메뉴 건너뛰기




Volumn 89, Issue 4, 1997, Pages 597-606

mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3' end

Author keywords

[No Author keywords available]

Indexed keywords

ARACHIDONATE 15 LIPOXYGENASE; REGULATOR PROTEIN;

EID: 0030772963     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80241-X     Document Type: Article
Times cited : (437)

References (56)
  • 1
    • 0028232357 scopus 로고
    • Tissue specific expression and cDNA structure of a human transcript encoding a nucleic acid [oligo(dC)] protein related to the pre-mRNA binding protein K
    • Aasheim, H.-C., Loukianova, T., Deggerdal, A., and Smeland, E.B. (1994). Tissue specific expression and cDNA structure of a human transcript encoding a nucleic acid [oligo(dC)] protein related to the pre-mRNA binding protein K. Nucl. Acids Res. 22, 959-964.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 959-964
    • Aasheim, H.-C.1    Loukianova, T.2    Deggerdal, A.3    Smeland, E.B.4
  • 2
    • 0024829771 scopus 로고
    • Optimized use of the firefly luciferase assay as a reporter gene in mammalian cell lines
    • Brasier, A.R., Tate, J.E., and Habener, J.F. (1989). Optimized use of the firefly luciferase assay as a reporter gene in mammalian cell lines. Biotechniques 7, 1116-1122.
    • (1989) Biotechniques , vol.7 , pp. 1116-1122
    • Brasier, A.R.1    Tate, J.E.2    Habener, J.F.3
  • 3
    • 0028894021 scopus 로고
    • Association of vav proto-oncogene product with poly(rC)-specific RNA-binding proteins
    • Bustelo, X.R., Suen, K.L., Michael, W.M., Dreyfuss, G., and Barbacid, M. (1995). Association of vav proto-oncogene product with poly(rC)-specific RNA-binding proteins. Mol. Cell. Biol. 15, 1324-1332.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1324-1332
    • Bustelo, X.R.1    Suen, K.L.2    Michael, W.M.3    Dreyfuss, G.4    Barbacid, M.5
  • 4
    • 0029030104 scopus 로고
    • Translational regulation in development
    • Curtis, D., Lehmann, R., and Zamore, P.D. (1995).Translational regulation in development. Cell 81, 171-178.
    • (1995) Cell , vol.81 , pp. 171-178
    • Curtis, D.1    Lehmann, R.2    Zamore, P.D.3
  • 5
    • 0026556814 scopus 로고
    • Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast
    • Dever, T.E., Feng, L., Wek, R.C., Cigan, R.M., Donahue, T.F., and Hinnebusch, A.G. (1992). Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68, 585-596.
    • (1992) Cell , vol.68 , pp. 585-596
    • Dever, T.E.1    Feng, L.2    Wek, R.C.3    Cigan, R.M.4    Donahue, T.F.5    Hinnebusch, A.G.6
  • 6
    • 0030059840 scopus 로고    scopus 로고
    • RNA recognition and translational regulation by a homeodomain protein
    • Dubnau, J., and Struhl, G. (1996). RNA recognition and translational regulation by a homeodomain protein. Nature 379, 694-699.
    • (1996) Nature , vol.379 , pp. 694-699
    • Dubnau, J.1    Struhl, G.2
  • 7
    • 0028217190 scopus 로고
    • Translational control of maternal glp-1 mRNA establishes an asymmetry in the C. elegans embryo
    • Evans, T.C., Crittenden, S.L., Kodoyianni, V., and Kimble, J. (1994). Translational control of maternal glp-1 mRNA establishes an asymmetry in the C. elegans embryo. Cell 77, 183-194.
    • (1994) Cell , vol.77 , pp. 183-194
    • Evans, T.C.1    Crittenden, S.L.2    Kodoyianni, V.3    Kimble, J.4
  • 8
    • 0024384141 scopus 로고
    • The complete sequence of the rabbit erythroid cell-specific 15-lipoxygenase mRNA: Comparison of the predicted amino acid sequence of the erythroid lipoxygenase with other lipoxygenases
    • Fleming, J., Thiele, B.J., Chester, J., O'Prey, J., Janetzky, S., Aitken, A., Anton, I.A., Rapoport, S.M., and Harrison, P. (1989).The complete sequence of the rabbit erythroid cell-specific 15-lipoxygenase mRNA: comparison of the predicted amino acid sequence of the erythroid lipoxygenase with other lipoxygenases. Gene 79, 181-188.
    • (1989) Gene , vol.79 , pp. 181-188
    • Fleming, J.1    Thiele, B.J.2    Chester, J.3    O'Prey, J.4    Janetzky, S.5    Aitken, A.6    Anton, I.A.7    Rapoport, S.M.8    Harrison, P.9
  • 9
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham, F.L., and Van der Eb, A.J. (1973). A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 52, 456-464.
    • (1973) Virology , vol.52 , pp. 456-464
    • Graham, F.L.1    Van der Eb, A.J.2
  • 10
    • 0027131432 scopus 로고
    • Recombinant iron-regulatory factor functions as an iron-responsive-element binding protein, a translational represser and an aconitase. A functional assay for translational repression and direct demonstration of the iron switch
    • Gray, N.K, Quick, S., Goossen, B., Constable, A., Hirling, H., Kühn, L., and Hentze, M.W. (1993). Recombinant iron-regulatory factor functions as an iron-responsive-element binding protein, a translational represser and an aconitase. A functional assay for translational repression and direct demonstration of the iron switch. Eur. J. Biochem. 218, 657-667.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 657-667
    • Gray, N.K.1    Quick, S.2    Goossen, B.3    Constable, A.4    Hirling, H.5    Kühn, L.6    Hentze, M.W.7
  • 11
    • 0028059555 scopus 로고
    • Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs
    • Gray, N.K., and Hentze, M.W. (1994). Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs. EMBO J. 13, 3882-3891.
    • (1994) EMBO J. , vol.13 , pp. 3882-3891
    • Gray, N.K.1    Hentze, M.W.2
  • 12
    • 0024283936 scopus 로고
    • A versatile in vitro and in vivo eukaryotic expression vector for protein engineering
    • Green, S., Issemann, I., and Sheer, E. (1988). A versatile in vitro and in vivo eukaryotic expression vector for protein engineering. Nucl. Acids Res. 16, 369.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 369
    • Green, S.1    Issemann, I.2    Sheer, E.3
  • 13
    • 0027200718 scopus 로고
    • Isolation of a murine gene encoding a nucleic acid-binding protein with homology to hnRNP K
    • Hahm, K., Kim, G., Turck, C.W., and Smale, S.T. (1993). Isolation of a murine gene encoding a nucleic acid-binding protein with homology to hnRNP K. Nucl. Acids Res. 21, 3894.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 3894
    • Hahm, K.1    Kim, G.2    Turck, C.W.3    Smale, S.T.4
  • 14
    • 0028029983 scopus 로고
    • CPEB is a specific factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation
    • Hake, L.E., and Richter, J.D. (1994). CPEB is a specific factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation. Cell 79, 617-627.
    • (1994) Cell , vol.79 , pp. 617-627
    • Hake, L.E.1    Richter, J.D.2
  • 15
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress
    • Hentze, M.W., and Kühn, L.C. (1996). Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress. Proc. Natl. Acad. Sci. USA 93, 8175-8182.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 16
    • 0028151657 scopus 로고
    • Translational control of GCN4: An in vivo barometer of initiation-factor activity
    • Hinnebusch, A.G. (1994). Translational control of GCN4: an in vivo barometer of initiation-factor activity. Trends Biochem. Sci. 19, 409-414.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 409-414
    • Hinnebusch, A.G.1
  • 17
    • 0028114049 scopus 로고
    • Novel signaling pathway suggested by SH3 domain-mediated p95vav/ heterogeneous ribonucleoprotein K interaction
    • Hobert, O., Jallal, B., Schlessinger, J., and Ullrich, A. (1994). Novel signaling pathway suggested by SH3 domain-mediated p95vav/ heterogeneous ribonucleoprotein K interaction. J. Biol. Chem. 269, 20225-20228.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20225-20228
    • Hobert, O.1    Jallal, B.2    Schlessinger, J.3    Ullrich, A.4
  • 20
    • 0024748029 scopus 로고
    • On the translational control of suicide in red cell development
    • Hunt, T. (1989). On the translational control of suicide in red cell development. Trends Biochem. Sci. 14, 393-394.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 393-394
    • Hunt, T.1
  • 22
    • 0027275266 scopus 로고
    • Cytoplasmic regulation of mRNA function: The importance of the 3′ untranslated region
    • Jackson, R.J. (1993). Cytoplasmic regulation of mRNA function: the importance of the 3′ untranslated region. Cell 74, 9-14.
    • (1993) Cell , vol.74 , pp. 9-14
    • Jackson, R.J.1
  • 23
    • 0021004695 scopus 로고
    • Preparation and use of nuclease-treated rabbit reticulocyte lysate for the translation of eukaryotic messenger RNA
    • Jackson, R.J., and Hunt, T. (1983). Preparation and use of nuclease-treated rabbit reticulocyte lysate for the translation of eukaryotic messenger RNA. Meth. Enzymol. 96, 50-74.
    • (1983) Meth. Enzymol. , vol.96 , pp. 50-74
    • Jackson, R.J.1    Hunt, T.2
  • 24
    • 0025145263 scopus 로고
    • Initiation of encephalomyocarditis virus RNA translation: The authentic initiation site is not selected by a scanning mechanism
    • Kaminski, A., Howell, M.T., and Jackson, R.J. (1990). Initiation of encephalomyocarditis virus RNA translation: the authentic initiation site is not selected by a scanning mechanism. EMBO J. 9, 3753-3759.
    • (1990) EMBO J. , vol.9 , pp. 3753-3759
    • Kaminski, A.1    Howell, M.T.2    Jackson, R.J.3
  • 25
    • 0029125496 scopus 로고
    • Identification of two KH domain proteins in the α-globin mRNP stability complex
    • Kiledjian, M., Wang, X., and Liebhaber, S.A. (1995). Identification of two KH domain proteins in the α-globin mRNP stability complex. EMBO J. 14, 4357-4364.
    • (1995) EMBO J. , vol.14 , pp. 4357-4364
    • Kiledjian, M.1    Wang, X.2    Liebhaber, S.A.3
  • 26
    • 0029823755 scopus 로고    scopus 로고
    • Regulated ribosomal frameshifting by an RNA-protein interaction
    • Kollmus, H., Hentze, M.W., and Hauser, H. (1996). Regulated ribosomal frameshifting by an RNA-protein interaction. RNA 2,316-323.
    • (1996) RNA , vol.2 , pp. 316-323
    • Kollmus, H.1    Hentze, M.W.2    Hauser, H.3
  • 27
    • 0029076374 scopus 로고
    • Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains
    • Letters, H., Dejgaard, K., and Celis, J.E. (1995). Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains. Eur. J. Biochem. 230, 447-453.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 447-453
    • Letters, H.1    Dejgaard, K.2    Celis, J.E.3
  • 28
    • 0028575316 scopus 로고
    • Error tolerant identification of peptides in sequence databases by peptide sequence tags
    • Mann, M., and Wilm, M.S. (1994). Error tolerant identification of peptides in sequence databases by peptide sequence tags. Anal. Chem. 66, 4390-4399.
    • (1994) Anal. Chem. , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.S.2
  • 29
    • 0026515523 scopus 로고
    • Characterization and primary structure of the poly (C)-binding heterogeneus nuclear ribonucleoprotein complex K protein
    • Matunis, M.J., Michael, W.M., and Dreyfuss, G. (1992) Characterization and primary structure of the poly (C)-binding heterogeneus nuclear ribonucleoprotein complex K protein. Mol. Cell. Biol. 12, 164-171.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 164-171
    • Matunis, M.J.1    Michael, W.M.2    Dreyfuss, G.3
  • 30
    • 0028224527 scopus 로고
    • Essential role for a heterogeneous nuclear ribonucleoprotein (hnRNP) in oogenesis: Hrp40 is absent from the germ line in the dorsoventral mutant squid
    • Matunis, E., Kelley, R., and Dreyfuss, G. (1994). Essential role for a heterogeneous nuclear ribonucleoprotein (hnRNP) in oogenesis: hrp40 is absent from the germ line in the dorsoventral mutant squid. Proc. Natl. Acad. Sci. USA 91, 2781-2784.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2781-2784
    • Matunis, E.1    Kelley, R.2    Dreyfuss, G.3
  • 31
    • 0026543785 scopus 로고
    • Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2
    • Mayeda, A., and Krainer, A.R. (1992). Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell 68, 365-375.
    • (1992) Cell , vol.68 , pp. 365-375
    • Mayeda, A.1    Krainer, A.R.2
  • 32
    • 0029917052 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K is a transcription factor
    • Michelotti, E.F., Michelotti, G.A., Aronsohn, A.I., and Levens, D. (1996). Heterogeneous nuclear ribonucleoprotein K is a transcription factor. Mol. Cell. Biol. 16, 2350-2360.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2350-2360
    • Michelotti, E.F.1    Michelotti, G.A.2    Aronsohn, A.I.3    Levens, D.4
  • 33
    • 0028867814 scopus 로고
    • The generally expressed hnRNP F is involved in a neural-specific pre-mRNA splicing event
    • Min, H., Chan, R.C., and Black, D.L. (1995). The generally expressed hnRNP F is involved in a neural-specific pre-mRNA splicing event. Genes Dev. 9, 2659-2671.
    • (1995) Genes Dev. , vol.9 , pp. 2659-2671
    • Min, H.1    Chan, R.C.2    Black, D.L.3
  • 34
    • 0028201735 scopus 로고
    • Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region
    • Ostareck-Lederer, A., Ostareck, D.H., Standart, N., and Thiele, B.J. (1994). Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region. EMBO J. 13, 1476-1481.
    • (1994) EMBO J. , vol.13 , pp. 1476-1481
    • Ostareck-Lederer, A.1    Ostareck, D.H.2    Standart, N.3    Thiele, B.J.4
  • 35
    • 0028929741 scopus 로고
    • Nitric oxide signaling to iron-regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts
    • Pantopoulos, K., and Hentze, M.W. (1995). Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proc. Natl. Acad. Sci. USA 92, 1267-1271.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1267-1271
    • Pantopoulos, K.1    Hentze, M.W.2
  • 36
    • 0027411587 scopus 로고
    • HnRNP proteins: Localization and transport between the nucleus and the cytoplasm
    • Piñol-Roma, S., and Dreyfuss, G. (1993). hnRNP proteins: localization and transport between the nucleus and the cytoplasm. Trends Biochem. Sci. 3, 151-155.
    • (1993) Trends Biochem. Sci. , vol.3 , pp. 151-155
    • Piñol-Roma, S.1    Dreyfuss, G.2
  • 37
    • 0022861651 scopus 로고
    • The maturational breakdown of mitochondria in reticulocytes
    • Rapoport, S.M., and Schewe, T. (1986).The maturational breakdown of mitochondria in reticulocytes. Biochem. Biophys. Acta 864, 471-495.
    • (1986) Biochem. Biophys. Acta , vol.864 , pp. 471-495
    • Rapoport, S.M.1    Schewe, T.2
  • 39
  • 40
    • 0022503366 scopus 로고
    • Enzymology and physiology of reticulocyte lipoxygenase: Comparison with other lipoxygenases
    • A. Meister, ed. New York: John Wiley and Sons, Inc.
    • Schewe, T., Rapoport, S.M., and Kühn, H. (1986). Enzymology and physiology of reticulocyte lipoxygenase: comparison with other lipoxygenases. In Advances in Enzymology and Related Areas of Molecular Biology, Volume 58, A. Meister, ed. (New York: John Wiley and Sons, Inc.), pp. 191-271.
    • (1986) Advances in Enzymology and Related Areas of Molecular Biology , vol.58 , pp. 191-271
    • Schewe, T.1    Rapoport, S.M.2    Kühn, H.3
  • 41
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996). Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Anal. Chem. 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 42
    • 0028070676 scopus 로고
    • Protein binding to 5′ untranslated region sites: General mechanism for translational regulation of mRNAs in human and yeast cells
    • Stripecke, R., Oliveira, C.C., McCarthy, J.E.G., and Hentze, M.W. (1994). Protein binding to 5′ untranslated region sites: general mechanism for translational regulation of mRNAs in human and yeast cells. Mol. Cell. Biol. 14, 5898-5909.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5898-5909
    • Stripecke, R.1    Oliveira, C.C.2    McCarthy, J.E.G.3    Hentze, M.W.4
  • 43
    • 0024009108 scopus 로고
    • Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities
    • Swanson, M.S., and Dreyfuss, G. (1988). Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities. Mol. Cell. Biol. 8, 2237-2241.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2237-2241
    • Swanson, M.S.1    Dreyfuss, G.2
  • 44
    • 0027182876 scopus 로고
    • Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter in vitro
    • Takimoto, M., Tomonaga, T., Matunis, M., Avigan, M., Krutzsch, H., Dreyfuss, G., and Levens D. (1993). Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter in vitro. J. Biol. Chem. 268, 18249-18258.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18249-18258
    • Takimoto, M.1    Tomonaga, T.2    Matunis, M.3    Avigan, M.4    Krutzsch, H.5    Dreyfuss, G.6    Levens, D.7
  • 45
    • 0028329195 scopus 로고
    • An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis
    • Taylor, S.J., and Shalloway, D. (1994). An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis. Nature 368, 867-871.
    • (1994) Nature , vol.368 , pp. 867-871
    • Taylor, S.J.1    Shalloway, D.2
  • 47
    • 0020433558 scopus 로고
    • Lipoxygenase m RNA in rabbit reticulocytes. Its isolation, characterization and translational repression
    • Thiele, B.J., Andree, H., Höhne, M., and Rapoport, S.M. (1982). Lipoxygenase m RNA in rabbit reticulocytes. Its isolation, characterization and translational repression. Eur. J. Biochem. 129, 133-141.
    • (1982) Eur. J. Biochem. , vol.129 , pp. 133-141
    • Thiele, B.J.1    Andree, H.2    Höhne, M.3    Rapoport, S.M.4
  • 48
    • 0028834524 scopus 로고
    • The K protein domain that recruits the interleukin 1-responsive K protein kinase lies adjacent to a cluster of c-Src and Vav SH3-binding sites
    • Van Seuningen, I., Ostrowski, J., Bustelo, X.R., Sleath, P.R., and Bomsztyk, K. (1995). The K protein domain that recruits the interleukin 1-responsive K protein kinase lies adjacent to a cluster of c-Src and Vav SH3-binding sites. J. Biol. Chem. 270, 26976-26985.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26976-26985
    • Van Seuningen, I.1    Ostrowski, J.2    Bustelo, X.R.3    Sleath, P.R.4    Bomsztyk, K.5
  • 49
    • 0028839055 scopus 로고
    • Detection and characterization of a 3′ untranslated region ribonucleoprotein complex associated with the human a-globin mRNA stability
    • Wang, X., Kiledjian, M., Weiss, I.M., and Liebhaber, S.A. (1995). Detection and characterization of a 3′ untranslated region ribonucleoprotein complex associated with the human a-globin mRNA stability. Mol. Cell. Biol. 15, 1769-1777.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1769-1777
    • Wang, X.1    Kiledjian, M.2    Weiss, I.M.3    Liebhaber, S.A.4
  • 51
    • 0027176987 scopus 로고
    • Springtime in the desert
    • Wickens, M. (1993). Springtime in the desert. Nature 363, 305-306.
    • (1993) Nature , vol.363 , pp. 305-306
    • Wickens, M.1
  • 52
    • 0001844614 scopus 로고    scopus 로고
    • Translational control of developmental decisions
    • J.W.B. Hershey, M.B. Mathews, and N. Sonenberg, eds. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Wickens, M., Kimble, J., and Strickland, S. (1996).Translational control of developmental decisions. In Translational Control, J.W.B. Hershey, M.B. Mathews, and N. Sonenberg, eds. (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press), pp. 411-450.
    • (1996) Translational Control , pp. 411-450
    • Wickens, M.1    Kimble, J.2    Strickland, S.3
  • 53
    • 0000217562 scopus 로고
    • Electrospray and Taylor-Cone theory, Dole's beam of macromolecules at last?
    • Wilm, M.S., and Mann, M. (1994). Electrospray and Taylor-Cone theory, Dole's beam of macromolecules at last? Int. J. Mass Spectrom. Ion Proc. 136, 167-180.
    • (1994) Int. J. Mass Spectrom. Ion Proc. , vol.136 , pp. 167-180
    • Wilm, M.S.1    Mann, M.2
  • 54
    • 0029685702 scopus 로고    scopus 로고
    • Analytical properties of the nano electrospray ion source
    • Wilm, M., and Mann, M. (1996). Analytical properties of the nano electrospray ion source. Anal. Chem. 68, 1-8.
    • (1996) Anal. Chem. , vol.68 , pp. 1-8
    • Wilm, M.1    Mann, M.2
  • 55
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano electrospray mass spectrometry
    • Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., and Mann, M. (1996a). Femtomole sequencing of proteins from polyacrylamide gels by nano electrospray mass spectrometry. Nature 379, 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 56
    • 0030033198 scopus 로고    scopus 로고
    • Parent ion scans of unseparated peptide mixtures
    • Wilm, M., Neubauer, G., and Mann, M. (1996b). Parent ion scans of unseparated peptide mixtures. Anal. Chem. 68, 527-533.
    • (1996) Anal. Chem. , vol.68 , pp. 527-533
    • Wilm, M.1    Neubauer, G.2    Mann, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.