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Volumn 49, Issue 324, 1998, Pages 1073-1079

The plant secretory system: Mechanisms, pathways and applications in biotechnology (Meeting held at York University, UK, 2-5 July 1997)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL PATHWAY; BIOTECHNOLOGY RESOURCES; PROTEIN SYNTHESIS; SECRETORY SYSTEM;

EID: 0031815792     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/49.324.1073     Document Type: Conference Paper
Times cited : (1)

References (13)
  • 1
    • 0031131626 scopus 로고    scopus 로고
    • Cloning and subcellular location of an Arabidopsis receptor-like protein that shares common features with protein-sorting receptors of eukaryotic cells
    • Ahmed SU, Bar-Peled M, Raikhel NV. 1997. Cloning and subcellular location of an Arabidopsis receptor-like protein that shares common features with protein-sorting receptors of eukaryotic cells. Plant Physiology 114, 325-36.
    • (1997) Plant Physiology , vol.114 , pp. 325-336
    • Ahmed, S.U.1    Bar-Peled, M.2    Raikhel, N.V.3
  • 2
    • 0031420939 scopus 로고    scopus 로고
    • Co-expression of the maize ?-zein and β- Zein genes results in stable accumulation of ?-zein in endoplasmic reticulum-derived protein bodies formed by β-zein
    • Bagga S, Adams HP, Rodriguez FD, Kemp JD, Sengupta-Gopalan C. 1997. Co-expression of the maize ?-zein and β- zein genes results in stable accumulation of ?-zein in endoplasmic reticulum-derived protein bodies formed by β-zein. The Plant Cell 9, 1683-96.
    • (1997) The Plant Cell , vol.9 , pp. 1683-1696
    • Bagga, S.1    Adams, H.P.2    Rodriguez, F.D.3    Kemp, J.D.4    Sengupta-Gopalan, C.5
  • 6
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito RR. 1997. ER quality control: the cytoplasmic connection. Cell 88, 427-30.
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 7
    • 0030900410 scopus 로고    scopus 로고
    • The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains
    • Lupattelli F, Pedrazzini E, Bollini R, Vitale A, Ceriotti A. 1997. The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains. The Plant Cell 9, 1-14.
    • (1997) The Plant Cell , vol.9 , pp. 1-14
    • Lupattelli, F.1    Pedrazzini, E.2    Bollini, R.3    Vitale, A.4    Ceriotti, A.5
  • 10
    • 0030296081 scopus 로고    scopus 로고
    • The vacuolar targeting signal of the 2S albumin from Brazil nut resides at the C terminus and involves the C-terminal propeptide as an essential element
    • Saalbach G, Rosso M, Schumann U. 1996. The vacuolar targeting signal of the 2S albumin from Brazil nut resides at the C terminus and involves the C-terminal propeptide as an essential element. Plant Physiology 112, 975-85.
    • (1996) Plant Physiology , vol.112 , pp. 975-985
    • Saalbach, G.1    Rosso, M.2    Schumann, U.3
  • 11
    • 0028236274 scopus 로고
    • Targeting of membrane proteins to endosomes and lysosomes
    • Sandoval IV, Bakke O. 1994. Targeting of membrane proteins to endosomes and lysosomes. Trends in Cell Biology 4, 292-7.
    • (1994) Trends in Cell Biology , vol.4 , pp. 292-297
    • Sandoval, I.V.1    Bakke, O.2
  • 12
    • 0031008564 scopus 로고    scopus 로고
    • The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates
    • Saris N, Holkeri H, Craven RA, Stirling CJ, Makarow M. 1997. The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates. Journal of Cell Biology 137, 813-24.
    • (1997) Journal of Cell Biology , vol.137 , pp. 813-824
    • Saris, N.1    Holkeri, H.2    Craven, R.A.3    Stirling, C.J.4    Makarow, M.5
  • 13
    • 0030993132 scopus 로고    scopus 로고
    • A recombinant protein of two high molecular weight glutenins alters gluten polymer formation in transgenic wheat
    • Shimoni Y, Blechl AE, Anderson OD, Galili G. 1997. A recombinant protein of two high molecular weight glutenins alters gluten polymer formation in transgenic wheat. Journal of Biological Chemistry 272, 15488-95.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 15488-15495
    • Shimoni, Y.1    Blechl, A.E.2    Anderson, O.D.3    Galili, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.