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Volumn 65, Issue 3, 2000, Pages 243-252

Identification of a glialblastoma cell differentiation factor-related gene mRNA in human microvascular endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL FACTOR; CASEIN KINASE II; COMPLEMENTARY DNA; ERYTHROPOIETIN; MESSENGER RNA; SUCCINIMIDE DERIVATIVE;

EID: 0034193734     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.2000.6176     Document Type: Article
Times cited : (6)

References (38)
  • 1
    • 0028239247 scopus 로고
    • Identification of multiple genes in bovine retinal pericytes altered by exposure to elevated levels of glucose by using mRNA differential display
    • Aiello L. P., Robinson G. S., Lin Y. W., Nishio Y., King G. L. Identification of multiple genes in bovine retinal pericytes altered by exposure to elevated levels of glucose by using mRNA differential display. Proc. Natl. Acad. Sci. USA. 91:1994;6231-6235.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6231-6235
    • Aiello, L.P.1    Robinson, G.S.2    Lin, Y.W.3    Nishio, Y.4    King, G.L.5
  • 2
    • 0028292228 scopus 로고
    • Number and location of AUUUA motifs: Role in regulating transiently expressed RNAs
    • Akashi M., Shaw G., Hachiya M., Elstner E., Suzuki G., Koeffler P. Number and location of AUUUA motifs: Role in regulating transiently expressed RNAs. Blood. 83:1994;3182-3187.
    • (1994) Blood , vol.83 , pp. 3182-3187
    • Akashi, M.1    Shaw, G.2    Hachiya, M.3    Elstner, E.4    Suzuki, G.5    Koeffler, P.6
  • 5
    • 0025681492 scopus 로고
    • Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors
    • Anderson D., Koch C. A., Grey L., Ellis C., Moran M., Pawson T. Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors. Science. 250:1990;979-982.
    • (1990) Science , vol.250 , pp. 979-982
    • Anderson, D.1    Koch, C.A.2    Grey, L.3    Ellis, C.4    Moran, M.5    Pawson, T.6
  • 6
    • 0027141519 scopus 로고
    • Number of CpG islands and genes in human and mouse
    • Antequera F., Bird A. Number of CpG islands and genes in human and mouse. Proc. Natl. Acad. Sci. USA. 90:1993;403-410.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 403-410
    • Antequera, F.1    Bird, A.2
  • 7
    • 0026758412 scopus 로고
    • The erythropoietin receptor and the molecular basis of signal transduction
    • Barber D. L., D'Andrea A. D. The erythropoietin receptor and the molecular basis of signal transduction. Semin. Hematol. 29:1992;293-304.
    • (1992) Semin. Hematol. , vol.29 , pp. 293-304
    • Barber, D.L.1    D'Andrea, A.D.2
  • 8
    • 0025944568 scopus 로고
    • Isolation, characterization and sequencing of the chicken apolipoprotein-AI-encoding gene
    • Bhattacharyya N., Chattapadhyay R., Hirsch A., Banerjee D. Isolation, characterization and sequencing of the chicken apolipoprotein-AI-encoding gene. Gene. 104:1991;163-168.
    • (1991) Gene , vol.104 , pp. 163-168
    • Bhattacharyya, N.1    Chattapadhyay, R.2    Hirsch, A.3    Banerjee, D.4
  • 9
    • 0028901357 scopus 로고
    • Recombinant human erythropoietin stimulates angiogenesis in vitro
    • Carlini R. G., Reyes A. A., Rothstein M. Recombinant human erythropoietin stimulates angiogenesis in vitro. Kidney Int. 47:1995;740-745.
    • (1995) Kidney Int. , vol.47 , pp. 740-745
    • Carlini, R.G.1    Reyes, A.A.2    Rothstein, M.3
  • 11
    • 0023658309 scopus 로고
    • Identification of p34 and p13, human homologs of the cell cycle regulators of fission yeast encoded by cdc2+ and suc1+
    • Draetta G., Brizuela L., Potashkin J., Beach D. Identification of p34 and p13, human homologs of the cell cycle regulators of fission yeast encoded by cdc2+ and suc1+. Cell. 50:1987;319-325.
    • (1987) Cell , vol.50 , pp. 319-325
    • Draetta, G.1    Brizuela, L.2    Potashkin, J.3    Beach, D.4
  • 12
    • 0025022491 scopus 로고
    • Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I
    • Drubin D. G., Mulholland J., Zhu Z., Botstein D. Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I. Nature. 343:1990;288-290.
    • (1990) Nature , vol.343 , pp. 288-290
    • Drubin, D.G.1    Mulholland, J.2    Zhu, Z.3    Botstein, D.4
  • 13
    • 0026784103 scopus 로고
    • Erythropoietin induces the tyrosine phosphorylation of its own receptor in human erythropoietin-responsive cells
    • Dusanter-Fourt I., Casadevall N., Lacombe C., Muller O., Billat C., Fischer S., Mayeux P. Erythropoietin induces the tyrosine phosphorylation of its own receptor in human erythropoietin-responsive cells. J Biol. Chem. 267:1992;10670-10675.
    • (1992) J Biol. Chem. , vol.267 , pp. 10670-10675
    • Dusanter-Fourt, I.1    Casadevall, N.2    Lacombe, C.3    Muller, O.4    Billat, C.5    Fischer, S.6    Mayeux, P.7
  • 14
    • 0025277259 scopus 로고
    • Prenyl proteins in eukaryotic cells: A new type of membrane anchor
    • Glomset J. A., Gelb M. H., Farnsworth C. C. Prenyl proteins in eukaryotic cells: A new type of membrane anchor. Trends Biochem. Sci. 15:1990;139-142.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 139-142
    • Glomset, J.A.1    Gelb, M.H.2    Farnsworth, C.C.3
  • 15
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Gorlich D. Transport into and out of the nucleus. EMBO J. 17:1998;2721-2727.
    • (1998) EMBO J. , vol.17 , pp. 2721-2727
    • Gorlich, D.1
  • 17
    • 0028802362 scopus 로고
    • The regulation of protein transport in the nucleus by phosphorylation
    • Jans D. A. The regulation of protein transport in the nucleus by phosphorylation. Biochem. J. 311:1995;705-716.
    • (1995) Biochem. J. , vol.311 , pp. 705-716
    • Jans, D.A.1
  • 18
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak M. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266:1991;19867-19870.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19867-19870
    • Kozak, M.1
  • 19
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0026674886 scopus 로고
    • Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction
    • Liang P., Pardee A. B. Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction. Science. 257:1992;967-971.
    • (1992) Science , vol.257 , pp. 967-971
    • Liang, P.1    Pardee, A.B.2
  • 22
    • 0026638821 scopus 로고
    • Association of the erythropoietion receptor with protein tyrosine kinase activity
    • Linnekin D., Evans G. A., D'Andrea A., Farrar W. L. Association of the erythropoietion receptor with protein tyrosine kinase activity. Proc. Natl. Acad. Sci. USA. 89:1992;6237-6241.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6237-6241
    • Linnekin, D.1    Evans, G.A.2    D'Andrea, A.3    Farrar, W.L.4
  • 23
    • 0017370015 scopus 로고
    • Use of N chlorosuccinimide/urea for the selective cleavage of tryptophanyl peptide bonds in proteins. Cytochrome c
    • Lischwe M. A., Sung M. T. Use of N chlorosuccinimide/urea for the selective cleavage of tryptophanyl peptide bonds in proteins. Cytochrome c. J. Biol. Chem. 252:1977;4976-4980.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4976-4980
    • Lischwe, M.A.1    Sung, M.T.2
  • 24
    • 0027978538 scopus 로고
    • Protein kinase C and mammary cell differentiation: Involvement of protein kinase C alpha in the induction of beta-casein expression
    • Marte B. M., Meyer T., Stabel S., Standke G. J., Jaken S., Fabbro D., Hynes N. E. Protein kinase C and mammary cell differentiation: Involvement of protein kinase C alpha in the induction of beta-casein expression. Cell Growth Differ. 5:1994;239-247.
    • (1994) Cell Growth Differ. , vol.5 , pp. 239-247
    • Marte, B.M.1    Meyer, T.2    Stabel, S.3    Standke, G.J.4    Jaken, S.5    Fabbro, D.6    Hynes, N.E.7
  • 25
    • 0025298967 scopus 로고
    • Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins
    • Matsuda M., Mayer B. J., Fukui Y., Hanafusa H. Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Science. 248:1991;1537-1539.
    • (1991) Science , vol.248 , pp. 1537-1539
    • Matsuda, M.1    Mayer, B.J.2    Fukui, Y.3    Hanafusa, H.4
  • 26
    • 0029281993 scopus 로고
    • SH3 domains: Minding your p's and q's
    • Mayer B. J., Eck M. J. SH3 domains: Minding your p's and q's. Curr. Biol. 5:1995;364-367.
    • (1995) Curr. Biol. , vol.5 , pp. 364-367
    • Mayer, B.J.1    Eck, M.J.2
  • 27
    • 0025332579 scopus 로고
    • Association of the v-crk oncogene product with phosphotyrosine containing proteins and protein kinase activity
    • Mayer B. J., Hanafusa H. Association of the v-crk oncogene product with phosphotyrosine containing proteins and protein kinase activity. Proc. Natl. Acad. Sci. USA. 87:1990;2638-2642.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2638-2642
    • Mayer, B.J.1    Hanafusa, H.2
  • 28
    • 0026601293 scopus 로고
    • Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo
    • Mayer B. J., Jackson P. K., Van Etten R. A., Baltimore D. Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo. Mol. Cell. Biol. 12:1992;609-618.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 609-618
    • Mayer, B.J.1    Jackson, P.K.2    Van Etten, R.A.3    Baltimore, D.4
  • 29
    • 0030636320 scopus 로고    scopus 로고
    • Erythropoietin receptor is expressed in rat hippocampal and cerebral cortical neurons, and erythropoietin prevents in vitro glutamate-induced neuronal death
    • Morishita E., Masuda M., Nagao M., Yasuda Y., Sasaki R. Erythropoietin receptor is expressed in rat hippocampal and cerebral cortical neurons, and erythropoietin prevents in vitro glutamate-induced neuronal death. Neuroscience. 76:1997;105-116.
    • (1997) Neuroscience , vol.76 , pp. 105-116
    • Morishita, E.1    Masuda, M.2    Nagao, M.3    Yasuda, Y.4    Sasaki, R.5
  • 30
    • 0029978536 scopus 로고    scopus 로고
    • Anti-erythropoietin receptor monoclonal antibody: Epitopemapping, quantification of the soluble receptor and detection of the solubilized transmembrane receptor and the receptor expressing cells
    • Morishita E., Narita H., Nishida M., Kawashima N., Yamagishi K., Masuda S., Nagao M., Hatta H., Sasaki R. Anti-erythropoietin receptor monoclonal antibody: Epitopemapping, quantification of the soluble receptor and detection of the solubilized transmembrane receptor and the receptor expressing cells. Blood. 88:1996;465-471.
    • (1996) Blood , vol.88 , pp. 465-471
    • Morishita, E.1    Narita, H.2    Nishida, M.3    Kawashima, N.4    Yamagishi, K.5    Masuda, S.6    Nagao, M.7    Hatta, H.8    Sasaki, R.9
  • 31
    • 0017089669 scopus 로고
    • 3′ non-coding region sequences in eukaryotic messenger RNA
    • Proudfoot N. J., Brownlee G. G. 3′ non-coding region sequences in eukaryotic messenger RNA. Nature. 263:1976;211-214.
    • (1976) Nature , vol.263 , pp. 211-214
    • Proudfoot, N.J.1    Brownlee, G.G.2
  • 32
    • 0025144506 scopus 로고
    • Characterization of the 47-kilodalton autosomal chronic granulomatous disease protein: Tissue-specific expression and transcriptional control by retinoic acid
    • Rodaway A. R. F., Teahan C. G., Casimir C. M., Segal A. W., Bentley D. L. Characterization of the 47-kilodalton autosomal chronic granulomatous disease protein: Tissue-specific expression and transcriptional control by retinoic acid. Mol. Cell. Biol. 10:1990;5388-5396.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5388-5396
    • Rodaway, A.R.F.1    Teahan, C.G.2    Casimir, C.M.3    Segal, A.W.4    Bentley, D.L.5
  • 33
    • 0029070907 scopus 로고
    • Epidermal growth factor induces the tyrosin phosphorylation and nuclear translocation of Stat 5 in mouse liver
    • Ruff-Jamison S., Chen K., Cohen S. Epidermal growth factor induces the tyrosin phosphorylation and nuclear translocation of Stat 5 in mouse liver. Proc. Natl. Acad. Sci. USA. 92:1995;4215-4218.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4215-4218
    • Ruff-Jamison, S.1    Chen, K.2    Cohen, S.3
  • 35
    • 0030799394 scopus 로고    scopus 로고
    • Protein phosphorylation sites regulate the function of the bipartite NLS of nucleolin
    • Schwab M. S., Dreyer C. Protein phosphorylation sites regulate the function of the bipartite NLS of nucleolin. Eur. J. Cell Biol. 73:1997;287-297.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 287-297
    • Schwab, M.S.1    Dreyer, C.2
  • 36
    • 0029655282 scopus 로고    scopus 로고
    • Translational efficiency is regulated by the length of the 3′ untranslated region
    • Tanguay R. L., Gallie D. R. Translational efficiency is regulated by the length of the 3′ untranslated region. Mol. Cell. Biol. 16:1996;146-156.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 146-156
    • Tanguay, R.L.1    Gallie, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.