메뉴 건너뛰기




Volumn 9, Issue 23, 2009, Pages 5214-5223

Native electrophoretic techniques to identify protein-protein interactions

Author keywords

Blue native electrophoresis; Clear native electrophoresis; Protein complex; Protein protein interaction; Supercomplex; Technology

Indexed keywords

GEL ELECTROPHORESIS; IN VIVO STUDY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; REVIEW;

EID: 73249127170     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900151     Document Type: Review
Times cited : (83)

References (82)
  • 1
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H., von Jagow, G., Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 1991, 199, 223-231.
    • (1991) Anal. Biochem , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 2
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger, H., Cramer, W. A., von Jagow, G., Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 1994, 217, 220-230.
    • (1994) Anal. Biochem , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 4
    • 28444497467 scopus 로고    scopus 로고
    • Advantages and limitations of clear native polyacrylamide gel electrophoresis
    • Wittig, I., Schägger, H., Advantages and limitations of clear native polyacrylamide gel electrophoresis. Proteomics 2005, 5, 4338-4346.
    • (2005) Proteomics , vol.5 , pp. 4338-4346
    • Wittig, I.1    Schägger, H.2
  • 5
    • 34547138661 scopus 로고    scopus 로고
    • High resolution clearnative electrophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes
    • Wittig, I., Karas, M., Schägger, H., High resolution clearnative electrophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes. Mol. Cell. Proteomics 2007, 6, 1215-1225.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1215-1225
    • Wittig, I.1    Karas, M.2    Schägger, H.3
  • 6
    • 36348941768 scopus 로고    scopus 로고
    • Functional assays in high resolution clear native gels to quantify mitochondrial complexes in human biopsies and cell-lines
    • Wittig, I., Carrozzo, R., Santorelli, F. M., Schägger, H., Functional assays in high resolution clear native gels to quantify mitochondrial complexes in human biopsies and cell-lines. Electrophoresis 2007, 28, 3811-3820.
    • (2007) Electrophoresis , vol.28 , pp. 3811-3820
    • Wittig, I.1    Carrozzo, R.2    Santorelli, F.M.3    Schägger, H.4
  • 7
    • 55749085411 scopus 로고    scopus 로고
    • Features and applications of bluenative and clear-native electrophoresis
    • Wittig, I., Schägger, H., Features and applications of bluenative and clear-native electrophoresis. Proteomics 2008, 8, 3974-3990.
    • (2008) Proteomics , vol.8 , pp. 3974-3990
    • Wittig, I.1    Schägger, H.2
  • 8
    • 33745943572 scopus 로고    scopus 로고
    • Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes
    • Krause, F., Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes. Electrophoresis 2006, 27, 2759-2781.
    • (2006) Electrophoresis , vol.27 , pp. 2759-2781
    • Krause, F.1
  • 9
    • 0347362791 scopus 로고    scopus 로고
    • Cardiolipin stabilizes respiratory chain supercomplexes
    • Pfeiffer, K., Gohil, V., Stuart, R. A., Hunte, C. et al., Cardiolipin stabilizes respiratory chain supercomplexes. J. Biol. Chem. 2003, 278, 52873-52880.
    • (2003) J. Biol. Chem , vol.278 , pp. 52873-52880
    • Pfeiffer, K.1    Gohil, V.2    Stuart, R.A.3    Hunte, C.4
  • 10
    • 43849109967 scopus 로고    scopus 로고
    • Characterization of domain-interfaces in monomeric and dimeric ATP synthase
    • Wittig, I., Stuart, R. A., Velours, J., Schägger, H., Characterization of domain-interfaces in monomeric and dimeric ATP synthase. Mol. Cell. Proteomics 2008, 7, 995-1004.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 995-1004
    • Wittig, I.1    Stuart, R.A.2    Velours, J.3    Schägger, H.4
  • 11
    • 34147218109 scopus 로고    scopus 로고
    • Electrophoretic methods to isolate protein complexes from mitochondria
    • Wittig, I., Schägger, H., Electrophoretic methods to isolate protein complexes from mitochondria. Methods Cell Biol. 2007, 80, 723-741.
    • (2007) Methods Cell Biol , vol.80 , pp. 723-741
    • Wittig, I.1    Schägger, H.2
  • 12
    • 4444347536 scopus 로고    scopus 로고
    • Hunte, C, von Jagow, G, Schägger, H, Eds, Academic Press, San Diego
    • Schägger, H., in: Hunte, C., von Jagow, G., Schägger, H. (Eds.), Membrane Protein Purification and Crystallization, Academic Press, San Diego 2003, pp. 105-130.
    • (2003) Membrane Protein Purification and Crystallization , pp. 105-130
    • Schägger, H.1
  • 14
    • 0036299012 scopus 로고    scopus 로고
    • Oligomeric state of membrane transport proteins analyzed with blue native electrophoresis and analytical ultracentrifugation
    • Heuberger, E. H., Veenhoff, L. M., Duurkens, R. H., Friesen, R. H., Poolman, B., Oligomeric state of membrane transport proteins analyzed with blue native electrophoresis and analytical ultracentrifugation. J. Mol. Biol. 2002, 317, 591-600.
    • (2002) J. Mol. Biol , vol.317 , pp. 591-600
    • Heuberger, E.H.1    Veenhoff, L.M.2    Duurkens, R.H.3    Friesen, R.H.4    Poolman, B.5
  • 15
    • 0028848239 scopus 로고
    • Native electrophoresis for isolation of mitochondrial oxidative phosphorylation protein complexes
    • Schägger, H., Native electrophoresis for isolation of mitochondrial oxidative phosphorylation protein complexes. Methods Enzymol. 1995, 260, 190-202.
    • (1995) Methods Enzymol , vol.260 , pp. 190-202
    • Schägger, H.1
  • 16
    • 0028816203 scopus 로고
    • Human diseases with defects in oxidative phosphorylation: I. Decreased amounts of assembled oxidative phosphorylation complexes in mitochondrial encephalomyopathies
    • Bentlage, H., De Coo, R., Ter Laak, H., Sengers, R., Human diseases with defects in oxidative phosphorylation: I. Decreased amounts of assembled oxidative phosphorylation complexes in mitochondrial encephalomyopathies. Eur. J. Biochem. 1995, 227, 909-915.
    • (1995) Eur. J. Biochem , vol.227 , pp. 909-915
    • Bentlage, H.1    De Coo, R.2    Ter Laak, H.3    Sengers, R.4
  • 17
    • 0028832212 scopus 로고
    • Analysis of oxidative phosphorylation complexes in cultured human fibroblasts and amniocytes by blue-nativeelectrophoresis using mitoplasts isolated with the help of digitonin
    • Klement, P., Nijtmans, L. G., van den Bogert, C., Houstek, J., Analysis of oxidative phosphorylation complexes in cultured human fibroblasts and amniocytes by blue-nativeelectrophoresis using mitoplasts isolated with the help of digitonin. Anal. Biochem. 1995, 231, 218-224.
    • (1995) Anal. Biochem , vol.231 , pp. 218-224
    • Klement, P.1    Nijtmans, L.G.2    van den Bogert, C.3    Houstek, J.4
  • 18
    • 0029980819 scopus 로고    scopus 로고
    • Electrophoretic separation of multiprotein complexes from blood platelets and cell lines: Technique for the analysis of diseases with defects in oxidative phosphorylation
    • Schägger, H., Bentlage, H., Ruitenbeek, W., Pfeiffer, K. et al., Electrophoretic separation of multiprotein complexes from blood platelets and cell lines: Technique for the analysis of diseases with defects in oxidative phosphorylation. Electrophoresis 1996, 17, 709-714.
    • (1996) Electrophoresis , vol.17 , pp. 709-714
    • Schägger, H.1    Bentlage, H.2    Ruitenbeek, W.3    Pfeiffer, K.4
  • 19
    • 0029924286 scopus 로고    scopus 로고
    • Electrophoretic techniques for isolation and quantitation of oxidative phosphorylation complexes from human tissues
    • Schägger, H., Electrophoretic techniques for isolation and quantitation of oxidative phosphorylation complexes from human tissues. Methods Enzymol. 1996, 264, 555-566.
    • (1996) Methods Enzymol , vol.264 , pp. 555-566
    • Schägger, H.1
  • 20
    • 0028869597 scopus 로고
    • Human diseases with defects in oxidative phosphorylation: II. F1F0 ATP-synthase defects in Alzheimeŕs disease revealed by blue native polyacrylamide gel electrophoresis
    • Schägger, H., Ohm, T., Human diseases with defects in oxidative phosphorylation: II. F1F0 ATP-synthase defects in Alzheimeŕs disease revealed by blue native polyacrylamide gel electrophoresis. Eur. J. Biochem. 1995, 227, 916-921.
    • (1995) Eur. J. Biochem , vol.227 , pp. 916-921
    • Schägger, H.1    Ohm, T.2
  • 21
    • 0029013434 scopus 로고
    • Quantification of oxidative phosphorylation enzymes after blue native electrophoresis and two-dimensional resolution: Normal complex I protein amounts in Parkinsońs disease conflict with reduced catalytic activities
    • Schägger, H., Quantification of oxidative phosphorylation enzymes after blue native electrophoresis and two-dimensional resolution: Normal complex I protein amounts in Parkinsońs disease conflict with reduced catalytic activities. Electrophoresis 1995, 16, 763-770.
    • (1995) Electrophoresis , vol.16 , pp. 763-770
    • Schägger, H.1
  • 22
    • 0029014974 scopus 로고
    • Cytochrome c oxidase in developing rat heart: Enzymatic properties and aminoterminal sequences suggest identity of the fetal heart and the adult liver isoform
    • Schägger, H., Noack, H., Halangk, W., Brandt, U., von Jagow, G., Cytochrome c oxidase in developing rat heart: Enzymatic properties and aminoterminal sequences suggest identity of the fetal heart and the adult liver isoform. Eur. J. Biochem. 1995, 230, 235-241.
    • (1995) Eur. J. Biochem , vol.230 , pp. 235-241
    • Schägger, H.1    Noack, H.2    Halangk, W.3    Brandt, U.4    von Jagow, G.5
  • 23
    • 0030111226 scopus 로고    scopus 로고
    • New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria
    • Jänsch, L., Kruft, V., Schmitz, U. K., Braun, H. P., New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria. Plant J. 1996, 9, 357-368.
    • (1996) Plant J , vol.9 , pp. 357-368
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 24
    • 0030829823 scopus 로고    scopus 로고
    • Analysis of the chloroplast protein complexes by bluenative polyacrylamide gelelectrophoresis
    • Kügler, M., Jänsch, L., Kruft, V., Schmitz, U. K., Braun, H. P., Analysis of the chloroplast protein complexes by bluenative polyacrylamide gelelectrophoresis. Photosynth. Res. 1997, 53, 35-44.
    • (1997) Photosynth. Res , vol.53 , pp. 35-44
    • Kügler, M.1    Jänsch, L.2    Kruft, V.3    Schmitz, U.K.4    Braun, H.P.5
  • 25
    • 20444398508 scopus 로고    scopus 로고
    • Disruption of a nuclear gene encoding a mitochondrial gamma carbonic anhydrase reduces complex I and supercomplex I+III2 levels and alters mitochondrial physiology in Arabidopsis
    • Perales, M., Eubel, H., Heinemeyer, J., Colaneri, A. et al., Disruption of a nuclear gene encoding a mitochondrial gamma carbonic anhydrase reduces complex I and supercomplex I+III2 levels and alters mitochondrial physiology in Arabidopsis. J. Mol. Biol. 2005, 350, 263-277.
    • (2005) J. Mol. Biol , vol.350 , pp. 263-277
    • Perales, M.1    Eubel, H.2    Heinemeyer, J.3    Colaneri, A.4
  • 26
    • 33745683588 scopus 로고    scopus 로고
    • Mapping the proteome of thylakoid membranes by de novo sequencing of intermembrane peptide domains
    • Granvogl, B., Reisinger, V., Eichacker, L. A., Mapping the proteome of thylakoid membranes by de novo sequencing of intermembrane peptide domains. Proteomics 2006, 6, 3681-3695.
    • (2006) Proteomics , vol.6 , pp. 3681-3695
    • Granvogl, B.1    Reisinger, V.2    Eichacker, L.A.3
  • 27
    • 33847701356 scopus 로고    scopus 로고
    • fused receptor domains act as high affinity cytokine-binding proteins
    • Characterization of the Interleukin (IL)-6 Inhibitor IL-6-RFP
    • Metz, S., Wiesinger, M., Vogt, M., Lauks, H. et al., Characterization of the Interleukin (IL)-6 Inhibitor IL-6-RFP: fused receptor domains act as high affinity cytokine-binding proteins. J. Biol. Chem. 2007, 282, 1238-1248.
    • (2007) J. Biol. Chem , vol.282 , pp. 1238-1248
    • Metz, S.1    Wiesinger, M.2    Vogt, M.3    Lauks, H.4
  • 28
    • 42249088081 scopus 로고    scopus 로고
    • How to analyze protein complexes by 2D blue native SDS-PAGE
    • Reisinger, V., Eichacker, L. A., How to analyze protein complexes by 2D blue native SDS-PAGE. Proteomics 2007, 7, Suppl 1, 6-16.
    • (2007) Proteomics , vol.7 , Issue.SUPPL. 1 , pp. 6-16
    • Reisinger, V.1    Eichacker, L.A.2
  • 29
    • 33847686377 scopus 로고    scopus 로고
    • Proteomic and functional alterations in brain mitochondria from Tg2576 mice occur before amyloid plaque deposition
    • Gillardon, F., Rist, W., Kussmaul, L., Vogel, J. et al., Proteomic and functional alterations in brain mitochondria from Tg2576 mice occur before amyloid plaque deposition. Proteomics 2007, 7, 605-616.
    • (2007) Proteomics , vol.7 , pp. 605-616
    • Gillardon, F.1    Rist, W.2    Kussmaul, L.3    Vogel, J.4
  • 30
    • 48949119270 scopus 로고    scopus 로고
    • a new look at the mitochondrial membrane proteome
    • Native-DIGE
    • Dani, D., Dencher, N. A., Native-DIGE: a new look at the mitochondrial membrane proteome. Biotechnol. J. 2008, 3, 817-822.
    • (2008) Biotechnol. J , vol.3 , pp. 817-822
    • Dani, D.1    Dencher, N.A.2
  • 31
    • 63349099933 scopus 로고    scopus 로고
    • Blue native DIGE as a tool for comparative analyses of protein complexes
    • Heinemeyer, J., Scheibe, B., Schmitz, U. K., Braun, H.-P., Blue native DIGE as a tool for comparative analyses of protein complexes. J. Proteomics 2009, 72, 539-544.
    • (2009) J. Proteomics , vol.72 , pp. 539-544
    • Heinemeyer, J.1    Scheibe, B.2    Schmitz, U.K.3    Braun, H.-P.4
  • 32
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlü, M., Morgan, M. E., Minden, J. S., Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlü, M.1    Morgan, M.E.2    Minden, J.S.3
  • 33
    • 0035289178 scopus 로고    scopus 로고
    • Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology
    • Tonge, R., Shaw, J., Middleton, B., Rowlinson, R. et al., Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 2001, 1, 377-396.
    • (2001) Proteomics , vol.1 , pp. 377-396
    • Tonge, R.1    Shaw, J.2    Middleton, B.3    Rowlinson, R.4
  • 34
    • 0030589133 scopus 로고    scopus 로고
    • Separation by blue native and colorless native polyacrylamide gel electrophoresis of the oxidative phosphorylation complexes of yeast mitochondria solubilized by different detergents: Specific staining of the different complexes
    • Grandier-Vazeille, X., Guerin, M., Separation by blue native and colorless native polyacrylamide gel electrophoresis of the oxidative phosphorylation complexes of yeast mitochondria solubilized by different detergents: specific staining of the different complexes. Anal. Biochem. 1996, 242, 248-254.
    • (1996) Anal. Biochem , vol.242 , pp. 248-254
    • Grandier-Vazeille, X.1    Guerin, M.2
  • 35
    • 0030853263 scopus 로고    scopus 로고
    • Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels
    • Zerbetto, E., Vergani, L., Dabbeni-Sala, F., Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels. Electrophoresis 1997, 18, 2059-2064.
    • (1997) Electrophoresis , vol.18 , pp. 2059-2064
    • Zerbetto, E.1    Vergani, L.2    Dabbeni-Sala, F.3
  • 36
    • 0022485169 scopus 로고
    • Purification and analysis of mitochondrial membrane proteins on nondenaturing gradient polyacrylamide gels
    • Kuonen, D. R., Roberts, P. J., Cottingham, I. R., Purification and analysis of mitochondrial membrane proteins on nondenaturing gradient polyacrylamide gels. Anal. Biochem. 1986, 153, 221-226.
    • (1986) Anal. Biochem , vol.153 , pp. 221-226
    • Kuonen, D.R.1    Roberts, P.J.2    Cottingham, I.R.3
  • 37
    • 0034669552 scopus 로고    scopus 로고
    • Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis
    • Jung, C., Higgins, C. M., Xu, Z., Measuring the quantity and activity of mitochondrial electron transport chain complexes in tissues of central nervous system using blue native polyacrylamide gel electrophoresis. Anal. Biochem. 2000, 286, 214-223.
    • (2000) Anal. Biochem , vol.286 , pp. 214-223
    • Jung, C.1    Higgins, C.M.2    Xu, Z.3
  • 38
    • 0034775551 scopus 로고    scopus 로고
    • Blue native polyacrylamide gel electrophoresis: A powerful tool in diagnosis of oxidative phosphorylation defects
    • Van Coster, R., Smet, J., George, E., De Meirleir, L. et al., Blue native polyacrylamide gel electrophoresis: a powerful tool in diagnosis of oxidative phosphorylation defects. Pediatr. Res. 2001, 50, 658-665.
    • (2001) Pediatr. Res , vol.50 , pp. 658-665
    • Van Coster, R.1    Smet, J.2    George, E.3    De Meirleir, L.4
  • 39
    • 0037086851 scopus 로고    scopus 로고
    • A quantitative histochemical assay for activities of mitochondrial electron transport chain complexes in mouse spinal cord sections
    • Jung, C., Higgins, C.M., Xu, Z., A quantitative histochemical assay for activities of mitochondrial electron transport chain complexes in mouse spinal cord sections. J. Neurosci. Methods 2002, 114, 165-172.
    • (2002) J. Neurosci. Methods , vol.114 , pp. 165-172
    • Jung, C.1    Higgins, C.M.2    Xu, Z.3
  • 40
    • 33644839474 scopus 로고    scopus 로고
    • Histochemical staining and quantification of plant mitochondrial respiratory chain complexes using blue-native polyacrylamide gel electrophoresis
    • Sabar, M., Balk, J., Leaver, C. J., Histochemical staining and quantification of plant mitochondrial respiratory chain complexes using blue-native polyacrylamide gel electrophoresis. Plant J. 2005, 44, 893-901.
    • (2005) Plant J , vol.44 , pp. 893-901
    • Sabar, M.1    Balk, J.2    Leaver, C.J.3
  • 41
    • 25844503496 scopus 로고    scopus 로고
    • Blue native polyacrylamide gel electrophoresis and the monitoring of malate- and oxaloacetate-producing enzymes
    • Singh, R., Chenier, D., Beriault, R., Mailloux, R. et al., Blue native polyacrylamide gel electrophoresis and the monitoring of malate- and oxaloacetate-producing enzymes. J. Biochem. Biophys. Methods 2005, 64, 189-199.
    • (2005) J. Biochem. Biophys. Methods , vol.64 , pp. 189-199
    • Singh, R.1    Chenier, D.2    Beriault, R.3    Mailloux, R.4
  • 42
    • 23844437729 scopus 로고    scopus 로고
    • Detection and purification of glucose 6-phosphate dehydrogenase, malic enzyme, and NADP-dependent isocitrate dehydrogenase by blue native polyacrylamide gel electrophoresis
    • Beriault, R., Chenier, D., Singh, R., Middaugh, J. et al., Detection and purification of glucose 6-phosphate dehydrogenase, malic enzyme, and NADP-dependent isocitrate dehydrogenase by blue native polyacrylamide gel electrophoresis. Electrophoresis 2005, 26, 2892-2897.
    • (2005) Electrophoresis , vol.26 , pp. 2892-2897
    • Beriault, R.1    Chenier, D.2    Singh, R.3    Middaugh, J.4
  • 43
    • 33751414342 scopus 로고    scopus 로고
    • In-gel activity staining of oxidized nicotinamide adenine dinucleotide kinase by blue native polyacrylamide gel electrophoresis
    • Mailloux, R. J., Singh, R., Appanna, V. D., In-gel activity staining of oxidized nicotinamide adenine dinucleotide kinase by blue native polyacrylamide gel electrophoresis. Anal. Biochem. 2006, 359, 210-215.
    • (2006) Anal. Biochem , vol.359 , pp. 210-215
    • Mailloux, R.J.1    Singh, R.2    Appanna, V.D.3
  • 44
    • 34247114586 scopus 로고    scopus 로고
    • Histochemical staining and quantification of dihydrolipoamide dehydrogenase diaphorase activity using blue native PAGE
    • Yan, L. J., Yang, S. H., Shu, H., Prokai, L., Forster, M. J., Histochemical staining and quantification of dihydrolipoamide dehydrogenase diaphorase activity using blue native PAGE. Electrophoresis 2007, 28, 1036-1045.
    • (2007) Electrophoresis , vol.28 , pp. 1036-1045
    • Yan, L.J.1    Yang, S.H.2    Shu, H.3    Prokai, L.4    Forster, M.J.5
  • 46
    • 0141757507 scopus 로고    scopus 로고
    • Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase
    • Seelert, H., Dencher, N. A., Müller, D. J., Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase. J. Mol. Biol. 2003, 333, 337-344.
    • (2003) J. Mol. Biol , vol.333 , pp. 337-344
    • Seelert, H.1    Dencher, N.A.2    Müller, D.J.3
  • 49
    • 26844548023 scopus 로고    scopus 로고
    • an angular association of monomers induces the strong curvature of the inner membrane
    • Structure of dimeric ATP synthase from mitochondria
    • Dudkina, N. V., Heinemeyer, J., Keegstra, W., Boekema, E. J., Braun, H.-P., Structure of dimeric ATP synthase from mitochondria: an angular association of monomers induces the strong curvature of the inner membrane. FEBS Lett. 2005, 579, 5769-5772.
    • (2005) FEBS Lett , vol.579 , pp. 5769-5772
    • Dudkina, N.V.1    Heinemeyer, J.2    Keegstra, W.3    Boekema, E.J.4    Braun, H.-P.5
  • 50
    • 24644520358 scopus 로고    scopus 로고
    • O bridging features and the structural basis of mitochondrial cristae biogenesis
    • Structure of dimeric mitochondrial ATP synthase
    • O bridging features and the structural basis of mitochondrial cristae biogenesis. Proc. Natl. Acad. Sci. USA 2005, 102, 12356-12358.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12356-12358
    • Minauro-Sanmiguel, F.1    Wilkens, S.2    Garcia, J.J.3
  • 51
    • 33646934708 scopus 로고    scopus 로고
    • Characterization of dimeric ATP synthase and cristae membrane ultrastructure from Saccharomyces and Polytomella mitochondria
    • Dudkina, N. V., Sunderhaus, S., Braun, H. P., Boekema, E. J., Characterization of dimeric ATP synthase and cristae membrane ultrastructure from Saccharomyces and Polytomella mitochondria. FEBS Lett. 2006, 580, 3427-3432.
    • (2006) FEBS Lett , vol.580 , pp. 3427-3432
    • Dudkina, N.V.1    Sunderhaus, S.2    Braun, H.P.3    Boekema, E.J.4
  • 53
    • 34249688217 scopus 로고    scopus 로고
    • A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria
    • Heinemeyer, J., Braun, H. P., Boekema, E. J., Kouril, R., A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria. J. Biol. Chem. 2007, 282, 12240-12248.
    • (2007) J. Biol. Chem , vol.282 , pp. 12240-12248
    • Heinemeyer, J.1    Braun, H.P.2    Boekema, E.J.3    Kouril, R.4
  • 54
    • 57649211340 scopus 로고    scopus 로고
    • Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato
    • Bultema, J. B., Braun, H. P., Boekema, E. J., Kouril, R., Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato. Biochim. Biophys. Acta 2009, 1787,60-67.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 60-67
    • Bultema, J.B.1    Braun, H.P.2    Boekema, E.J.3    Kouril, R.4
  • 55
    • 14744270722 scopus 로고    scopus 로고
    • Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III
    • Dudkina, N. V., Eubel, H., Keegstra, W., Boekema, E. J., Braun, H. P., Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III. Proc. Natl. Acad. Sci. USA 2005, 102, 3225-3229.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3225-3229
    • Dudkina, N.V.1    Eubel, H.2    Keegstra, W.3    Boekema, E.J.4    Braun, H.P.5
  • 56
    • 37549064026 scopus 로고    scopus 로고
    • 2 supercomplex from Zea mays at 11-13 A resolution: Assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I
    • 2 supercomplex from Zea mays at 11-13 A resolution: assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I. Biochim. Biophys. Acta 2008, 1777, 84-93.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 84-93
    • Peters, K.1    Dudkina, N.V.2    Jänsch, L.3    Braun, H.P.4    Boekema, E.J.5
  • 57
    • 57049094966 scopus 로고    scopus 로고
    • mitochondrial supercomplexes
    • The higher level of organization of the oxidative phosphorylation system
    • Dudkina, N. V., Sunderhaus, S., Boekema, E. J., Braun, H. P., The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes. J. Bioenerg. Biomembr. 2008, 40, 419-424.
    • (2008) J. Bioenerg. Biomembr , vol.40 , pp. 419-424
    • Dudkina, N.V.1    Sunderhaus, S.2    Boekema, E.J.3    Braun, H.P.4
  • 58
    • 34447643582 scopus 로고    scopus 로고
    • A novel approach to analyze membrane proteins by laser mass spectrometry: From protein subunits to the integral complex
    • Morgner, N., Kleinschroth, T., Barth, H. D., Ludwig, B., Brutschy, B., A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex. J. Am. Soc. Mass Spectrom. 2007, 18, 1429-1438.
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 1429-1438
    • Morgner, N.1    Kleinschroth, T.2    Barth, H.D.3    Ludwig, B.4    Brutschy, B.5
  • 60
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., Song, O., A novel genetic system to detect protein-protein interactions. Nature 1989, 340, 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 61
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M. et al., A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 1999, 17, 1030-1032.
    • (1999) Nat. Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4
  • 62
    • 34147218109 scopus 로고    scopus 로고
    • Electrophoretic methods to isolate protein complexes from mitochondria
    • Wittig, I., Schägger, H., Electrophoretic methods to isolate protein complexes from mitochondria. Methods Cell Biol. 2007, 80, 723-741.
    • (2007) Methods Cell Biol , vol.80 , pp. 723-741
    • Wittig, I.1    Schägger, H.2
  • 63
    • 26844507129 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae translational activator Cbs1p is associated with translationally active mitochondrial ribosomes
    • Krause-Buchholz, U., Schöbel, K., Lauffer, S., Rödel, G., Saccharomyces cerevisiae translational activator Cbs1p is associated with translationally active mitochondrial ribosomes. Biol. Chem. 2005, 386, 407-415.
    • (2005) Biol. Chem , vol.386 , pp. 407-415
    • Krause-Buchholz, U.1    Schöbel, K.2    Lauffer, S.3    Rödel, G.4
  • 64
    • 0141692862 scopus 로고    scopus 로고
    • Fatty acid biosynthesis in mitochondria of grasses: Malonylcoenzyme A is generated by amitochondrial-localized acetylcoenzyme A carboxylase
    • Focke, M., Gieringer, E., Schwan, S., Jänsch, L. et al., Fatty acid biosynthesis in mitochondria of grasses: malonylcoenzyme A is generated by amitochondrial-localized acetylcoenzyme A carboxylase. Plant Physiol. 2003, 133, 875-884.
    • (2003) Plant Physiol , vol.133 , pp. 875-884
    • Focke, M.1    Gieringer, E.2    Schwan, S.3    Jänsch, L.4
  • 65
    • 23044467754 scopus 로고    scopus 로고
    • Characterization of four variant forms of human propionyl-CoA carboxylase expressed in Escherichia coli
    • Jiang, H., Rao, K. S., Yee, V. C., Kraus, J. P., Characterization of four variant forms of human propionyl-CoA carboxylase expressed in Escherichia coli. J. Biol. Chem. 2005, 280, 27719-27727.
    • (2005) J. Biol. Chem , vol.280 , pp. 27719-27727
    • Jiang, H.1    Rao, K.S.2    Yee, V.C.3    Kraus, J.P.4
  • 66
    • 33748346853 scopus 로고    scopus 로고
    • A complexomic study of Escherichia coli using twodimensional blue native/SDS polyacrylamide gel electrophoresis
    • Lasserre, J. P., Beyne, E., Pyndiah, S., Lapaillerie, D., A complexomic study of Escherichia coli using twodimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 2006, 27, 3306-3321.
    • (2006) Electrophoresis , vol.27 , pp. 3306-3321
    • Lasserre, J.P.1    Beyne, E.2    Pyndiah, S.3    Lapaillerie, D.4
  • 67
    • 36849052316 scopus 로고    scopus 로고
    • Human geranylgeranyl diphosphate synthase is an octamer in solution
    • Miyagi, Y., Matsumura, Y., Sagami, H., Human geranylgeranyl diphosphate synthase is an octamer in solution. J. Biochem. (Tokyo) 2007, 142, 377-381.
    • (2007) J. Biochem. (Tokyo) , vol.142 , pp. 377-381
    • Miyagi, Y.1    Matsumura, Y.2    Sagami, H.3
  • 68
    • 33751414342 scopus 로고    scopus 로고
    • In-gel activity staining of oxidized nicotinamide adenine dinucleotide kinase by blue native polyacrylamide gel electrophoresis
    • Mailloux, R. J., Singh, R., Appanna, V. D., In-gel activity staining of oxidized nicotinamide adenine dinucleotide kinase by blue native polyacrylamide gel electrophoresis. Anal. Biochem. 2006, 359, 210-215. ]
    • (2006) Anal. Biochem , vol.359 , pp. 210-215
    • Mailloux, R.J.1    Singh, R.2    Appanna, V.D.3
  • 69
    • 25844503496 scopus 로고    scopus 로고
    • Blue native polyacrylamide gel electrophoresis and the monitoring of malate- and oxaloacetate-producing enzymes
    • Singh, R., Chenier, D., Beriault, R., Mailloux, R., Blue native polyacrylamide gel electrophoresis and the monitoring of malate- and oxaloacetate-producing enzymes. J. Biochem. Biophys. Methods 2005, 64, 189-199.
    • (2005) J. Biochem. Biophys. Methods , vol.64 , pp. 189-199
    • Singh, R.1    Chenier, D.2    Beriault, R.3    Mailloux, R.4
  • 70
    • 33845416970 scopus 로고    scopus 로고
    • Implications for PA28 and 19S regulatory complexes
    • Global organization and function of mammalian cytosolic proteasome pools
    • Shibatani, T., Carlson, E. J., Larabee, F., McCormack, A. L., Global organization and function of mammalian cytosolic proteasome pools: Implications for PA28 and 19S regulatory complexes. Mol. Biol. Cell 2006, 17, 4962-4971.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4962-4971
    • Shibatani, T.1    Carlson, E.J.2    Larabee, F.3    McCormack, A.L.4
  • 72
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger, H., Pfeiffer, K., Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 2000, 19, 1777-1783.
    • (2000) EMBO J , vol.19 , pp. 1777-1783
    • Schägger, H.1    Pfeiffer, K.2
  • 73
    • 0034674060 scopus 로고    scopus 로고
    • 1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria
    • 1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria. J. Biol. Chem. 2000, 275, 18093-18098.
    • (2000) J. Biol. Chem , vol.275 , pp. 18093-18098
    • Cruciat, C.M.1    Brunner, S.2    Baumann, F.3    Neupert, W.4    Stuart, R.A.5
  • 76
    • 23844540312 scopus 로고    scopus 로고
    • Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria
    • Zhang, M., Mileykovskaya, E., Dowhan, W., Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria. J. Biol. Chem. 2005, 280, 29403-29408.
    • (2005) J. Biol. Chem , vol.280 , pp. 29403-29408
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 77
    • 27644437287 scopus 로고    scopus 로고
    • Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: Implications for Barth Syndrome
    • Brandner, K., Mick, D. U., Frazier, A. E., Taylor, R. D. et al., Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth Syndrome. Mol. Biol. Cell 2005, 16, 5202-5214.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5202-5214
    • Brandner, K.1    Mick, D.U.2    Frazier, A.E.3    Taylor, R.D.4
  • 78
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients
    • McKenzie, M., Lazarou, M., Thorburn, D. R., Ryan, M. T., Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients. J. Mol. Biol. 2006, 361, 462-469.
    • (2006) J. Mol. Biol , vol.361 , pp. 462-469
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 80
    • 66249138891 scopus 로고    scopus 로고
    • N. ubel, E., Wittig, I., Kerscher, S., Brandt, U., Schägger, H., Two-dimensional native electrophoretic analysis of respiratory supercomplexes from Yarrowia lipolytica. Proteomics 2009, in press.
    • N. ubel, E., Wittig, I., Kerscher, S., Brandt, U., Schägger, H., Two-dimensional native electrophoretic analysis of respiratory supercomplexes from Yarrowia lipolytica. Proteomics 2009, in press.
  • 81
    • 63449114764 scopus 로고    scopus 로고
    • Twodimensional native electrophoresis for functional assays of mitochondrial complexes
    • in press
    • Wumaier, Z., Nübel, E., Wittig, I., Schägger, H., Twodimensional native electrophoresis for functional assays of mitochondrial complexes. Methods Enzymol. 2009, in press.
    • (2009) Methods Enzymol
    • Wumaier, Z.1    Nübel, E.2    Wittig, I.3    Schägger, H.4
  • 82
    • 3543043510 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification
    • Rais, I., Karas, M., Schägger, H., Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification. Proteomics 2004, 4, 2567-2571.
    • (2004) Proteomics , vol.4 , pp. 2567-2571
    • Rais, I.1    Karas, M.2    Schägger, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.