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Volumn 5, Issue 4, 2008, Pages 603-617

Complementary methods to assist subcellular fractionation in organellar proteomics

Author keywords

Centrifugation; FAOS; Fluorescence assisted organelle sorting; Free flow electrophoresis; Immunoisolation; Organelle; Proteomics; Subcellular fractionation

Indexed keywords

DEOXYRIBONUCLEASE; DEXTRAN; DIGITOXIN; IOHEXOL; RIBONUCLEASE; SILICON DIOXIDE;

EID: 51149109591     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/14789450.5.4.603     Document Type: Review
Times cited : (45)

References (96)
  • 1
    • 2942617034 scopus 로고    scopus 로고
    • Has the yo-yo stopped? An assessment of human protein-coding gene number
    • Southan C. Has the yo-yo stopped? An assessment of human protein-coding gene number. Proteomics 4(6), 1712-1726 (2004).
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1712-1726
    • Southan, C.1
  • 2
    • 37648999313 scopus 로고    scopus 로고
    • Distinguishing protein-coding and noncoding genes in the human genome
    • Clamp M, Fry B, Kamal M et al. Distinguishing protein-coding and noncoding genes in the human genome. Proc. Natl Acad. Sci. USA 104(49), 19428-19433 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.49 , pp. 19428-19433
    • Clamp, M.1    Fry, B.2    Kamal, M.3
  • 3
    • 10644268451 scopus 로고    scopus 로고
    • Zooming in: Fractionation strategies in proteomics
    • Stasyk T, Huber LA. Zooming in: fractionation strategies in proteomics. Proteomics 4(12), 3704-3716 (2004).
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3704-3716
    • Stasyk, T.1    Huber, L.A.2
  • 4
    • 33749523582 scopus 로고    scopus 로고
    • Organellar proteomics: Turning inventories into insights
    • 79, 874-879
    • Andersen JS, Mann M. Organellar proteomics: turning inventories into insights. EMBO Rep. 7(9), 874-879 (2006).
    • (2006) EMBO Rep
    • Andersen, J.S.1    Mann, M.2
  • 7
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R. Mass spectrometry and protein analysis. Science 312(5771), 212-217 (2006).
    • (2006) Science , vol.312 , Issue.5771 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 8
    • 33750728385 scopus 로고    scopus 로고
    • Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications
    • Qian WJ, Jacobs JM, Liu T, Camp DG, Smith RD. Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications. Mol. Cell Proteomics 5(10), 1727-1744 (2006).
    • (2006) Mol. Cell Proteomics , vol.5 , Issue.10 , pp. 1727-1744
    • Qian, W.J.1    Jacobs, J.M.2    Liu, T.3    Camp, D.G.4    Smith, R.D.5
  • 9
    • 33745960413 scopus 로고    scopus 로고
    • Proteomics technology in systems biology
    • Smith JC, Figeys D. Proteomics technology in systems biology. Mol. Biosyst. 2(8), 364-370 (2006).
    • (2006) Mol. Biosyst , vol.2 , Issue.8 , pp. 364-370
    • Smith, J.C.1    Figeys, D.2
  • 10
    • 27744468403 scopus 로고    scopus 로고
    • Proteomics of organelles and large cellular structures
    • Review of the recent organellar proteomic work, •
    • Yates JR III, Gilchrist A, Howell KE, Bergeron JJ. Proteomics of organelles and large cellular structures. Nat. Rev. Mol. Cell Biol. 6(9), 702-714 (2005). • Review of the recent organellar proteomic work.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , Issue.9 , pp. 702-714
    • Yates III, J.R.1    Gilchrist, A.2    Howell, K.E.3    Bergeron, J.J.4
  • 11
    • 34047109196 scopus 로고    scopus 로고
    • Bodzon-Kulakowska A, Bierczynska-Krzysik A, Dylag T et al. Methods for samples preparation in proteomic research. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 849(1-2), 1-31 (2007). • Comprehensive review of sample preparation for current proteomic research.
    • Bodzon-Kulakowska A, Bierczynska-Krzysik A, Dylag T et al. Methods for samples preparation in proteomic research. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 849(1-2), 1-31 (2007). • Comprehensive review of sample preparation for current proteomic research.
  • 13
    • 33749256309 scopus 로고    scopus 로고
    • Methods for proteomics in neuroscience
    • Tannu NS, Hemby SE. Methods for proteomics in neuroscience. Prog. Brain Res. 158, 41-82 (2006).
    • (2006) Prog. Brain Res , vol.158 , pp. 41-82
    • Tannu, N.S.1    Hemby, S.E.2
  • 14
    • 33750142806 scopus 로고    scopus 로고
    • Purification techniques of subcellular compartments for analytical and preparative purposes
    • Aubry L, Klein G. Purification techniques of subcellular compartments for analytical and preparative purposes. Methods Mol. Biol. 346, 171-185 (2006).
    • (2006) Methods Mol. Biol , vol.346 , pp. 171-185
    • Aubry, L.1    Klein, G.2
  • 15
    • 0021800788 scopus 로고
    • Characterization of protein transport between successive compartments of the Golgi apparatus: Asymmetric properties of donor and acceptor activities in a cell-free system
    • Balch WE, Rothman JE. Characterization of protein transport between successive compartments of the Golgi apparatus: asymmetric properties of donor and acceptor activities in a cell-free system. Arch. Biochem. Biophys. 240(1), 413-425 (1985).
    • (1985) Arch. Biochem. Biophys , vol.240 , Issue.1 , pp. 413-425
    • Balch, W.E.1    Rothman, J.E.2
  • 16
    • 0034632218 scopus 로고    scopus 로고
    • Fractionation of cells and subcellular particles with Percoll
    • Pertoft H. Fractionation of cells and subcellular particles with Percoll. J. Biochem. Biophys. Methods 44(1-2), 1-30 (2000).
    • (2000) J. Biochem. Biophys. Methods , vol.44 , Issue.1-2 , pp. 1-30
    • Pertoft, H.1
  • 17
    • 0343136934 scopus 로고
    • A substance for aqueous density gradients
    • Holter H, Moller KM. A substance for aqueous density gradients. Exp. Cell Res. 15(3), 631-632 (1958).
    • (1958) Exp. Cell Res , vol.15 , Issue.3 , pp. 631-632
    • Holter, H.1    Moller, K.M.2
  • 18
    • 0014930202 scopus 로고
    • A model for the behavior of vesicles in density gradients: Implications for fractionation
    • Steck TL, Straus JH, Wallach DF. A model for the behavior of vesicles in density gradients: implications for fractionation. Biochim. Biophys. Acta 203(3), 385-393 (1970).
    • (1970) Biochim. Biophys. Acta , vol.203 , Issue.3 , pp. 385-393
    • Steck, T.L.1    Straus, J.H.2    Wallach, D.F.3
  • 19
    • 33845500104 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of the secretory pathway
    • Determination of proteome of the components of the early secretory pathway using a quantitative approach, •
    • Gilchrist A, Au CE, Hiding J et al. Quantitative proteomics analysis of the secretory pathway. Cell 127(6), 1265-1281 (2006). • Determination of proteome of the components of the early secretory pathway using a quantitative approach.
    • (2006) Cell , vol.127 , Issue.6 , pp. 1265-1281
    • Gilchrist, A.1    Au, C.E.2    Hiding, J.3
  • 20
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): In search of its identity and function
    • Appenzeller-Herzog C , Hauri HP. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J. Cell Sci. 119(Pt 11), 2173-2183 (2006).
    • (2006) J. Cell Sci , vol.119 , Issue.PART 11 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 21
    • 6344283102 scopus 로고
    • Predicting subcellular localization via protein motif co-occurrence
    • 2004
    • Scott MS, Thomas DY, Hallett MT. Predicting subcellular localization via protein motif co-occurrence. Genome Res. 14(10A), 1957-1966 (2004).
    • (1957) Genome Res , Issue.10 A , pp. 14
    • Scott, M.S.1    Thomas, D.Y.2    Hallett, M.T.3
  • 22
    • 38449111109 scopus 로고    scopus 로고
    • Organelle proteome variation among different cell types: Lessons from nuclear membrane proteins
    • Kavanagh DM, Powell WE, Malik P, Lazou V, Schirmer EC. Organelle proteome variation among different cell types: lessons from nuclear membrane proteins. Subcell. Biochem. 43, 51-76 (2007).
    • (2007) Subcell. Biochem , vol.43 , pp. 51-76
    • Kavanagh, D.M.1    Powell, W.E.2    Malik, P.3    Lazou, V.4    Schirmer, E.C.5
  • 23
    • 33748547288 scopus 로고    scopus 로고
    • Guilt by association: The nuclear envelope proteome and disease
    • Wilkie GS, Schirmer EC. Guilt by association: the nuclear envelope proteome and disease. Mol. Cell Proteomics 5(10), 1865-1875 (2006).
    • (2006) Mol. Cell Proteomics , vol.5 , Issue.10 , pp. 1865-1875
    • Wilkie, G.S.1    Schirmer, E.C.2
  • 24
    • 33644917973 scopus 로고    scopus 로고
    • Deciphering the human nucleolar proteome
    • Coute Y, Burgess JA, Diaz JJ et al. Deciphering the human nucleolar proteome. Mass Spectrom. Rev. 25(2), 215-234 (2006).
    • (2006) Mass Spectrom. Rev , vol.25 , Issue.2 , pp. 215-234
    • Coute, Y.1    Burgess, J.A.2    Diaz, J.J.3
  • 25
    • 33750805030 scopus 로고    scopus 로고
    • Molecular anatomy of a trafficking organelle
    • Assessment of the physical properties and protein and lipid composition of the synaptic vesicle using systems biology approach, ••
    • Takamori S, Holt M, Stenius K et al. Molecular anatomy of a trafficking organelle. Cell 127(4), 831-846 (2006). •• Assessment of the physical properties and protein and lipid composition of the synaptic vesicle using systems biology approach.
    • (2006) Cell , vol.127 , Issue.4 , pp. 831-846
    • Takamori, S.1    Holt, M.2    Stenius, K.3
  • 27
    • 33745846820 scopus 로고    scopus 로고
    • Screening the receptorome: An efficient approach for drug discovery and target validation
    • Strachan RT, Ferrara G, Roth BL. Screening the receptorome: an efficient approach for drug discovery and target validation. Drug Discov. Today 11(15-16), 708-716 (2006).
    • (2006) Drug Discov. Today , vol.11 , Issue.15-16 , pp. 708-716
    • Strachan, R.T.1    Ferrara, G.2    Roth, B.L.3
  • 28
    • 27444435955 scopus 로고    scopus 로고
    • Ahram M, Springer DL. Large-scale proteomic analysis of membrane proteins. Expert Rev. Proteomics 1(3), 293-302 (2004).
    • Ahram M, Springer DL. Large-scale proteomic analysis of membrane proteins. Expert Rev. Proteomics 1(3), 293-302 (2004).
  • 29
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni V, Molloy M, Rabilloud T. Membrane proteins and proteomics: un amour impossible? Electrophoresis 21(6), 1054-1070 (2000).
    • (2000) Electrophoresis , vol.21 , Issue.6 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 31
    • 0016364196 scopus 로고
    • Analytical study of microsomes and isolated subcellular membranes from rat liver. 3. Subfractionation of the microsomal fraction by isopycnic and differential centrifugation in density gradients
    • Beaufay H, Amar-Costesec A, Thines-Sempoux D, Wibo M, Robbi M, Berthet J. Analytical study of microsomes and isolated subcellular membranes from rat liver. 3. Subfractionation of the microsomal fraction by isopycnic and differential centrifugation in density gradients. J. Cell Biol. 61(1), 213-231 (1974).
    • (1974) J. Cell Biol , vol.61 , Issue.1 , pp. 213-231
    • Beaufay, H.1    Amar-Costesec, A.2    Thines-Sempoux, D.3    Wibo, M.4    Robbi, M.5    Berthet, J.6
  • 32
    • 2142721825 scopus 로고    scopus 로고
    • HysTag - a novel proteomic quantification tool applied to differential display analysis of membrane proteins from distinct areas of mouse brain
    • Olsen JV, Andersen JR, Nielsen PA et al. HysTag - a novel proteomic quantification tool applied to differential display analysis of membrane proteins from distinct areas of mouse brain. Mol. Cell Proteomics 3(1), 82-92 (2004).
    • (2004) Mol. Cell Proteomics , vol.3 , Issue.1 , pp. 82-92
    • Olsen, J.V.1    Andersen, J.R.2    Nielsen, P.A.3
  • 33
    • 33846376260 scopus 로고    scopus 로고
    • Quantitative proteomic profiling of membrane proteins from the mouse brain cortex, hippocampus, and cerebellum using the HysTag reagent: Mapping of neurotransmitter receptors and ion channels
    • Quantitative and comparative profiling of plasma membrane peptides between distinct brain regions revealing significant variation, ••
    • Olsen JV, Nielsen PA, Andersen JR, Mann M, Wisniewski JR. Quantitative proteomic profiling of membrane proteins from the mouse brain cortex, hippocampus, and cerebellum using the HysTag reagent: mapping of neurotransmitter receptors and ion channels. Brain Res. 1134(1), 95-106 (2007). •• Quantitative and comparative profiling of plasma membrane peptides between distinct brain regions revealing significant variation.
    • (2007) Brain Res , vol.1134 , Issue.1 , pp. 95-106
    • Olsen, J.V.1    Nielsen, P.A.2    Andersen, J.R.3    Mann, M.4    Wisniewski, J.R.5
  • 34
    • 28444481017 scopus 로고    scopus 로고
    • Phagocytosis: At the crossroads of innate and adaptive immunity
    • Jutras I, Desjardins M. Phagocytosis: at the crossroads of innate and adaptive immunity. Annu. Rev. Cell Dev. Biol. 21, 511-527 (2005).
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 511-527
    • Jutras, I.1    Desjardins, M.2
  • 35
    • 34250169069 scopus 로고    scopus 로고
    • Phagosome proteomes open the way to a better understanding of phagosome function
    • Griffiths G, Mayorga L. Phagosome proteomes open the way to a better understanding of phagosome function. Genome Biol. 8(3), 207 (2007).
    • (2007) Genome Biol , vol.8 , Issue.3 , pp. 207
    • Griffiths, G.1    Mayorga, L.2
  • 36
    • 45249098956 scopus 로고    scopus 로고
    • Contributions of proteomics to understanding phagosome maturation
    • Review of the recent proteomic studies performed on the phagosome, •
    • Rogers LD, Foster LJ. Contributions of proteomics to understanding phagosome maturation. Cell Microbiol. 10(7), 1405-1412 (2008). • Review of the recent proteomic studies performed on the phagosome.
    • (2008) Cell Microbiol , vol.10 , Issue.7 , pp. 1405-1412
    • Rogers, L.D.1    Foster, L.J.2
  • 37
    • 0014592287 scopus 로고
    • Phagocytosis of latex beads by Acahamoeba castellanii (Neff ). 3. Isolation of the phagocytic vesicles and their membranes
    • Wetzel MG, Korn ED. Phagocytosis of latex beads by Acahamoeba castellanii (Neff ). 3. Isolation of the phagocytic vesicles and their membranes. J. Cell Biol. 43(1), 90-104 (1969).
    • (1969) J. Cell Biol , vol.43 , Issue.1 , pp. 90-104
    • Wetzel, M.G.1    Korn, E.D.2
  • 38
    • 0035825154 scopus 로고    scopus 로고
    • The phagosome proteome: Insight into phagosome functions
    • Garin J, Diez R, Kieffer S et al. The phagosome proteome: insight into phagosome functions. J. Cell Biol. 152(1), 165-180 (2001).
    • (2001) J. Cell Biol , vol.152 , Issue.1 , pp. 165-180
    • Garin, J.1    Diez, R.2    Kieffer, S.3
  • 39
    • 0038316341 scopus 로고    scopus 로고
    • ER-mediated phagocytosis: A new membrane for new functions
    • Desjardins M. ER-mediated phagocytosis: a new membrane for new functions. Nat. Rev. Immunol. 3(4), 280-291 (2003).
    • (2003) Nat. Rev. Immunol , vol.3 , Issue.4 , pp. 280-291
    • Desjardins, M.1
  • 40
    • 33846080260 scopus 로고    scopus 로고
    • A systems biology analysis of the Drosophila phagosome
    • Determination of the phagosome's proteome/interactome and assessment of the contribution of the identified proteins in phagocytosis using RNAis, ••
    • Stuart LM, Boulais J, Charriere GM et al. A systems biology analysis of the Drosophila phagosome. Nature 445(7123), 95-101 (2007). •• Determination of the phagosome's proteome/interactome and assessment of the contribution of the identified proteins in phagocytosis using RNAis.
    • (2007) Nature , vol.445 , Issue.7123 , pp. 95-101
    • Stuart, L.M.1    Boulais, J.2    Charriere, G.M.3
  • 41
    • 0347473809 scopus 로고    scopus 로고
    • Gaining confidence in high-throughput protein interaction networks
    • Bader JS, Chaudhuri A, Rothberg JM, Chant J. Gaining confidence in high-throughput protein interaction networks. Nat. Biotechnol. 22(1), 78-85 (2004).
    • (2004) Nat. Biotechnol , vol.22 , Issue.1 , pp. 78-85
    • Bader, J.S.1    Chaudhuri, A.2    Rothberg, J.M.3    Chant, J.4
  • 42
    • 0035211290 scopus 로고    scopus 로고
    • Identification of potential interaction networks using sequence-based searches for conserved protein-protein interactions or "interologs
    • Matthews LR, Vaglio P, Reboul J et al. Identification of potential interaction networks using sequence-based searches for conserved protein-protein interactions or "interologs". Genome Res. 11(12), 2120-2126 (2001).
    • (2001) Genome Res , vol.11 , Issue.12 , pp. 2120-2126
    • Matthews, L.R.1    Vaglio, P.2    Reboul, J.3
  • 45
    • 33847084336 scopus 로고    scopus 로고
    • Tissue heterogeneity of the mammalian mitochondrial proteome
    • Johnson DT, Harris RA, French S et al. Tissue heterogeneity of the mammalian mitochondrial proteome. Am. J. Physiol. Cell Physiol. 292(2), C689-C697 (2007).
    • (2007) Am. J. Physiol. Cell Physiol , vol.292 , Issue.2
    • Johnson, D.T.1    Harris, R.A.2    French, S.3
  • 47
    • 33846390427 scopus 로고    scopus 로고
    • Building the power house: Recent advances in mitochondrial studies through proteomics and systems biology
    • Vo TD, Palsson BO. Building the power house: recent advances in mitochondrial studies through proteomics and systems biology. Am. J. Physiol. Cell Physiol. 292(1), C164-C177 (2007).
    • (2007) Am. J. Physiol. Cell Physiol , vol.292 , Issue.1
    • Vo, T.D.1    Palsson, B.O.2
  • 48
    • 0037337777 scopus 로고    scopus 로고
    • Omics' of the mitochondrion
    • Westermann B, Neupert W. 'Omics' of the mitochondrion. Nat. Biotechnol. 21(3), 239-240 (2003).
    • (2003) Nat. Biotechnol , vol.21 , Issue.3 , pp. 239-240
    • Westermann, B.1    Neupert, W.2
  • 49
    • 0034856468 scopus 로고    scopus 로고
    • One-step subcellular fractionation of rat liver tissue using a Nycodenz density gradient prepared by freezing-thawing and two-dimensional sodium dodecyl sulfate electrophoresis profiles of the main fraction of organelles
    • Murayama K, Fujimura T, Morita M, Shindo N. One-step subcellular fractionation of rat liver tissue using a Nycodenz density gradient prepared by freezing-thawing and two-dimensional sodium dodecyl sulfate electrophoresis profiles of the main fraction of organelles. Electrophoresis 22(14), 2872-2880 (2001).
    • (2001) Electrophoresis , vol.22 , Issue.14 , pp. 2872-2880
    • Murayama, K.1    Fujimura, T.2    Morita, M.3    Shindo, N.4
  • 50
    • 0037336905 scopus 로고    scopus 로고
    • Characterization of the human heart mitochondrial proteome
    • Taylor SW, Fahy E, Zhang B et al. Characterization of the human heart mitochondrial proteome. Nat. Biotechnol. 21(3), 281-286 (2003).
    • (2003) Nat. Biotechnol , vol.21 , Issue.3 , pp. 281-286
    • Taylor, S.W.1    Fahy, E.2    Zhang, B.3
  • 51
    • 10744226861 scopus 로고    scopus 로고
    • Improved proteome analysis of Saccharomyces cerevisiae mitochondria by free-flow electrophoresis
    • Zischka H, Weber G, Weber PJ et al. Improved proteome analysis of Saccharomyces cerevisiae mitochondria by free-flow electrophoresis. Proteomics 3(6), 906-916 (2003).
    • (2003) Proteomics , vol.3 , Issue.6 , pp. 906-916
    • Zischka, H.1    Weber, G.2    Weber, P.J.3
  • 52
    • 33751422323 scopus 로고    scopus 로고
    • Differential analysis of Saccharomyces cerevisiae mitochondria by free flow electrophoresis
    • Zischka H, Braun RJ, Marantidis EP et al. Differential analysis of Saccharomyces cerevisiae mitochondria by free flow electrophoresis. Mol. Cell Proteomics 5(11), 2185-2200 (2006).
    • (2006) Mol. Cell Proteomics , vol.5 , Issue.11 , pp. 2185-2200
    • Zischka, H.1    Braun, R.J.2    Marantidis, E.P.3
  • 53
    • 44049087349 scopus 로고    scopus 로고
    • Isolation of highly pure rat liver mitochondria with the aid of zone-electrophoresis in a free flow device (ZE-FFE)
    • Zischka H, Lichtmannegger J, Jagemann N et al. Isolation of highly pure rat liver mitochondria with the aid of zone-electrophoresis in a free flow device (ZE-FFE). Methods Mol. Biol. 424, 333-348 (2008).
    • (2008) Methods Mol. Biol , vol.424 , pp. 333-348
    • Zischka, H.1    Lichtmannegger, J.2    Jagemann, N.3
  • 54
    • 35448934538 scopus 로고    scopus 로고
    • Free-flow electrophoresis for purification of plant mitochondria by surface charge
    • Eubel H, Lee CP, Kuo J, Meyer EH, Taylor NL, Millar AH. Free-flow electrophoresis for purification of plant mitochondria by surface charge. Plant J. 52(3), 583-594 (2007).
    • (2007) Plant J , vol.52 , Issue.3 , pp. 583-594
    • Eubel, H.1    Lee, C.P.2    Kuo, J.3    Meyer, E.H.4    Taylor, N.L.5    Millar, A.H.6
  • 55
    • 4444269513 scopus 로고    scopus 로고
    • Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins
    • Ghosh D, Krokhin O, Antonovici M et al. Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins. J. Proteome Res. 3(4), 841-850 (2004).
    • (2004) J. Proteome Res , vol.3 , Issue.4 , pp. 841-850
    • Ghosh, D.1    Krokhin, O.2    Antonovici, M.3
  • 56
    • 21244465513 scopus 로고    scopus 로고
    • Within the cell: Analytical techniques for subcellular analysis
    • Olson KJ, Ahmadzadeh H, Arriaga EA. Within the cell: analytical techniques for subcellular analysis. Anal. Bioanal. Chem. 382(4), 906-917 (2005).
    • (2005) Anal. Bioanal. Chem , vol.382 , Issue.4 , pp. 906-917
    • Olson, K.J.1    Ahmadzadeh, H.2    Arriaga, E.A.3
  • 57
    • 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 Biomed. Sci. Appl. 722(1-2), 89-102 (1999).
    • (1999) J. Chromatogr. B Biomed. Sci. Appl , vol.722 , Issue.1-2 , pp. 89-102
    • Pasquali, C.1    Fialka, I.2    Huber, L.A.3
  • 58
    • 33745946236 scopus 로고    scopus 로고
    • Use of magnetic beads with immobilized monoclonal antibodies for isolation of highly pure plasma membranes
    • Proteomic analysis of the immunoisolated plasma membranes from rat liver and hepatocellular carcinoma cell lines, •
    • Lawson EL, Clifton JG, Huang F, Li X, Hixson DC, Josic D. Use of magnetic beads with immobilized monoclonal antibodies for isolation of highly pure plasma membranes. Electrophoresis 27(13), 2747-2758 (2006). • Proteomic analysis of the immunoisolated plasma membranes from rat liver and hepatocellular carcinoma cell lines.
    • (2006) Electrophoresis , vol.27 , Issue.13 , pp. 2747-2758
    • Lawson, E.L.1    Clifton, J.G.2    Huang, F.3    Li, X.4    Hixson, D.C.5    Josic, D.6
  • 59
    • 33846634111 scopus 로고    scopus 로고
    • Immunoaffinity purification of plasma membrane with secondary antibody superparamagnetic beads for proteomic analysis
    • Zhang L, Wang X, Peng X et al. Immunoaffinity purification of plasma membrane with secondary antibody superparamagnetic beads for proteomic analysis. J. Proteome Res. 6(1), 34-43 (2007).
    • (2007) J. Proteome Res , vol.6 , Issue.1 , pp. 34-43
    • Zhang, L.1    Wang, X.2    Peng, X.3
  • 60
    • 0345791524 scopus 로고    scopus 로고
    • Proteomic analysis of rat liver peroxisome: Presence of peroxisome-specific isozyme of Lon protease
    • Kikuchi M, Hatano N, Yokota S, Shimozawa N, Imanaka T, Taniguchi H. Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease. J. Biol. Chem. 279(1), 421-428 (2004).
    • (2004) J. Biol. Chem , vol.279 , Issue.1 , pp. 421-428
    • Kikuchi, M.1    Hatano, N.2    Yokota, S.3    Shimozawa, N.4    Imanaka, T.5    Taniguchi, H.6
  • 62
    • 34249808797 scopus 로고    scopus 로고
    • The synaptic vesicle proteome
    • Burre J, Volknandt W. The synaptic vesicle proteome. J. Neurochem. 101(6), 1448-1462 (2007).
    • (2007) J. Neurochem , vol.101 , Issue.6 , pp. 1448-1462
    • Burre, J.1    Volknandt, W.2
  • 63
    • 29144493185 scopus 로고    scopus 로고
    • Immunoisolation of two synaptic vesicle pools from synaptosomes: A proteomics analysis
    • Morciano M, Burre J, Corvey C, Karas M, Zimmermann H, Volknandt W. Immunoisolation of two synaptic vesicle pools from synaptosomes: a proteomics analysis. J. Neurochem. 95(6), 1732-1745 (2005).
    • (2005) J. Neurochem , vol.95 , Issue.6 , pp. 1732-1745
    • Morciano, M.1    Burre, J.2    Corvey, C.3    Karas, M.4    Zimmermann, H.5    Volknandt, W.6
  • 64
    • 33846892783 scopus 로고    scopus 로고
    • Immunoisolation and subfractionation of synaptic vesicle proteins
    • Burre J, Zimmermann H, Volknandt W. Immunoisolation and subfractionation of synaptic vesicle proteins. Anal. Biochem. 362(2), 172-181 (2007).
    • (2007) Anal. Biochem , vol.362 , Issue.2 , pp. 172-181
    • Burre, J.1    Zimmermann, H.2    Volknandt, W.3
  • 65
    • 0025345820 scopus 로고
    • Application of avidin-biotin technology to affinity-based separations
    • Bayer EA, Wilchek M. Application of avidin-biotin technology to affinity-based separations. J. Chromatogr. 510, 3-11 (1990).
    • (1990) J. Chromatogr , vol.510 , pp. 3-11
    • Bayer, E.A.1    Wilchek, M.2
  • 66
    • 1842529218 scopus 로고    scopus 로고
    • Proteomic analysis of integral plasma membrane proteins
    • Zhao Y, Zhang W, Kho Y, Zhao Y. Proteomic analysis of integral plasma membrane proteins. Anal. Chem. 76(7), 1817-1823 (2004).
    • (2004) Anal. Chem , vol.76 , Issue.7 , pp. 1817-1823
    • Zhao, Y.1    Zhang, W.2    Kho, Y.3    Zhao, Y.4
  • 67
    • 3042668954 scopus 로고    scopus 로고
    • Flow cytometry: An introduction
    • Givan AL. Flow cytometry: an introduction. Methods Mol. Biol. 263, 1-32 (2004).
    • (2004) Methods Mol. Biol , vol.263 , pp. 1-32
    • Givan, A.L.1
  • 69
    • 34447527235 scopus 로고    scopus 로고
    • Modern flow cytometry: A practical approach
    • Tung JW, Heydari K, Tirouvanziam R et al. Modern flow cytometry: a practical approach. Clin. Lab. Med. 27(3), 453-468, (2007).
    • (2007) Clin. Lab. Med , vol.27 , Issue.3 , pp. 453-468
    • Tung, J.W.1    Heydari, K.2    Tirouvanziam, R.3
  • 70
    • 0035220017 scopus 로고    scopus 로고
    • Principles of flow cytometry: An overview
    • Givan AL. Principles of flow cytometry: an overview. Methods Cell Biol. 63, 19-50 (2001).
    • (2001) Methods Cell Biol , vol.63 , pp. 19-50
    • Givan, A.L.1
  • 71
    • 0345678101 scopus 로고
    • Analysis and isolation of endocytic vesicles by flow cytometry and sorting: Demonstration of three kinetically distinct compartments involved in fluid-phase endocytosis
    • Murphy RF. Analysis and isolation of endocytic vesicles by flow cytometry and sorting: demonstration of three kinetically distinct compartments involved in fluid-phase endocytosis. Proc. Natl Acad. Sci. USA 82(24), 8523-8526 (1985).
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , Issue.24 , pp. 8523-8526
    • Murphy, R.F.1
  • 72
    • 0039742749 scopus 로고    scopus 로고
    • Cell biologists sort things out: Analysis and purification of intracellular organelles by flow cytometry
    • Bock G, Steinlein P, Huber LA. Cell biologists sort things out: analysis and purification of intracellular organelles by flow cytometry. Trends Cell Biol. 7(12), 499-503 (1997).
    • (1997) Trends Cell Biol , vol.7 , Issue.12 , pp. 499-503
    • Bock, G.1    Steinlein, P.2    Huber, L.A.3
  • 73
    • 0028881976 scopus 로고
    • Green fluorescent protein as a marker for gene expression and cell biology of mycobacterial interactions with macrophages
    • Dhandayuthapani S, Via LE, Thomas CA, Horowitz PM, Deretic D, Deretic V. Green fluorescent protein as a marker for gene expression and cell biology of mycobacterial interactions with macrophages. Mol. Microbiol. 17(5), 901-912 (1995).
    • (1995) Mol. Microbiol , vol.17 , Issue.5 , pp. 901-912
    • Dhandayuthapani, S.1    Via, L.E.2    Thomas, C.A.3    Horowitz, P.M.4    Deretic, D.5    Deretic, V.6
  • 74
    • 0030057708 scopus 로고    scopus 로고
    • Functional heterogeneity of an isolated mitochondrial population revealed by cytofluorometric analysis at the single organelle level
    • Cossarizza A, Ceccarelli D, Masini A. Functional heterogeneity of an isolated mitochondrial population revealed by cytofluorometric analysis at the single organelle level. Exp. Cell Res. 222(1), 84-94 (1996).
    • (1996) Exp. Cell Res , vol.222 , Issue.1 , pp. 84-94
    • Cossarizza, A.1    Ceccarelli, D.2    Masini, A.3
  • 75
    • 0026767241 scopus 로고
    • Flow cytometry and sorting of amphibian bladder endocytic vesicles containing ADH-sensitive water channels
    • van der Goot FG, Seigneur A, Gaucher JC, Ripoche P. Flow cytometry and sorting of amphibian bladder endocytic vesicles containing ADH-sensitive water channels. J. Membr. Biol. 128(2), 133-139 (1992).
    • (1992) J. Membr. Biol , vol.128 , Issue.2 , pp. 133-139
    • van der Goot, F.G.1    Seigneur, A.2    Gaucher, J.C.3    Ripoche, P.4
  • 76
    • 0024306294 scopus 로고
    • Flow-cytometric analysis of endocytic compartments
    • Wilson RB, Murphy RF. Flow-cytometric analysis of endocytic compartments. Methods Cell Biol. 31, 293-317 (1989).
    • (1989) Methods Cell Biol , vol.31 , pp. 293-317
    • Wilson, R.B.1    Murphy, R.F.2
  • 77
    • 0348134930 scopus 로고    scopus 로고
    • Isolation of mast cell secretory lysosomes using flow cytometry
    • Rajotte D, Stearns CD, Kabcenell AK. Isolation of mast cell secretory lysosomes using flow cytometry. Cytometry A 55(2), 94-101 (2003).
    • (2003) Cytometry A , vol.55 , Issue.2 , pp. 94-101
    • Rajotte, D.1    Stearns, C.D.2    Kabcenell, A.K.3
  • 78
    • 51149089844 scopus 로고    scopus 로고
    • Flow cytometry-assisted purification and proteomic analysis of the corticotropes dense-core secretory granules
    • In Press
    • Gauthier DJ, Sobota JA, Ferraro F, Mains RE, Lazure C. Flow cytometry-assisted purification and proteomic analysis of the corticotropes dense-core secretory granules. Proteomics (2008) (In Press).
    • (2008) Proteomics
    • Gauthier, D.J.1    Sobota, J.A.2    Ferraro, F.3    Mains, R.E.4    Lazure, C.5
  • 79
    • 34347373451 scopus 로고    scopus 로고
    • Proteomics analysis of insulin secretory granules
    • Brunner Y, Coute Y, Iezzi M et al. Proteomics analysis of insulin secretory granules. Mol. Cell Proteomics 6(6), 1007-1017 (2007).
    • (2007) Mol. Cell Proteomics , vol.6 , Issue.6 , pp. 1007-1017
    • Brunner, Y.1    Coute, Y.2    Iezzi, M.3
  • 80
    • 2542459327 scopus 로고    scopus 로고
    • Proteomic analysis of rat atrial secretory granules: A platform for testable hypotheses
    • Muth E, Driscoll WJ, Smalstig A, Goping G, Mueller GP. Proteomic analysis of rat atrial secretory granules: a platform for testable hypotheses. Biochim. Biophys. Acta 1699(1-2), 263-275 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1699 , Issue.1-2 , pp. 263-275
    • Muth, E.1    Driscoll, W.J.2    Smalstig, A.3    Goping, G.4    Mueller, G.P.5
  • 81
    • 34249295158 scopus 로고    scopus 로고
    • Proteomics of neuroendocrine secretory vesicles reveal distinct functional systems for biosynthesis and exocytosis of peptide hormones and neurotransmitters
    • Wegrzyn J, Lee J, Neveu JM, Lane WS, Hook V. Proteomics of neuroendocrine secretory vesicles reveal distinct functional systems for biosynthesis and exocytosis of peptide hormones and neurotransmitters. J. Proteome Res. 6(5), 1652-1665 (2007).
    • (2007) J. Proteome Res , vol.6 , Issue.5 , pp. 1652-1665
    • Wegrzyn, J.1    Lee, J.2    Neveu, J.M.3    Lane, W.S.4    Hook, V.5
  • 84
    • 34347260679 scopus 로고    scopus 로고
    • Proteomics in 2005/2006: Developments, applications and challenges
    • Smith JC, Lambert JP, Elisma F, Figeys D. Proteomics in 2005/2006: developments, applications and challenges. Anal. Chem. 79(12), 4325-4343 (2007).
    • (2007) Anal. Chem , vol.79 , Issue.12 , pp. 4325-4343
    • Smith, J.C.1    Lambert, J.P.2    Elisma, F.3    Figeys, D.4
  • 86
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster LJ, De Hoog CL, Mann M. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl Acad. Sci USA 100(10), 5813-5818 (2003).
    • (2003) Proc. Natl Acad. Sci USA , vol.100 , Issue.10 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 87
    • 34248155322 scopus 로고    scopus 로고
    • Function prediction of uncharacterized proteins
    • Hawkins T, Kihara D. Function prediction of uncharacterized proteins. J. Bioinform. Comput. Biol. 5(1), 1-30 (2007).
    • (2007) J. Bioinform. Comput. Biol , vol.5 , Issue.1 , pp. 1-30
    • Hawkins, T.1    Kihara, D.2
  • 88
    • 33846680167 scopus 로고    scopus 로고
    • Identification of conserved protein complexes based on a model of protein network evolution
    • Hirsh E, Sharan R. Identification of conserved protein complexes based on a model of protein network evolution. Bioinformatics 23(2), E170-E176 (2007).
    • (2007) Bioinformatics , vol.23 , Issue.2
    • Hirsh, E.1    Sharan, R.2
  • 89
    • 33750600611 scopus 로고    scopus 로고
    • Proteome informatics I: Bioinformatics tools for processing experimental data
    • Palagi PM, Hernandez P, Walther D, Appel RD. Proteome informatics I: bioinformatics tools for processing experimental data. Proteomics 6(20), 5435-5444 (2006).
    • (2006) Proteomics , vol.6 , Issue.20 , pp. 5435-5444
    • Palagi, P.M.1    Hernandez, P.2    Walther, D.3    Appel, R.D.4
  • 90
    • 33846051741 scopus 로고    scopus 로고
    • MAPU: Max-Planck unified database of organellar, cellular, tissue and body fluid proteomes
    • Zhang Y, Zhang Y, Adachi J et al. MAPU: Max-Planck unified database of organellar, cellular, tissue and body fluid proteomes. Nucleic Acids Res. 35, D771-D779 (2007).
    • (2007) Nucleic Acids Res , vol.35
    • Zhang, Y.1    Zhang, Y.2    Adachi, J.3
  • 91
    • 34249871616 scopus 로고    scopus 로고
    • The hard cell: From proteomics to a whole cell model
    • Betts MJ, Russell RB. The hard cell: from proteomics to a whole cell model. FEBS Lett. 581(15), 2870-2876 (2007).
    • (2007) FEBS Lett , vol.581 , Issue.15 , pp. 2870-2876
    • Betts, M.J.1    Russell, R.B.2
  • 92
    • 1642372806 scopus 로고    scopus 로고
    • FM-dyes as experimental probes for dissecting vesicle trafficking in living plant cells
    • Bolte S, Talbot C, Boutte Y, Catrice O, Read ND, Satiat-Jeunemaitre B. FM-dyes as experimental probes for dissecting vesicle trafficking in living plant cells. J. Microsc. 214(Pt 2), 159-173 (2004).
    • (2004) J. Microsc , vol.214 , Issue.PART 2 , pp. 159-173
    • Bolte, S.1    Talbot, C.2    Boutte, Y.3    Catrice, O.4    Read, N.D.5    Satiat-Jeunemaitre, B.6
  • 93
    • 34548580938 scopus 로고    scopus 로고
    • Use of fluorescent quantum dot bioconjugates for cellular imaging of immune cells, cell organelle labeling, and nanomedicine: Surface modification regulates biological function, including cytotoxicity
    • Hoshino A, Manabe N, Fujioka K, Suzuki K, Yasuhara M, Yamamoto K. Use of fluorescent quantum dot bioconjugates for cellular imaging of immune cells, cell organelle labeling, and nanomedicine: surface modification regulates biological function, including cytotoxicity. J. Artif. Organs 10(3), 149-157 (2007).
    • (2007) J. Artif. Organs , vol.10 , Issue.3 , pp. 149-157
    • Hoshino, A.1    Manabe, N.2    Fujioka, K.3    Suzuki, K.4    Yasuhara, M.5    Yamamoto, K.6
  • 94
    • 38349006477 scopus 로고    scopus 로고
    • Advances in fluorescent protein technology
    • Shaner NC, Patterson GH, Davidson MW. Advances in fluorescent protein technology. J. Cell Sci. 120(Pt 24), 4247-4260 (2007).
    • (2007) J. Cell Sci , vol.120 , Issue.PART 24 , pp. 4247-4260
    • Shaner, N.C.1    Patterson, G.H.2    Davidson, M.W.3
  • 95
    • 34547144255 scopus 로고    scopus 로고
    • Enhanced separation of membranes during free flow zonal electrophoresis in plants
    • Barkla BJ, Vera-Estrella R, Pantoja O. Enhanced separation of membranes during free flow zonal electrophoresis in plants. Anal. Chem. 79(14), 5181-5187 (2007).
    • (2007) Anal. Chem , vol.79 , Issue.14 , pp. 5181-5187
    • Barkla, B.J.1    Vera-Estrella, R.2    Pantoja, O.3
  • 96
    • 36148989234 scopus 로고    scopus 로고
    • Proteomic analysis of plasma membrane and secretory vesicles from human neutrophils
    • Jethwaney D, Islam MR, Leidal KG et al. Proteomic analysis of plasma membrane and secretory vesicles from human neutrophils. Proteome Sci. 5, 12 (2007).
    • (2007) Proteome Sci , vol.5 , pp. 12
    • Jethwaney, D.1    Islam, M.R.2    Leidal, K.G.3


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