메뉴 건너뛰기




Volumn 162, Issue 1, 2013, Pages 24-38

Specialized roles of the conserved subunit OST3/6 of the oligosaccharyltransferase complex in innate immunity and tolerance to abiotic stresses

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; AT1G61790 PROTEIN, ARABIDOPSIS; BRI1 PROTEIN, ARABIDOPSIS; CELLULASE; CELLULOSE; DOLICHYL DIPHOSPHOOLIGOSACCHARIDE PROTEIN GLYCOTRANSFERASE; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE - PROTEIN GLYCOTRANSFERASE; EFR PROTEIN, ARABIDOPSIS; GLYCOPROTEIN; GLYCOSYLTRANSFERASE; HYBRID PROTEIN; KOR1 PROTEIN, ARABIDOPSIS; MANNITOL; MEMBRANE PROTEIN; PATTERN RECOGNITION RECEPTOR; PROTEIN KINASE; SODIUM CHLORIDE; TUNICAMYCIN;

EID: 84877017128     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.113.215509     Document Type: Article
Times cited : (47)

References (64)
  • 1
    • 0347683429 scopus 로고    scopus 로고
    • Ultraviolet-C overexposure induces programmed cell death in Arabidopsis, which is mediated by caspase-like activities and which can be suppressed by caspase inhibitors, p35 and Defender against Apoptotic Death
    • Danon A, Rotari VI, Gordon A, Mailhac N, Gallois P (2004) Ultraviolet-C overexposure induces programmed cell death in Arabidopsis, which is mediated by caspase-like activities and which can be suppressed by caspase inhibitors, p35 and Defender against Apoptotic Death. J Biol Chem 279: 779-787
    • (2004) J Biol Chem , vol.279 , pp. 779-787
    • Danon, A.1    Rotari, V.I.2    Gordon, A.3    Mailhac, N.4    Gallois, P.5
  • 2
    • 80054083632 scopus 로고    scopus 로고
    • Arabidopsis thaliana alpha1,2-glucosyltransferase (ALG10) is required for efficient N-glycosylation and leaf growth
    • Farid A, Pabst M, Schoberer J, Altmann F, Glössl J, Strasser R (2011) Arabidopsis thaliana alpha1,2-glucosyltransferase (ALG10) is required for efficient N-glycosylation and leaf growth. Plant J 68: 314-325
    • (2011) Plant J , vol.68 , pp. 314-325
    • Farid, A.1    Pabst, M.2    Schoberer, J.3    Altmann, F.4    Glössl, J.5    Strasser, R.6
  • 3
    • 0035059281 scopus 로고    scopus 로고
    • Genomic-scale comparison of sequence- and structurebased methods of function prediction: Does structure provide additional insight?
    • Fetrow JS, Siew N, Di Gennaro JA, Martinez-Yamout M, Dyson HJ, Skolnick J (2001) Genomic-scale comparison of sequence- and structurebased methods of function prediction: does structure provide additional insight? Protein Sci 10: 1005-1014
    • (2001) Protein Sci , vol.10 , pp. 1005-1014
    • Fetrow, J.S.1    Siew, N.2    Di Gennaro, J.A.3    Martinez-Yamout, M.4    Dyson, H.J.5    Skolnick, J.6
  • 4
    • 57749115778 scopus 로고    scopus 로고
    • Comparative analyses of Arabidopsis complex glycan1 mutants and genetic interaction with staurosporin and temperature sensitive3a
    • Frank J, Kaulfürst-Soboll H, Rips S, Koiwa H, von Schaewen A (2008) Comparative analyses of Arabidopsis complex glycan1 mutants and genetic interaction with staurosporin and temperature sensitive3a. Plant Physiol 148: 1354-1367
    • (2008) Plant Physiol , vol.148 , pp. 1354-1367
    • Frank, J.1    Kaulfürst-Soboll, H.2    Rips, S.3    Koiwa, H.4    von Schaewen, A.5
  • 6
    • 0033634664 scopus 로고    scopus 로고
    • FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis
    • Gómez-Gómez L, Boller T (2000) FLS2: an LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis. Mol Cell 5: 1003-1011
    • (2000) Mol Cell , vol.5 , pp. 1003-1011
    • Gómez-Gómez, L.1    Boller, T.2
  • 7
    • 78049479360 scopus 로고    scopus 로고
    • A ubiquitin-10 promoter-based vector set for fluorescent protein tagging facilitates temporal stability and native protein distribution in transient and stable expression studies
    • Grefen C, Donald N, Hashimoto K, Kudla J, Schumacher K, Blatt MR (2010) A ubiquitin-10 promoter-based vector set for fluorescent protein tagging facilitates temporal stability and native protein distribution in transient and stable expression studies. Plant J 64: 355-365
    • (2010) Plant J , vol.64 , pp. 355-365
    • Grefen, C.1    Donald, N.2    Hashimoto, K.3    Kudla, J.4    Schumacher, K.5    Blatt, M.R.6
  • 9
    • 62549084306 scopus 로고    scopus 로고
    • Multiple mechanism-mediated retention of a defective brassinosteroid receptor in the endoplasmic reticulum of Arabidopsis
    • Hong Z, Jin H, Tzfira T, Li J (2008) Multiple mechanism-mediated retention of a defective brassinosteroid receptor in the endoplasmic reticulum of Arabidopsis. Plant Cell 20: 3418-3429
    • (2008) Plant Cell , vol.20 , pp. 3418-3429
    • Hong, Z.1    Jin, H.2    Tzfira, T.3    Li, J.4
  • 10
    • 84863926126 scopus 로고    scopus 로고
    • Evolutionarily conserved glycan signal to degrade aberrant brassinosteroid receptors in Arabidopsis
    • Hong Z, Kajiura H, Su W, Jin H, Kimura A, Fujiyama K, Li J (2012) Evolutionarily conserved glycan signal to degrade aberrant brassinosteroid receptors in Arabidopsis. Proc Natl Acad Sci USA 109: 11437-11442
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 11437-11442
    • Hong, Z.1    Kajiura, H.2    Su, W.3    Jin, H.4    Kimura, A.5    Fujiyama, K.6    Li, J.7
  • 11
    • 84860015488 scopus 로고    scopus 로고
    • Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulumassociated degradation of glycoproteins
    • Hüttner S, Veit C, Schoberer J, Grass J, Strasser R (2012) Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulumassociated degradation of glycoproteins. Plant Mol Biol 79: 21-33
    • (2012) Plant Mol Biol , vol.79 , pp. 21-33
    • Hüttner, S.1    Veit, C.2    Schoberer, J.3    Grass, J.4    Strasser, R.5
  • 12
    • 34250346376 scopus 로고    scopus 로고
    • Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control
    • Jin H, Yan Z, Nam KH, Li J (2007) Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control. Mol Cell 26: 821-830
    • (2007) Mol Cell , vol.26 , pp. 821-830
    • Jin, H.1    Yan, Z.2    Nam, K.H.3    Li, J.4
  • 15
    • 0029131507 scopus 로고
    • Functional characterization of Ost3p: Loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates
    • Karaoglu D, Kelleher DJ, Gilmore R (1995) Functional characterization of Ost3p: loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates. J Cell Biol 130: 567-577
    • (1995) J Cell Biol , vol.130 , pp. 567-577
    • Karaoglu, D.1    Kelleher, D.J.2    Gilmore, R.3
  • 16
    • 0031437891 scopus 로고    scopus 로고
    • The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p
    • Karaoglu D, Kelleher DJ, Gilmore R (1997) The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p. J Biol Chem 272: 32513-32520
    • (1997) J Biol Chem , vol.272 , pp. 32513-32520
    • Karaoglu, D.1    Kelleher, D.J.2    Gilmore, R.3
  • 17
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic ligosaccharyltransferase
    • Kelleher DJ, Gilmore R (2006) An evolving view of the eukaryotic ligosaccharyltransferase. Glycobiology 16: 47R-62R
    • (2006) Glycobiology , vol.16
    • Kelleher, D.J.1    Gilmore, R.2
  • 18
    • 0038294237 scopus 로고    scopus 로고
    • Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
    • Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R (2003) Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell 12: 101-111
    • (2003) Mol Cell , vol.12 , pp. 101-111
    • Kelleher, D.J.1    Karaoglu, D.2    Mandon, E.C.3    Gilmore, R.4
  • 19
    • 0038236204 scopus 로고    scopus 로고
    • Determination of the membrane topology of Ost4p and its subunit interactions in the oligosaccharyltransferase complex in Saccharomyces cerevisiae
    • Kim H, Yan Q, Von Heijne G, Caputo GA, Lennarz WJ (2003) Determination of the membrane topology of Ost4p and its subunit interactions in the oligosaccharyltransferase complex in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 100: 7460-7464
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7460-7464
    • Kim, H.1    Yan, Q.2    von Heijne, G.3    Caputo, G.A.4    Lennarz, W.J.5
  • 20
    • 0032960606 scopus 로고    scopus 로고
    • The oligosaccharyltransferase complex from yeast
    • Knauer R, Lehle L (1999a) The oligosaccharyltransferase complex from yeast. Biochim Biophys Acta 1426: 259-273
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 259-273
    • Knauer, R.1    Lehle, L.2
  • 21
    • 0033546328 scopus 로고    scopus 로고
    • The oligosaccharyltransferase complex from Saccharomyces cerevisiae: Isolation of the OST6 gene, its synthetic interaction with OST3, and analysis of the native complex
    • Knauer R, Lehle L (1999b) The oligosaccharyltransferase complex from Saccharomyces cerevisiae: isolation of the OST6 gene, its synthetic interaction with OST3, and analysis of the native complex. J Biol Chem 274: 17249-17256
    • (1999) J Biol Chem , vol.274 , pp. 17249-17256
    • Knauer, R.1    Lehle, L.2
  • 22
    • 10744227882 scopus 로고    scopus 로고
    • The STT3a subunit isoform of the Arabidopsis oligosaccharyltransferase controls adaptive responses to salt/osmotic stress
    • Koiwa H, Li F, McCully MG, Mendoza I, Koizumi N, Manabe Y, Nakagawa Y, Zhu J, Rus A, Pardo JM, et al (2003) The STT3a subunit isoform of the Arabidopsis oligosaccharyltransferase controls adaptive responses to salt/osmotic stress. Plant Cell 15: 2273-2284
    • (2003) Plant Cell , vol.15 , pp. 2273-2284
    • Koiwa, H.1    Li, F.2    McCully, M.G.3    Mendoza, I.4    Koizumi, N.5    Manabe, Y.6    Nakagawa, Y.7    Zhu, J.8    Rus, A.9    Pardo, J.M.10
  • 24
    • 19444372339 scopus 로고    scopus 로고
    • Mutants in DEFECTIVE GLYCOSYLATION, an Arabidopsis homolog of an oligosaccharyltransferase complex subunit, show protein underglycosylation and defects in cell differentiation and growth
    • Lerouxel O, Mouille G, Andème-Onzighi C, Bruyant MP, Séveno M, Loutelier-Bourhis C, Driouich A, Höfte H, Lerouge P (2005) Mutants in DEFECTIVE GLYCOSYLATION, an Arabidopsis homolog of an oligosaccharyltransferase complex subunit, show protein underglycosylation and defects in cell differentiation and growth. Plant J 42: 455-468
    • (2005) Plant J , vol.42 , pp. 455-468
    • Lerouxel, O.1    Mouille, G.2    Andème-Onzighi, C.3    Bruyant, M.P.4    Séveno, M.5    Loutelier-Bourhis, C.6    Driouich, A.7    Höfte, H.8    Lerouge, P.9
  • 25
    • 0030866902 scopus 로고    scopus 로고
    • A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction
    • Li J, Chory J (1997) A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction. Cell 90: 929-938
    • (1997) Cell , vol.90 , pp. 929-938
    • Li, J.1    Chory, J.2
  • 27
    • 84868121407 scopus 로고    scopus 로고
    • Myrosinases TGG1 and TGG2 from Arabidopsis thaliana contain exclusively oligomannosidic N-glycans
    • Liebminger E, Grass J, Jez J, Neumann L, Altmann F, Strasser R (2012) Myrosinases TGG1 and TGG2 from Arabidopsis thaliana contain exclusively oligomannosidic N-glycans. Phytochemistry 84: 24-30
    • (2012) Phytochemistry , vol.84 , pp. 24-30
    • Liebminger, E.1    Grass, J.2    Jez, J.3    Neumann, L.4    Altmann, F.5    Strasser, R.6
  • 29
    • 76049084352 scopus 로고    scopus 로고
    • Uncoupling of sustained MAMP receptor signaling from early outputs in an Arabidopsis endoplasmic reticulum glucosidase II allele
    • Lu X, Tintor N, Mentzel T, Kombrink E, Boller T, Robatzek S, Schulze-Lefert P, Saijo Y (2009) Uncoupling of sustained MAMP receptor signaling from early outputs in an Arabidopsis endoplasmic reticulum glucosidase II allele. Proc Natl Acad Sci USA 106: 22522-22527
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 22522-22527
    • Lu, X.1    Tintor, N.2    Mentzel, T.3    Kombrink, E.4    Boller, T.5    Robatzek, S.6    Schulze-Lefert, P.7    Saijo, Y.8
  • 30
    • 0037327305 scopus 로고    scopus 로고
    • Genomic analysis of the unfolded protein response in Arabidopsis shows its connection to important cellular processes
    • Martínez IM, Chrispeels MJ (2003) Genomic analysis of the unfolded protein response in Arabidopsis shows its connection to important cellular processes. Plant Cell 15: 561-576
    • (2003) Plant Cell , vol.15 , pp. 561-576
    • Martínez, I.M.1    Chrispeels, M.J.2
  • 32
    • 79961171901 scopus 로고    scopus 로고
    • Oligosaccharyltransferase: The central enzyme of N-linked protein glycosylation
    • Mohorko E, Glockshuber R, Aebi M (2011) Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation. J Inherit Metab Dis 34: 869-878
    • (2011) J Inherit Metab Dis , vol.34 , pp. 869-878
    • Mohorko, E.1    Glockshuber, R.2    Aebi, M.3
  • 33
    • 0034771917 scopus 로고    scopus 로고
    • Characterization of a functional soluble form of a Brassica napus membrane-anchored endo-1,4-b-glucanase heterologously expressed in Pichia pastoris
    • Mølhøj M, Ulvskov P, Dal Degan F (2001) Characterization of a functional soluble form of a Brassica napus membrane-anchored endo-1,4-b-glucanase heterologously expressed in Pichia pastoris. Plant Physiol 127: 674-684
    • (2001) Plant Physiol , vol.127 , pp. 674-684
    • Mølhøj, M.1    Ulvskov, P.2    Dal Degan, F.3
  • 36
    • 0032189651 scopus 로고    scopus 로고
    • A plasma membrane-bound putative endo-1,4-beta-D-glucanase is required for normal wall assembly and cell elongation in Arabidopsis
    • Nicol F, His I, Jauneau A, Vernhettes S, Canut H, Höfte H (1998) A plasma membrane-bound putative endo-1,4-beta-D-glucanase is required for normal wall assembly and cell elongation in Arabidopsis. EMBO J 17: 5563-5576
    • (1998) EMBO J , vol.17 , pp. 5563-5576
    • Nicol, F.1    His, I.2    Jauneau, A.3    Vernhettes, S.4    Canut, H.5    Höfte, H.6
  • 39
    • 59349097787 scopus 로고    scopus 로고
    • N-Glycan production in the endoplasmic reticulum of plants
    • Pattison RJ, Amtmann A (2009) N-Glycan production in the endoplasmic reticulum of plants. Trends Plant Sci 14: 92-99
    • (2009) Trends Plant Sci , vol.14 , pp. 92-99
    • Pattison, R.J.1    Amtmann, A.2
  • 40
    • 84869134251 scopus 로고    scopus 로고
    • The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation
    • Roboti P, High S (2012) The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation. J Cell Sci 125: 3474-3484
    • (2012) J Cell Sci , vol.125 , pp. 3474-3484
    • Roboti, P.1    High, S.2
  • 41
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada C, Kelleher DJ, Gilmore R (2009) Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell 136: 272-283
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 43
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • Schmittgen TD, Livak KJ (2008) Analyzing real-time PCR data by the comparative C(T) method. Nat Protoc 3: 1101-1108
    • (2008) Nat Protoc , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 44
    • 58149185093 scopus 로고    scopus 로고
    • Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes
    • Schoberer J, Vavra U, Stadlmann J, Hawes C, Mach L, Steinkellner H, Strasser R (2009) Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes. Traffic 10: 101-115
    • (2009) Traffic , vol.10 , pp. 101-115
    • Schoberer, J.1    Vavra, U.2    Stadlmann, J.3    Hawes, C.4    Mach, L.5    Steinkellner, H.6    Strasser, R.7
  • 45
    • 61649089751 scopus 로고    scopus 로고
    • Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency
    • Schulz BL, Aebi M (2009) Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency. Mol Cell Proteomics 8: 357-364
    • (2009) Mol Cell Proteomics , vol.8 , pp. 357-364
    • Schulz, B.L.1    Aebi, M.2
  • 47
    • 27944459619 scopus 로고    scopus 로고
    • Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit
    • Schwarz M, Knauer R, Lehle L (2005) Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit. FEBS Lett 579: 6564-6568
    • (2005) FEBS Lett , vol.579 , pp. 6564-6568
    • Schwarz, M.1    Knauer, R.2    Lehle, L.3
  • 48
    • 17644366824 scopus 로고    scopus 로고
    • Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits
    • Shibatani T, David LL, McCormack AL, Frueh K, Skach WR (2005) Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry 44: 5982-5992
    • (2005) Biochemistry , vol.44 , pp. 5982-5992
    • Shibatani, T.1    David, L.L.2    McCormack, A.L.3    Frueh, K.4    Skach, W.R.5
  • 49
    • 28444437028 scopus 로고    scopus 로고
    • The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast
    • Spirig U, Bodmer D, Wacker M, Burda P, Aebi M (2005) The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast. Glycobiology 15: 1396-1406
    • (2005) Glycobiology , vol.15 , pp. 1396-1406
    • Spirig, U.1    Bodmer, D.2    Wacker, M.3    Burda, P.4    Aebi, M.5
  • 50
    • 1542358140 scopus 로고    scopus 로고
    • Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose
    • Strasser R, Altmann F, Mach L, Glössl J, Steinkellner H (2004) Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose. FEBS Lett 561: 132-136
    • (2004) FEBS Lett , vol.561 , pp. 132-136
    • Strasser, R.1    Altmann, F.2    Mach, L.3    Glössl, J.4    Steinkellner, H.5
  • 52
    • 84860213183 scopus 로고    scopus 로고
    • Probing the Arabidopsis flagellin receptor: FLS2-FLS2 association and the contributions of specific domains to signaling function
    • Sun W, Cao Y, Jansen Labby K, Bittel P, Boller T, Bent AF (2012) Probing the Arabidopsis flagellin receptor: FLS2-FLS2 association and the contributions of specific domains to signaling function. Plant Cell 24: 1096-1113
    • (2012) Plant Cell , vol.24 , pp. 1096-1113
    • Sun, W.1    Cao, Y.2    Jansen Labby, K.3    Bittel, P.4    Boller, T.5    Bent, A.F.6
  • 54
    • 77955138743 scopus 로고    scopus 로고
    • Requirement of a homolog of glucosidase II beta-subunit for EFRmediated defense signaling in Arabidopsis thaliana
    • von Numers N, Survila M, Aalto M, Batoux M, Heino P, Palva ET, Li J (2010) Requirement of a homolog of glucosidase II beta-subunit for EFRmediated defense signaling in Arabidopsis thaliana. Mol Plant 3: 740-750
    • (2010) Mol Plant , vol.3 , pp. 740-750
    • von Numers, N.1    Survila, M.2    Aalto, M.3    Batoux, M.4    Heino, P.5    Palva, E.T.6    Li, J.7
  • 55
    • 0027640147 scopus 로고
    • Isolation of a mutant Arabidopsis plant that lacks N-acetyl glucosaminyl transferase I and is unable to synthesize Golgi-modified complex N-linked glycans
    • von Schaewen A, Sturm A, O'Neill J, Chrispeels MJ (1993) Isolation of a mutant Arabidopsis plant that lacks N-acetyl glucosaminyl transferase I and is unable to synthesize Golgi-modified complex N-linked glycans. Plant Physiol 102: 1109-1118
    • (1993) Plant Physiol , vol.102 , pp. 1109-1118
    • von Schaewen, A.1    Sturm, A.2    O'Neill, J.3    Chrispeels, M.J.4
  • 56
    • 45149090440 scopus 로고    scopus 로고
    • A LysM receptor-like kinase plays a critical role in chitin signaling and fungal resistance in Arabidopsis
    • Wan J, Zhang XC, Neece D, Ramonell KM, Clough S, Kim SY, Stacey MG, Stacey G (2008) A LysM receptor-like kinase plays a critical role in chitin signaling and fungal resistance in Arabidopsis. Plant Cell 20: 471-481
    • (2008) Plant Cell , vol.20 , pp. 471-481
    • Wan, J.1    Zhang, X.C.2    Neece, D.3    Ramonell, K.M.4    Clough, S.5    Kim, S.Y.6    Stacey, M.G.7    Stacey, G.8
  • 57
    • 18644369120 scopus 로고    scopus 로고
    • Induction of protein secretory pathway is required for systemic acquired resistance
    • Wang D, Weaver ND, Kesarwani M, Dong X (2005) Induction of protein secretory pathway is required for systemic acquired resistance. Science 308: 1036-1040
    • (2005) Science , vol.308 , pp. 1036-1040
    • Wang, D.1    Weaver, N.D.2    Kesarwani, M.3    Dong, X.4
  • 58
    • 13544268336 scopus 로고    scopus 로고
    • Unraveling the mechanism of protein N-glycosylation
    • Yan A, Lennarz WJ (2005a) Unraveling the mechanism of protein N-glycosylation. J Biol Chem 280: 3121-3124
    • (2005) J Biol Chem , vol.280 , pp. 3121-3124
    • Yan, A.1    Lennarz, W.J.2
  • 59
    • 28444451884 scopus 로고    scopus 로고
    • Two oligosaccharyl transferase complexes exist in yeast and associate with two different translocons
    • Yan A, Lennarz WJ (2005b) Two oligosaccharyl transferase complexes exist in yeast and associate with two different translocons. Glycobiology 15: 1407-1415
    • (2005) Glycobiology , vol.15 , pp. 1407-1415
    • Yan, A.1    Lennarz, W.J.2
  • 60
    • 0037033113 scopus 로고    scopus 로고
    • Studies on the function of oligosaccharyl transferase subunits: Stt3p is directly involved in the glycosylation process
    • Yan Q, Lennarz WJ (2002) Studies on the function of oligosaccharyl transferase subunits: Stt3p is directly involved in the glycosylation process. J Biol Chem 277: 47692-47700
    • (2002) J Biol Chem , vol.277 , pp. 47692-47700
    • Yan, Q.1    Lennarz, W.J.2
  • 61
    • 71649099280 scopus 로고    scopus 로고
    • LEW3, encoding a putative alpha- 1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana
    • Zhang M, Henquet M, Chen Z, Zhang H, Zhang Y, Ren X, van der Krol S, Gonneau M, Bosch D, Gong Z (2009) LEW3, encoding a putative alpha- 1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana. Plant J 60: 983-999
    • (2009) Plant J , vol.60 , pp. 983-999
    • Zhang, M.1    Henquet, M.2    Chen, Z.3    Zhang, H.4    Zhang, Y.5    Ren, X.6    van der Krol, S.7    Gonneau, M.8    Bosch, D.9    Gong, Z.10
  • 62
    • 70349449921 scopus 로고    scopus 로고
    • Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and vertebrate embryonic development
    • Zhou H, Clapham DE (2009) Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and vertebrate embryonic development. Proc Natl Acad Sci USA 106: 15750-15755
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15750-15755
    • Zhou, H.1    Clapham, D.E.2
  • 63
    • 84861427459 scopus 로고    scopus 로고
    • Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery
    • Zielinska DF, Gnad F, Schropp K, Wiśniewski JR, Mann M (2012) Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548
    • (2012) Mol Cell , vol.46 , pp. 542-548
    • Zielinska, D.F.1    Gnad, F.2    Schropp, K.3    Wiśniewski, J.R.4    Mann, M.5
  • 64
    • 33646525169 scopus 로고    scopus 로고
    • Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation
    • Zipfel C, Kunze G, Chinchilla D, Caniard A, Jones JD, Boller T, Felix G (2006) Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation. Cell 125: 749-760
    • (2006) Cell , vol.125 , pp. 749-760
    • Zipfel, C.1    Kunze, G.2    Chinchilla, D.3    Caniard, A.4    Jones, J.D.5    Boller, T.6    Felix, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.