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Volumn 40, Issue 9, 2013, Pages 5451-5464

Heterologous expression of rice calnexin (OsCNX) confers drought tolerance in Nicotiana tabacum

Author keywords

Abiotic stress; Ca2+ signaling; Calnexin; Draught; ER stress

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALNEXIN; MANNITOL;

EID: 84883283106     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-013-2643-y     Document Type: Article
Times cited : (41)

References (54)
  • 1
    • 77957758520 scopus 로고    scopus 로고
    • Calcineurin interacts with PERK and dephosphorylates calnexin to relieve ER stress in mammals and frogs
    • 10.1371/journal.pone.0011925 20700529
    • Bollo M, Paredes RM, Holstein D, Zheleznova N, Camacho P, Lechleiter JD (2010) Calcineurin interacts with PERK and dephosphorylates calnexin to relieve ER stress in mammals and frogs. PLoS One 5:e11925
    • (2010) PLoS One , vol.5 , pp. 11925
    • Bollo, M.1    Paredes, R.M.2    Holstein, D.3    Zheleznova, N.4    Camacho, P.5    Lechleiter, J.D.6
  • 2
    • 34250745700 scopus 로고    scopus 로고
    • The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation)
    • 10.1042/BJ20061890 1:CAS:528:DC%2BD2sXlvVShu78%3D 17521290
    • Brodsky JL (2007) The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation). Biochem J 404:353-363
    • (2007) Biochem J , vol.404 , pp. 353-363
    • Brodsky, J.L.1
  • 3
    • 71749088618 scopus 로고    scopus 로고
    • Calnexin phosphorylation attenuates the release of partially misfolded alpha 1-antitrypsin to the secretory pathway
    • 10.1074/jbc.M109.053165 1:CAS:528:DC%2BD1MXhsFWitLnL 19815548
    • Cameron PH, Chevet E, Pluquet O, Thomas DY, Bergeron JJ (2009) Calnexin phosphorylation attenuates the release of partially misfolded alpha 1-antitrypsin to the secretory pathway. J Biol Chem 284:34570-34579
    • (2009) J Biol Chem , vol.284 , pp. 34570-34579
    • Cameron, P.H.1    Chevet, E.2    Pluquet, O.3    Thomas, D.Y.4    Bergeron, J.J.5
  • 4
    • 79551669975 scopus 로고    scopus 로고
    • Die for living better: Plants modify root system architecture through inducing PCD in root meristem under severe water stress
    • 10.4161/psb.5.12.13811 21139433
    • Cao M, Li X (2010) Die for living better: plants modify root system architecture through inducing PCD in root meristem under severe water stress. Plant Signal Behav 5:1645-1646
    • (2010) Plant Signal Behav , vol.5 , pp. 1645-1646
    • Cao, M.1    Li, X.2
  • 5
    • 71749083375 scopus 로고    scopus 로고
    • Induced ER chaperones regulate a receptor-like kinase to mediate antiviral innate immune response in plants
    • 10.1016/j.chom.2009.10.005 1:CAS:528:DC%2BD1MXhsF2gs73J
    • Caplan JL, Zhu X, Mamillapalli P, Marathe R, Anandalakshmi R, Dinesh-Kumar SP (2009) Induced ER chaperones regulate a receptor-like kinase to mediate antiviral innate immune response in plants. Cell Host Microb 6:457-469
    • (2009) Cell Host Microb , vol.6 , pp. 457-469
    • Caplan, J.L.1    Zhu, X.2    Mamillapalli, P.3    Marathe, R.4    Anandalakshmi, R.5    Dinesh-Kumar, S.P.6
  • 6
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • 10.1074/jbc.R700048200 1:CAS:528:DC%2BD1cXksFagsrY%3D 18303019
    • Caramelo JJ, Parodi AJ (2008) Getting in and out from calnexin/calreticulin cycles. J Biol Chem 283:10221-10225
    • (2008) J Biol Chem , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 7
    • 0031867912 scopus 로고    scopus 로고
    • Effect of N-glycosylation on the folding and quality control of plant proteins
    • Ceirotti A, Duranti M, Bollini R (1998) Effect of N-glycosylation on the folding and quality control of plant proteins. J Exp Bot 49:1091-1103
    • (1998) J Exp Bot , vol.49 , pp. 1091-1103
    • Ceirotti, A.1    Duranti, M.2    Bollini, R.3
  • 8
    • 77952583799 scopus 로고    scopus 로고
    • Calnexin phosphorylation: Linking cytoplasmic signaling to endoplasmic reticulum lumenal functions
    • 10.1016/j.semcdb.2009.12.005 1:CAS:528:DC%2BC3cXmsleks7s%3D
    • Chevet E, Smirle J, Cameron PH, Thomas DY, Bergeron JJ (2010) Calnexin phosphorylation: linking cytoplasmic signaling to endoplasmic reticulum lumenal functions. Sem Cell Dev Biol 21:486-490
    • (2010) Sem Cell Dev Biol , vol.21 , pp. 486-490
    • Chevet, E.1    Smirle, J.2    Cameron, P.H.3    Thomas, D.Y.4    Bergeron, J.J.5
  • 9
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • 10.1016/0003-2697(87)90021-2 1:CAS:528:DyaL2sXitFSns7Y%3D
    • Chomczynski P, Sacchi N (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Annal Biochem 162:156-159
    • (1987) Annal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 10
    • 50649083308 scopus 로고    scopus 로고
    • A new branch of endoplasmic reticulum stress signaling and the osmotic signal converge on plant-specific asparagine-rich proteins to promote cell death
    • Costa MDL, Reis PAB, Valente MAS, Irsigler AST, Carvalho CM, Loureiro ME (2008) A new branch of endoplasmic reticulum stress signaling and the osmotic signal converge on plant-specific asparagine-rich proteins to promote cell death. J Biol Chem 283:20209-20219
    • (2008) J Biol Chem , vol.283 , pp. 20209-20219
    • Mdl, C.1    Pab, R.2    Mas, V.3    Ast, I.4    Carvalho, C.M.5    Loureiro, M.E.6
  • 11
    • 33344455077 scopus 로고    scopus 로고
    • The zinc-finger protein Zat12 plays a central role in reactive oxygen and abiotic stress signaling in Arabidopsis
    • 10.1104/pp.105.068254 1:CAS:528:DC%2BD2MXhtFCgsb7E 16183833
    • Davletova S, Schlauch K, Coutu J, Mittler R (2005) The zinc-finger protein Zat12 plays a central role in reactive oxygen and abiotic stress signaling in Arabidopsis. Plant Physiol 139:847-856
    • (2005) Plant Physiol , vol.139 , pp. 847-856
    • Davletova, S.1    Schlauch, K.2    Coutu, J.3    Mittler, R.4
  • 12
    • 79751529515 scopus 로고    scopus 로고
    • The evolutionary history of calreticulin and calnexin genes in green plants
    • 10.1007/s10709-010-9544-y 21222018
    • Del Bem LE (2011) The evolutionary history of calreticulin and calnexin genes in green plants. Genetica 139:255-259
    • (2011) Genetica , vol.139 , pp. 255-259
    • Del Bem, L.E.1
  • 13
    • 0000479431 scopus 로고
    • Isolation of plant DNA from fresh tissue
    • Doyle JJ, Doyle JL (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
  • 14
    • 77953174652 scopus 로고    scopus 로고
    • An endoplasmic reticulum response pathway mediates programmed cell death of root tip induced by water stress in Arabidopsis
    • 10.1111/j.1469-8137.2010.03207.x 1:CAS:528:DC%2BC3cXnsVejt7g%3D 20298483
    • Duan Y, Zhang W, Li B, Wang Y, Li K, Han C, Zhang Y, Li X (2010) An endoplasmic reticulum response pathway mediates programmed cell death of root tip induced by water stress in Arabidopsis. New Phytol 186:681-695
    • (2010) New Phytol , vol.186 , pp. 681-695
    • Duan, Y.1    Zhang, W.2    Li, B.3    Wang, Y.4    Li, K.5    Han, C.6    Zhang, Y.7    Li, X.8
  • 15
    • 0032706075 scopus 로고    scopus 로고
    • Calnexin from Pisum sativum: Cloning of the cDNA and characterization of the encoded protein
    • 10.1089/104454999314854 1:CAS:528:DyaK1MXnvVagsL0%3D 10595399
    • Ehtesham NZ, Phan TN, Gaikwad A, Sopory SK, Tuteja N (1999) Calnexin from Pisum sativum: cloning of the cDNA and characterization of the encoded protein. DNA Cell Biol 18:853-862
    • (1999) DNA Cell Biol , vol.18 , pp. 853-862
    • Ehtesham, N.Z.1    Phan, T.N.2    Gaikwad, A.3    Sopory, S.K.4    Tuteja, N.5
  • 16
    • 55849100775 scopus 로고    scopus 로고
    • A membrane-tethered transcription factor defines a branch of the heat stress response in Arabidopsis thaliana
    • USA
    • Gao H, Brandizzi F, Benning C, Larkin RM (2008) A membrane-tethered transcription factor defines a branch of the heat stress response in Arabidopsis thaliana. Proc Natl Acad Sci USA 105:16398-16403
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 16398-16403
    • Gao, H.1    Brandizzi, F.2    Benning, C.3    Larkin, R.M.4
  • 17
    • 0031131581 scopus 로고    scopus 로고
    • A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane
    • 10.1104/pp.114.1.345 1:CAS:528:DyaK2sXjtleht78%3D 9159955
    • Gillikin JW, Zhang F, Coleman CE, Bass HW, Larkins BA, Boston RS (1997) A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane. Plant Physiol 114:345-352
    • (1997) Plant Physiol , vol.114 , pp. 345-352
    • Gillikin, J.W.1    Zhang, F.2    Coleman, C.E.3    Bass, H.W.4    Larkins, B.A.5    Boston, R.S.6
  • 19
    • 0027415665 scopus 로고
    • Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein
    • 1:CAS:528:DyaK3sXkt1ejtLw%3D 8454626
    • Huang L, Franklin AE, Hoffman NE (1993) Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein. J Biol Chem 268:6560-6566
    • (1993) J Biol Chem , vol.268 , pp. 6560-6566
    • Huang, L.1    Franklin, A.E.2    Hoffman, N.E.3
  • 21
    • 43149097164 scopus 로고    scopus 로고
    • Molecular cloning and characterization of wheat calreticulin (CRT) gene involved in drought-stressed responses
    • Jia XY, Xu CY, Jing RL, Li RZ, Mao XG, Wang JP, Chang XP (2008) Molecular cloning and characterization of wheat calreticulin (CRT) gene involved in drought-stressed responses. J Exp Bot 59:739-751
    • (2008) J Exp Bot , vol.59 , pp. 739-751
    • Jia, X.Y.1    Xu, C.Y.2    Jing, R.L.3    Li, R.Z.4    Mao, X.G.5    Wang, J.P.6    Chang, X.P.7
  • 22
    • 69449095737 scopus 로고    scopus 로고
    • A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum
    • 10.1073/pnas.0906144106 1:CAS:528:DC%2BD1MXhtVKks73O 19597144
    • Jin H, Hong Z, Su W, Li J (2009) A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum. Proc Natl Acad Sci USA 106:13612-13617
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13612-13617
    • Jin, H.1    Hong, Z.2    Su, W.3    Li, J.4
  • 23
    • 22144447152 scopus 로고    scopus 로고
    • Gene expression in response to endoplasmic reticulum stress in Arabidopsis thaliana
    • 10.1111/j.1742-4658.2005.04770.x 1:CAS:528:DC%2BD2MXmtFKrurY%3D 15978049
    • Kamauchi S, Nakatani H, Nakano C, Urade R (2005) Gene expression in response to endoplasmic reticulum stress in Arabidopsis thaliana. FEBS J 272:3461-3476
    • (2005) FEBS J , vol.272 , pp. 3461-3476
    • Kamauchi, S.1    Nakatani, H.2    Nakano, C.3    Urade, R.4
  • 24
    • 67849103829 scopus 로고    scopus 로고
    • Calcium and calmodulin-mediated regulation of gene expression in plants
    • 10.1093/mp/ssn091 1:CAS:528:DC%2BD1MXovV2msbY%3D 19529824
    • Kim MC, Chung WS, Yun D, Cho MJ (2009) Calcium and calmodulin-mediated regulation of gene expression in plants. Mol Plant 2:13-21
    • (2009) Mol Plant , vol.2 , pp. 13-21
    • Kim, M.C.1    Chung, W.S.2    Yun, D.3    Cho, M.J.4
  • 25
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin
    • 10.1074/jbc.273.22.13367 1:CAS:528:DyaK1cXjvVejsLs%3D 9593662
    • Klee CB, Ren H, Wang X (1998) Regulation of the calmodulin-stimulated protein phosphatase, calcineurin. J Biol Chem 273:13367-13370
    • (1998) J Biol Chem , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 26
    • 0028832726 scopus 로고
    • Cloning of two cDNAs encoding calnexin-like proteins from maize (Zea mays) leaves: Identification of potential calcium-binding domains
    • 10.1016/0378-1119(95)00537-G
    • Kwiatkowski BA, Zielinkska-Kwiatkowska AG, Migdalski A, Kleczkowski LA, Wasilweska LD (1995) Cloning of two cDNAs encoding calnexin-like proteins from maize (Zea mays) leaves: identification of potential calcium-binding domains. Gene 65:219-222
    • (1995) Gene , vol.65 , pp. 219-222
    • Kwiatkowski, B.A.1    Zielinkska-Kwiatkowska, A.G.2    Migdalski, A.3    Kleczkowski, L.A.4    Wasilweska, L.D.5
  • 27
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • 10.1016/j.sbi.2009.06.004 1:CAS:528:DC%2BD1MXht1ylsLzP 19616933
    • Lederkremer GZ (2009) Glycoprotein folding, quality control and ER-associated degradation. Curr Opin Struct Biol 19:515-523
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 515-523
    • Lederkremer, G.Z.1
  • 28
    • 78049457576 scopus 로고    scopus 로고
    • Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants
    • 10.1105/tpc.110.078154 1:CAS:528:DC%2BC3cXhsVKjs7rP 20876830
    • Liu JX, Howell SH (2010) Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants. Plant Cell 22:2930-2942
    • (2010) Plant Cell , vol.22 , pp. 2930-2942
    • Liu, J.X.1    Howell, S.H.2
  • 29
    • 79960039043 scopus 로고    scopus 로고
    • The endoplasmic reticulum-associated degradation is necessary for plant salt tolerance
    • 10.1038/cr.2010.181 1:CAS:528:DC%2BC3MXmvFOgurw%3D 21187857
    • Liu L, Cui F, Li Q, Yin B, Zhang H, Lin B, Wu Y, Xia R, Tang S, Xie Q (2011) The endoplasmic reticulum-associated degradation is necessary for plant salt tolerance. Cell Res 21:957-969
    • (2011) Cell Res , vol.21 , pp. 957-969
    • Liu, L.1    Cui, F.2    Li, Q.3    Yin, B.4    Zhang, H.5    Lin, B.6    Wu, Y.7    Xia, R.8    Tang, S.9    Xie, Q.10
  • 30
    • 58149500279 scopus 로고    scopus 로고
    • The CBL-CIPK network in plant calcium signaling
    • 10.1016/j.tplants.2008.10.005 1:CAS:528:DC%2BD1MXntVyhuw%3D%3D 19054707
    • Luan S (2009) The CBL-CIPK network in plant calcium signaling. Trends Plant Sci 14:37-42
    • (2009) Trends Plant Sci , vol.14 , pp. 37-42
    • Luan, S.1
  • 31
    • 0242437811 scopus 로고    scopus 로고
    • Calreticulin is an upstream regulator of calcineurin
    • 10.1016/j.bbrc.2003.08.040 1:CAS:528:DC%2BD3sXovVeit7Y%3D 14623303
    • Lynch J, Michalak M (2003) Calreticulin is an upstream regulator of calcineurin. Biochem Biophys Res Commun 311:1173-1179
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 1173-1179
    • Lynch, J.1    Michalak, M.2
  • 32
    • 23144451257 scopus 로고    scopus 로고
    • ERAD: The long road to destruction
    • 10.1038/ncb0805-766 1:CAS:528:DC%2BD2MXmvVCltbw%3D 16056268
    • Meusser B, Hirsch C, Jarosch E, Sommer T (2005) ERAD: the long road to destruction. Nat Cell Biol 7:766-772
    • (2005) Nat Cell Biol , vol.7 , pp. 766-772
    • Meusser, B.1    Hirsch, C.2    Jarosch, E.3    Sommer, T.4
  • 33
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco cultures
    • 10.1111/j.1399-3054.1962.tb08052.x 1:CAS:528:DyaF3sXksFKm
    • Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco cultures. Physiol Plant 15:473-479
    • (1962) Physiol Plant , vol.15 , pp. 473-479
    • Murashige, T.1    Skoog, F.2
  • 35
    • 0027982729 scopus 로고
    • Calreticulin: Not just another calcium-binding protein
    • 10.1007/BF00925962 1:CAS:528:DyaK2cXmslCmtrw%3D 7816058
    • Nash PD, Opas M, Michalak M (1994) Calreticulin: not just another calcium-binding protein. Mol Cell Biochem 135:71-78
    • (1994) Mol Cell Biochem , vol.135 , pp. 71-78
    • Nash, P.D.1    Opas, M.2    Michalak, M.3
  • 36
    • 4344598305 scopus 로고    scopus 로고
    • Nck-dependent activation of extracellular signal-regulated kinase-1 and regulation of cell survival during endoplasmic reticulum stress
    • 10.1091/mbc.E03-11-0851 1:CAS:528:DC%2BD2cXnt1ektr0%3D 15201339
    • Nguyen DT, Kebache S, Fazel A, Wong HN, Jenna S, Emadali A (2004) Nck-dependent activation of extracellular signal-regulated kinase-1 and regulation of cell survival during endoplasmic reticulum stress. Mol Biol Cell 15:4248-4260
    • (2004) Mol Biol Cell , vol.15 , pp. 4248-4260
    • Nguyen, D.T.1    Kebache, S.2    Fazel, A.3    Wong, H.N.4    Jenna, S.5    Emadali, A.6
  • 37
    • 77952389740 scopus 로고    scopus 로고
    • Comparative analysis of soybean plasma membrane proteins under osmotic stress using gel-based and LC MS/MS-based proteomics approaches
    • 10.1002/pmic.200900632 1:CAS:528:DC%2BC3cXmtVyltbs%3D 20209511
    • Nouri MZ, Komatsu S (2010) Comparative analysis of soybean plasma membrane proteins under osmotic stress using gel-based and LC MS/MS-based proteomics approaches. Proteomics 10:1930-1945
    • (2010) Proteomics , vol.10 , pp. 1930-1945
    • Nouri, M.Z.1    Komatsu, S.2
  • 38
    • 84855955817 scopus 로고    scopus 로고
    • Characterization of calnexin in soybean roots and hypocotyls under osmotic stress
    • 10.1016/j.phytochem.2011.11.005 1:CAS:528:DC%2BC38Xht1Wqtbw%3D 22169501
    • Nouri MZ, Hiraga S, Yanagawa Y, Sunohara Y, Matsumoto H, Komatsu S (2012) Characterization of calnexin in soybean roots and hypocotyls under osmotic stress. Phytochemistry 74:20-29
    • (2012) Phytochemistry , vol.74 , pp. 20-29
    • Nouri, M.Z.1    Hiraga, S.2    Yanagawa, Y.3    Sunohara, Y.4    Matsumoto, H.5    Komatsu, S.6
  • 39
    • 0027057336 scopus 로고
    • Casein kinase II phosphorylation of signal sequence receptor alpha and the associated membrane chaperone calnexin
    • 1:CAS:528:DyaK38XmtVOlt7k%3D 1331100
    • Ou WJ, Thomas DY, Bell AW, Bergeron JJ (1992) Casein kinase II phosphorylation of signal sequence receptor alpha and the associated membrane chaperone calnexin. J Biol Chem 267:23789-23796
    • (1992) J Biol Chem , vol.267 , pp. 23789-23796
    • Ou, W.J.1    Thomas, D.Y.2    Bell, A.W.3    Bergeron, J.J.4
  • 40
    • 0033756733 scopus 로고    scopus 로고
    • A DNA helicase from Pisum sativum is homologous to translation initiation factor and stimulates topoisomerase activity
    • 10.1046/j.1365-313x.2000.00869.x 1:CAS:528:DC%2BD3cXosFSrt7Y%3D 11069696
    • Pham XH, Reddy MK, Ehtesham NZ, Matta B, Tuteja N (2000) A DNA helicase from Pisum sativum is homologous to translation initiation factor and stimulates topoisomerase activity. Plant J 24:219-229
    • (2000) Plant J , vol.24 , pp. 219-229
    • Pham, X.H.1    Reddy, M.K.2    Ehtesham, N.Z.3    Matta, B.4    Tuteja, N.5
  • 41
    • 0034640960 scopus 로고    scopus 로고
    • 2+ oscillations via an interaction with SERCA2b
    • 10.1083/jcb.149.6.1235 1:CAS:528:DC%2BD3cXktFansrs%3D 10851021
    • 2+ oscillations via an interaction with SERCA2b. J Cell Biol 149:1235-1248
    • (2000) J Cell Biol , vol.149 , pp. 1235-1248
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.3
  • 42
    • 84873134136 scopus 로고    scopus 로고
    • Calnexin: A candidate for crosstalk of ER stress and abiotic stress in plants
    • Glasgow, 1-4 July 2011
    • Sarwat M (2011) Calnexin: a candidate for crosstalk of ER stress and abiotic stress in plants. In: Society for experimental biology annual meeting 2011, Glasgow, 1-4 July 2011, p 4.26
    • (2011) : Society for Experimental Biology Annual Meeting 2011 , pp. 426
    • Sarwat, M.1
  • 43
    • 35348845440 scopus 로고    scopus 로고
    • Calnexin: A versatile calcium binding integral membrane chaperone of endoplasmic reticulum
    • Sarwat M, Tuteja N (2007) Calnexin: a versatile calcium binding integral membrane chaperone of endoplasmic reticulum. Calcium Bind Proteins 2:36-43
    • (2007) Calcium Bind Proteins , vol.2 , pp. 36-43
    • Sarwat, M.1    Tuteja, N.2
  • 44
    • 84883287677 scopus 로고    scopus 로고
    • Overexpression of rice calnexin protect transgenic tobacco plants from ER stress
    • Prague, 30 June-3 July 2010
    • Sarwat M, Tuteja N (2010) Overexpression of rice calnexin protect transgenic tobacco plants from ER stress. In: Society of experimental biology annual meeting 2010, Prague, 30 June-3 July 2010
    • (2010) : Society of Experimental Biology Annual Meeting 2010
    • Sarwat, M.1    Tuteja, N.2
  • 46
    • 84887999905 scopus 로고    scopus 로고
    • Phytohormones and microRNAs as sensors and regulators of leaf senescence: Assigning macro roles to small molecules
    • doi: 10.1016/j.biotechadv.2013.02.003
    • Sarwat M, Naqvi A R, Ahmad P, Ashraf M, Akram NA (2013b) Phytohormones and microRNAs as sensors and regulators of leaf senescence: assigning macro roles to small molecules. Biotech Adv. doi: 10.1016/j.biotechadv.2013.02.003
    • (2013) Biotech Adv
    • Sarwat, M.1    Naqvi, A.R.2    Ahmad, P.3    Ashraf, M.4    Akram, N.A.5
  • 47
    • 66449115640 scopus 로고    scopus 로고
    • The HSP90-SGT1 chaperone complex for NLR immune sensors
    • Shirasu K (2009) The HSP90-SGT1 chaperone complex for NLR immune sensors. Annu Rev Plant Biol 60:139-164
    • (2009) Annu Rev Plant Biol , vol.60 , pp. 139-164
    • Shirasu, K.1
  • 49
    • 34247210084 scopus 로고    scopus 로고
    • Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response
    • 10.1073/pnas.0611735104 1:CAS:528:DC%2BD2sXjtlaisbw%3D 17360436
    • Wang S, Narendra S, Fedoroff N (2007) Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response. Proc Natl Acad Sci USA 104:3817-3822
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 3817-3822
    • Wang, S.1    Narendra, S.2    Fedoroff, N.3
  • 50
    • 70350125202 scopus 로고    scopus 로고
    • 2+-decoding signaling network: Function and perspectives
    • 10.1111/j.1469-8137.2009.02938.x 1:CAS:528:DC%2BD1MXhsVOgs7vE 19860013
    • 2+-decoding signaling network: function and perspectives. New Phytol 184:517-528
    • (2009) New Phytol , vol.184 , pp. 517-528
    • Weinl, S.1    Kudla, J.2
  • 51
    • 0032479438 scopus 로고    scopus 로고
    • Conserved in vivo phosphorylation of calnexin at casein kinase II sites as well as a C/proline-directed kinase site
    • 10.1074/jbc.273.27.17227 1:CAS:528:DyaK1cXkt12hu7Y%3D 9642293
    • Wong HN, Ward MA, Bell AW, Chevet E, Bains S, Blackstock WP (1998) Conserved in vivo phosphorylation of calnexin at casein kinase II sites as well as a C/proline-directed kinase site. J Biol Chem 273:17227-17235
    • (1998) J Biol Chem , vol.273 , pp. 17227-17235
    • Wong, H.N.1    Ward, M.A.2    Bell, A.W.3    Chevet, E.4    Bains, S.5    Blackstock, W.P.6
  • 52
    • 79958043215 scopus 로고    scopus 로고
    • The unfolded protein response is triggered by a plant viral movement protein
    • 10.1104/pp.111.174110 1:CAS:528:DC%2BC3MXnvFWrtr4%3D 21474436
    • Ye C, Dickman MB, Whitham SA, Payton M, Verchot J (2011) The unfolded protein response is triggered by a plant viral movement protein. Plant Physiol 156:741-755
    • (2011) Plant Physiol , vol.156 , pp. 741-755
    • Ye, C.1    Dickman, M.B.2    Whitham, S.A.3    Payton, M.4    Verchot, J.5
  • 54
    • 2942755868 scopus 로고    scopus 로고
    • Signaling the unfolded protein response from the endoplasmic reticulum
    • 10.1074/jbc.R400008200 1:CAS:528:DC%2BD2cXkvVWhtb8%3D 15070890
    • Zhang K, Kaufman RJ (2004) Signaling the unfolded protein response from the endoplasmic reticulum. J Biol Chem 279:25935-25938
    • (2004) J Biol Chem , vol.279 , pp. 25935-25938
    • Zhang, K.1    Kaufman, R.J.2


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