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Volumn 394, Issue 1, 2006, Pages 115-124

Gene expression patterns and catalytic properties of UDP-D-glucose 4-epimerases from barley (Hordeum vulgare L.)

Author keywords

Barley; Gene expression; Nucleotide sugar; Plant cell wall; UDP D glucose 4 epimerase (UGE); UDP GlcNAc

Indexed keywords

BIOLOGICAL ORGANS; CATALYSIS; GLUCOSE; SPECTROPHOTOMETRY; SUGARS;

EID: 32944477384     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051329     Document Type: Article
Times cited : (43)

References (50)
  • 1
    • 0034863672 scopus 로고    scopus 로고
    • Molecular genetics of nucleotide sugar interconversion pathways in plants
    • Reiter, W. D. and Vanzin, G. F. (2001) Molecular genetics of nucleotide sugar interconversion pathways in plants. Plant Mol. Biol. 47, 95-113
    • (2001) Plant Mol. Biol. , vol.47 , pp. 95-113
    • Reiter, W.D.1    Vanzin, G.F.2
  • 2
    • 2442434678 scopus 로고    scopus 로고
    • Nucleotide sugar interconversions and cell wall biosynthesis: How to bring the inside to the outside
    • Seifert, G. J. (2004) Nucleotide sugar interconversions and cell wall biosynthesis: how to bring the inside to the outside. Curr. Opin. Plant Biol. 7, 277-284
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 277-284
    • Seifert, G.J.1
  • 3
    • 27244440372 scopus 로고    scopus 로고
    • Characterization and expression patterns of UDP-D-glucuronate decarboxylase genes in barley
    • Zhang, Q., Shirley, N., Lahnstein, J. and Fincher, G. B. (2005) Characterization and expression patterns of UDP-D-glucuronate decarboxylase genes in barley. Plant Physiol. 138, 131-141
    • (2005) Plant Physiol. , vol.138 , pp. 131-141
    • Zhang, Q.1    Shirley, N.2    Lahnstein, J.3    Fincher, G.B.4
  • 4
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 Å resolution
    • Bauer, A. J., Rayment, I., Frey, P. A. and Holden, H. M. (1992) The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 Å resolution. Proteins 12, 372-381
    • (1992) Proteins , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 5
    • 0035878066 scopus 로고    scopus 로고
    • UDP-galactose 4-epimerase from Escherichia coli: Formation of catalytic site during reversible folding
    • Barat, B. and Bhattacharyya, D. (2001) UDP-galactose 4-epimerase from Escherichia coli: formation of catalytic site during reversible folding. Arch. Biochem. Biophys. 391, 188-196
    • (2001) Arch. Biochem. Biophys. , vol.391 , pp. 188-196
    • Barat, B.1    Bhattacharyya, D.2
  • 6
    • 0030038192 scopus 로고    scopus 로고
    • Functional expression of uridine 5′-diphospho-glucose 4-epimerase (EC 5.1.3.2) from Arabidopsis thaliana in Saccharomyces cerevisiae and Escherichia coli
    • Dörmann, P. and Benning, C. (1996) Functional expression of uridine 5′-diphospho-glucose 4-epimerase (EC 5.1.3.2) from Arabidopsis thaliana in Saccharomyces cerevisiae and Escherichia coli. Arch. Biochem. Biophys. 327, 27-34
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 27-34
    • Dörmann, P.1    Benning, C.2
  • 7
    • 0032142978 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a UDP-glucose 4-epimerase gene (gaZE) and its expression in pea tissues
    • Lake, M. R., Williamson, C. L. and Slocum, R. D. (1998) Molecular cloning and characterization of a UDP-glucose 4-epimerase gene (gaZE) and its expression in pea tissues. Plant Physiol. Biochem. 36, 555-562
    • (1998) Plant Physiol. Biochem. , vol.36 , pp. 555-562
    • Lake, M.R.1    Williamson, C.L.2    Slocum, R.D.3
  • 8
    • 0345086430 scopus 로고    scopus 로고
    • Isolation and expression of two cDNA clones encoding UDP-glucose epimerase expressed in developing seeds of the endospermous legume guar
    • Joersbo, M., Pedersen, S. G., Nielsen, J. E., Marcussen, J. and Brunstedt, J. (1999) Isolation and expression of two cDNA clones encoding UDP-glucose epimerase expressed in developing seeds of the endospermous legume guar. Plant Sci. 142. 147-153
    • (1999) Plant Sci. , vol.142 , pp. 147-153
    • Joersbo, M.1    Pedersen, S.G.2    Nielsen, J.E.3    Marcussen, J.4    Brunstedt, J.5
  • 9
    • 16644371952 scopus 로고    scopus 로고
    • The biosynthesis of UDP-galacturonic acid in plants. Functional cloning and characterization of Arabidopsis UDP-D-glucuronic acid 4-epimerase
    • Gu, X. and Bar-Peled, M. (2004) The biosynthesis of UDP-galacturonic acid in plants. Functional cloning and characterization of Arabidopsis UDP-D-glucuronic acid 4-epimerase. Plant Physiol. 136, 4256-4264
    • (2004) Plant Physiol. , vol.136 , pp. 4256-4264
    • Gu, X.1    Bar-Peled, M.2
  • 10
    • 3543019727 scopus 로고    scopus 로고
    • The biosynthesis of D-galacturonate in plants. Functional cloning and characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from Arabidopsis
    • Mølhøj, M., Verma, R. and Reiter, W. D. (2004) The biosynthesis of D-galacturonate in plants. Functional cloning and characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from Arabidopsis. Plant Physiol. 135, 1221-1230
    • (2004) Plant Physiol. , vol.135 , pp. 1221-1230
    • Mølhøj, M.1    Verma, R.2    Reiter, W.D.3
  • 11
    • 0037329646 scopus 로고    scopus 로고
    • The biosynthesis of L-arabinose in plants: Molecular cloning and characterization of a Golgi-localized UDP-D-xylose 4-epimerase encoded by the MUR4 gene of Arabidopsis
    • Burget, E. G., Verma, R., Molhoj, M. and Reiter, W. D. (2003) The biosynthesis of L-arabinose in plants: molecular cloning and characterization of a Golgi-localized UDP-D-xylose 4-epimerase encoded by the MUR4 gene of Arabidopsis. Plant Cell 15, 523-531
    • (2003) Plant Cell , vol.15 , pp. 523-531
    • Burget, E.G.1    Verma, R.2    Molhoj, M.3    Reiter, W.D.4
  • 12
    • 0028008831 scopus 로고
    • Genetics of galactose metabolism of Erwinia amylovora and its influence on polysaccharide synthesis and virulence of the fire blight pathogen
    • Metzger, M., Bellemann, P., Bugert, P. and Geider, K. (1994) Genetics of galactose metabolism of Erwinia amylovora and its influence on polysaccharide synthesis and virulence of the fire blight pathogen. J. Bacteriol. 176, 450-459
    • (1994) J. Bacteriol. , vol.176 , pp. 450-459
    • Metzger, M.1    Bellemann, P.2    Bugert, P.3    Geider, K.4
  • 13
    • 0025766941 scopus 로고
    • The Rhizobium meliloti exoZ/ exoB fragment of megaplasmid 2: ExoB functions as a UDP-glucose 4-epimerase and ExoZ shows homology to NodX of Rhizobium leguminosarum biovar viciae strain TOM
    • Buendia, A. M., Enenkel, B., Koplin, R., Niehaus, K., Arnold, W. and Puhler, A. (1991) The Rhizobium meliloti exoZ/ exoB fragment of megaplasmid 2: ExoB functions as a UDP-glucose 4-epimerase and ExoZ shows homology to NodX of Rhizobium leguminosarum biovar viciae strain TOM. Mol. Microbiol. 5, 1519-1530
    • (1991) Mol. Microbiol. , vol.5 , pp. 1519-1530
    • Buendia, A.M.1    Enenkel, B.2    Koplin, R.3    Niehaus, K.4    Arnold, W.5    Puhler, A.6
  • 14
    • 0037195250 scopus 로고    scopus 로고
    • Galactose biosynthesis in Arabidopsis: Genetic evidence for substrate channeling from UDP-D-galactose into cell wall polymers
    • Seifert, G. J., Barber, C., Wells, B., Dolan, L. and Roberts, K. (2002) Galactose biosynthesis in Arabidopsis: genetic evidence for substrate channeling from UDP-D-galactose into cell wall polymers. Curr. Biol. 12, 1840-1845
    • (2002) Curr. Biol. , vol.12 , pp. 1840-1845
    • Seifert, G.J.1    Barber, C.2    Wells, B.3    Dolan, L.4    Roberts, K.5
  • 16
    • 0842307342 scopus 로고    scopus 로고
    • The CesA gene family of barley. Quantitative analysis of transcripts reveals two groups of co-expressed genes
    • Burton, R. A., Shirley, N. J., King, B. J., Harvey, A. J. and Fincher, G. B. (2004) The CesA gene family of barley. Quantitative analysis of transcripts reveals two groups of co-expressed genes. Plant Physiol. 134, 224-236
    • (2004) Plant Physiol. , vol.134 , pp. 224-236
    • Burton, R.A.1    Shirley, N.J.2    King, B.J.3    Harvey, A.J.4    Fincher, G.B.5
  • 17
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 18
    • 0032506030 scopus 로고    scopus 로고
    • Large-scale protein structure modeling of the Saccharomyces cerevisiae genome
    • Sanchez, R. and Sali, A. (1998) Large-scale protein structure modeling of the Saccharomyces cerevisiae genome. Proc. Natl. Acad. Sci. U.S.A. 95, 13597-13602
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13597-13602
    • Sanchez, R.1    Sali, A.2
  • 19
    • 0038386050 scopus 로고    scopus 로고
    • 3D-Jury: A simple approach to improve protein structure predictions
    • Ginalski, K., Elofsson, A., Fischer, D. and Rychlewski, L. (2003) 3D-Jury: a simple approach to improve protein structure predictions. Bioinformatics 19, 1015-1018
    • (2003) Bioinformatics , vol.19 , pp. 1015-1018
    • Ginalski, K.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 20
    • 0021760092 scopus 로고
    • A comprehensive set of seguence analysis programs for the VAX
    • Devereux, J., Haeberli, P. and Smithies, O. (1984) A comprehensive set of seguence analysis programs for the VAX. Nucleic Acids Res. 12, 387-395
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 21
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith, T. F. and Waterman, M. S. (1981) Identification of common molecular subsequences. J. Mol. Biol. 147, 195-197
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 22
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 23
    • 84988115618 scopus 로고
    • Validation of the general purpose Tripos 5.2 force field
    • Clark, M., Cramer, R. D. and Van Opdenbosch, N. (1989) Validation of the general purpose Tripos 5.2 force field. J. Comp. Chem. 10, 982-1012
    • (1989) J. Comp. Chem. , vol.10 , pp. 982-1012
    • Clark, M.1    Cramer, R.D.2    Van Opdenbosch, N.3
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 0021035009 scopus 로고
    • Co-purification and characterization of UDP-glucose 4-epimerase and UDP-N-acetylglucosamine 4-epimerase from porcine submaxillary glands
    • Piller, F., Hanlon, M. H. and Hill, R. L. (1983) Co-purification and characterization of UDP-glucose 4-epimerase and UDP-N-acetylglucosamine 4-epimerase from porcine submaxillary glands. J. Biol. Chem. 258, 10774-10778
    • (1983) J. Biol. Chem. , vol.258 , pp. 10774-10778
    • Piller, F.1    Hanlon, M.H.2    Hill, R.L.3
  • 26
    • 0037327814 scopus 로고    scopus 로고
    • High-resolution crystal structure of Trypanosoma brucei UDP-galactose 4′-epimerase: A potential target for structure-based development of novel trypanocides
    • Shaw, M. P., Bond, C. S., Roper, J. R., Gourley, D. G., Ferguson, M. A. and Hunter, W. N. (2003) High-resolution crystal structure of Trypanosoma brucei UDP-galactose 4′-epimerase: a potential target for structure-based development of novel trypanocides. Mol. Biochem. Parasitol. 126, 173-180
    • (2003) Mol. Biochem. Parasitol. , vol.126 , pp. 173-180
    • Shaw, M.P.1    Bond, C.S.2    Roper, J.R.3    Gourley, D.G.4    Ferguson, M.A.5    Hunter, W.N.6
  • 28
    • 0035805630 scopus 로고    scopus 로고
    • Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site
    • Thoden, J. B., Wohlers, T. M., Fridovich-Keil, J. L. and Holden, H. M. (2001) Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site. J. Biol. Chem. 276, 15131-15136
    • (2001) J. Biol. Chem. , vol.276 , pp. 15131-15136
    • Thoden, J.B.1    Wohlers, T.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 29
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47, 392-400
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 30
    • 20444377995 scopus 로고    scopus 로고
    • Biosynthesis of UDP-xylose: Characterization of membrane-bound AtUxs2
    • Pattathil, S., Harper, A. D. and Bar-Peled, M. (2005) Biosynthesis of UDP-xylose: characterization of membrane-bound AtUxs2. Planta 221, 538-548
    • (2005) Planta , vol.221 , pp. 538-548
    • Pattathil, S.1    Harper, A.D.2    Bar-Peled, M.3
  • 32
    • 0026078287 scopus 로고
    • Spatial organization of the assembly pathways of glycoproteins and complex polysaccharides in the Golgi apparatus of plants
    • Moore, P. J., Swords, K. M., Lynch, M. A. and Staehelin, L. A. (1991) Spatial organization of the assembly pathways of glycoproteins and complex polysaccharides in the Golgi apparatus of plants. J. Cell Biol. 112, 589-602
    • (1991) J. Cell Biol. , vol.112 , pp. 589-602
    • Moore, P.J.1    Swords, K.M.2    Lynch, M.A.3    Staehelin, L.A.4
  • 33
    • 0037031838 scopus 로고    scopus 로고
    • Transport of UDP-galactose in plants. Identification and functional characterization of AtUTr1, an Arabidopsis thaliana UDP-galactose/UDP-glucose transporter
    • Norambuena, L., Marchant, L., Berninsone, P., Hirschberg, C. B., Silva, H. and Orellana, A. (2002) Transport of UDP-galactose in plants. Identification and functional characterization of AtUTr1, an Arabidopsis thaliana UDP-galactose/UDP-glucose transporter. J. Biol. Chem. 277, 32923-32929
    • (2002) J. Biol. Chem. , vol.277 , pp. 32923-32929
    • Norambuena, L.1    Marchant, L.2    Berninsone, P.3    Hirschberg, C.B.4    Silva, H.5    Orellana, A.6
  • 34
    • 0000642736 scopus 로고
    • Nucleoside diphosphate sugar 4-epimerases. I. Uridine diphosphate glucose 4-epimerase of wheat germ
    • Fan, D. F. and Feingold, D. S. (1969) Nucleoside diphosphate sugar 4-epimerases. I. Uridine diphosphate glucose 4-epimerase of wheat germ. Plant Physiol. 44, 599-604
    • (1969) Plant Physiol. , vol.44 , pp. 599-604
    • Fan, D.F.1    Feingold, D.S.2
  • 35
    • 0141678903 scopus 로고    scopus 로고
    • The biosynthesis of the branched-chain sugar D-apiose in plants: Functional cloning and characterization of a UDP-D-apiose/UDP-D-xylose synthase from Arabidopsis
    • Molhoj, M., Verma, R. and Reiter, W. D. (2003) The biosynthesis of the branched-chain sugar D-apiose in plants: functional cloning and characterization of a UDP-D-apiose/UDP-D-xylose synthase from Arabidopsis. Plant J. 35, 693-703
    • (2003) Plant J. , vol.35 , pp. 693-703
    • Molhoj, M.1    Verma, R.2    Reiter, W.D.3
  • 36
    • 0036909251 scopus 로고    scopus 로고
    • Recombinant UDP-glucose dehydrogenase from soybean
    • Hinterberg, B., Klos, C. and Tenhaken, R. (2002) Recombinant UDP-glucose dehydrogenase from soybean. Plant Physiol. Biochem. 40, 1011-1017
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 1011-1017
    • Hinterberg, B.1    Klos, C.2    Tenhaken, R.3
  • 37
    • 0036431530 scopus 로고    scopus 로고
    • Purification and kinetic properties of UDP-glucose dehydrogenase from sugarcane
    • Turner, W. and Botha, F. C. (2002) Purification and kinetic properties of UDP-glucose dehydrogenase from sugarcane. Arch. Biochem. Biophys. 407, 209-216
    • (2002) Arch. Biochem. Biophys. , vol.407 , pp. 209-216
    • Turner, W.1    Botha, F.C.2
  • 38
    • 0030832007 scopus 로고    scopus 로고
    • Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli
    • Liu, Y., Thoden, J. B., Kim, J., Berger, E., Gulick, A. M., Ruzicka, F. J., Holden, H. M. and Frey, P. A. (1997) Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 36, 10675-10684
    • (1997) Biochemistry , vol.36 , pp. 10675-10684
    • Liu, Y.1    Thoden, J.B.2    Kim, J.3    Berger, E.4    Gulick, A.M.5    Ruzicka, F.J.6    Holden, H.M.7    Frey, P.A.8
  • 39
    • 0015854774 scopus 로고
    • β-glucan synthesis by cell-free extracts from Lolium multiflorum endosperm
    • Smith, M. M. and Stone, B. A. (1973) β-Glucan synthesis by cell-free extracts from Lolium multiflorum endosperm. Biochim. Biophys. Acta 313, 72-94
    • (1973) Biochim. Biophys. Acta , vol.313 , pp. 72-94
    • Smith, M.M.1    Stone, B.A.2
  • 40
    • 0038060802 scopus 로고
    • Growth inhibition and metabolite pool levels in plant tissues fed D-glucosamine and D-galactose
    • Roberts, R. M., Heishman, A. and Wicklin, C. (1971) Growth inhibition and metabolite pool levels in plant tissues fed D-glucosamine and D-galactose. Plant Physiol. 48, 36-42
    • (1971) Plant Physiol. , vol.48 , pp. 36-42
    • Roberts, R.M.1    Heishman, A.2    Wicklin, C.3
  • 41
    • 84989726756 scopus 로고
    • Galactose inhibition of auxin-induced cell elongation in oat coleoptile segments
    • Yamamoto, R. and Masuda, Y. (1984) Galactose inhibition of auxin-induced cell elongation in oat coleoptile segments. Physiol. Plant. 61, 321-326
    • (1984) Physiol. Plant. , vol.61 , pp. 321-326
    • Yamamoto, R.1    Masuda, Y.2
  • 42
    • 0000509336 scopus 로고
    • Sugar nucleotide transformations in plants
    • (Stumpf, P. K. and Conn, E. E., eds.), Academic Press, New York
    • Feingold, D. S. and Avigad, G. (1980) Sugar nucleotide transformations in plants. In The Biochemistry of Plants: A Comprehensive Treatise (Stumpf, P. K. and Conn, E. E., eds.), pp. 101-170, Academic Press, New York
    • (1980) The Biochemistry of Plants: A Comprehensive Treatise , pp. 101-170
    • Feingold, D.S.1    Avigad, G.2
  • 43
    • 0037178867 scopus 로고    scopus 로고
    • Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks
    • Thoden, J. B., Henderson, J. M., Fridovich-Keil, J. L. and Holden, H. M. (2002) Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks. J. Biol. Chem. 277, 27528-27534
    • (2002) J. Biol. Chem. , vol.277 , pp. 27528-27534
    • Thoden, J.B.1    Henderson, J.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 44
    • 0242321241 scopus 로고    scopus 로고
    • The Bacillus subtilis Gne (GneA, GalE) protein can catalyse UDP-glucose as well as UDP-N-acetylglucosamine 4-epimerisation
    • Soldo, B., Scotti, C., Karamata, D. and Lazarevic, V. (2003) The Bacillus subtilis Gne (GneA, GalE) protein can catalyse UDP-glucose as well as UDP-N-acetylglucosamine 4-epimerisation. Gene 319, 65-69
    • (2003) Gene , vol.319 , pp. 65-69
    • Soldo, B.1    Scotti, C.2    Karamata, D.3    Lazarevic, V.4
  • 45
    • 2542500431 scopus 로고    scopus 로고
    • Crystal structure of WbpP, a genuine UDP-N-acetylglucosamine 4-epimerase from Pseudomonas aeruginosa: Substrate specificity in UDP-hexose 4-epimerases
    • Ishiyama, N., Creuzenet, C., Lam, J. S. and Berghuis, A. M. (2004) Crystal structure of WbpP, a genuine UDP-N-acetylglucosamine 4-epimerase from Pseudomonas aeruginosa: substrate specificity in UDP-hexose 4-epimerases. J. Biol. Chem. 279, 22635-22642
    • (2004) J. Biol. Chem. , vol.279 , pp. 22635-22642
    • Ishiyama, N.1    Creuzenet, C.2    Lam, J.S.3    Berghuis, A.M.4
  • 46
    • 0034673977 scopus 로고    scopus 로고
    • Crystallographic evidence for Tyr157 functioning as the active site base in human UDP-galactose 4-epimerase
    • Thoden, J. B., Wohlers, T. M., Fridovich-Keil, J. L. and Holden, H. M. (2000) Crystallographic evidence for Tyr157 functioning as the active site base in human UDP-galactose 4-epimerase. Biochemistry 39, 5691-5701
    • (2000) Biochemistry , vol.39 , pp. 5691-5701
    • Thoden, J.B.1    Wohlers, T.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 47
    • 0035077832 scopus 로고    scopus 로고
    • O-glycosylation of the mucin type
    • Hanisch, F. G. (2001) O-glycosylation of the mucin type. Biol. Chem. 382, 143-149
    • (2001) Biol. Chem. , vol.382 , pp. 143-149
    • Hanisch, F.G.1
  • 49
    • 0033832777 scopus 로고    scopus 로고
    • Metabolic activity decreased as an adaptive response to low internal oxygen in growing potato tubers
    • Geigenberger, P., Fernie, A. R., Gibon, Y., Christ, M. and Stitt, M. (2000) Metabolic activity decreased as an adaptive response to low internal oxygen in growing potato tubers. Biol. Chem. 381, 723-740
    • (2000) Biol. Chem. , vol.381 , pp. 723-740
    • Geigenberger, P.1    Fernie, A.R.2    Gibon, Y.3    Christ, M.4    Stitt, M.5
  • 50
    • 0000785517 scopus 로고
    • Genetic control of root hair development in Arabidopsis thaliana
    • Schiefelbein, J. W. and Somerville, C. (1990) Genetic control of root hair development in Arabidopsis thaliana. Plant Cell 2, 235-243
    • (1990) Plant Cell , vol.2 , pp. 235-243
    • Schiefelbein, J.W.1    Somerville, C.2


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