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Volumn 160, Issue 3, 2012, Pages 1597-1612

Genomics and localization of the arabidopsis DHHC-cysteine-rich domain s-acyltransferase protein family

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EID: 84868324295     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.112.203968     Document Type: Article
Times cited : (80)

References (70)
  • 1
    • 30944443590 scopus 로고    scopus 로고
    • Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis
    • Abrami L, Leppla SH, van der Goot FG (2006) Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis. J Cell Biol 172: 309-320
    • (2006) J Cell Biol , vol.172 , pp. 309-320
    • Abrami, L.1    Leppla, S.H.2    van der Goot, F.G.3
  • 2
    • 33846159104 scopus 로고    scopus 로고
    • Plant G protein heterotrimers require dual lipidation motifs of Ga and Gg and do not dissociate upon activation
    • Adjobo-Hermans MJ, Goedhart J, Gadella TW Jr (2006) Plant G protein heterotrimers require dual lipidation motifs of Ga and Gg and do not dissociate upon activation. J Cell Sci 119: 5087-5097
    • (2006) J Cell Sci , vol.119 , pp. 5087-5097
    • Adjobo-Hermans, M.J.1    Goedhart, J.2    Gadella Jr., T.W.3
  • 4
    • 61449149636 scopus 로고    scopus 로고
    • Palmitoylation cycles and regulation of protein function (Review)
    • Baekkeskov S, Kanaani J (2009) Palmitoylation cycles and regulation of protein function (Review). Mol Membr Biol 26: 42-54
    • (2009) Mol Membr Biol , vol.26 , pp. 42-54
    • Baekkeskov, S.1    Kanaani, J.2
  • 6
    • 84863480170 scopus 로고    scopus 로고
    • S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses
    • Batisti_c O, Rehers M, Akerman A, Schlücking K, Steinhorst L, Yalovsky S, Kudla J (2012) S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses. Cell Res 22: 1155-1168
    • (2012) Cell Res , vol.22 , pp. 1155-1168
    • Batistic, O.1    Rehers, M.2    Akerman, A.3    Schlücking, K.4    Steinhorst, L.5    Yalovsky, S.6    Kudla, J.7
  • 8
    • 73849141867 scopus 로고    scopus 로고
    • CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores
    • Batisti_c O, Waadt R, Steinhorst L, Held K, Kudla J (2010) CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores. Plant J 61: 211-222
    • (2010) Plant J , vol.61 , pp. 211-222
    • Batistic, O.1    Waadt, R.2    Steinhorst, L.3    Held, K.4    Kudla, J.5
  • 10
    • 0037051906 scopus 로고    scopus 로고
    • Differential stability of tetraspanin/tetraspanin interactions: Role of palmitoylation
    • Charrin S, Manié S, Oualid M, Billard M, Boucheix C, Rubinstein E (2002) Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation. FEBS Lett 516: 139-144
    • (2002) FEBS Lett , vol.516 , pp. 139-144
    • Charrin, S.1    Manié, S.2    Oualid, M.3    Billard, M.4    Boucheix, C.5    Rubinstein, E.6
  • 11
    • 77949505988 scopus 로고    scopus 로고
    • PALM: A paralleled and integrated framework for phylogenetic inference with automatic likelihood model selectors
    • Chen SH, Su SY, Lo CZ, Chen KH, Huang TJ, Kuo BH, Lin CY (2009) PALM: a paralleled and integrated framework for phylogenetic inference with automatic likelihood model selectors. PLoS ONE 4: e8116
    • (2009) PLoS ONE , vol.4
    • Chen, S.H.1    Su, S.Y.2    Lo, C.Z.3    Chen, K.H.4    Huang, T.J.5    Kuo, B.H.6    Lin, C.Y.7
  • 14
    • 64249172320 scopus 로고    scopus 로고
    • A novel motif at the C-terminus of palmitoyltransferases is essential for Swf1 and Pfa3 function in vivo
    • González Montoro A, Quiroga R, Maccioni HJ, Valdez Taubas J (2009) A novel motif at the C-terminus of palmitoyltransferases is essential for Swf1 and Pfa3 function in vivo. Biochem J 419: 301-308
    • (2009) Biochem J , vol.419 , pp. 301-308
    • González Montoro, A.1    Quiroga, R.2    Maccioni, H.J.3    Valdez Taubas, J.4
  • 15
    • 79957617680 scopus 로고    scopus 로고
    • The palmitoyl transferase DHHC2 targets a dynamic membrane cycling pathway: Regulation by a C-terminal domain
    • Greaves J, Carmichael JA, Chamberlain LH (2011) The palmitoyl transferase DHHC2 targets a dynamic membrane cycling pathway: regulation by a C-terminal domain. Mol Biol Cell 22: 1887-1895
    • (2011) Mol Biol Cell , vol.22 , pp. 1887-1895
    • Greaves, J.1    Carmichael, J.A.2    Chamberlain, L.H.3
  • 16
    • 17844378983 scopus 로고    scopus 로고
    • The human Kv11 channel is palmitoylated, modulating voltage sensing: Identification of a palmitoylation consensus sequence
    • Gubitosi-Klug RA, Mancuso DJ, Gross RW (2005) The human Kv1.1 channel is palmitoylated, modulating voltage sensing: Identification of a palmitoylation consensus sequence. Proc Natl Acad Sci USA 102: 5964-5968
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5964-5968
    • Gubitosi-Klug, R.A.1    Mancuso, D.J.2    Gross, R.W.3
  • 17
    • 0033499326 scopus 로고    scopus 로고
    • Plant protein serine/threonine kinases: Classification and functions
    • Hardie DG (1999) Plant protein serine/threonine kinases: classification and functions. Annu Rev Plant Physiol Plant Mol Biol 50: 97-131
    • (1999) Annu Rev Plant Physiol Plant Mol Biol , vol.50 , pp. 97-131
    • Hardie, D.G.1
  • 18
    • 61449113906 scopus 로고    scopus 로고
    • Protein S-acylation in plants (Review)
    • Hemsley PA (2009) Protein S-acylation in plants (Review). Mol Membr Biol 26: 114-125
    • (2009) Mol Membr Biol , vol.26 , pp. 114-125
    • Hemsley, P.A.1
  • 19
    • 44649139158 scopus 로고    scopus 로고
    • Multiple roles for protein palmitoylation in plants
    • Hemsley PA, Grierson CS (2008) Multiple roles for protein palmitoylation in plants. Trends Plant Sci 13: 295-302
    • (2008) Trends Plant Sci , vol.13 , pp. 295-302
    • Hemsley, P.A.1    Grierson, C.S.2
  • 20
    • 82955207208 scopus 로고    scopus 로고
    • The ankyrin repeats and DHHC S-acyl transferase domain of AKR1 act independently to regulate switching from vegetative to mating states in yeast
    • Hemsley PA, Grierson CS (2011) The ankyrin repeats and DHHC S-acyl transferase domain of AKR1 act independently to regulate switching from vegetative to mating states in yeast. PLoS ONE 6: e28799
    • (2011) PLoS ONE , vol.6
    • Hemsley, P.A.1    Grierson, C.S.2
  • 21
    • 30844460508 scopus 로고    scopus 로고
    • The TIP GROWTH DEFECTIVE1 S-acyl transferase regulates plant cell growth in Arabidopsis
    • Hemsley PA, Kemp AC, Grierson CS (2005) The TIP GROWTH DEFECTIVE1 S-acyl transferase regulates plant cell growth in Arabidopsis. Plant Cell 17: 2554-2563
    • (2005) Plant Cell , vol.17 , pp. 2554-2563
    • Hemsley, P.A.1    Kemp, A.C.2    Grierson, C.S.3
  • 23
    • 67649882018 scopus 로고    scopus 로고
    • Analysis of DHHC acyltransferases implies overlapping substrate specificity and a two-step reaction mechanism
    • Hou H, John Peter AT, Meiringer C, Subramanian K, Ungermann C (2009) Analysis of DHHC acyltransferases implies overlapping substrate specificity and a two-step reaction mechanism. Traffic 10: 1061-1073
    • (2009) Traffic , vol.10 , pp. 1061-1073
    • Hou, H.1    John Peter, A.T.2    Meiringer, C.3    Subramanian, K.4    Ungermann, C.5
  • 25
    • 2442600242 scopus 로고    scopus 로고
    • Numerous posttranslational modifications provide opportunities for the intricate regulation of metabolic enzymes at multiple levels
    • Huber SC, Hardin SC (2004) Numerous posttranslational modifications provide opportunities for the intricate regulation of metabolic enzymes at multiple levels. Curr Opin Plant Biol 7: 318-322
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 318-322
    • Huber, S.C.1    Hardin, S.C.2
  • 26
    • 0037336675 scopus 로고    scopus 로고
    • The first 238 amino acids of the human lamin B receptor are targeted to the nuclear envelope in plants
    • Irons SL, Evans DE, Brandizzi F (2003) The first 238 amino acids of the human lamin B receptor are targeted to the nuclear envelope in plants. J Exp Bot 54: 943-950
    • (2003) J Exp Bot , vol.54 , pp. 943-950
    • Irons, S.L.1    Evans, D.E.2    Brandizzi, F.3
  • 28
    • 0027516185 scopus 로고
    • One-step purification of recombinant human papillomavirus type 16 E7 oncoprotein and its binding to the retinoblastoma gene product
    • Kasher MS, Wakulchik M, Cook JA, Smith MC (1993) One-step purification of recombinant human papillomavirus type 16 E7 oncoprotein and its binding to the retinoblastoma gene product. Biotechniques 14: 630-641
    • (1993) Biotechniques , vol.14 , pp. 630-641
    • Kasher, M.S.1    Wakulchik, M.2    Cook, J.A.3    Smith, M.C.4
  • 29
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • Katoh K, Toh H (2008) Recent developments in the MAFFT multiple sequence alignment program. Brief Bioinform 9: 286-298
    • (2008) Brief Bioinform , vol.9 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 30
    • 0842328861 scopus 로고    scopus 로고
    • Calcium sensors and their interacting protein kinases: Genomics of the Arabidopsis and rice CBL-CIPK signaling networks
    • Kolukisaoglu U, Weinl S, Blazevic D, Batisti_c O, Kudla J (2004) Calcium sensors and their interacting protein kinases: genomics of the Arabidopsis and rice CBL-CIPK signaling networks. Plant Physiol 134: 43-58
    • (2004) Plant Physiol , vol.134 , pp. 43-58
    • Kolukisaoglu, U.1    Weinl, S.2    Blazevic, D.3    Batistic, O.4    Kudla, J.5
  • 31
    • 45949109669 scopus 로고    scopus 로고
    • MEGA: A biologist-centric software for evolutionary analysis of DNA and protein sequences
    • Kumar S, Nei M, Dudley J, Tamura K (2008) MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences. Brief Bioinform 9: 299-306
    • (2008) Brief Bioinform , vol.9 , pp. 299-306
    • Kumar, S.1    Nei, M.2    Dudley, J.3    Tamura, K.4
  • 34
    • 33845934490 scopus 로고    scopus 로고
    • Ankyrin repeat: A unique motif mediating protein-protein interactions
    • Li J, Mahajan A, Tsai MD (2006) Ankyrin repeat: a unique motif mediating protein-protein interactions. Biochemistry 45: 15168-15178
    • (2006) Biochemistry , vol.45 , pp. 15168-15178
    • Li, J.1    Mahajan, A.2    Tsai, M.D.3
  • 35
    • 77951225186 scopus 로고    scopus 로고
    • DHHC5 interacts with PDZ domain 3 of postsynaptic density-95 (PSD-95) protein and plays a role in learning and memory
    • Li Y, Hu J, Höfer K, Wong AM, Cooper JD, Birnbaum SG, Hammer RE, Hofmann SL (2010) DHHC5 interacts with PDZ domain 3 of postsynaptic density-95 (PSD-95) protein and plays a role in learning and memory. J Biol Chem 285: 13022-13031
    • (2010) J Biol Chem , vol.285 , pp. 13022-13031
    • Li, Y.1    Hu, J.2    Höfer, K.3    Wong, A.M.4    Cooper, J.D.5    Birnbaum, S.G.6    Hammer, R.E.7    Hofmann, S.L.8
  • 36
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • Lobo S, Greentree WK, Linder ME, Deschenes RJ (2002) Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J Biol Chem 277: 41268-41273
    • (2002) J Biol Chem , vol.277 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 37
    • 0142057022 scopus 로고    scopus 로고
    • Protein phosphatases in plants
    • Luan S (2003) Protein phosphatases in plants. Annu Rev Plant Biol 54: 63-92
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 63-92
    • Luan, S.1
  • 38
    • 79952116426 scopus 로고    scopus 로고
    • InterPro protein classification
    • McDowall J, Hunter S (2011) InterPro protein classification. Methods Mol Biol 694: 37-47
    • (2011) Methods Mol Biol , vol.694 , pp. 37-47
    • McDowall, J.1    Hunter, S.2
  • 39
    • 78649662343 scopus 로고    scopus 로고
    • Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes
    • Mitchell DA, Mitchell G, Ling Y, Budde C, Deschenes RJ (2010) Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes. J Biol Chem 285: 38104-38114
    • (2010) J Biol Chem , vol.285 , pp. 38104-38114
    • Mitchell, D.A.1    Mitchell, G.2    Ling, Y.3    Budde, C.4    Deschenes, R.J.5
  • 40
    • 33744826797 scopus 로고    scopus 로고
    • Protein palmitoylation by a family of DHHC protein S-acyltransferases
    • Mitchell DA, Vasudevan A, Linder ME, Deschenes RJ (2006) Protein palmitoylation by a family of DHHC protein S-acyltransferases. J Lipid Res 47: 1118-1127
    • (2006) J Lipid Res , vol.47 , pp. 1118-1127
    • Mitchell, D.A.1    Vasudevan, A.2    Linder, M.E.3    Deschenes, R.J.4
  • 41
    • 77950865637 scopus 로고    scopus 로고
    • Sumoylation and other ubiquitin-like posttranslational modifications in plants
    • Miura K, Hasegawa PM (2010) Sumoylation and other ubiquitin-like posttranslational modifications in plants. Trends Cell Biol 20: 223-232
    • (2010) Trends Cell Biol , vol.20 , pp. 223-232
    • Miura, K.1    Hasegawa, P.M.2
  • 42
    • 34848907786 scopus 로고    scopus 로고
    • Protein lipidation
    • Nadolski MJ, Linder ME (2007) Protein lipidation. FEBS J 274: 5202-5210
    • (2007) FEBS J , vol.274 , pp. 5202-5210
    • Nadolski, M.J.1    Linder, M.E.2
  • 43
    • 33646830442 scopus 로고    scopus 로고
    • Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins
    • Ohno Y, Kihara A, Sano T, Igarashi Y (2006) Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins. Biochim Biophys Acta 1761: 474-483
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 474-483
    • Ohno, Y.1    Kihara, A.2    Sano, T.3    Igarashi, Y.4
  • 44
    • 33748571452 scopus 로고    scopus 로고
    • Palmitoylation plays a role in targeting Vac8p to specific membrane subdomains
    • Peng Y, Tang F, Weisman LS (2006) Palmitoylation plays a role in targeting Vac8p to specific membrane subdomains. Traffic 7: 1378-1387
    • (2006) Traffic , vol.7 , pp. 1378-1387
    • Peng, Y.1    Tang, F.2    Weisman, L.S.3
  • 46
    • 0043123123 scopus 로고    scopus 로고
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments
    • Poirot O, O'Toole E, Notredame C (2003) Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments. Nucleic Acids Res 31: 3503-3506
    • (2003) Nucleic Acids Res , vol.31 , pp. 3503-3506
    • Poirot, O.1    O'Toole, E.2    Notredame, C.3
  • 47
    • 15044343147 scopus 로고    scopus 로고
    • Transmembrane topology of the protein palmitoyl transferase Akr1
    • Politis EG, Roth AF, Davis NG (2005) Transmembrane topology of the protein palmitoyl transferase Akr1. J Biol Chem 280: 10156-10163
    • (2005) J Biol Chem , vol.280 , pp. 10156-10163
    • Politis, E.G.1    Roth, A.F.2    Davis, N.G.3
  • 51
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase
    • Roth AF, Feng Y, Chen L, Davis NG (2002) The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase. J Cell Biol 159: 23-28
    • (2002) J Cell Biol , vol.159 , pp. 23-28
    • Roth, A.F.1    Feng, Y.2    Chen, L.3    Davis, N.G.4
  • 53
    • 0031860289 scopus 로고    scopus 로고
    • TIP1 is required for both tip growth and non-tip growth in Arabidopsis
    • Ryan E, Grierson CS, Cavell A, Steer M, Dolan L (1998) TIP1 is required for both tip growth and non-tip growth in Arabidopsis. New Phytol 138: 49-58
    • (1998) New Phytol , vol.138 , pp. 49-58
    • Ryan, E.1    Grierson, C.S.2    Cavell, A.3    Steer, M.4    Dolan, L.5
  • 55
    • 0027689370 scopus 로고
    • Pollen tube and roothair tip growth is disrupted in a mutant of Arabidopsis thaliana
    • Schiefelbein J, Galway M, Masucci J, Ford S (1993) Pollen tube and roothair tip growth is disrupted in a mutant of Arabidopsis thaliana. Plant Physiol 103: 979-985
    • (1993) Plant Physiol , vol.103 , pp. 979-985
    • Schiefelbein, J.1    Galway, M.2    Masucci, J.3    Ford, S.4
  • 57
    • 70450188170 scopus 로고    scopus 로고
    • Protein lipid modifications in signaling and subcellular targeting
    • Sorek N, Bloch D, Yalovsky S (2009) Protein lipid modifications in signaling and subcellular targeting. Curr Opin Plant Biol 12: 714-720
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 714-720
    • Sorek, N.1    Bloch, D.2    Yalovsky, S.3
  • 58
    • 33947266606 scopus 로고    scopus 로고
    • Activation status-coupled transient S acylation determines membrane partitioning of a plant Rho-related GTPase
    • Sorek N, Poraty L, Sternberg H, Bar E, Lewinsohn E, Yalovsky S (2007) Activation status-coupled transient S acylation determines membrane partitioning of a plant Rho-related GTPase. Mol Cell Biol 27: 2144-2154
    • (2007) Mol Cell Biol , vol.27 , pp. 2144-2154
    • Sorek, N.1    Poraty, L.2    Sternberg, H.3    Bar, E.4    Lewinsohn, E.5    Yalovsky, S.6
  • 60
    • 2542459287 scopus 로고    scopus 로고
    • The palmitoyltransferase of the cation-dependent mannose 6-phosphate receptor cycles between the plasma membrane and endosomes
    • Stöckli J, Rohrer J (2004) The palmitoyltransferase of the cation-dependent mannose 6-phosphate receptor cycles between the plasma membrane and endosomes. Mol Biol Cell 15: 2617-2626
    • (2004) Mol Biol Cell , vol.15 , pp. 2617-2626
    • Stöckli, J.1    Rohrer, J.2
  • 61
    • 45149098473 scopus 로고    scopus 로고
    • Post-translational modification of host proteins in pathogen-triggered defence signalling in plants
    • Stulemeijer IJ, Joosten MH (2008) Post-translational modification of host proteins in pathogen-triggered defence signalling in plants. Mol Plant Pathol 9: 545-560
    • (2008) Mol Plant Pathol , vol.9 , pp. 545-560
    • Stulemeijer, I.J.1    Joosten, M.H.2
  • 63
    • 0035801358 scopus 로고    scopus 로고
    • Ara6, a plantunique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana
    • Ueda T, Yamaguchi M, Uchimiya H, Nakano A (2001) Ara6, a plantunique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana. EMBO J 20: 4730-4741
    • (2001) EMBO J , vol.20 , pp. 4730-4741
    • Ueda, T.1    Yamaguchi, M.2    Uchimiya, H.3    Nakano, A.4
  • 64
    • 23044444831 scopus 로고    scopus 로고
    • Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation
    • Valdez-Taubas J, Pelham H (2005) Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation. EMBO J 24: 2524-2532
    • (2005) EMBO J , vol.24 , pp. 2524-2532
    • Valdez-Taubas, J.1    Pelham, H.2
  • 65
    • 44949161848 scopus 로고    scopus 로고
    • In planta visualization of protein interactions using bimolecular fluorescence complementation (BiFC)
    • 2008, pdbprot4995
    • Waadt R, Kudla J (2008) In planta visualization of protein interactions using bimolecular fluorescence complementation (BiFC). CSH Protoc 2008: pdb. prot4995
    • (2008) CSH Protoc
    • Waadt, R.1    Kudla, J.2
  • 67
    • 0032498794 scopus 로고    scopus 로고
    • Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole
    • Wang YX, Catlett NL, Weisman LS (1998) Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. J Cell Biol 140: 1063-1074
    • (1998) J Cell Biol , vol.140 , pp. 1063-1074
    • Wang, Y.X.1    Catlett, N.L.2    Weisman, L.S.3
  • 69
    • 76649102423 scopus 로고    scopus 로고
    • Proteome scale characterization of human S-acylated proteins in lipid raftenriched and non-raft membranes
    • Yang W, Di Vizio D, Kirchner M, Steen H, Freeman MR (2010) Proteome scale characterization of human S-acylated proteins in lipid raftenriched and non-raft membranes. Mol Cell Proteomics 9: 54-70
    • (2010) Mol Cell Proteomics , vol.9 , pp. 54-70
    • Yang, W.1    Di Vizio, D.2    Kirchner, M.3    Steen, H.4    Freeman, M.R.5
  • 70
    • 34250619111 scopus 로고    scopus 로고
    • Dual lipid modification of Arabidopsis Gg-subunits is required for efficient plasma membrane targeting
    • Zeng Q, Wang X, Running MP (2007) Dual lipid modification of Arabidopsis Gg-subunits is required for efficient plasma membrane targeting. Plant Physiol 143: 1119-1131
    • (2007) Plant Physiol , vol.143 , pp. 1119-1131
    • Zeng, Q.1    Wang, X.2    Running, M.P.3


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