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Volumn 3, Issue MAY, 2012, Pages

Recent advances on the posttranslational modifications of EXTs and their roles in plant cell walls

Author keywords

Cell expansion; Extensins; O glycoproteins; O glycosylation; Plant cell wall; Proline hydroxylation

Indexed keywords


EID: 84883208564     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2012.00093     Document Type: Review
Times cited : (46)

References (78)
  • 2
    • 70350029421 scopus 로고    scopus 로고
    • Prolyl-4-hydroxylase (AtP4H1) mediates and mimics low oxygen response in Arabidopsis thaliana
    • Asif, M. H., Trivedi, P. K., Misra, P., and Nath, P. (2009). Prolyl-4-hydroxylase (AtP4H1) mediates and mimics low oxygen response in Arabidopsis thaliana. Funct. Integr. Genomics 9, 525-535.
    • (2009) Funct. Integr. Genomics , vol.9 , pp. 525-535
    • Asif, M.H.1    Trivedi, P.K.2    Misra, P.3    Nath, P.4
  • 3
    • 0037355250 scopus 로고    scopus 로고
    • Whole-genome comparison of leucine-rich repeat extensins in Arabidopsisand rice. A conserved family of cell wall proteins form a vegetative and a reproductive clade
    • Baumberger, N., Doesseger, B., Guyot, R., Diet, A., Parsons, R. L., Clark, M. A., Simmons, M. P., Bedinger, P., Goff, S. A., Ringli, C., and Keller, B. (2003a). Whole-genome comparison of leucine-rich repeat extensins in Arabidopsisand rice. A conserved family of cell wall proteins form a vegetative and a reproductive clade. Plant Physiol. 131, 1313-1326.
    • (2003) Plant Physiol. , vol.131 , pp. 1313-1326
    • Baumberger, N.1    Doesseger, B.2    Guyot, R.3    Diet, A.4    Parsons, R.L.5    Clark, M.A.6    Simmons, M.P.7    Bedinger, P.8    Goff, S.A.9    Ringli, C.10    Keller, B.11
  • 4
    • 0037629264 scopus 로고    scopus 로고
    • Synergistic interaction of the two paralogous Arabidopsis genes LRX1 and LRX2 in cell wall formation during root hair development
    • Baumberger, N., Steiner, M., Ryser, U., Keller, B., and Ringli, C. (2003b). Synergistic interaction of the two paralogous Arabidopsis genes LRX1 and LRX2 in cell wall formation during root hair development. Plant J. 35, 71-81.
    • (2003) Plant J. , vol.35 , pp. 71-81
    • Baumberger, N.1    Steiner, M.2    Ryser, U.3    Keller, B.4    Ringli, C.5
  • 5
    • 0035337065 scopus 로고    scopus 로고
    • The chimeric leucine-rich repeat/extensin cell wall protein LRX1 is required for root hair morphogenesis in Arabidopsis thaliana
    • Baumberger, N., Ringli, C., and Keller, B. (2001). The chimeric leucine-rich repeat/extensin cell wall protein LRX1 is required for root hair morphogenesis in Arabidopsis thaliana. Genes Dev. 15, 1128-1139.
    • (2001) Genes Dev. , vol.15 , pp. 1128-1139
    • Baumberger, N.1    Ringli, C.2    Keller, B.3
  • 6
    • 0033765229 scopus 로고    scopus 로고
    • Expression of AtPRP3, a proline-rich structural cell wall protein fromArabidopsis is regulated by cell-type-specific developmental pathways involved in root hair formation
    • Bernhardt, C., and Tierney, M. L. (2000). Expression of AtPRP3, a proline-rich structural cell wall protein fromArabidopsis is regulated by cell-type-specific developmental pathways involved in root hair formation. Plant Physiol. 122, 705-714.
    • (2000) Plant Physiol. , vol.122 , pp. 705-714
    • Bernhardt, C.1    Tierney, M.L.2
  • 7
    • 35548967108 scopus 로고    scopus 로고
    • Structural analysis of linear hydroxyproline-bound O-glycans of Chlamydomonas reinhardtii-conservation of the inner core in Chlamydomonas and land plants
    • Bollig, K., Lamshoft, M., Schweimer, K., Marner, F. J., Budzikiewicz, H., and Waffenschmidt, S. (2007). Structural analysis of linear hydroxyproline-bound O-glycans of Chlamydomonas reinhardtii-conservation of the inner core in Chlamydomonas and land plants. Carbohydr. Res. 342, 2557-2566.
    • (2007) Carbohydr. Res. , vol.342 , pp. 2557-2566
    • Bollig, K.1    Lamshoft, M.2    Schweimer, K.3    Marner, F.J.4    Budzikiewicz, H.5    Waffenschmidt, S.6
  • 8
    • 0029963544 scopus 로고    scopus 로고
    • Di-isodityrosine, a novel tetrametric derivative of tyrosine in plant cell wall proteins: A new potential cross-link
    • Brady, J. D., Sadler, I. H., and Fry, S. C. (1996). Di-isodityrosine, a novel tetrametric derivative of tyrosine in plant cell wall proteins: a new potential cross-link. Biochem. J. 315(Pt 1), 323-327.
    • (1996) Biochem. J. , vol.315 , Issue.PART 1 , pp. 323-327
    • Brady, J.D.1    Sadler, I.H.2    Fry, S.C.3
  • 9
    • 0032007587 scopus 로고    scopus 로고
    • Pulcherosine, an oxidatively coupled trimer of tyrosine in plant cell walls: Its role in cross-link formation
    • Brady, J. D., Sadler, I. H., and Fry, S. C. (1998). Pulcherosine, an oxidatively coupled trimer of tyrosine in plant cell walls: its role in cross-link formation. Phytochemistry 47, 349-353.
    • (1998) Phytochemistry , vol.47 , pp. 349-353
    • Brady, J.D.1    Sadler, I.H.2    Fry, S.C.3
  • 10
    • 0029175039 scopus 로고
    • Purification and partial characterization of tomato extensin peroxidase
    • Brownleader, M. D., Ahmed, N., Trevan, M., Chaplin, M. F., and Dey, P. M. (1995). Purification and partial characterization of tomato extensin peroxidase. Plant Physiol. 109, 1115-1123.
    • (1995) Plant Physiol. , vol.109 , pp. 1115-1123
    • Brownleader, M.D.1    Ahmed, N.2    Trevan, M.3    Chaplin, M.F.4    Dey, P.M.5
  • 11
    • 0027349625 scopus 로고
    • Purification of extension from cell walls of tomato (hybrid ofLycopersicon esculentum and L. peruvianum) cells in suspension culture
    • Brownleader, M. D., and Dey, P. M. (1993). Purification of extension from cell walls of tomato (hybrid ofLycopersicon esculentum and L. peruvianum) cells in suspension culture. Planta 191, 457-469.
    • (1993) Planta , vol.191 , pp. 457-469
    • Brownleader, M.D.1    Dey, P.M.2
  • 12
    • 0034032156 scopus 로고    scopus 로고
    • Role of extensin peroxidase in tomato (Lycopersicon esculentum Mill.) seedling growth
    • Brownleader, M. D., Hopkins, J., Mobasheri, A., Dey, P. M., Jackson, P., and Trevan, M. (2000). Role of extensin peroxidase in tomato (Lycopersicon esculentum Mill.) seedling growth. Planta 210, 668-676.
    • (2000) Planta , vol.210 , pp. 668-676
    • Brownleader, M.D.1    Hopkins, J.2    Mobasheri, A.3    Dey, P.M.4    Jackson, P.5    Trevan, M.6
  • 14
    • 27644525170 scopus 로고    scopus 로고
    • Growth of the plant cell wall
    • Cosgrove, D. J. (2005). Growth of the plant cell wall. Nat. Rev. Mol. Cell Biol. 11, 850-861.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 850-861
    • Cosgrove, D.J.1
  • 15
    • 77955967051 scopus 로고    scopus 로고
    • A simple method for gene expression and chromatin profiling of individual cell types within a tissue
    • Deal, R. B., and Henikoff, S. (2010). A simple method for gene expression and chromatin profiling of individual cell types within a tissue. Dev. Cell 18, 1030-1040.
    • (2010) Dev. Cell , vol.18 , pp. 1030-1040
    • Deal, R.B.1    Henikoff, S.2
  • 16
    • 34249830161 scopus 로고    scopus 로고
    • Molecular characterization of two Arabidopsis thaliana glycosyltransferase mutants, rra1 and rra2, which have a reduced residual arabinose content in a polymer tightly associated with the cellulosic wall residue
    • Egelund, J., Obel, N., Ulvskov, P., Geshi, N., Pauly, M., Bacic, A., and Larsen Petersen, B. (2007). Molecular characterization of two Arabidopsis thaliana glycosyltransferase mutants, rra1 and rra2, which have a reduced residual arabinose content in a polymer tightly associated with the cellulosic wall residue. Plant Mol. Biol. 64, 439-449.
    • (2007) Plant Mol. Biol. , vol.64 , pp. 439-449
    • Egelund, J.1    Obel, N.2    Ulvskov, P.3    Geshi, N.4    Pauly, M.5    Bacic, A.6    Larsen Petersen, B.7
  • 18
    • 0035814919 scopus 로고    scopus 로고
    • Glycosylated polyproline II rods with kinks as a structural motif in plant hydroxyproline-rich glycoproteins
    • Ferris, P. J., Woessner, J. P., Waffenschmidt, S., Kilz, S., Drees, J., and Goodenough, U. W. (2001). Glycosylated polyproline II rods with kinks as a structural motif in plant hydroxyproline-rich glycoproteins. Biochemistry 40, 2978-2987.
    • (2001) Biochemistry , vol.40 , pp. 2978-2987
    • Ferris, P.J.1    Woessner, J.P.2    Waffenschmidt, S.3    Kilz, S.4    Drees, J.5    Goodenough, U.W.6
  • 19
    • 0033378417 scopus 로고    scopus 로고
    • Characterization and expression of four proline-rich cell wall protein genes in Arabidopsis encoding two distinct subsets of multiple domain proteins
    • Fowler, T. J., Bernhardt, C., and Tierney, M. L. (1999). Characterization and expression of four proline-rich cell wall protein genes in Arabidopsis encoding two distinct subsets of multiple domain proteins. Plant Physiol. 121, 1081-1092.
    • (1999) Plant Physiol. , vol.121 , pp. 1081-1092
    • Fowler, T.J.1    Bernhardt, C.2    Tierney, M.L.3
  • 20
    • 0020483177 scopus 로고
    • Isodityrosine, a new cross-linking amino acid from plant cell wall glycoprotein
    • Fry, S. C. (1982). Isodityrosine, a new cross-linking amino acid from plant cell wall glycoprotein. Biochem. J. 204, 449-455.
    • (1982) Biochem. J. , vol.204 , pp. 449-455
    • Fry, S.C.1
  • 21
    • 70149083484 scopus 로고    scopus 로고
    • Identification of plant cell wall mutants by means of a forward chemical genetic approach using hydrolases
    • Gille, S., Hänsel, U., Ziemann, M., and Pauly, M. (2009). Identification of plant cell wall mutants by means of a forward chemical genetic approach using hydrolases. Proc. Natl. Acad. Sci. U.S.A. 106, 14699-704.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 14699-14704
    • Gille, S.1    Hänsel, U.2    Ziemann, M.3    Pauly, M.4
  • 22
    • 0036016444 scopus 로고    scopus 로고
    • The cell wall hydroxyproline-rich glycoprotein RSH is essential for normal embryo development in Arabidopsis
    • Hall, Q., and Cannon, M. C. (2002). The cell wall hydroxyproline-rich glycoprotein RSH is essential for normal embryo development in Arabidopsis. Plant Cell 14, 1161-1172.
    • (2002) Plant Cell , vol.14 , pp. 1161-1172
    • Hall, Q.1    Cannon, M.C.2
  • 23
    • 11244311665 scopus 로고    scopus 로고
    • Di-isodityrosine is the intermolecular cross-link of isodityrosine-rich extensin analogs cross-linked in vitro
    • Held, M. A., Tan, L., Kamyab, A., Hare, M., Shpak, E., and Kieliszewski, M. J. (2004). Di-isodityrosine is the intermolecular cross-link of isodityrosine-rich extensin analogs cross-linked in vitro. J. Biol. Chem. 279, 55474-55482.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55474-55482
    • Held, M.A.1    Tan, L.2    Kamyab, A.3    Hare, M.4    Shpak, E.5    Kieliszewski, M.J.6
  • 24
    • 0037189554 scopus 로고    scopus 로고
    • Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides
    • Hieta, R., and Myllyharju, J. (2002). Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides. J. Biol. Chem. 277, 23965-23971.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23965-23971
    • Hieta, R.1    Myllyharju, J.2
  • 25
    • 34548394230 scopus 로고    scopus 로고
    • Sentinels at the wall: Cell wall receptors and sensors
    • Humphrey, T. V., Bonetta, D. T., and Goring, D. R. (2007). Sentinels at the wall: cell wall receptors and sensors. New Phytol. 176, 7-21.
    • (2007) New Phytol. , vol.176 , pp. 7-21
    • Humphrey, T.V.1    Bonetta, D.T.2    Goring, D.R.3
  • 26
    • 33747144246 scopus 로고    scopus 로고
    • Dodeca-CLE peptides as suppressors of plant stem cell differentiation
    • Ito, Y., Nakanomyo, I., Motose, H., Iwamoto, K., Sawa, S., Dohmae, N., and Fukuda, H. (2006). Dodeca-CLE peptides as suppressors of plant stem cell differentiation. Science 313, 842-845.
    • (2006) Science , vol.313 , pp. 842-845
    • Ito, Y.1    Nakanomyo, I.2    Motose, H.3    Iwamoto, K.4    Sawa, S.5    Dohmae, N.6    Fukuda, H.7
  • 27
    • 0035193692 scopus 로고    scopus 로고
    • Rapid deposition of extensin during the elicitation of grapevine callus cultures is specifically catalyzed by a 40-kiloDalton peroxidase
    • Jackson, P. A., Galinha, C. I., Pereira, C. S., Fortunato, A., Soares, N. C., Amâncio, S. B., and Pinto Ricardo, C. P. (2001). Rapid deposition of extensin during the elicitation of grapevine callus cultures is specifically catalyzed by a 40-kiloDalton peroxidase. Plant Physiol. 127, 1065-1076.
    • (2001) Plant Physiol. , vol.127 , pp. 1065-1076
    • Jackson, P.A.1    Galinha, C.I.2    Pereira, C.S.3    Fortunato, A.4    Soares, N.C.5    Amâncio, S.B.6    Pinto Ricardo, C.P.7
  • 28
    • 33644852136 scopus 로고    scopus 로고
    • Analysis of the root-hair morphogenesis transcriptome reveals the molecular identity of six genes with roles in root-hair development in Arabidopsis
    • Jones, M. A., Raymond, M. J., and Smirnoff, N. (2006). Analysis of the root-hair morphogenesis transcriptome reveals the molecular identity of six genes with roles in root-hair development in Arabidopsis. Plant J. 45, 83-100.
    • (2006) Plant J. , vol.45 , pp. 83-100
    • Jones, M.A.1    Raymond, M.J.2    Smirnoff, N.3
  • 29
    • 0024289220 scopus 로고
    • Prolyl 4-hydroxylase from Volvox carteri. A low-Mr enzyme antigenically related to the a subunit of the vertebrate enzyme
    • Kaska, D. D., Myllylä, R., Günzler, V., Gibor, A., and Kivirikko, K. I. (1988). Prolyl 4-hydroxylase from Volvox carteri. A low-Mr enzyme antigenically related to the a subunit of the vertebrate enzyme. Biochem. J. 256, 257-263.
    • (1988) Biochem. J. , vol.256 , pp. 257-263
    • Kaska, D.D.1    Myllylä, R.2    Günzler, V.3    Gibor, A.4    Kivirikko, K.I.5
  • 30
    • 34249824288 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii has multiple prolyl 4-hydroxylases, one of which is essential for proper cell wall assembly
    • Keskiaho, K., Hieta, R., Sormunen, R., and Myllyharju, J. (2007). Chlamydomonas reinhardtii has multiple prolyl 4-hydroxylases, one of which is essential for proper cell wall assembly. Plant Cell 19, 256-269.
    • (2007) Plant Cell , vol.19 , pp. 256-269
    • Keskiaho, K.1    Hieta, R.2    Sormunen, R.3    Myllyharju, J.4
  • 31
    • 0035371614 scopus 로고    scopus 로고
    • The latest hype on Hyp-O-glycosylation codes
    • Kieliszewski, M. J. (2001). The latest hype on Hyp-O-glycosylation codes. Phytochemistry 57, 319-323.
    • (2001) Phytochemistry , vol.57 , pp. 319-323
    • Kieliszewski, M.J.1
  • 32
    • 0028371792 scopus 로고
    • Extensin: Repetitive motifs, functional sites, post-translational codes, and phylogeny
    • Kieliszewski, M. J., and Lamport, D. T. A. (1994). Extensin: repetitive motifs, functional sites, post-translational codes, and phylogeny. Plant J. 5, 157-172.
    • (1994) Plant J. , vol.5 , pp. 157-172
    • Kieliszewski, M.J.1    Lamport, D.T.A.2
  • 34
    • 0024656034 scopus 로고
    • Trypsin cleaves lysylproline in a hydroxyproline-rich glycoprotein from Zea mays
    • Kieliszewski, M. J., Leykam, J. F., and Lamport, D. T. A. (1989). Trypsin cleaves lysylproline in a hydroxyproline-rich glycoprotein from Zea mays. Pept. Res. 2, 246-248.
    • (1989) Pept. Res. , vol.2 , pp. 246-248
    • Kieliszewski, M.J.1    Leykam, J.F.2    Lamport, D.T.A.3
  • 35
    • 33747107058 scopus 로고    scopus 로고
    • A plant peptide encoded by CLV3 identified by in situ MALDI-TOF MS analysis
    • Kondo, T., Sawa, S., Kinoshita, A., Mizuno, S., Kakimoto, T., Fukuda, H., and Sakagam, Y. (2006). A plant peptide encoded by CLV3 identified by in situ MALDI-TOF MS analysis. Science 313, 845-848.
    • (2006) Science , vol.313 , pp. 845-848
    • Kondo, T.1    Sawa, S.2    Kinoshita, A.3    Mizuno, S.4    Kakimoto, T.5    Fukuda, H.6    Sakagam, Y.7
  • 36
    • 37549013372 scopus 로고    scopus 로고
    • The active site of an algal prolyl 4-hydroxylase has a large structural plasticity. The active site of an algal prolyl 4-hydroxylase has a large structural plasticity
    • Koski, M. K., Hieta, R., Böllner, C., Kivirikko, K. I., Myllyharju, J., and Wierenga, R. K. (2007). The active site of an algal prolyl 4-hydroxylase has a large structural plasticity. The active site of an algal prolyl 4-hydroxylase has a large structural plasticity. J. Biol. Chem. 282, 37112-37123.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37112-37123
    • Koski, M.K.1    Hieta, R.2    Böllner, C.3    Kivirikko, K.I.4    Myllyharju, J.5    Wierenga, R.K.6
  • 37
    • 69949136771 scopus 로고    scopus 로고
    • The crystal structure of an algal prolyl 4-hydroxylase complexed with a proline-rich peptide reveals a novel buried tripeptide binding motif. J
    • Koski, M. K., Hieta, R., Hirsilä, M., Rönkä, A., Myllyharju, J., and Wierenga, R. K. (2009). The crystal structure of an algal prolyl 4-hydroxylase complexed with a proline-rich peptide reveals a novel buried tripeptide binding motif.J. Biol. Chem. 284, 25290-25301.
    • (2009) Biol. Chem. , vol.284 , pp. 25290-25301
    • Koski, M.K.1    Hieta, R.2    Hirsilä, M.3    Rönkä, A.4    Myllyharju, J.5    Wierenga, R.K.6
  • 38
    • 79955992743 scopus 로고    scopus 로고
    • Role of the extensin superfamily in primary cell wall architecture
    • Lamport, D. T., Kieliszewski, M. J., Chen, Y., and Cannon, M. C. (2011). Role of the extensin superfamily in primary cell wall architecture. Plant Physiol. 156, 11-19.
    • (2011) Plant Physiol. , vol.156 , pp. 11-19
    • Lamport, D.T.1    Kieliszewski, M.J.2    Chen, Y.3    Cannon, M.C.4
  • 39
    • 0001516436 scopus 로고
    • Oxygen fixation into hydroxyproline of plant cell wall protein
    • Lamport, D. T. A. (1963). Oxygen fixation into hydroxyproline of plant cell wall protein. J. Biol. Chem. 238, 1438-1440.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1438-1440
    • Lamport, D.T.A.1
  • 40
    • 0000475757 scopus 로고
    • Hydroxyproline-O-glycosidic linkage of the plant cell wall glycoprotein extensin
    • Lamport, D. T. A. (1967). Hydroxyproline-O-glycosidic linkage of the plant cell wall glycoprotein extensin. Nature216, 1322-1324.
    • (1967) Nature , vol.216 , pp. 1322-1324
    • Lamport, D.T.A.1
  • 41
    • 0002919461 scopus 로고
    • Structure, biosynthesis and significance of cell wall glycoproteins
    • in eds F. A. Loewus, and V. C. Runeckles (Plenum Publishing, New York)
    • Lamport, D. T. A. (1977). "Structure, biosynthesis and significance of cell wall glycoproteins, " in Recent Advances in Phytochemistry, eds F. A. Loewus, and V. C. Runeckles (Plenum Publishing, New York), 79-115.
    • (1977) Recent Advances in Phytochemistry , pp. 79-115
    • Lamport, D.T.A.1
  • 43
    • 0001593842 scopus 로고
    • Hydroxyproline in primary cell walls of higher plants
    • Lamport, D. T. A., and Northcote, D. H. (1960). Hydroxyproline in primary cell walls of higher plants. Nature 188, 665-666.
    • (1960) Nature , vol.188 , pp. 665-666
    • Lamport, D.T.A.1    Northcote, D.H.2
  • 44
    • 34547925245 scopus 로고    scopus 로고
    • Between-species analysis of short-repeat modules in cell wall and sex-related hydroxyproline-rich glycoproteins of Chlamydomonas
    • Lee, J. H., Waffenschmidt, S., Small, L., and Goodenough, U. (2007). Between-species analysis of short-repeat modules in cell wall and sex-related hydroxyproline-rich glycoproteins of Chlamydomonas. Plant Physiol. 144, 1813-1826.
    • (2007) Plant Physiol. , vol.144 , pp. 1813-1826
    • Lee, J.H.1    Waffenschmidt, S.2    Small, L.3    Goodenough, U.4
  • 45
    • 0028518676 scopus 로고
    • A style-specific hydroxyproline-rich glycoprotein with properties of both extensins and arabinogalactan proteins
    • Lind, J. L., Bacic, A., Clarke, A. E., and Anderson, M. A. (1994). A style-specific hydroxyproline-rich glycoprotein with properties of both extensins and arabinogalactan proteins. Plant J. 6, 491-502.
    • (1994) Plant J. , vol.6 , pp. 491-502
    • Lind, J.L.1    Bacic, A.2    Clarke, A.E.3    Anderson, M.A.4
  • 46
    • 0031874712 scopus 로고    scopus 로고
    • In vitro cross-linking of extensin precursors by mustard extracellular isoforms of peroxidase that respond either to phytochrome or to wounding
    • Magliano, T. M. A., and Casal, J. J. (1998). In vitro cross-linking of extensin precursors by mustard extracellular isoforms of peroxidase that respond either to phytochrome or to wounding. J. Exp. Bot. 49, 1491-1499.
    • (1998) J. Exp. Bot. , vol.49 , pp. 1491-1499
    • Magliano, T.M.A.1    Casal, J.J.2
  • 47
    • 77956097951 scopus 로고    scopus 로고
    • Secreted peptide signals required for maintenance of root stem cell niche in Arabidopsis
    • Matsuzaki, Y., Ogawa-Ohnishi, M., Mori, A., and Matsubayashi, Y. (2010). Secreted peptide signals required for maintenance of root stem cell niche in Arabidopsis. Science 329, 1065-1067.
    • (2010) Science , vol.329 , pp. 1065-1067
    • Matsuzaki, Y.1    Ogawa-Ohnishi, M.2    Mori, A.3    Matsubayashi, Y.4
  • 48
    • 0037358282 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis
    • Myllyharju, J. (2003). Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis. Matrix Biol. 22, 15-24.
    • (2003) Matrix Biol. , vol.22 , pp. 15-24
    • Myllyharju, J.1
  • 49
    • 50649120554 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets
    • Myllyharju, J. (2008). Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets. Ann. Med. 40, 402-417.
    • (2008) Ann. Med. , vol.40 , pp. 402-417
    • Myllyharju, J.1
  • 52
    • 77950800689 scopus 로고    scopus 로고
    • Contiguous O-galactosylation of 4(R)-hydroxy-l-proline residues forms very stable polyproline II helices
    • Owens, N. W., Stetefeld, J., Lattová, E., and Schweizer, F. (2010). Contiguous O-galactosylation of 4(R)-hydroxy-l-proline residues forms very stable polyproline II helices. J. Am. Chem. Soc. 132, 5036-5042.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5036-5042
    • Owens, N.W.1    Stetefeld, J.2    Lattová, E.3    Schweizer, F.4
  • 53
    • 3242752669 scopus 로고    scopus 로고
    • The plant peroxidase multigenic family in rice and its evolution in green plants
    • Passardi, F., Longet, D., Penel, C., and Dunand, C. (2004). The plant peroxidase multigenic family in rice and its evolution in green plants. Phytochemistry 65, 1879-1893.
    • (2004) Phytochemistry , vol.65 , pp. 1879-1893
    • Passardi, F.1    Longet, D.2    Penel, C.3    Dunand, C.4
  • 54
    • 0142103316 scopus 로고    scopus 로고
    • A biochemical and molecular characterization of LEP1, an extensin peroxidase from lupin
    • Price, N. J., Pinheiro, C., Soares, C. M., Ashford, D. A., Ricardo, C. P., and Jackson, P. A. (2003). A biochemical and molecular characterization of LEP1, an extensin peroxidase from lupin. J. Biol. Chem. 278, 41389-41399.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41389-41399
    • Price, N.J.1    Pinheiro, C.2    Soares, C.M.3    Ashford, D.A.4    Ricardo, C.P.5    Jackson, P.A.6
  • 55
    • 0029347207 scopus 로고
    • Solubilization and partial characterization of extensin fragments from cell walls of cotton suspension cultures: Evidence for a covalent cross-link between extensin and pectin
    • Qi, X., Behrens, B. X., West, P. R., and Mort, A. J. (1995). Solubilization and partial characterization of extensin fragments from cell walls of cotton suspension cultures: evidence for a covalent cross-link between extensin and pectin. Plant Physiol. 108, 1691-1701.
    • (1995) Plant Physiol. , vol.108 , pp. 1691-1701
    • Qi, X.1    Behrens, B.X.2    West, P.R.3    Mort, A.J.4
  • 56
    • 77955669078 scopus 로고    scopus 로고
    • The hydroxyproline-rich glycoprotein domain of the Arabidopsis LRX1 requires Tyr for function but not for insolubilization in the cell wall
    • Ringli, C. (2010). The hydroxyproline-rich glycoprotein domain of the Arabidopsis LRX1 requires Tyr for function but not for insolubilization in the cell wall. Plant J. 63, 662-669.
    • (2010) Plant J. , vol.63 , pp. 662-669
    • Ringli, C.1
  • 58
    • 0041529525 scopus 로고    scopus 로고
    • Systemic signaling in tomato plants for defense against herbivores: Isolation and characterization of three novel defense-signaling glycopeptides hormones coded in a single precursor gene
    • Ryan, C. A., and Pearce, G. (2003). Systemic signaling in tomato plants for defense against herbivores: isolation and characterization of three novel defense-signaling glycopeptides hormones coded in a single precursor gene. J. Biol. Chem. 278, 30044-30050.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30044-30050
    • Ryan, C.A.1    Pearce, G.2
  • 59
    • 0030131115 scopus 로고    scopus 로고
    • Isolation of pl 4.6 extensin peroxidase from tomato cell suspension cultures and identification of Val-Tyr-Lys as putative intermolecular cross-link site
    • Schnabelrauch, L. S., Kieliszewski, M., Upham, B. L., Alizedeh, H., and Lamport, D. T. (1996). Isolation of pl 4.6 extensin peroxidase from tomato cell suspension cultures and identification of Val-Tyr-Lys as putative intermolecular cross-link site. Plant J. 4, 477-489.
    • (1996) Plant J. , vol.4 , pp. 477-489
    • Schnabelrauch, L.S.1    Kieliszewski, M.2    Upham, B.L.3    Alizedeh, H.4    Lamport, D.T.5
  • 60
    • 84901040491 scopus 로고    scopus 로고
    • Identification of novel peptidyl serine O-galactosyltransferase gene family in plants
    • in Melbourne, July 23-30, IBC2011 Abstract 116
    • Shimma, Y., Saito, F., Suyama, A., Oka, T., Yoko-o, T., Matsuoka, K., and Jigami, Y. (2011). "Identification of novel peptidyl serine O-galactosyltransferase gene family in plants, " in XVIII International Botanical Congress, Melbourne, July 23-30, IBC2011 Abstract 116.
    • (2011) XVIII International Botanical Congress
    • Shimma, Y.1    Saito, F.2    Suyama, A.3    Oka, T.4    Yoko-o, T.5    Matsuoka, K.6    Jigami, Y.7
  • 61
    • 77953193626 scopus 로고    scopus 로고
    • A bioinformatics approach to the identification, classification, and analysis of hydroxyproline-rich glycoproteins
    • Showalter, A. M., Keppler, B., Lichtenberg, J., Gu, D., and Welch, L. R. (2010). A bioinformatics approach to the identification, classification, and analysis of hydroxyproline-rich glycoproteins. Plant Physiol. 153, 485-513.
    • (2010) Plant Physiol. , vol.153 , pp. 485-513
    • Showalter, A.M.1    Keppler, B.2    Lichtenberg, J.3    Gu, D.4    Welch, L.R.5
  • 62
    • 0035815610 scopus 로고    scopus 로고
    • Contiguous hydroxyproline residues direct hydroxyproline arabinosylation in Nicotiana tabacum
    • Shpak, E., Barbar, E., Leykam, J. F., and Kieliszewski, M. J. (2001). Contiguous hydroxyproline residues direct hydroxyproline arabinosylation in Nicotiana tabacum. J. Biol. Chem. 276, 11272-11278.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11272-11278
    • Shpak, E.1    Barbar, E.2    Leykam, J.F.3    Kieliszewski, M.J.4
  • 63
    • 0033592904 scopus 로고    scopus 로고
    • Synthetic genes for glycoprotein design and the elucidation of hydroxyproline-O-glycosylation codes
    • Shpak, E., Leykam, J. F., and Kieliszewski, M. J. (1999). Synthetic genes for glycoprotein design and the elucidation of hydroxyproline-O-glycosylation codes. Proc. Natl. Acad. Sci. U.S.A. 96, 14736-14741.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14736-14741
    • Shpak, E.1    Leykam, J.F.2    Kieliszewski, M.J.3
  • 66
    • 0000078814 scopus 로고
    • The role of carbohydrate in maintaining extensin in an extended conformation
    • Stafstrom, J. P., and Staehelin, L. A. (1986). The role of carbohydrate in maintaining extensin in an extended conformation. Plant Physiol. 81, 242-246.
    • (1986) Plant Physiol. , vol.81 , pp. 242-246
    • Stafstrom, J.P.1    Staehelin, L.A.2
  • 67
    • 0031889952 scopus 로고    scopus 로고
    • Biochemistry of the extracellular matrix of Volvox
    • Sumper, M., and Hallmann, A. (1998). Biochemistry of the extracellular matrix of Volvox. Int. Rev. Cytol. 180, 51-85.
    • (1998) Int. Rev. Cytol. , vol.180 , pp. 51-85
    • Sumper, M.1    Hallmann, A.2
  • 68
    • 0019888657 scopus 로고
    • Plant prolyl hydroxylase recognizes poly(l-proline) II helix
    • Tanaka, M., Sato, K., and Uchida, T. (1981). Plant prolyl hydroxylase recognizes poly(l-proline) II helix. J. Biol. Chem. 256, 11397-11400.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11397-11400
    • Tanaka, M.1    Sato, K.2    Uchida, T.3
  • 69
    • 12544255287 scopus 로고    scopus 로고
    • Characterization of a second Arabidopsis thaliana prolyl 4-hydroxylase with distinct substrate specificity
    • Tiainen, P., Myllyharju, J., and Koivunen, P. (2005). Characterization of a second Arabidopsis thaliana prolyl 4-hydroxylase with distinct substrate specificity. J. Biol. Chem. 280, 1142-1148.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1142-1148
    • Tiainen, P.1    Myllyharju, J.2    Koivunen, P.3
  • 71
    • 0000724838 scopus 로고
    • Reinforced polyproline II conformation in a hydroxyproline-rich cell wall glycoprotein from carrot root
    • Van Holst, G. J., and Varner, J. E. (1984). Reinforced polyproline II conformation in a hydroxyproline-rich cell wall glycoprotein from carrot root. Plant Physiol. 74, 247-251.
    • (1984) Plant Physiol. , vol.74 , pp. 247-251
    • Van Holst, G.J.1    Varner, J.E.2
  • 74
    • 34447322538 scopus 로고    scopus 로고
    • Arabidopsis prolyl 4-hydroxylases are differentially expressed in response to hypoxia, anoxia and mechanical wounding
    • Vlad, F., Spano, T., Vlad, D., Bou Daher, F., Ouelhadj, A., and Kalaitzis, P. (2007). Arabidopsis prolyl 4-hydroxylases are differentially expressed in response to hypoxia, anoxia and mechanical wounding. Physiol. Plant130, 471-483.
    • (2007) Physiol. Plant , vol.130 , pp. 471-483
    • Vlad, F.1    Spano, T.2    Vlad, D.3    Bou Daher, F.4    Ouelhadj, A.5    Kalaitzis, P.6
  • 76
    • 67650175435 scopus 로고    scopus 로고
    • Cis-element-and transcriptome-based screening of root hair-specific genes and their functional characterization in Arabidopsis
    • Won, S. K., Lee, Y. J., Yeon Lee, H., Kyung Heo, Y., Cho, M., and Hyung-Taeg, C. (2009). Cis-element-and transcriptome-based screening of root hair-specific genes and their functional characterization in Arabidopsis. Plant Physiol. 150, 1459-1473.
    • (2009) Plant Physiol. , vol.150 , pp. 1459-1473
    • Won, S.K.1    Lee, Y.J.2    Yeon Lee, H.3    Kyung Heo, Y.4    Cho, M.5    Hyung-Taeg, C.6
  • 77
    • 12744261335 scopus 로고    scopus 로고
    • Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum
    • Yuasa, K., Toyooka, K., Fukuda, H., and Matsuoka, K. (2005). Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum. Plant J. 41, 81-94.
    • (2005) Plant J. , vol.41 , pp. 81-94
    • Yuasa, K.1    Toyooka, K.2    Fukuda, H.3    Matsuoka, K.4
  • 78
    • 0036692336 scopus 로고    scopus 로고
    • Tomato LeAGP-1 arabinogalactan-protein purified from transgenic tobacco corroborates the Hyp contiguity hypothesis
    • Zhao, Z. D., Tan, L., Showalter, A. M., Lamport, D. T. A., and Kieliszewski, M. J. (2002). Tomato LeAGP-1 arabinogalactan-protein purified from transgenic tobacco corroborates the Hyp contiguity hypothesis. Plant J. 31, 431-444.
    • (2002) Plant J. , vol.31 , pp. 431-444
    • Zhao, Z.D.1    Tan, L.2    Showalter, A.M.3    Lamport, D.T.A.4    Kieliszewski, M.J.5


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