메뉴 건너뛰기




Volumn 19, Issue 5, 1999, Pages 497-508

Profilin in Phaseolus vulgaris is encoded by two genes (only one expressed in root nodules) but multiple isoforms are generated in vivo by phosphorylation on tyrosine residues

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL LABELING; CYTOSKELETON; DNA DNA HYBRIDIZATION; DNA PROBE; GENE INDUCTION; IMMUNOPRECIPITATION; MULTIGENE FAMILY; NODULATION; PLANT EXTRACT; PLANT GENETICS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROFILIN; PROTEIN DETECTION; PROTEIN PHOSPHORYLATION; PROTEIN TYROSINE KINASE; RESTRICTION ENZYME ANALYSIS; RNA TRANSLATION; TRANSCRIPTION REGULATION; TYROSINE PHOSPHATASE; WESTERN BLOTTING;

EID: 18144447988     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1999.00542.x     Document Type: Article
Times cited : (51)

References (81)
  • 1
    • 0028153875 scopus 로고
    • Elucidation of the poly-L-proline binding site in Acanthamoeba profilin I by NMR spectroscopy
    • Archer, J.S., Vinks, V.K., Pollard, T.D. and Torchia, D.A. (1994) Elucidation of the poly-L-proline binding site in Acanthamoeba profilin I by NMR spectroscopy. FEBS Lett. 357, 145-151.
    • (1994) FEBS Lett. , vol.357 , pp. 145-151
    • Archer, J.S.1    Vinks, V.K.2    Pollard, T.D.3    Torchia, D.A.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0030958087 scopus 로고    scopus 로고
    • Cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin
    • Chang, F., Drubin, D. and Nurse, P. (1997) Cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J. Cell Biol. 137, 169-182.
    • (1997) J. Cell Biol. , vol.137 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 6
    • 0030209449 scopus 로고    scopus 로고
    • Arabidopsis profilins are functionally similar to yeast profilins: Identification of a vascular bundle-specific profilin and pollen-specific profilin
    • Christensen, H.E.M., Ramachandran, S., Tan Chio-Tee, Surana, U., Dong, C.-H. and Chua, N.-H. (1996) Arabidopsis profilins are functionally similar to yeast profilins: identification of a vascular bundle-specific profilin and pollen-specific profilin. Plant J. 10, 269-279.
    • (1996) Plant J. , vol.10 , pp. 269-279
    • Christensen, H.E.M.1    Ramachandran, S.2    Tan Chio-Tee., C.-T.3    Surana, U.4    Dong, C.-H.5    Chua, N.-H.6
  • 7
    • 0032100337 scopus 로고    scopus 로고
    • A potential signalling role for profilin in pollen of Papaver rhoeas
    • Clarke, S.R., Staiger, C.J., Gibbon, B.C. and Frankling-Tong, V. (1998) A potential signalling role for profilin in pollen of Papaver rhoeas. Plant Cell, 10, 967-979.
    • (1998) Plant Cell , vol.10 , pp. 967-979
    • Clarke, S.R.1    Staiger, C.J.2    Gibbon, B.C.3    Frankling-Tong, V.4
  • 8
    • 0027615677 scopus 로고
    • Tyrosine phosphorylation of alpha-tubulin is an early response to NGF and pp. 60v-src in PC12 cells
    • Cox, M.E. and Maness, P.F. (1993) Tyrosine phosphorylation of alpha-tubulin is an early response to NGF and pp. 60v-src in PC12 cells. J. Mol. Neurosci. 4, 63-72.
    • (1993) J. Mol. Neurosci. , vol.4 , pp. 63-72
    • Cox, M.E.1    Maness, P.F.2
  • 9
    • 0029959214 scopus 로고    scopus 로고
    • In vivo phosphorylation of actin in Physarum polycephalum. Study of the substrate specificity of the actin-fragmin kinase
    • De Corte, V., Gettemans, J., Eaelkens, E. and Vandekerckhove, J. (1996) In vivo phosphorylation of actin in Physarum polycephalum. Study of the substrate specificity of the actin-fragmin kinase. Eur. J. Biochem. 241, 901-908.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 901-908
    • De Corte, V.1    Gettemans, J.2    Eaelkens, E.3    Vandekerckhove, J.4
  • 12
    • 0000479431 scopus 로고
    • Isolation of plant DNA from fresh tissue
    • Doyle, J.J., Doyle, J.L. and Hortorin, L.B.H. (1990) Isolation of plant DNA from fresh tissue. Focus, 12, 13-15.
    • (1990) Focus , vol.12 , pp. 13-15
    • Doyle, J.J.1    Doyle, J.L.2    Hortorin, L.B.H.3
  • 13
    • 0028105664 scopus 로고
    • Inhibition of plant plasma membrane phosphoinositide phospholipase-C by the actin-binding protein, profilin
    • Drøbak, B.K., Watkins, P.A.C., Valenta, R., Dove, S.K., Lloyd, C.W. and Staiger, C.J. (1994) Inhibition of plant plasma membrane phosphoinositide phospholipase-C by the actin-binding protein, profilin. Plant J. 6, 389-400.
    • (1994) Plant J. , vol.6 , pp. 389-400
    • Drøbak, B.K.1    Watkins, P.A.C.2    Valenta, R.3    Dove, S.K.4    Lloyd, C.W.5    Staiger, C.J.6
  • 14
    • 0027345809 scopus 로고
    • MsERK1: A mitogen-activated protein kinase from a flowering plant
    • Duerr, B., Gawienowski, M., Ropp, T. and Jacobs, T. (1993) MsERK1: a mitogen-activated protein kinase from a flowering plant. Plant Cell, 5, 87-96.
    • (1993) Plant Cell , vol.5 , pp. 87-96
    • Duerr, B.1    Gawienowski, M.2    Ropp, T.3    Jacobs, T.4
  • 16
    • 0027359378 scopus 로고
    • Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp. 60src substrate
    • Flynn, D.C., Leu, T.H., Reynolds, A.B. and Parsons, J.T. (1993) Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp. 60src substrate. Mol. Cell Biol. 13, 7892-7900.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 7892-7900
    • Flynn, D.C.1    Leu, T.H.2    Reynolds, A.B.3    Parsons, J.T.4
  • 18
    • 0032560564 scopus 로고    scopus 로고
    • Histidine kinase activity of the ETR1 ethylene receptor from Arabidopsis
    • Gamble, R.L., Coonfield, M.L. and Schaller, G.E. (1998) Histidine kinase activity of the ETR1 ethylene receptor from Arabidopsis. Proc. Natl Acad. Sci. USA, 95, 7825-7829.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7825-7829
    • Gamble, R.L.1    Coonfield, M.L.2    Schaller, G.E.3
  • 19
    • 0003122907 scopus 로고
    • Phosphodipeptide mapping and phosphoaminoacid analysis on cellulose thin-layer plates
    • (Hardie, D.G., ed.) Oxford: IRL Press
    • van der Geer, P., Luo, K., Sefton, B.M. and Hunter, T. (1993) Phosphodipeptide mapping and phosphoaminoacid analysis on cellulose thin-layer plates. In Protein Phosphorylation. A Practical Approach Volume 2 (Hardie, D.G., ed.) Oxford: IRL Press, pp. 31-59.
    • (1993) Protein Phosphorylation. A Practical Approach , vol.2 , pp. 31-59
    • Van Der Geer, P.1    Luo, K.2    Sefton, B.M.3    Hunter, T.4
  • 20
    • 0032100347 scopus 로고    scopus 로고
    • Pollen profilin functions depends on interaction with proline-rich motifs
    • Gibbon, B.C., Zonia, L.E., Kovar, D.R., Hussey, P.J. and Staiger, C.J. (1998) Pollen profilin functions depends on interaction with proline-rich motifs. Plant Cell, 10, 981-993.
    • (1998) Plant Cell , vol.10 , pp. 981-993
    • Gibbon, B.C.1    Zonia, L.E.2    Kovar, D.R.3    Hussey, P.J.4    Staiger, C.J.5
  • 23
    • 0029155492 scopus 로고
    • Histidine and tyrosine phosphorylation in pea mitochondria: Evidence for protein phosphorylation in respiratory redox signalling
    • Håkansson, G. and Allen, J.F. (1995) Histidine and tyrosine phosphorylation in pea mitochondria: evidence for protein phosphorylation in respiratory redox signalling. FEBS Lett. 372, 238-242.
    • (1995) FEBS Lett. , vol.372 , pp. 238-242
    • Håkansson, G.1    Allen, J.F.2
  • 25
    • 0028674557 scopus 로고
    • Actin-binding proteins in cell motility
    • Hatano, S. (1994) Actin-binding proteins in cell motility. Int. Rev. Cytology, 156, 199-273.
    • (1994) Int. Rev. Cytology , vol.156 , pp. 199-273
    • Hatano, S.1
  • 26
    • 0030138167 scopus 로고    scopus 로고
    • The Arabidopsis profilin gene family. Evidence for an ancient split between constitutive and pollen-specific profilin genes
    • Huang, S., McDowell, J.M., Weise, M.J. and Meagher, R.B. (1996) The Arabidopsis profilin gene family. Evidence for an ancient split between constitutive and pollen-specific profilin genes. Plant Physiol. 111, 115-126.
    • (1996) Plant Physiol. , vol.111 , pp. 115-126
    • Huang, S.1    McDowell, J.M.2    Weise, M.J.3    Meagher, R.B.4
  • 27
    • 0030927327 scopus 로고    scopus 로고
    • Bni1p and Bnr1p: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae
    • Imamura, H., Tanaka, K., Hihara, T., Umikawa, M., Kamei, T., Takahashi, K., Sasaki, T. and Takai, Y. (1997) Bni1p and Bnr1p: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J. 16, 2745-2755.
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5    Takahashi, K.6    Sasaki, T.7    Takai, Y.8
  • 28
    • 0002631401 scopus 로고    scopus 로고
    • Protein phosphorylation during Coconut zygotic embryo development
    • Islas-Flores, I., Oropeza, C. and Hernandez-Sotomayor, S.M.T. (1998) Protein Phosphorylation during Coconut zygotic embryo development. Plant Physiol. 118, 257-263.
    • (1998) Plant Physiol. , vol.118 , pp. 257-263
    • Islas-Flores, I.1    Oropeza, C.2    Hernandez-Sotomayor, S.M.T.3
  • 30
    • 0028803976 scopus 로고
    • Stress-induced tyrosine phosphorylation of actin in Dictyostelium cells and localization of the phosphorylation site to tyrosine-53 adjacent to the DNAse I binding loop
    • Jungbluth, A., Eckerskon, C., Gerish, G., Lottpeich, F., Stocker, S. and Schweiger, A. (1995) Stress-induced tyrosine phosphorylation of actin in Dictyostelium cells and localization of the phosphorylation site to tyrosine-53 adjacent to the DNAse I binding loop. FEBS Lett. 375, 87-90.
    • (1995) FEBS Lett. , vol.375 , pp. 87-90
    • Jungbluth, A.1    Eckerskon, C.2    Gerish, G.3    Lottpeich, F.4    Stocker, S.5    Schweiger, A.6
  • 31
    • 0030851599 scopus 로고    scopus 로고
    • Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): Implications for actin-based Listeria motility
    • Kang, F., Laine, R.O., Bubb, M.R., Southwick, F.S. and Purich, D.L. (1997) Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): Implications for actin-based Listeria motility. Biochemistry, 36, 8334-8392.
    • (1997) Biochemistry , vol.36 , pp. 8334-8392
    • Kang, F.1    Laine, R.O.2    Bubb, M.R.3    Southwick, F.S.4    Purich, D.L.5
  • 32
    • 0031572866 scopus 로고    scopus 로고
    • Kinase activity of EnvZ, an osmoregulatory signal transducing protein of Escherichia coli
    • Kenney, L.J. (1997) Kinase activity of EnvZ, an osmoregulatory signal transducing protein of Escherichia coli. Arch. Biochem. Biophys. 346, 303-311.
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 303-311
    • Kenney, L.J.1
  • 33
    • 0031729828 scopus 로고    scopus 로고
    • High levels of tyrosine phosphorylation: Correlation with the dormant state of Dictyostelium spores
    • Kishi, Y., Clements, C., Mahadeo, D.C., Cotter, D.A. and Sameshima, M. (1998) High levels of tyrosine phosphorylation: correlation with the dormant state of Dictyostelium spores. J. Cell Sci. 111, 2923-2932.
    • (1998) J. Cell Sci. , vol.111 , pp. 2923-2932
    • Kishi, Y.1    Clements, C.2    Mahadeo, D.C.3    Cotter, D.A.4    Sameshima, M.5
  • 34
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: Elements that control interactions of cytoplasmic signalling proteins
    • Koch, A.C., Anderson, D., Moran, M.F., Ellis, C. and Powson, T. (1991) SH2 and SH3 Domains: Elements that control interactions of cytoplasmic signalling proteins. Science, 252, 668-674.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, A.C.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Powson, T.5
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0032127612 scopus 로고    scopus 로고
    • Protein phosphatases and signalling cascades in higher plants
    • Luan, S. (1998) Protein phosphatases and signalling cascades in higher plants. Trends in Plant Sci. 3, 271-275.
    • (1998) Trends in Plant Sci. , vol.3 , pp. 271-275
    • Luan, S.1
  • 38
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography
    • Machesky, L.M., Atkinson, S.J., Ampe, C., Vanderkerckove, J. and Pollard, T.D. (1994) Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography. J. Cell Biol. 127, 107-115.
    • (1994) J. Cell Biol. , vol.127 , pp. 107-115
    • Machesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vanderkerckove, J.4    Pollard, T.D.5
  • 39
    • 0027358716 scopus 로고
    • Profilin as a potential mediator of membrane-cytoskeleton communication
    • Machesky, L.M. and Pollard, T.D. (1993) Profilin as a potential mediator of membrane-cytoskeleton communication. Trends in Cell Biol. 3, 381-385.
    • (1993) Trends in Cell Biol. , vol.3 , pp. 381-385
    • Machesky, L.M.1    Pollard, T.D.2
  • 40
    • 0031039519 scopus 로고    scopus 로고
    • Tubulin post-translational modifications-enzymes and their mechanisms of action
    • MacRae, T.H. (1997) Tubulin post-translational modifications-enzymes and their mechanisms of action. Eur. J. Biochem. 244, 265-278.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 265-278
    • MacRae, T.H.1
  • 41
    • 0345434969 scopus 로고    scopus 로고
    • The ompB operon partially determines differental expression of OmpC in Salmonella typhi and Escherichia coli
    • Martinez-Flores, I., Cano, R., Bustamante, V.H., Calva, E. and Puente, J.L. (1999) The ompB operon partially determines differental expression of OmpC in Salmonella typhi and Escherichia coli. J. Bacteriol. 181, 556-562.
    • (1999) J. Bacteriol. , vol.181 , pp. 556-562
    • Martinez-Flores, I.1    Cano, R.2    Bustamante, V.H.3    Calva, E.4    Puente, J.L.5
  • 42
    • 0031882005 scopus 로고    scopus 로고
    • Molecular cloning of a novel fimbrin-like cDNA from Arabidopsis thaliana
    • McCurdy, D.W. and Kim, M. (1998) Molecular cloning of a novel fimbrin-like cDNA from Arabidopsis thaliana. Plant Mol. Biol. 36, 23-31.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 23-31
    • McCurdy, D.W.1    Kim, M.2
  • 43
    • 0031778398 scopus 로고    scopus 로고
    • Members of the Arabidopsis actin gene family are widely dispersed in the genome
    • McKinney, E.C. and Meagher, R.B. (1998) Members of the Arabidopsis actin gene family are widely dispersed in the genome. Genetics, 149, 663-675.
    • (1998) Genetics , vol.149 , pp. 663-675
    • McKinney, E.C.1    Meagher, R.B.2
  • 44
    • 0029132450 scopus 로고
    • The impact of historical contingency on gene phylogeny: Plant actin diversity
    • (Hecht, M.K. MacIntyre, R.J. and Klegg, M.T., eds) New York: Plenum Press
    • Meagher, R.B. (1995) The impact of historical contingency on gene phylogeny: plant actin diversity. In Evolutionary Biology (Hecht, M.K. MacIntyre, R.J. and Klegg, M.T., eds) New York: Plenum Press, pp. 195-215.
    • (1995) Evolutionary Biology , pp. 195-215
    • Meagher, R.B.1
  • 45
    • 0029152581 scopus 로고
    • Molecular cloning and characterization profilin from tobacco (Nicotiana tabacum): Increased profilin expression during pollen maturation
    • Mittermann, I., Swoboda, I., Pierson, E., Eller, N., Kraft, D., Valenta, R. and Heberle-Bors, E. (1995) Molecular cloning and characterization profilin from tobacco (Nicotiana tabacum): increased profilin expression during pollen maturation. Plant Mol. Biol. 27, 137-146.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 137-146
    • Mittermann, I.1    Swoboda, I.2    Pierson, E.3    Eller, N.4    Kraft, D.5    Valenta, R.6    Heberle-Bors, E.7
  • 46
    • 0028154459 scopus 로고
    • Characterization of two cDNAs that encode MAP kinase homologues in Arabidopsis thaliana and analysis of the possible role of auxin in activating such kinase activities in cultured cells
    • Mizoguchi, T., Gotoh, Y., Nishida, E., Yamaguchi-Shinozaki, K., Hayashida, N., Iwasaki, T., Kamada, H. and Shinosaki, K. (1994) Characterization of two cDNAs that encode MAP kinase homologues in Arabidopsis thaliana and analysis of the possible role of auxin in activating such kinase activities in cultured cells. Plant J. 5, 111-122.
    • (1994) Plant J. , vol.5 , pp. 111-122
    • Mizoguchi, T.1    Gotoh, Y.2    Nishida, E.3    Yamaguchi-Shinozaki, K.4    Hayashida, N.5    Iwasaki, T.6    Kamada, H.7    Shinosaki, K.8
  • 47
    • 0031013737 scopus 로고    scopus 로고
    • Environmental stress response in plants: The role of mitogen-activated protein kinases
    • Mizoguchi, T., Ichimura, K. and Shinozaki, K. (1997) Environmental stress response in plants: the role of mitogen-activated protein kinases. Trends in Biotech. 15, 15-19.
    • (1997) Trends in Biotech. , vol.15 , pp. 15-19
    • Mizoguchi, T.1    Ichimura, K.2    Shinozaki, K.3
  • 48
    • 0032504617 scopus 로고    scopus 로고
    • Purification of an actin-binding protein composed of 115-kDa polypeptide from pollen tubes of lily
    • Nakayasu, T., Yokota, E. and Shimmen, T. (1998) Purification of an actin-binding protein composed of 115-kDa polypeptide from pollen tubes of lily. Biochem. Biophys. Res. Commun. 249, 61-65.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 61-65
    • Nakayasu, T.1    Yokota, E.2    Shimmen, T.3
  • 49
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.M. (1975) High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.M.1
  • 52
    • 0345464680 scopus 로고    scopus 로고
    • Evidence of protein-tyrosine activity in Catharanthus roseus roots transformed by Agrobacterium rhizogenes
    • Rodríguez-Zapata, L.C. and Hernández-Sotomayor, S.M.T. (1998) Evidence of protein-tyrosine activity in Catharanthus roseus roots transformed by Agrobacterium rhizogenes. Planta, 204, 70-77.
    • (1998) Planta , vol.204 , pp. 70-77
    • Rodríguez-Zapata, L.C.1    Hernández-Sotomayor, S.M.T.2
  • 54
    • 0032053115 scopus 로고    scopus 로고
    • Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity
    • Smertenko, A.P., Jiang, C.-J., Simmons, N.J., Weeds, A.G., Davies, D.R. and Hussey, P. (1998) Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity. Plant J. 14, 187-193.
    • (1998) Plant J. , vol.14 , pp. 187-193
    • Smertenko, A.P.1    Jiang, C.-J.2    Simmons, N.J.3    Weeds, A.G.4    Davies, D.R.5    Hussey, P.6
  • 55
    • 0030835855 scopus 로고    scopus 로고
    • Profilin and actin-depolymerizing factor: Modulators of actin organization in plants
    • Staiger, C.J., Gibbon, B.C., Kovar, D.R. and Zonia, L.E. (1997) Profilin and actin-depolymerizing factor: modulators of actin organization in plants. Trends in Plant Sci. 7, 275-281.
    • (1997) Trends in Plant Sci. , vol.7 , pp. 275-281
    • Staiger, C.J.1    Gibbon, B.C.2    Kovar, D.R.3    Zonia, L.E.4
  • 56
  • 57
    • 0028385716 scopus 로고
    • Microinjected profilin affects cytoplasmic streaming in plant cells by rapidly depolymerizing actin microfilaments
    • Staiger, C.J., Yuang, M., Valenta, R., Shaw, P.J., Warn, R.M. and Lloyd, C.W. (1994) Microinjected profilin affects cytoplasmic streaming in plant cells by rapidly depolymerizing actin microfilaments. Curr. Biol. 4, 215-219.
    • (1994) Curr. Biol. , vol.4 , pp. 215-219
    • Staiger, C.J.1    Yuang, M.2    Valenta, R.3    Shaw, P.J.4    Warn, R.M.5    Lloyd, C.W.6
  • 59
    • 0028873887 scopus 로고
    • Transient activation and tyrosine phosphorylation of a protein kinase in tobacco cells treated with a fungal elicitor
    • Suzuki, K. and Shinshi, H. (1995) Transient activation and tyrosine phosphorylation of a protein kinase in tobacco cells treated with a fungal elicitor. Plant Cell, 7, 639-647.
    • (1995) Plant Cell , vol.7 , pp. 639-647
    • Suzuki, K.1    Shinshi, H.2
  • 60
    • 0022409564 scopus 로고
    • Poly (L-proline)-binding proteins from chick embryos are profilin and a profilactin
    • Tanaka, M. and Shibata, H. (1985) Poly (L-proline)-binding proteins from chick embryos are profilin and a profilactin. Eur. J. Biochem. 151, 291-297.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 291-297
    • Tanaka, M.1    Shibata, H.2
  • 61
    • 0029589267 scopus 로고
    • The cell biology of infection by intracellular bacterial pathogens
    • Theriot, J.A. (1995) The cell biology of infection by intracellular bacterial pathogens. Ann. Rev. Cell Dev. Biol. 7, 213-239.
    • (1995) Ann. Rev. Cell Dev. Biol. , vol.7 , pp. 213-239
    • Theriot, J.A.1
  • 62
    • 0027739978 scopus 로고
    • The three faces of profilin
    • Theriot, J.A. and Mitchison, T.J. (1993) The three faces of profilin. Cell, 75, 835-838.
    • (1993) Cell , vol.75 , pp. 835-838
    • Theriot, J.A.1    Mitchison, T.J.2
  • 63
    • 0023056735 scopus 로고
    • Evidence of the activity of tyrosine kinase (s) and of the presence of phosphotyrosine proteins in pea plantlets
    • Torruella, M., Casano, L.M. and Vallejos, R.H. (1986) Evidence of the activity of tyrosine kinase (s) and of the presence of phosphotyrosine proteins in pea plantlets. J. Biol. Chem. 261, 6651-6653.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6651-6653
    • Torruella, M.1    Casano, L.M.2    Vallejos, R.H.3
  • 64
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, J., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl Acad. Sci. USA, 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, J.1    Staehelin, T.2    Gordon, J.3
  • 65
    • 85046112389 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in proteins of maize seedlings
    • Trojanek, J., Ek, P.S., Muszyñska, G. and Engström, L. (1996) Tyrosine phosphorylation in proteins of maize seedlings. Eur. J. Biochem. 253, 338-344.
    • (1996) Eur. J. Biochem. , vol.253 , pp. 338-344
    • Trojanek, J.1    Ek, P.S.2    Muszyñska, G.3    Engström, L.4
  • 66
    • 0026542305 scopus 로고
    • Profilins constitute a novel family of functional plant pan-allergens
    • Valenta, R., Duchene, M., Ebner, C., et al. (1992) Profilins constitute a novel family of functional plant pan-allergens. J. Exp. Med. 175, 377-385.
    • (1992) J. Exp. Med. , vol.175 , pp. 377-385
    • Valenta, R.1    Duchene, M.2    Ebner, C.3
  • 67
    • 0025887036 scopus 로고
    • Identification of profilin as a novel pollen allergen; IgE autoreactivity in sensitized individuals
    • Valenta, R., Duchene, M., Pettenburger, K., et al. (1991) Identification of profilin as a novel pollen allergen; IgE autoreactivity in sensitized individuals. Science, 253, 557-560.
    • (1991) Science , vol.253 , pp. 557-560
    • Valenta, R.1    Duchene, M.2    Pettenburger, K.3
  • 68
    • 0027364291 scopus 로고
    • Identification of profilin as an actin-binding protein in higher plants
    • Valenta, R., Ferreira, F., Grote, M., et al. (1993) Identification of profilin as an actin-binding protein in higher plants. J. Biol. Chem. 268, 22777-22781.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22777-22781
    • Valenta, R.1    Ferreira, F.2    Grote, M.3
  • 69
    • 0031432209 scopus 로고    scopus 로고
    • Probing the plant-actin cytoskeleton during cytokinesis and interphase by profilin microinjection
    • Valster, A.M., Pierson, E.S., Valenta, R., Hepler, P.K. and Emons, A.M.C. (1997) Probing the plant-actin cytoskeleton during cytokinesis and interphase by profilin microinjection. Plant Cell. 9, 1815-1824.
    • (1997) Plant Cell. , vol.9 , pp. 1815-1824
    • Valster, A.M.1    Pierson, E.S.2    Valenta, R.3    Hepler, P.K.4    Emons, A.M.C.5
  • 70
    • 0030909875 scopus 로고    scopus 로고
    • Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum
    • Vidali, L. and Hepler, P.K. (1997) Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum. Cell Motil. Cytoskeleton, 36, 323-338.
    • (1997) Cell Motil. Cytoskeleton , vol.36 , pp. 323-338
    • Vidali, L.1    Hepler, P.K.2
  • 72
    • 0030911424 scopus 로고    scopus 로고
    • P140mDia, a mammalian homolog of Drosophila diaphanos, is a target protein for Rho small GTPase and is a ligand for profilin
    • Watanabe, N., Madaule, P., Reid, T., et al. (1997) p140mDia, a mammalian homolog of Drosophila diaphanos, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16, 3044-3056.
    • (1997) EMBO J. , vol.16 , pp. 3044-3056
    • Watanabe, N.1    Madaule, P.2    Reid, T.3
  • 73
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch, M.D., Iwamatsu, A. and Mitchinson, T.J. (1997) Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature, 385, 265-269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchinson, T.J.3
  • 74
    • 0032479578 scopus 로고    scopus 로고
    • Interaction between the human Arp2/3 complex and Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch, M.D., Rosenblatt, J., Skoble, J., Portnoy, D.A. and Mitchinson, T.J. (1998) Interaction between the human Arp2/3 complex and Listeria monocytogenes ActA protein in actin filament nucleation. Science, 281, 105-108.
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchinson, T.J.5
  • 75
    • 0032076827 scopus 로고    scopus 로고
    • Molecular characterization of a tyrosine-specific protein phosphatase encoded by a stress-responsive gene in Arabidopsis
    • Xu, Q., Fu, H.-H., Gupta, R. and Luan, S. (1998) Molecular characterization of a tyrosine-specific protein phosphatase encoded by a stress-responsive gene in Arabidopsis. Plant Cell, 10, 849-857.
    • (1998) Plant Cell , vol.10 , pp. 849-857
    • Xu, Q.1    Fu, H.-H.2    Gupta, R.3    Luan, S.4
  • 76
    • 0000514378 scopus 로고
    • Association of phosphatidylinositol 4-kinase with the plant cytoskeleton
    • Xu, P., Lloyd, C.W., Staiger, C.J. and Drøbak, B.K. (1992) Association of phosphatidylinositol 4-kinase with the plant cytoskeleton. Plant Cell, 4, 941-951.
    • (1992) Plant Cell , vol.4 , pp. 941-951
    • Xu, P.1    Lloyd, C.W.2    Staiger, C.J.3    Drøbak, B.K.4
  • 77
    • 0027463634 scopus 로고
    • Purification and characterization of a phosphatidylinositol 4-kinase activator in carrot cells
    • Yang, W., Burkhart, W., Cavallius, J., Merick, W.C. and Boss, W.F. (1993) Purification and characterization of a phosphatidylinositol 4-kinase activator in carrot cells. J. Biol. Chem. 268, 392-398.
    • (1993) J. Biol. Chem. , vol.268 , pp. 392-398
    • Yang, W.1    Burkhart, W.2    Cavallius, J.3    Merick, W.C.4    Boss, W.F.5
  • 78
    • 0000806896 scopus 로고    scopus 로고
    • Actin-bundling protein isolated from pollen tubes of Lily
    • Yokota, E., Takahara, K. and Shimmen, T. (1998) Actin-bundling protein isolated from pollen tubes of Lily. Plant Physiol. 116, 1421-1429.
    • (1998) Plant Physiol. , vol.116 , pp. 1421-1429
    • Yokota, E.1    Takahara, K.2    Shimmen, T.3
  • 79
    • 0032033087 scopus 로고    scopus 로고
    • Molecular cloning and mRNA localization of tomato pollen profilin
    • Yu, L.X., Nasrallah, J., Valenta, R. and Parthasarathy, M.V. (1998) Molecular cloning and mRNA localization of tomato pollen profilin. Plant Mol. Biol. 36, 699-707.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 699-707
    • Yu, L.X.1    Nasrallah, J.2    Valenta, R.3    Parthasarathy, M.V.4
  • 81
    • 0032505113 scopus 로고    scopus 로고
    • Actin cytoskeleton: The Arp2/3 complex gets to the point
    • Zigmond, S.H. (1998) Actin cytoskeleton: The Arp2/3 complex gets to the point. Curr. Biol. 8, R654-R657.
    • (1998) Curr. Biol. , vol.8
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.