메뉴 건너뛰기




Volumn 16, Issue 4, 2005, Pages 345-353

Comparison of Golgi apparatus and endoplasmic reticulum proteins from livers of juvenile and aged rats using a novel technique for separation and enrichment of organelles

Author keywords

Continuous flow ultracentrifugation; Endoplasmic reticulum; Golgi apparatus; Organelle enrichment; Organelle separation

Indexed keywords


EID: 84867548442     PISSN: 15240215     EISSN: 19434731     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (12)

References (28)
  • 1
    • 0037176230 scopus 로고    scopus 로고
    • The functional proteomics toolbox: Methods and applications
    • Hunter TC, Andon NL, Koller A, et al. The functional proteomics toolbox: methods and applications. J Chromatogr B 2002;782:165-181.
    • (2002) J Chromatogr B , vol.782 , pp. 165-181
    • Hunter, T.C.1    Andon, N.L.2    Koller, A.3
  • 2
    • 0042921676 scopus 로고    scopus 로고
    • Application of separation technologies to proteomics research
    • Isaaq HJ. Application of separation technologies to proteomics research. Adv Prot Chem 2003;65:249-269.
    • (2003) Adv Prot Chem , vol.65 , pp. 249-269
    • Isaaq, H.J.1
  • 3
    • 0036745679 scopus 로고    scopus 로고
    • Methods for fractionation, separation an profiling of proteins
    • Isaaq HJ, Conrads TP, Janini GM, et al. Methods for fractionation, separation an profiling of proteins. Electrophoresis 2002;23:3048-3061.
    • (2002) Electrophoresis , vol.23 , pp. 3048-3061
    • Isaaq, H.J.1    Conrads, T.P.2    Janini, G.M.3
  • 4
    • 0038555473 scopus 로고    scopus 로고
    • Strategies for the enrichment and identification of basic proteins in proteome projects
    • Bae S-H, Harris AG, Hains PG, et al. Strategies for the enrichment and identification of basic proteins in proteome projects. Proteomics 2003;3:569-579.
    • (2003) Proteomics , vol.3 , pp. 569-579
    • Bae, S.-H.1    Harris, A.G.2    Hains, P.G.3
  • 5
    • 0033838003 scopus 로고    scopus 로고
    • Towards high performance two-dimensional gel electrophoresis using ultrazoom gels
    • Hoving H, Voshol H, van Oostrum J. Towards high performance two-dimensional gel electrophoresis using ultrazoom gels. Electrophoresis 2000;21:2617-2621.
    • (2000) Electrophoresis , vol.21 , pp. 2617-2621
    • Hoving, H.1    Voshol, H.2    van Oostrum, J.3
  • 6
    • 0034095972 scopus 로고    scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg A, Obermaier C, Boguth G, et al. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 2000;21:1037-1053.
    • (2000) Electrophoresis , vol.21 , pp. 1037-1053
    • Görg, A.1    Obermaier, C.2    Boguth, G.3
  • 7
    • 0035225641 scopus 로고    scopus 로고
    • Chromatographic separations as a prelude to two-dimensional electrophoresis inproteomics analysis
    • Butt A, Davison MD, Smith GJ, et al. Chromatographic separations as a prelude to two-dimensional electrophoresis inproteomics analysis. Proteomics 2001;1:42-53.
    • (2001) Proteomics , vol.1 , pp. 42-53
    • Butt, A.1    Davison, M.D.2    Smith, G.J.3
  • 8
    • 0036917339 scopus 로고    scopus 로고
    • Sample prefractionation with Sephadex isoelectric focusing prior to narrow pH range two-dimensional gels
    • Görg A, Boguth G, Köpf A, et al. Sample prefractionation with Sephadex isoelectric focusing prior to narrow pH range two-dimensional gels. Proteomics 2002;2:1652-1657.
    • (2002) Proteomics , vol.2 , pp. 1652-1657
    • Görg, A.1    Boguth, G.2    Köpf, A.3
  • 9
    • 0033063592 scopus 로고    scopus 로고
    • Subcellular fractionation, electromigration analysis and mapping of organelles
    • Pasquali C, Fialka I, Huber LA. Subcellular fractionation, electromigration analysis and mapping of organelles. J Chromatogr B 1999;722:89-102.
    • (1999) J Chromatogr B , vol.722 , pp. 89-102
    • Pasquali, C.1    Fialka, I.2    Huber, L.A.3
  • 10
    • 3042606558 scopus 로고    scopus 로고
    • Annotating proteins from endoplasmic reticulum and Golgi apparatus in eukaryotic proteomes
    • Wrzeszczynski KO, Rost B. Annotating proteins from endoplasmic reticulum and Golgi apparatus in eukaryotic proteomes. Cell Mol Life Sci 2004;61:1341-1353.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1341-1353
    • Wrzeszczynski, K.O.1    Rost, B.2
  • 12
    • 0033769457 scopus 로고    scopus 로고
    • Proteomes of rat liver Golgi complex: Minor proteins are identified through sequential fractionation
    • Taylor RS, Wu CC, Hays LG, et al. Proteomes of rat liver Golgi complex: Minor proteins are identified through sequential fractionation. Electrophoresis 2000;21:3441-3459.
    • (2000) Electrophoresis , vol.21 , pp. 3441-3459
    • Taylor, R.S.1    Wu, C.C.2    Hays, L.G.3
  • 13
    • 0035895890 scopus 로고    scopus 로고
    • Proteomics characterization of abundant Golgi membrane proteins
    • Bell AW, Ward MA, Blackstock WP, et al. Proteomics characterization of abundant Golgi membrane proteins. J Biol Chem 2001;276:5152-5165.
    • (2001) J Biol Chem , vol.276 , pp. 5152-5165
    • Bell, A.W.1    Ward, M.A.2    Blackstock, W.P.3
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0029955716 scopus 로고    scopus 로고
    • Possible association of Chaperonin 60 with secretory proteins in pancreatic acinar cells
    • Le Gall IM and Bendayan M. Possible association of Chaperonin 60 with secretory proteins in pancreatic acinar cells. J Histochem Cytochem 1996;44:743-749.
    • (1996) J Histochem Cytochem , vol.44 , pp. 743-749
    • Le Gall, I.M.1    Bendayan, M.2
  • 18
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorhonuclear leukocyte
    • Borregaard N, Cowland JB. Granules of the human neutrophilic polymorhonuclear leukocyte. Blood 1997;89:3503-3521.
    • (1997) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 19
    • 0033525855 scopus 로고    scopus 로고
    • Intracellular proteolytic processing of the heavy chain of rat pre-α-inhibitor
    • Thuveson M and Fries E. Intracellular proteolytic processing of the heavy chain of rat pre-α-inhibitor. J Biol Chem 1999;274:6741-6746.
    • (1999) J Biol Chem , vol.274 , pp. 6741-6746
    • Thuveson, M.1    Fries, E.2
  • 20
    • 0036080131 scopus 로고    scopus 로고
    • The transporter associated with antigen processing: Function and implication in human disease
    • Lankat-Buttgereit B, Tampé R. The transporter associated with antigen processing: function and implication in human disease. Physiol Rev 2002;82:187-204.
    • (2002) Physiol Rev , vol.82 , pp. 187-204
    • Lankat-Buttgereit, B.1    Tampé, R.2
  • 21
    • 0032584740 scopus 로고    scopus 로고
    • A formiminotransferase cyclodeaminase isoform is localized to the Golgi complex and can mediate interaction of trans-Golgi network-derived vesicles with microtubules
    • Hennig D, Scales SJ, Moreau A, et al. A formiminotransferase cyclodeaminase isoform is localized to the Golgi complex and can mediate interaction of trans-Golgi network-derived vesicles with microtubules. J Biol Chem 1998;273:19602-19611.
    • (1998) J Biol Chem , vol.273 , pp. 19602-19611
    • Hennig, D.1    Scales, S.J.2    Moreau, A.3
  • 22
    • 0032584725 scopus 로고    scopus 로고
    • 58K, a microtubule-binding Golgi protein, is a formimiminotransferase cyclodeaminase
    • Bashour A-M, Bloom GS. 58K, a microtubule-binding Golgi protein, is a formimiminotransferase cyclodeaminase. J Biol Chem 1998;273:19612-19617.
    • (1998) J Biol Chem , vol.273 , pp. 19612-19617
    • Bashour, A.-M.1    Bloom, G.S.2
  • 23
    • 0032509448 scopus 로고    scopus 로고
    • Molecular cloning, characterization and dynamics of rat formiminotransferase cyclodeaminase
    • 33850-33834
    • Gao Y, Alvarez C, Nelson DS, et al. Molecular cloning, characterization and dynamics of rat formiminotransferase cyclodeaminase. J Biol Chem 1998;273:33850-33834.
    • (1998) J Biol Chem , vol.273
    • Gao, Y.1    Alvarez, C.2    Nelson, D.S.3
  • 24
    • 0028795422 scopus 로고
    • Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: Comparison with protein disulfide isomerase
    • Lundstrom-Ljung J, Birnbach U, Rupp K, et al. Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase. FEBS Lett 1995;357:305-308.
    • (1995) FEBS Lett , vol.357 , pp. 305-308
    • Lundstrom-Ljung, J.1    Birnbach, U.2    Rupp, K.3
  • 25
    • 8544263881 scopus 로고    scopus 로고
    • AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation
    • Zhong X, Shen Y, Ballar P, et al. AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation. J Biol Chem 2004;279:45676-45684.
    • (2004) J Biol Chem , vol.279 , pp. 45676-45684
    • Zhong, X.1    Shen, Y.2    Ballar, P.3
  • 26
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the the cytosolic ubiquitin-proteasome pathway
    • Hiller MM, Finger A, Schweiger M, et al. ER degradation of a misfolded luminal protein by the the cytosolic ubiquitin-proteasome pathway. Science 1996, 273, 1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3
  • 27
    • 0034331033 scopus 로고    scopus 로고
    • The meteoric rise of regulated intracellular proteolysis
    • Mayer RJ. The meteoric rise of regulated intracellular proteolysis. Nature Rev Mol Cell Biol 2000;1:145-148.
    • (2000) Nature Rev Mol Cell Biol , vol.1 , pp. 145-148
    • Mayer, R.J.1
  • 28
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L, Helenius A. Quality control in the endoplasmic reticulum. Nature Rev Mol Cell Biol 2003;4:181-191.
    • (2003) Nature Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.