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Volumn 258, Issue 1, 2000, Pages 162-170

Immunocytochemical and biochemical characterization of FMRP, FXR1P, and FXR2P in the mouse

Author keywords

Fmrp; Fragile X syndrome; Fxr1p; Fxr2p; Localization; Mouse tissues

Indexed keywords

FRAGILE X MENTAL RETARDATION PROTEIN; PROTEIN FXR1; PROTEIN FXR2; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 0342757873     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2000.4932     Document Type: Article
Times cited : (151)

References (40)
  • 1
    • 0026721759 scopus 로고
    • Three families with high expression of a fragile site at Xq27.3, lack of anomalies at the FMR-1 CpG island, and no clear phenotypic association
    • Oberlé I., Boue J., Croquette M. F., Voelckel M. A., Mattei M. G., Mandel J. L. Three families with high expression of a fragile site at Xq27.3, lack of anomalies at the FMR-1 CpG island, and no clear phenotypic association. Am. J. Med. Genet. 43:1992;224-231.
    • (1992) Am. J. Med. Genet. , vol.43 , pp. 224-231
    • Oberlé, I.1    Boue, J.2    Croquette, M.F.3    Voelckel, M.A.4    Mattei, M.G.5    Mandel, J.L.6
  • 7
    • 0027176361 scopus 로고
    • The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation
    • Devys D., Lutz Y., Rouyer N., Bellocq J. P., Mandel J. L. The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation. Nature Genet. 4:1993;335-340.
    • (1993) Nature Genet. , vol.4 , pp. 335-340
    • Devys, D.1    Lutz, Y.2    Rouyer, N.3    Bellocq, J.P.4    Mandel, J.L.5
  • 8
    • 0001966753 scopus 로고    scopus 로고
    • Physical and behavioral phenotype
    • R. J. Hagerman, & A. C. Silverman. Baltimore: The John Hopkins University Press
    • Hagerman R. J. Physical and behavioral phenotype. Hagerman R. J., Silverman A. C. Fragile X Syndrome: Diagnosis, Treatment and Research. 1996;3-87 The John Hopkins University Press, Baltimore.
    • (1996) Fragile X Syndrome: Diagnosis, Treatment and Research , pp. 3-87
    • Hagerman, R.J.1
  • 14
    • 0027715424 scopus 로고
    • Enhanced expression of the murine FMR1 gene during germ cell proliferation suggests a special function in both the male and the female gonad
    • Bächner D., Manca A., Steinbach P., Wöhrle D., Just W., Vogel W., Hameister H., Poustka A. Enhanced expression of the murine FMR1 gene during germ cell proliferation suggests a special function in both the male and the female gonad. Hum. Mol. Genet. 2:1993;2043-2050.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 2043-2050
    • Bächner, D.1    Manca, A.2    Steinbach, P.3    Wöhrle, D.4    Just, W.5    Vogel, W.6    Hameister, H.7    Poustka, A.8
  • 16
    • 0027300283 scopus 로고
    • Nucleus basalis magnocellularis and hippocampus are the major sites of FMR-1 expression in the human fetal brain
    • Abitbol M., Menini C., Delezoide A. L., Rhyner T., Vekemans M., Mallet J. Nucleus basalis magnocellularis and hippocampus are the major sites of FMR-1 expression in the human fetal brain. Nature Genet. 4:1993;147-153.
    • (1993) Nature Genet. , vol.4 , pp. 147-153
    • Abitbol, M.1    Menini, C.2    Delezoide, A.L.3    Rhyner, T.4    Vekemans, M.5    Mallet, J.6
  • 22
    • 0031046778 scopus 로고    scopus 로고
    • Fragile X mental retardation protein: Nucleocytoplasmic shuttling and association with somatodendritic ribosomes
    • Feng Y., Gutekunst C. A., Eberhart D. E., Yi H., Warren S. T., Hersch S. M. Fragile X mental retardation protein: Nucleocytoplasmic shuttling and association with somatodendritic ribosomes. J. Neurosci. 17:1997;1539-1547.
    • (1997) J. Neurosci. , vol.17 , pp. 1539-1547
    • Feng, Y.1    Gutekunst, C.A.2    Eberhart, D.E.3    Yi, H.4    Warren, S.T.5    Hersch, S.M.6
  • 25
    • 0028971722 scopus 로고
    • The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2
    • Zhang Y., Oconnor J. P., Siomi M. C., Srinivasan S., Dutra A., Nussbaum R. L., Dreyfuss G. The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2. EMBO J. 14:1995;5358-5366.
    • (1995) EMBO J. , vol.14 , pp. 5358-5366
    • Zhang, Y.1    Oconnor, J.P.2    Siomi, M.C.3    Srinivasan, S.4    Dutra, A.5    Nussbaum, R.L.6    Dreyfuss, G.7
  • 26
    • 0029816723 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is a ribosonucleoprotein containing both nuclear localization and nuclear export signals
    • Eberhart D. E., Malter H. E., Feng Y., Warren S. T. The fragile X mental retardation protein is a ribosonucleoprotein containing both nuclear localization and nuclear export signals. Hum. Mol. Genet. 5:1996;1083-1091.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1083-1091
    • Eberhart, D.E.1    Malter, H.E.2    Feng, Y.3    Warren, S.T.4
  • 27
    • 0030760613 scopus 로고    scopus 로고
    • The fragile X mental retardation protein is associated with poly(A)(+) mRNA in actively translating polyribosomes
    • Corbin F., Bouillon M., Fortin A., Morin S., Rousseau F., Khandjian E. W. The fragile X mental retardation protein is associated with poly(A)(+) mRNA in actively translating polyribosomes. Hum. Mol. Genet. 6:1997;1465-1472.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1465-1472
    • Corbin, F.1    Bouillon, M.2    Fortin, A.3    Morin, S.4    Rousseau, F.5    Khandjian, E.W.6
  • 28
    • 0033231022 scopus 로고    scopus 로고
    • Oligomerization properties of fragile-X mental-retardation protein (FMRP) and the fragile-X-related proteins FXR1P and FXR2P
    • Tamanini F., Van Unen L., Bakker C., Sacchi N., Galjaard H., Oostra B. A., Hoogeveen A. T. Oligomerization properties of fragile-X mental-retardation protein (FMRP) and the fragile-X-related proteins FXR1P and FXR2P. Biochem. J. 343:1999;517-523.
    • (1999) Biochem. J. , vol.343 , pp. 517-523
    • Tamanini, F.1    Van Unen, L.2    Bakker, C.3    Sacchi, N.4    Galjaard, H.5    Oostra, B.A.6    Hoogeveen, A.T.7
  • 29
  • 30
    • 0031310667 scopus 로고    scopus 로고
    • FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association
    • Feng Y., Absher D., Eberhart D. E., Brown V., Malter H. E., Warren S. T. FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association. Mol. Cell. 1:1997;109-118.
    • (1997) Mol. Cell , vol.1 , pp. 109-118
    • Feng, Y.1    Absher, D.2    Eberhart, D.E.3    Brown, V.4    Malter, H.E.5    Warren, S.T.6
  • 31
    • 0033499661 scopus 로고    scopus 로고
    • Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X-related proteins as components of the complex
    • Ceman S., Brown V., Warren S. T. Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X-related proteins as components of the complex. Mol. Cell. Biol. 19:1999;7925-7932.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7925-7932
    • Ceman, S.1    Brown, V.2    Warren, S.T.3
  • 34
    • 0032758839 scopus 로고    scopus 로고
    • A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein
    • Bardoni B., Schenck A., Mandel J. L. A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein. Hum. Mol. Genet. 8:1999;2557-2566.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2557-2566
    • Bardoni, B.1    Schenck, A.2    Mandel, J.L.3
  • 36
    • 0032562608 scopus 로고    scopus 로고
    • Structure and function in the nucleus
    • Lamond A. I., Earnshaw W. C. Structure and function in the nucleus. Science. 280:1998;547-553.
    • (1998) Science , vol.280 , pp. 547-553
    • Lamond, A.I.1    Earnshaw, W.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.