozawa, K.3    Kunishita, T.4    Tabira, T.5
  • 49
    • 0032488995 scopus 로고    scopus 로고
    • The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass
    • 49. Capell A., Grünberg J., Pesold B., Diehlmann A., Citron M., Nixon R., Beyreuther K., Selkoe D. J., and Haass C. (1998) The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass. J. Biol. Chem. 273, 3205-3211.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3205-3211
    • Capell, A.1    Grünberg, J.2    Pesold, B.3    Diehlmann, A.4    Citron, M.5    Nixon, R.6    Beyreuther, K.7    Selkoe, D.J.8    Haass, C.9
  • 54
    • 0030575338 scopus 로고    scopus 로고
    • Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: Evidence that Alzheimer mutations affect proteolytic processing
    • 54. Mercken M., Takahashi H., Honda T., Sato K., Murayama M., Nakazato Y., Noguchi K., Imahori K., and Takashima A. (1996) Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: evidence that Alzheimer mutations affect proteolytic processing. FEBS Lett. 389, 297-303.
    • (1996) FEBS Lett. , vol.389 , pp. 297-303
    • Mercken, M.1    Takahashi, H.2    Honda, T.3    Sato, K.4    Murayama, M.5    Nakazato, Y.6    Noguchi, K.7    Imahori, K.8    Takashima, A.9
  • 59
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • 59. Kim T-W., Pettingell W. H., Jung Y-K., Kovacs D. M., and Tanzi R. E. (1997) Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science 277, 373-376.
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.-W.1    Pettingell, W.H.2    Jung, Y.-K.3    Kovacs, D.M.4    Tanzi, R.E.5
  • 60
    • 0038785079 scopus 로고    scopus 로고
    • Alzheimer's disease associated presenilin-1 holoprotein and its 18-20 kDa C-terminal fragment are death substrates for proteases of the caspase family
    • 60. Grünberg J., Walter J., Loetscher H., Deuschle U., Jacobsen H., and Haass C. (1998) Alzheimer's disease associated presenilin-1 holoprotein and its 18-20 kDa C-terminal fragment are death substrates for proteases of the caspase family. Biochemistry 37, 2263-2270.
    • (1998) Biochemistry , vol.37 , pp. 2263-2270
    • Grünberg, J.1    Walter, J.2    Loetscher, H.3    Deuschle, U.4    Jacobsen, H.5    Haass, C.6
  • 62
    • 0031473796 scopus 로고    scopus 로고
    • On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues
    • 62. Dewji N. N., Do C., and Singer S. J. (1997) On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues. Proc. Natl. Acad. Sci. USA 94, 14,031-14,036.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14031-14036
    • Dewji, N.N.1    Do, C.2    Singer, S.J.3
  • 63
    • 0031950118 scopus 로고    scopus 로고
    • Proteasome inhibitors prevent the degradation of familial Alzheimer's disease-linked presenilin 1 and trigger increased Aβ42 secretion by human cells
    • 63. Marambaud P., Ancolio K., Lopez-Perez E., and Checler F. (1998) Proteasome inhibitors prevent the degradation of familial Alzheimer's disease-linked presenilin 1 and trigger increased Aβ42 secretion by human cells. Mol. Med. 4, 146-156.
    • (1998) Mol. Med. , vol.4 , pp. 146-156
    • Marambaud, P.1    Ancolio, K.2    Lopez-Perez, E.3    Checler, F.4
  • 65
    • 0033610863 scopus 로고    scopus 로고
    • Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation
    • 65. Steiner H., Capell A., Pesold B., Citron M., Kloetzel P. M., Selkoe D. J., Romig H., Mendla K., and Haass C. (1998) Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J. Biol. Chem. 273, 32,322-32,331.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32322-32331
    • Steiner, H.1    Capell, A.2    Pesold, B.3    Citron, M.4    Kloetzel, P.M.5    Selkoe, D.J.6    Romig, H.7    Mendla, K.8    Haass, C.9
  • 67
    • 0032501149 scopus 로고    scopus 로고
    • Alzheimer's disease-linked mutation of presenilin 2 (N141I-PS2) drastically lowers APPα secretion: Control by the proteasome
    • 67. Marambaud P., Alves da Costa C., Ancolio K., and Checler F. (1998) Alzheimer's disease-linked mutation of presenilin 2 (N141I-PS2) drastically lowers APPα secretion: control by the proteasome. Biochem. Biophys. Res. Commun. 252, 134-138.
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 134-138
    • Marambaud, P.1    Alves Da Costa, C.2    Ancolio, K.3    Checler, F.4
  • 68
    • 0033054564 scopus 로고    scopus 로고
    • C-terminal maturation fragments of presenilin 1 and 2 control secretion of APPα and Aβ by human cells and are degraded by the proteasome
    • 68. Alves da Costa C., Ancolio K., and Checler F. (1999) C-terminal maturation fragments of presenilin 1 and 2 control secretion of APPα and Aβ by human cells and are degraded by the proteasome. Mol. Med. 5, 160-168.
    • (1999) Mol. Med. , vol.5 , pp. 160-168
    • Alves Da Costa, C.1    Ancolio, K.2    Checler, F.3
  • 69
    • 0029116848 scopus 로고
    • Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • 69. Levitan D. and Greenwald I. (1995) Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 377, 351-354.
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 73
    • 0033535555 scopus 로고    scopus 로고
    • Neurogenic phenotypes and altered Notch processing in drosophila presenilin mutants
    • 73. Ye Y., Lukinova N., and Fortini M. E. (1999) Neurogenic phenotypes and altered Notch processing in drosophila presenilin mutants. Nature 398, 525-529.
    • (1999) Nature , vol.398 , pp. 525-529
    • Ye, Y.1    Lukinova, N.2    Fortini, M.E.3
  • 74
    • 0033535508 scopus 로고    scopus 로고
    • Presenilin is required for activity and nuclear access of Notch in drosophila
    • 74. Struhl G. and Greenwald I. (1999) Presenilin is required for activity and nuclear access of Notch in drosophila. Nature 398, 522-525.
    • (1999) Nature , vol.398 , pp. 522-525
    • Struhl, G.1    Greenwald, I.2
  • 76
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • 76. Wolfe M. S., Xia W., Ostaszewski B. L., Diehl T. S., Kimberly W. T., and Selkoe D. J. (1999) Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 80
    • 0032545273 scopus 로고    scopus 로고
    • Abrogation of the presenilin 1/β-catenin interaction and preservation of the heterodimeric presenilin 1 complex following caspase activation
    • 80. Tesco G., Kim T-W., Dielhmann A., Beyreuther K., and Tanzi R. (1998) Abrogation of the presenilin 1/β-catenin interaction and preservation of the heterodimeric presenilin 1 complex following caspase activation. J. Biol. Chem. 273,33,909-33,914.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33909-33914
    • Tesco, G.1    Kim, T.-W.2    Dielhmann, A.3    Beyreuther, K.4    Tanzi, R.5
  • 83
    • 0030922421 scopus 로고    scopus 로고
    • Presenilins, genes for life and death
    • 83. Haass C. (1997) Presenilins, genes for life and death. Neurons 18,687-690.
    • (1997) Neurons , vol.18 , pp. 687-690
    • Haass, C.1
  • 84
    • 0030761094 scopus 로고    scopus 로고
    • The presenilins and Alzheimer's disease
    • 84. Hutton M. and Hardy J. (1997) The presenilins and Alzheimer's disease. Human Mol. Genet. 6, 1639-1646.
    • (1997) Human Mol. Genet. , vol.6 , pp. 1639-1646
    • Hutton, M.1    Hardy, J.2
  • 85
    • 0031982670 scopus 로고    scopus 로고
    • Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease
    • 85. Mattson M. P., Gue Q., Furukawa K., and Pedersen W. A. (1998) Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease. J. Neurochem. 70, 1-14.
    • (1998) J. Neurochem. , vol.70 , pp. 1-14
    • Mattson, M.P.1    Gue, Q.2    Furukawa, K.3    Pedersen, W.A.4
  • 86
    • 0032693331 scopus 로고    scopus 로고
    • Presenilins: Multifunctional proteins involved in Alzheimer's disease Pathology
    • in press
    • 86. Checler F. (1999) Presenilins: multifunctional proteins involved in Alzheimer's disease Pathology. LIFE, in press.
    • (1999) LIFE
    • Checler, F.1
  • 89
    • 0031721511 scopus 로고    scopus 로고
    • Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment
    • 89. Buxbaum J. D., Choi E-K., Luo Y., Lilliehook C., Crowley A. C., Merriam D. E., and Wasco W. (1998) Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment. Nature Med. 4, 1177-1181.
    • (1998) Nature Med. , vol.4 , pp. 1177-1181
    • Buxbaum, J.D.1    Choi, E.-K.2    Luo, Y.3    Lilliehook, C.4    Crowley, A.C.5    Merriam, D.E.6    Wasco, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.