DOI: 10.1016/j.jbiosc.2011.09.011. Arabidopsis β1,2-xylosyltransferase: Substrate specificity and participation in the plant-specific N-glycosylation pathway

Arabidopsis β1,2-xylosyltransferase: Substrate specificity and participation in the plant-specific N-glycosylation pathway

10.1016/j.jbiosc.2011.09.011

Crossref journal-article

Elsevier BV

Journal of Bioscience and Bioengineering (78)

Bibliography

Kajiura, H., Okamoto, T., Misaki, R., Matsuura, Y., & Fujiyama, K. (2012). Arabidopsis Î²1,2-xylosyltransferase: Substrate specificity and participation in the plant-specific N-glycosylation pathway. Journal of Bioscience and Bioengineering, 113(1), 48â54.

Authors 5

Hiroyuki Kajiura (first)
Toru Okamoto (additional)
Ryo Misaki (additional)
Yoshiharu Matsuura (additional)
Kazuhito Fujiyama (additional)

References 27 Referenced 27

10.1126/science.291.5512.2364 / Science / Intracellular function of N-linked glycans by Helenius (2001)
10.1093/glycob/3.2.97 / Glycobiology / Biological roles of oligosaccharides: all of the theories are correct by Varki (1993)
10.1146/annurev.biochem.73.011303.073752 / Annu. Rev. Biochem. / Roles of N-linked glycans in the endoplasmic reticulum by Helenius (2004)
10.1146/annurev.bi.54.070185.003215 / Annu. Rev. Biochem. / Assembly of asparagine-linked oligosaccharides by Kornfeld (1985)
10.1016/S0014-5793(00)01443-5 / FEBS Lett. / Molecular cloning and functional expression of β1, 2-xylosyltransferase cDNA from Arabidopsis thaliana by Strasser (2000)
10.1016/S0304-4165(01)00151-9 / Biochim. Biophys. Acta / Cloning and expression of cDNAs encoding α1,3-fucosyltransferase homologues from Arabidopsis thaliana by Wilson (2001)
10.1016/j.phytochem.2006.07.007 / Phytochemistry / Molecular cloning and heterologous expression of β1,2-xylosyltransferase and core α1,3-fucosyltransferase from maize by Bondili (2006)
10.1105/tpc.107.052985 / Plant Cell / A unique β1,3-galactosyltransferase is indispensable for the biosynthesis of N-glycans containing Lewis a structures in Arabidopsis thaliana by Strasser (2007)
10.1042/BJ20042091 / Biochem. J. / Arabidopsis thaliana β1,2-xylosyltransferase: an unusual glycosyltransferase with the potential to act at multiple stages of the plant N-glycosylation pathway by Bencúr (2005)
10.1111/j.1467-7652.2008.00353.x / Plant Biotechnol. J. / Down-regulated expression of plant-specific glycoepitopes in alfalfa by Sourrouille (2008)
10.1046/j.0960-7412.2002.01604.x / Plant J. / Structural requirements for Arabidopsis β1,2-xylosyltransferase activity and targeting to the Golgi by Pagny (2003)
10.1074/jbc.275.15.11451 / J. Biol. Chem. / β(1,2)-Xylose and α(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens by van Ree (2000)
10.1159/000096114 / Int. Arch. Allergy Immunol. / The role of protein glycosylation in allergy by Altmann (2007)
10.1073/pnas.96.8.4692 / Proc. Natl. Acad. Sci. USA / Stable expression of human β1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns by Palacpac (1999)
10.1271/bbb.65.2482 / Biosci. Biotechnol. Biochem. / Glycoproteins secreted from suspension-cultured tobacco BY2 cells have distinct glycan structures from intracellular glycoproteins by Misaki (2001)
10.1093/glycob/cwq028 / Glycobiology / Arabidopsis thaliana ALG3 mutant synthesizes immature oligosaccharides in the ER and accumulates unique N-glycans by Kajiura (2010)
10.1152/physiol.00005.2004 / Physiology / The pH of the secretory pathway: measurement, determinants, and regulation by Paroutis (2004)
10.1111/j.1365-313X.2005.02648.x / Plant J. / Molecular cloning and characterization of Arabidopsis thaliana Golgi α-mannosidase II, a key enzyme in the formation of complex N-glycans in plants by Strasser (2006)
10.1074/jbc.M110.196097 / J. Biol. Chem. / Reduced immunogenicity of Arabidopsis hybrid glycosylation1 (hgl1) N-glycans due to altered accessibility of xylose and core fucose epitopes by Kaulfuerst-Soboll (2011)
10.1111/j.1467-7652.2009.00497.x / Plant Biotechnol. J. / Plant-specific glycosylation patterns in the context of therapeutic protein production by Gomord (2010)
10.1105/tpc.105.036400 / Plant Cell / Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway by Saint-Jore-Dupas (2006)
10.1073/pnas.0800237105 / Proc. Natl. Acad. Sci. USA / Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus by Kang (2008)
10.1104/pp.102.4.1109 / Plant Physiol. / Isolation of a mutant Arabidopsis plant that lacks N-acetyl glucosaminyl transferase I and is unable to synthesize Golgi-modified complex N-linked glycans by von Schaewen (1993)
10.1016/S0014-5793(04)00150-4 / FEBS Lett. / Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose by Strasser (2004)
10.1021/bp0001516 / Biotechnol. Prog. / Expression and purification of functional human r-1-antitrypsin from cultured plant cells by Huang (2001)
10.1073/pnas.0600879103 / Proc. Natl. Acad. Sci. USA / An antibody produced in tobacco expressing a hybrid β-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes by Bakker (2006)
10.1111/j.1467-7652.2009.00414.x / Plant Biotechnol. J. / Transient co-expression for fast and high-yield production of antibodies with human-like N-glycans in plant by Vézina (2009)

Dates

Type	When
Created	13 years, 9 months ago (Nov. 14, 2011, 11:25 a.m.)
Deposited	1 year, 3 months ago (May 20, 2024, 3:28 p.m.)
Indexed	1 year, 2 months ago (June 9, 2024, 3:51 a.m.)
Issued	13 years, 7 months ago (Jan. 1, 2012)
Published	13 years, 7 months ago (Jan. 1, 2012)
Published Print	13 years, 7 months ago (Jan. 1, 2012)

Funders 0

None

BibTeX

@article{Kajiura_2012, title={Arabidopsis β1,2-xylosyltransferase: Substrate specificity and participation in the plant-specific N-glycosylation pathway}, volume={113}, ISSN={1389-1723}, url={http://dx.doi.org/10.1016/j.jbiosc.2011.09.011}, DOI={10.1016/j.jbiosc.2011.09.011}, number={1}, journal={Journal of Bioscience and Bioengineering}, publisher={Elsevier BV}, author={Kajiura, Hiroyuki and Okamoto, Toru and Misaki, Ryo and Matsuura, Yoshiharu and Fujiyama, Kazuhito}, year={2012}, month=jan, pages={48–54} }

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      "value": "Journal of Bioscience and Bioengineering",
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    },
    {
      "value": "https://doi.org/10.1016/j.jbiosc.2011.09.011",
      "name": "articlelink",
      "label": "CrossRef DOI link to publisher maintained version"
    },
    {
      "value": "article",
      "name": "content_type",
      "label": "Content Type"
    },
    {
      "value": "Copyright \u00a9 2011 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.",
      "name": "copyright",
      "label": "Copyright"
    }
  ]
}