메뉴 건너뛰기




Volumn 26, Issue 3, 2013, Pages 330-344

Structural basis for interactions of the Phytophthora sojae RxLR effector Avh5 with phosphatidylinositol 3-phosphate and for host cell entry

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; POLYPHOSPHOINOSITIDE; PROTEIN;

EID: 84874088579     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI-07-12-0184-R     Document Type: Article
Times cited : (52)

References (74)
  • 4
    • 84856104303 scopus 로고    scopus 로고
    • Endoplasmic reticulum PI (3) P lipid binding targets malaria proteins to the host cell
    • Bhattacharjee, S., Stahelin, R. V., Speicher, K. D., Speicher, D. W., and Haldar, K. 2012. Endoplasmic reticulum PI (3) P lipid binding targets malaria proteins to the host cell. Cell 148:201-212.
    • (2012) Cell , vol.148 , pp. 201-212
    • Bhattacharjee, S.1    Stahelin, R.V.2    Speicher, K.D.3    Speicher, D.W.4    Haldar, K.5
  • 8
    • 61349097249 scopus 로고    scopus 로고
    • Distinct amino acids of the Phytophthora infestans effector AVR3a condition activation of R3a hypersensitivity and suppression of cell death
    • Bos, J. I., Chaparro-Garcia, A., Quesada-Ocampo, L. M., McSpadden Gardener, B. B., and Kamoun, S. 2009. Distinct amino acids of the Phytophthora infestans effector AVR3a condition activation of R3a hypersensitivity and suppression of cell death. Mol. Plant-Microbe Interact. 22:269-281.
    • (2009) Mol. Plant-Microbe Interact. , vol.22 , pp. 269-281
    • Bos, J.I.1    Chaparro-Garcia, A.2    Quesada-Ocampo, L.M.3    McSpadden Gardener, B.B.4    Kamoun, S.5
  • 9
    • 80052281811 scopus 로고    scopus 로고
    • Structures of Phytophthora RXLR effector proteins: A conserved but adaptable fold underpins functional diversity
    • Boutemy, L. S., King, S. R., Win, J., Hughes, R. K., Clarke, T. A., Blumenschein, T. M., Kamoun, S., and Banfield, M. J. 2011. Structures of Phytophthora RXLR effector proteins: A conserved but adaptable fold underpins functional diversity. J. Biol. Chem. 286:35834-35842.
    • (2011) J. Biol. Chem. , vol.286 , pp. 35834-35842
    • Boutemy, L.S.1    King, S.R.2    Win, J.3    Hughes, R.K.4    Clarke, T.A.5    Blumenschein, T.M.6    Kamoun, S.7    Banfield, M.J.8
  • 10
    • 0026507634 scopus 로고
    • 3-and 4-Phosphorylated phosphatidylinositols in the aquatic plant Spirodela polyrhiza L
    • Brearley, C. A., and Hanke, D. E. 1992. 3-and 4-Phosphorylated phosphatidylinositols in the aquatic plant Spirodela polyrhiza L. Biochem. J. 283:255-260.
    • (1992) Biochem. J. , vol.283 , pp. 255-260
    • Brearley, C.A.1    Hanke, D.E.2
  • 11
    • 72449187567 scopus 로고    scopus 로고
    • DANGLE: A Bayesian inferential method for predicting protein backbone dihedral angles and secondary structure
    • Cheung, M. S., Maguire, M. L., Stevens, T. J., and Broadhurst, R. W. 2010. DANGLE: A Bayesian inferential method for predicting protein backbone dihedral angles and secondary structure. J. Magn. Reson. Ser. B 202:223-233.
    • (2010) J. Magn. Reson. Ser. B , vol.202 , pp. 223-233
    • Cheung, M.S.1    Maguire, M.L.2    Stevens, T.J.3    Broadhurst, R.W.4
  • 14
  • 16
    • 54849416178 scopus 로고    scopus 로고
    • RXLR-mediated entry of Phytophthora sojae effector Avr1b into soybean cells does not require pathogen-encoded machinery
    • Dou, D., Kale, S. D., Wang, X., Jiang, R. H., Bruce, N. A., Arredondo, F. D., Zhang, X., and Tyler, B. M. 2008b. RXLR-mediated entry of Phytophthora sojae effector Avr1b into soybean cells does not require pathogen-encoded machinery. Plant Cell 20:1930-1947.
    • (2008) Plant Cell , vol.20 , pp. 1930-1947
    • Dou, D.1    Kale, S.D.2    Wang, X.3    Jiang, R.H.4    Bruce, N.A.5    Arredondo, F.D.6    Zhang, X.7    Tyler, B.M.8
  • 17
    • 80052276859 scopus 로고    scopus 로고
    • Showdown at the RXLR motif: Serious differences of opinion in how effector proteins from filamentous eukaryotic pathogens enter plant cells
    • Ellis, J. G., and Dodds, P. N. 2011. Showdown at the RXLR motif: Serious differences of opinion in how effector proteins from filamentous eukaryotic pathogens enter plant cells. Proc. Natl. Acad. Sci. U. S. A. 108:14381-14382.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 14381-14382
    • Ellis, J.G.1    Dodds, P.N.2
  • 18
    • 32544456877 scopus 로고    scopus 로고
    • The problem of how fungal and oomycete avirulence proteins enter plant cells
    • Ellis, J., Catanzariti, A. M., and Dodds, P. 2006. The problem of how fungal and oomycete avirulence proteins enter plant cells. Trends Plant Sci. 11:61-63.
    • (2006) Trends Plant Sci. , vol.11 , pp. 61-63
    • Ellis, J.1    Catanzariti, A.M.2    Dodds, P.3
  • 20
    • 42249098860 scopus 로고    scopus 로고
    • PHytophthora infestans: The plant (and R gene) destroyer
    • Fry, W. 2008. Phytophthora infestans: The plant (and R gene) destroyer. Mol. Plant Pathol. 9:385-402.
    • (2008) Mol. Plant Pathol. , vol.9 , pp. 385-402
    • Fry, W.1
  • 22
    • 0000041361 scopus 로고
    • A common-sense approach to peak picking in 2-dimensional, 3-dimensional, and 4-dimensional spectra using automatic computer-analysis of contour diagrams
    • Garrett, D. S., Powers, R., Gronenborn, A. M., and Clore, G. M. 1991. A common-sense approach to peak picking in 2-dimensional, 3-dimensional, and 4-dimensional spectra using automatic computer-analysis of contour diagrams. J. Magn. Reson. 95:214-220.
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 23
    • 77953286311 scopus 로고    scopus 로고
    • Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy
    • Gautier, A., Mott, H. R., Bostock, M. J., Kirkpatrick, J. P., and Nietlispach, D. 2010. Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy. Nat. Struct. Mol. Biol. 17:768-774.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 768-774
    • Gautier, A.1    Mott, H.R.2    Bostock, M.J.3    Kirkpatrick, J.P.4    Nietlispach, D.5
  • 24
    • 46949102074 scopus 로고    scopus 로고
    • PHosphatidylinositol 4-phosphate accumulates extracellularly upon xylanase treatment in tomato cell suspensions
    • Gonorazky, G., Laxalt, A. M., Testerink, C., Munnik, T., and De La Canal, L. 2008. Phosphatidylinositol 4-phosphate accumulates extracellularly upon xylanase treatment in tomato cell suspensions. Plant Cell Environ. 31:1051-1062.
    • (2008) Plant Cell Environ. , vol.31 , pp. 1051-1062
    • Gonorazky, G.1    Laxalt, A.M.2    Testerink, C.3    Munnik, T.4    De La Canal, L.5
  • 25
    • 81355145249 scopus 로고    scopus 로고
    • PHosphatidylinositol 4-phosphate is associated to extracellular lipoproteic fractions and is detected in tomato apoplastic fluids
    • Gonorazky, G., Laxalt, A. M., Dekker, H. L., Rep, M., Munnik, T., Testerink, C., and De La Canal, L. 2012. Phosphatidylinositol 4-phosphate is associated to extracellular lipoproteic fractions and is detected in tomato apoplastic fluids. Plant Biol. (Stuttg.) 14:41-49.
    • (2012) Plant Biol. (Stuttg.) , vol.14 , pp. 41-49
    • Gonorazky, G.1    Laxalt, A.M.2    Dekker, H.L.3    Rep, M.4    Munnik, T.5    Testerink, C.6    De La Canal, L.7
  • 26
    • 58949099702 scopus 로고    scopus 로고
    • Plasmodium falciparum and Hyaloperonospora parasitica effector translocation motifs are functional in Phytophthora infestans
    • Grouffaud, S., Van West, P., Avrova, A. O., Birch, P. R., and Whisson, S. C. 2008. Plasmodium falciparum and Hyaloperonospora parasitica effector translocation motifs are functional in Phytophthora infestans. Microbiology 154:3743-3751.
    • (2008) Microbiology , vol.154 , pp. 3743-3751
    • Grouffaud, S.1    Van West, P.2    Avrova, A.O.3    Birch, P.R.4    Whisson, S.C.5
  • 27
    • 43949175202 scopus 로고
    • Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization
    • Grzesiek, S., Anglister, J., and Bax, A. 1993. Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization. J. Magn. Reson. 101:114-119.
    • (1993) J. Magn. Reson. , vol.101 , pp. 114-119
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 28
    • 80455150284 scopus 로고    scopus 로고
    • Rust secreted protein Ps87 is conserved in diverse fungal pathogens and contains a RXLR-like motif sufficient for translocation into plant cells
    • Gu, B., Kale, S. D., Wang, Q., Wang, D., Pan, Q., Cao, H., Meng, Y., Kang, Z., Tyler, B. M., and Shan, W. 2011. Rust secreted protein Ps87 is conserved in diverse fungal pathogens and contains a RXLR-like motif sufficient for translocation into plant cells. PLoS ONE 6:e27217. Published online.
    • (2011) PLoS ONE , vol.6
    • Gu, B.1    Kale, S.D.2    Wang, Q.3    Wang, D.4    Pan, Q.5    Cao, H.6    Meng, Y.7    Kang, Z.8    Tyler, B.M.9    Shan, W.10
  • 30
    • 0034932783 scopus 로고    scopus 로고
    • Signal and nutrient exchange at biotrophic plant-fungus interfaces
    • Hahn, M., and Mendgen, K. 2001. Signal and nutrient exchange at biotrophic plant-fungus interfaces. Curr. Opin. Plant Biol. 4:322-327.
    • (2001) Curr. Opin. Plant Biol. , vol.4 , pp. 322-327
    • Hahn, M.1    Mendgen, K.2
  • 32
    • 84871783446 scopus 로고    scopus 로고
    • Mechanisms and evolution of virulence in oomycetes
    • Jiang, R. H. Y., and Tyler, B. M. 2012. Mechanisms and evolution of virulence in oomycetes. Annu. Rev. Phytopathol. 50:295-318.
    • (2012) Annu. Rev. Phytopathol. , vol.50 , pp. 295-318
    • Jiang, R.H.Y.1    Tyler, B.M.2
  • 33
    • 42449116668 scopus 로고    scopus 로고
    • RXLR effector reservoir in two Phytophthora species is dominated by a single rapidly evolving superfamily with more than 700 members
    • Jiang, R. H., Tripathy, S., Govers, F., and Tyler, B. M. 2008. RXLR effector reservoir in two Phytophthora species is dominated by a single rapidly evolving superfamily with more than 700 members. Proc. Natl. Acad. Sci. U. S. A. 105:4874-4879.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 4874-4879
    • Jiang, R.H.1    Tripathy, S.2    Govers, F.3    Tyler, B.M.4
  • 34
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones, J. D., and Dangl, J. L. 2006. The plant immune system. Nature 444:323-329.
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.1    Dangl, J.L.2
  • 35
    • 81055138494 scopus 로고    scopus 로고
    • Entry of oomycete and fungal effectors into plant and animal host cells
    • Kale, S. D., and Tyler, B. M. 2011. Entry of oomycete and fungal effectors into plant and animal host cells. Cell Microbiol. 13:1839-1848.
    • (2011) Cell Microbiol. , vol.13 , pp. 1839-1848
    • Kale, S.D.1    Tyler, B.M.2
  • 37
    • 0035098276 scopus 로고    scopus 로고
    • Trafficking of phosphatidylinositol 3-phosphate from the trans-Golgi network to the lumen of the central vacuole in plant cells
    • Kim, D. H., Eu, Y. J., Yoo, C. M., Kim, Y. W., Pih, K. T., Jin, J. B., Kim, S. J., Stenmark, H., and Hwang, I. 2001. Trafficking of phosphatidylinositol 3-phosphate from the trans-Golgi network to the lumen of the central vacuole in plant cells. Plant Cell 13:287-301.
    • (2001) Plant Cell , vol.13 , pp. 287-301
    • Kim, D.H.1    Eu, Y.J.2    Yoo, C.M.3    Kim, Y.W.4    Pih, K.T.5    Jin, J.B.6    Kim, S.J.7    Stenmark, H.8    Hwang, I.9
  • 38
    • 34748816375 scopus 로고    scopus 로고
    • Mechanistic similarities in docking of the FYVE and PX domains to phosphatidylinositol 3-phosphate containing membranes
    • Kutateladze, T. G. 2007. Mechanistic similarities in docking of the FYVE and PX domains to phosphatidylinositol 3-phosphate containing membranes. Prog. Lipid Res. 46:315-327.
    • (2007) Prog. Lipid Res. , vol.46 , pp. 315-327
    • Kutateladze, T.G.1
  • 39
    • 77953762012 scopus 로고    scopus 로고
    • Translation of the phosphoinositide code by PI effectors
    • Kutateladze, T. G. 2010. Translation of the phosphoinositide code by PI effectors. Nat. Chem. Biol. 6:507-513.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 507-513
    • Kutateladze, T.G.1
  • 42
    • 48549097111 scopus 로고    scopus 로고
    • Roles of phosphatidylinositol 3-kinase in root hair growth
    • Lee, Y., Bak, G., Choi, Y., Chuang, W. I., and Cho, H. T. 2008. Roles of phosphatidylinositol 3-kinase in root hair growth. Plant Physiol. 147:624-635.
    • (2008) Plant Physiol. , vol.147 , pp. 624-635
    • Lee, Y.1    Bak, G.2    Choi, Y.3    Chuang, W.I.4    Cho, H.T.5
  • 43
    • 84855258469 scopus 로고    scopus 로고
    • Structural elucidation and functional characterization of the Hyaloperonospora arabidopsidis effector protein ATR13
    • Leonelli, L., Pelton, J., Schoeffler, A., Dahlbeck, D., Berger, J., Wemmer, D. E., and Staskawicz, B. 2011. Structural elucidation and functional characterization of the Hyaloperonospora arabidopsidis effector protein ATR13. PLoS Pathog. 7:e1002428. Published online.
    • (2011) PLoS Pathog. , vol.7
    • Leonelli, L.1    Pelton, J.2    Schoeffler, A.3    Dahlbeck, D.4    Berger, J.5    Wemmer, D.E.6    Staskawicz, B.7
  • 44
    • 84862811544 scopus 로고    scopus 로고
    • Patterns of plant subcellular responses to successful oomycete infections reveal differences in host cell reprogramming and endocytic trafficking
    • Lu, Y. J., Schornack, S., Spallek, T., Geldner, N., Chory, J., Schellmann, S., Schumacher, K., Kamoun, S., and Robatzek, S. 2012. Patterns of plant subcellular responses to successful oomycete infections reveal differences in host cell reprogramming and endocytic trafficking. Cell Microbiol. 14:682-697.
    • (2012) Cell Microbiol. , vol.14 , pp. 682-697
    • Lu, Y.J.1    Schornack, S.2    Spallek, T.3    Geldner, N.4    Chory, J.5    Schellmann, S.6    Schumacher, K.7    Kamoun, S.8    Robatzek, S.9
  • 45
    • 10344250457 scopus 로고    scopus 로고
    • Targeting malaria virulence and remodeling proteins to the host erythrocyte
    • Marti, M., Good, R. T., Rug, M., Knuepfer, E., and Cowman, A. F. 2004. Targeting malaria virulence and remodeling proteins to the host erythrocyte. Science 306:1930-1933.
    • (2004) Science , vol.306 , pp. 1930-1933
    • Marti, M.1    Good, R.T.2    Rug, M.3    Knuepfer, E.4    Cowman, A.F.5
  • 46
    • 0028981718 scopus 로고
    • Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells
    • Matsuoka, K., Bassham, D. C., Raikhel, N. V., and Nakamura, K. 1995. Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells. J. Cell Biol. 130:1307-1318.
    • (1995) J. Cell Biol. , vol.130 , pp. 1307-1318
    • Matsuoka, K.1    Bassham, D.C.2    Raikhel, N.V.3    Nakamura, K.4
  • 47
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R., and Kay, L. E. 1994. Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. Ser. B 103:203-216.
    • (1994) J. Magn. Reson. Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 48
    • 33746288421 scopus 로고    scopus 로고
    • Determining selectivity of phosphoinositide-binding domains
    • Narayan, K., and Lemmon, M. A. 2006. Determining selectivity of phosphoinositide-binding domains. Methods 39:122-133.
    • (2006) Methods , vol.39 , pp. 122-133
    • Narayan, K.1    Lemmon, M.A.2
  • 50
    • 77955889106 scopus 로고    scopus 로고
    • Internalization of flax rust avirulence proteins into flax and tobacco cells can occur in the absence of the pathogen
    • Rafiqi, M., Gan, P. H., Ravensdale, M., Lawrence, G. J., Ellis, J. G., Jones, D. A., Hardham, A. R., and Dodds, P. N. 2010. Internalization of flax rust avirulence proteins into flax and tobacco cells can occur in the absence of the pathogen. Plant Cell 22:2017-2032.
    • (2010) Plant Cell , vol.22 , pp. 2017-2032
    • Rafiqi, M.1    Gan, P.H.2    Ravensdale, M.3    Lawrence, G.J.4    Ellis, J.G.5    Jones, D.A.6    Hardham, A.R.7    Dodds, P.N.8
  • 51
    • 43149106933 scopus 로고    scopus 로고
    • PHospholipids are present in extracellular fluids of imbibing sunflower seeds and are modulated by hormonal treatments
    • Regente, M., Corti Monzon, G., and De La Canal, L. 2008. Phospholipids are present in extracellular fluids of imbibing sunflower seeds and are modulated by hormonal treatments. J. Exp. Bot. 59:553-562.
    • (2008) J. Exp. Bot. , vol.59 , pp. 553-562
    • Regente, M.1    Corti Monzon, G.2    De La Canal, L.3
  • 54
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • Sreerama, N., and Woody, R. W. 2004. Computation and analysis of protein circular dichroism spectra. Methods Enzymol. 383:318-351.
    • (2004) Methods Enzymol. , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 55
    • 60849100515 scopus 로고    scopus 로고
    • Common and contrasting themes in host cell-targeted effectors from bacterial, fungal, oomycete and nematode plant symbionts described using the Gene Ontology
    • Torto-Alalibo, T., Collmer, C. W., Lindeberg, M., Bird, D., Collmer, A., and Tyler, B. M. 2009. Common and contrasting themes in host cell-targeted effectors from bacterial, fungal, oomycete and nematode plant symbionts described using the Gene Ontology. BMC Microbiol. 9(Suppl. 1):S3.
    • (2009) BMC Microbiol. , vol.9 , Issue.SUPPL. 1
    • Torto-Alalibo, T.1    Collmer, C.W.2    Lindeberg, M.3    Bird, D.4    Collmer, A.5    Tyler, B.M.6
  • 57
    • 60849116153 scopus 로고    scopus 로고
    • Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology
    • Tseng, T. T., Tyler, B. M., and Setubal, J. C. 2009. Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology. BMC Microbiol 9:52.
    • (2009) BMC Microbiol , vol.9 , pp. 52
    • Tseng, T.T.1    Tyler, B.M.2    Setubal, J.C.3
  • 58
    • 0036031519 scopus 로고    scopus 로고
    • Molecular basis of recognition between Phytophthora pathogens and their hosts
    • Tyler, B. M. 2002. Molecular basis of recognition between Phytophthora pathogens and their hosts. Annu. Rev. Phytopathol. 40:137-167.
    • (2002) Annu. Rev. Phytopathol. , vol.40 , pp. 137-167
    • Tyler, B.M.1
  • 59
    • 33846110344 scopus 로고    scopus 로고
    • PHytophthora sojae: Root rot pathogen of soybean and model oomycete
    • Tyler, B. M. 2007. Phytophthora sojae: Root rot pathogen of soybean and model oomycete. Mol. Plant Pathol. 8:1-8.
    • (2007) Mol. Plant Pathol. , vol.8 , pp. 1-8
    • Tyler, B.M.1
  • 60
    • 58149293042 scopus 로고    scopus 로고
    • Entering and breaking: Virulence effector proteins of oomycete plant pathogens
    • Tyler, B. M. 2009. Entering and breaking: Virulence effector proteins of oomycete plant pathogens. Cell Microbiol. 11:13-20.
    • (2009) Cell Microbiol. , vol.11 , pp. 13-20
    • Tyler, B.M.1
  • 61
    • 81355158995 scopus 로고    scopus 로고
    • Entry of oomycete and fungal effectors into host cells
    • F. Martin and S. Kamoun, eds. Wiley-Blackwell, Oxford
    • Tyler, B. M. 2011. Entry of oomycete and fungal effectors into host cells. Pages 243-278 in: Effectors in Plant-Microbe Interactions. F. Martin and S. Kamoun, eds. Wiley-Blackwell, Oxford.
    • (2011) Effectors in Plant-Microbe Interactions , pp. 243-278
    • Tyler, B.M.1
  • 69
    • 84868311076 scopus 로고    scopus 로고
    • The avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans, forms homodimers through its predicted translocation region and does not specifically bind phospholipids
    • Wawra, S., Agacan, M., Boddey, J. A., Davidson, I., Gachon, C. M., Zanda, M., Grouffaud, S., Whisson, S. C., Birch, P. R., Porter, A. J., and Van West, P. 2012a. The avirulence protein 3a (AVR3a) from the potato pathogen Phytophthora infestans, forms homodimers through its predicted translocation region and does not specifically bind phospholipids. J. Biol. Chem. 287:38101-38109.
    • (2012) J. Biol. Chem. , vol.287 , pp. 38101-38109
    • Wawra, S.1    Agacan, M.2    Boddey, J.A.3    Davidson, I.4    Gachon, C.M.5    Zanda, M.6    Grouffaud, S.7    Whisson, S.C.8    Birch, P.R.9    Porter, A.J.10    Van West, P.11
  • 71
    • 59449105295 scopus 로고    scopus 로고
    • 2+-regulated pool of phosphatidylinositol-3-phosphate produced by phosphatidylinositol 3-kinase C2alpha on neurosecretory vesicles
    • 2+-regulated pool of phosphatidylinositol-3- phosphate produced by phosphatidylinositol 3-kinase C2alpha on neurosecretory vesicles. Mol. Biol. Cell 19:5593-5603.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5593-5603
    • Wen, P.J.1    Osborne, S.L.2    Morrow, I.C.3    Parton, R.G.4    Domin, J.5    Meunier, F.A.6
  • 73
    • 84857479035 scopus 로고    scopus 로고
    • Sequence divergent RXLR effectors share a structural fold conserved across plant pathogenic oomycete species
    • Win, J., Krasileva, K. V., Kamoun, S., Shirasu, K., Staskawicz, B. J., and Banfield, M. J. 2012. Sequence divergent RXLR effectors share a structural fold conserved across plant pathogenic oomycete species. PLoS Pathog. 8:e1002400. Published online.
    • (2012) PLoS Pathog. , vol.8
    • Win, J.1    Krasileva, K.V.2    Kamoun, S.3    Shirasu, K.4    Staskawicz, B.J.5    Banfield, M.J.6
  • 74
    • 80052302918 scopus 로고    scopus 로고
    • PHosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity
    • Yaeno, T., Li, H., Chaparro-Garcia, A., Schornack, S., Koshiba, S., Watanabe, S., Kigawa, T., Kamoun, S., and Shirasu, K. 2011. Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity. Proc. Natl. Acad. Sci. U. S. A. 108:14682-14687.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 14682-14687
    • Yaeno, T.1    Li, H.2    Chaparro-Garcia, A.3    Schornack, S.4    Koshiba, S.5    Watanabe, S.6    Kigawa, T.7    Kamoun, S.8    Shirasu, K.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.