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Volumn 80, Issue , 2011, Pages 247-271

Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes

Author keywords

ATP synthase; ES; ion channels; ion mobility; membrane complexes; proteomics

Indexed keywords

AMINO ACID; HYDROGEN; LIPID; MEMBRANE PROTEIN; PROTEIN SUBUNIT;

EID: 79959456892     PISSN: 00664154     EISSN: 00664154     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-062309-093307     Document Type: Article
Times cited : (129)

References (123)
  • 1
    • 4644327652 scopus 로고    scopus 로고
    • Native protein mass spectrometry: From intact oligomers to functional machineries
    • DOI 10.1016/j.cbpa.2004.08.006, PII S1367593104001048
    • van den Heuvel RH, Heck AJ. 2004. Native protein mass spectrometry: from intact oligomers to functional machineries. Curr. Opin. Chem. Biol. 8:519-526. (Pubitemid 39278349)
    • (2004) Current Opinion in Chemical Biology , vol.8 , Issue.5 , pp. 519-526
    • Van Den Heuvel, R.H.H.1    Heck, A.J.R.2
  • 3
    • 19944432588 scopus 로고    scopus 로고
    • The flight of macromolecular complexes in a mass spectrometer
    • discuss 89-91
    • Sobott F, McCammonMG, HernandezH, Robinson CV. 2005. The flight of macromolecular complexes in a mass spectrometer. Philos. Trans. A 363:379-89; discuss. 89-91.
    • (2005) Philos. Trans. A , vol.363 , pp. 379-89
    • Sobott, F.1    McCammon, M.G.2    Hernandez, H.3    Robinson, C.V.4
  • 4
    • 33646013923 scopus 로고    scopus 로고
    • Mass spectrometry of macromolecular assemblies: Preservation and dissociation
    • Benesch JL, Robinson CV. 2006. Mass spectrometry of macromolecular assemblies: preservation and dissociation. Curr. Opin. Struct. Biol. 16:245-251.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 245-251
    • Benesch, J.L.1    Robinson, C.V.2
  • 5
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon M, Robinson CV. 2007. The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu. Rev. Biochem. 76:167-193.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 6
    • 34548215681 scopus 로고    scopus 로고
    • Protein complexes in the gas phase: Technology for structural genomics and proteomics
    • DOI 10.1021/cr068289b
    • Benesch JLP, Ruotolo BT, Simmons DA, Robinson CV. 2007. Protein complexes in the gas phase: technology for structural genomics and proteomics. Chem. Rev. 107:3544-567. (Pubitemid 47322744)
    • (2007) Chemical Reviews , vol.107 , Issue.8 , pp. 3544-3567
    • Benesch, J.L.P.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinsons, C.V.4
  • 7
    • 77950339600 scopus 로고    scopus 로고
    • How far can we go with structural mass spectrometry of protein complexes?
    • SharonM. 2010. How far can we go with structural mass spectrometry of protein complexes? J. Am. Soc. Mass. Spectrom. 21:487-500.
    • (2010) J. Am. Soc. Mass. Spectrom. , vol.21 , pp. 487-500
    • Sharon, M.1
  • 8
    • 77956181968 scopus 로고    scopus 로고
    • When proteomics meets structural biology
    • Zhou M, Robinson CV. 2010. When proteomics meets structural biology. Trends Biochem. Sci. 35:522-529.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 522-529
    • Zhou, M.1    Robinson, C.V.2
  • 9
    • 34548409975 scopus 로고    scopus 로고
    • Identification ofmembrane proteins frommammalian cell/tissue using methanol-facilitated solubilization and tryptic digestion coupled with 2D-LC-MS/MS
    • Blonder J, Chan KC, Issaq HJ, Veenstra TD. 2006. Identification ofmembrane proteins frommammalian cell/tissue using methanol-facilitated solubilization and tryptic digestion coupled with 2D-LC-MS/MS. Nat. Protoc. 1:2784-790.
    • (2006) Nat. Protoc. , vol.1 , pp. 2784-2790
    • Blonder, J.1    Chan, K.C.2    Issaq, H.J.3    Veenstra, T.D.4
  • 10
    • 55749084664 scopus 로고    scopus 로고
    • Strategies for shotgun identification of integral membrane proteins by tandem mass spectrometry
    • Lu B, McClatchy DB, Kim JY, Yates JR 3rd. 2008. Strategies for shotgun identification of integral membrane proteins by tandem mass spectrometry. Proteomics 8:3947-955.
    • (2008) Proteomics , vol.8 , pp. 3947-3955
    • Lu, B.1    McClatchy, D.B.2    Kim, J.Y.3    Yates Iii, J.R.4
  • 11
    • 70349776701 scopus 로고    scopus 로고
    • Enrichment and preparation of plasma membrane proteins from Arabidopsis thaliana for global proteomic analysis using liquid chromatography-tandem mass spectrometry
    • Mitra SK, Clouse SD, Goshe MB. 2009. Enrichment and preparation of plasma membrane proteins from Arabidopsis thaliana for global proteomic analysis using liquid chromatography-tandem mass spectrometry. Methods Mol. Biol. 564:341-355.
    • (2009) Methods Mol. Biol. , vol.564 , pp. 341-355
    • Mitra, S.K.1    Clouse, S.D.2    Goshe, M.B.3
  • 12
    • 67049158006 scopus 로고    scopus 로고
    • An efficient organic solvent based extraction method for the proteomic analysis of Arabidopsis plasma membranes
    • Mitra SK, Walters BT, Clouse SD, Goshe MB. 2009. An efficient organic solvent based extraction method for the proteomic analysis of Arabidopsis plasma membranes. J. Proteome Res. 8:2752-767.
    • (2009) J. Proteome Res. , vol.8 , pp. 2752-2767
    • Mitra, S.K.1    Walters, B.T.2    Clouse, S.D.3    Goshe, M.B.4
  • 13
    • 67649713420 scopus 로고    scopus 로고
    • Thematic review series: Proteomics Proteomic analysis of lipid-protein complexes
    • Vaisar T. 2009. Thematic review series: proteomics. Proteomic analysis of lipid-protein complexes. J. Lipid. Res. 50:781-786.
    • (2009) J. Lipid. Res. , vol.50 , pp. 781-786
    • Vaisar, T.1
  • 14
    • 77957232334 scopus 로고    scopus 로고
    • Advances in shotgun proteomics and the analysis of membrane proteomes
    • Gilmore JM, Washburn MP. 2010. Advances in shotgun proteomics and the analysis of membrane proteomes. J. Proteomics 73:2078-091.
    • (2010) J. Proteomics , vol.73 , pp. 2078-2091
    • Gilmore, J.M.1    Washburn, M.P.2
  • 15
    • 77951839609 scopus 로고    scopus 로고
    • Post-translational modifications of integral membrane proteins resolved by top-downFourier transform mass spectrometry with collisionally activated dissociation
    • Ryan CM, Souda P, Bassilian S, Ujwal R, Zhang J, et al. 2010. Post-translational modifications of integral membrane proteins resolved by top-downFourier transform mass spectrometry with collisionally activated dissociation. Mol. Cell. Proteomics 9:791-803.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 791-803
    • Ryan, C.M.1    Souda, P.2    Bassilian, S.3    Ujwal, R.4    Zhang, J.5
  • 16
    • 76649102423 scopus 로고    scopus 로고
    • Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes
    • Yang W, Di Vizio D, Kirchner M, Steen H, Freeman MR. 2010. Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes. Mol. Cell. Proteomics 9:54-70.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 54-70
    • Yang, W.1    Di Vizio, D.2    Kirchner, M.3    Steen, H.4    Freeman, M.R.5
  • 17
    • 46249089993 scopus 로고    scopus 로고
    • Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins
    • DOI 10.1038/nature06977, PII NATURE06977
    • Joh NH, Min A, Faham S, Whitelegge JP, Yang D, et al. 2008. Modest stabilization by most hydrogenbonded side-chain interactions in membrane proteins. Nature 453:1266-270. (Pubitemid 351913594)
    • (2008) Nature , vol.453 , Issue.7199 , pp. 1266-1270
    • Joh, N.H.1    Min, A.2    Faham, S.3    Whitelegge, J.P.4    Yang, D.5    Woods Jr., V.L.6    Bowie, J.U.7
  • 18
    • 33947599164 scopus 로고    scopus 로고
    • Defining the interacting regions between apomyoglobin and lipid membrane by hydrogen/deuterium exchange coupled to mass spectrometry
    • DOI 10.1016/j.jmb.2007.02.014, PII S0022283607001817
    • Man P, Montagner C, Vernier G, Dublet B, Chenal A, et al. 2007. Defining the interacting regions between apomyoglobin and lipid membrane by hydrogen/deuterium exchange coupled to mass spectrometry. J. Mol. Biol. 368:464-472. (Pubitemid 46483485)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.2 , pp. 464-472
    • Man, P.1    Montagner, C.2    Vernier, G.3    Dublet, B.4    Chenal, A.5    Forest, E.6    Forge, V.7
  • 19
    • 33745041235 scopus 로고    scopus 로고
    • Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes
    • DOI 10.1146/annurev.biophys.35.040405.102050
    • Takamoto K, Chance MR. 2006. Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes. Annu. Rev. Biophys. Biomol. Struct. 35:251-276. (Pubitemid 43877378)
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 251-276
    • Takamoto, K.1    Chance, M.R.2
  • 20
    • 77954635392 scopus 로고    scopus 로고
    • Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry
    • Gupta S, Bavro VN, D'Mello R, Tucker SJ, Venien-Bryan C, Chance MR. 2010. Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry. Structure 18:839-846.
    • (2010) Structure , vol.18 , pp. 839-846
    • Gupta, S.1    Bavro, V.N.2    D'Mello, R.3    Tucker, S.J.4    Venien-Bryan, C.5    Chance, M.R.6
  • 21
    • 75749117507 scopus 로고    scopus 로고
    • Visualizing water molecules in transmembrane proteins using radiolytic labeling methods
    • Orban T, Gupta S, Palczewski K, Chance MR. 2010. Visualizing water molecules in transmembrane proteins using radiolytic labeling methods. Biochemistry 49:827-834.
    • (2010) Biochemistry , vol.49 , pp. 827-834
    • Orban, T.1    Gupta, S.2    Palczewski, K.3    Chance, M.R.4
  • 22
    • 33744816815 scopus 로고    scopus 로고
    • Subunit architecture of multimeric complexes isolated directly from cells
    • DOI 10.1038/sj.embor.7400702, PII 7400702
    • Hernandez H, Dziembowski A, Taverner T, Seraphin B, Robinson CV. 2006. Subunit architecture of multimeric complexes isolated directly from cells. EMBO Rep. 7:605-610. (Pubitemid 43827327)
    • (2006) EMBO Reports , vol.7 , Issue.6 , pp. 605-610
    • Hernandez, H.1    Dziembowski, A.2    Taverner, T.3    Seraphin, B.4    Robinson, C.V.5
  • 23
    • 35148816658 scopus 로고    scopus 로고
    • Structural biology of RNA polymerase III: Mass spectrometry elucidates subcomplex architecture
    • DOI 10.1016/j.str.2007.07.016, PII S0969212607002912
    • Lorenzen K, Vannini A, Cramer P, Heck AJ. 2007. Structural biology of RNA polymerase III: mass spectrometry elucidates subcomplex architecture. Structure 15:1237-245. (Pubitemid 47539158)
    • (2007) Structure , vol.15 , Issue.10 , pp. 1237-1245
    • Lorenzen, K.1    Vannini, A.2    Cramer, P.3    Heck, A.J.R.4
  • 24
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: A bridge between interactomics and structural biology
    • Heck AJ. 2008. Native mass spectrometry: a bridge between interactomics and structural biology. Nat. Methods 5:927-933.
    • (2008) Nat. Methods , vol.5 , pp. 927-933
    • Heck, A.J.1
  • 25
    • 57449083256 scopus 로고    scopus 로고
    • Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3
    • Zhou M, Sandercock AM, Fraser CS, Ridlova G, Stephens E, et al. 2008. Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3. Proc. Natl. Acad. Sci. USA 105:18139-144.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 18139-18144
    • Zhou, M.1    Sandercock, A.M.2    Fraser, C.S.3    Ridlova, G.4    Stephens, E.5
  • 26
    • 46249083761 scopus 로고    scopus 로고
    • Assembly reflects evolution of protein complexes
    • DOI 10.1038/nature06942, PII NATURE06942
    • Levy ED, Boeri Erba E, Robinson CV, Teichmann SA. 2008. Assembly reflects evolution of protein complexes. Nature 453:1262-265. (Pubitemid 351913589)
    • (2008) Nature , vol.453 , Issue.7199 , pp. 1262-1265
    • Levy, E.D.1    Erba, E.B.2    Robinson, C.V.3    Teichmann, S.A.4
  • 27
    • 58149191374 scopus 로고    scopus 로고
    • Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality
    • Sharon M, Mao H, Boeri Erba E, Stephens E, Zheng N, Robinson CV. 2009. Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality. Structure 17:31-40.
    • (2009) Structure , vol.17 , pp. 31-40
    • Sharon, M.1    Mao, H.2    Boeri Erba, E.3    Stephens, E.4    Zheng, N.5    Robinson, C.V.6
  • 29
    • 0345413247 scopus 로고    scopus 로고
    • Phospholipid complexation and association with apolipoprotein C-II: Insights from mass spectrometry
    • Hanson CL, Ilag LL, Malo J, Hatters DM, Howlett GJ, Robinson CV. 2003. Phospholipid complexation and association with apolipoprotein C-II: insights from mass spectrometry. Biophys. J. 85:3802-812. (Pubitemid 37490290)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 3802-3812
    • Hanson, C.L.1    Ilag, L.L.2    Malo, J.3    Hatters, D.M.4    Howlett, G.J.5    Robinson, C.V.6
  • 30
    • 0037464463 scopus 로고    scopus 로고
    • + channel KcsA with membrane phospholipids as studied by ESI mass spectrometry
    • DOI 10.1016/S0014-5793(03)00282-5
    • Demmers JA, van Dalen A, de Kruijff B, Heck AJ, Killian JA. 2003. Interaction of the K+ channel KcsA with membrane phospholipids as studied by ESI mass spectrometry. FEBS Lett. 541:28-32. (Pubitemid 36428912)
    • (2003) FEBS Letters , vol.541 , Issue.1-3 , pp. 28-32
    • Demmers, J.A.A.1    Van Dalen, A.2    De Kruijff, B.3    Heck, A.J.R.4    Killian, J.A.5
  • 31
    • 34447643582 scopus 로고    scopus 로고
    • A novel approach to analyze membrane proteins by laser mass spectrometry: From protein subunits to the integral complex
    • DOI 10.1016/j.jasms.2007.04.013, PII S1044030507003741
    • Morgner N, Kleinschroth T, Barth HD, Ludwig B, Brutschy B. 2007. A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex. J. Am. Soc. Mass Spectrom. 18:1429-438. (Pubitemid 47088995)
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , Issue.8 , pp. 1429-1438
    • Morgner, N.1    Kleinschroth, T.2    Barth, H.-D.3    Ludwig, B.4    Brutschy, B.5
  • 32
    • 65649105054 scopus 로고    scopus 로고
    • Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy
    • Vonck J, Pisa KY, Morgner N, Brutschy B, M̈uller V. 2009. Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy. J. Biol. Chem. 284:10110-119.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10110-10119
    • Vonck, J.1    Pisa, K.Y.2    Morgner, N.3    Brutschy, B.4    M̈uller, V.5
  • 34
    • 77955053798 scopus 로고    scopus 로고
    • Multiply charged gas-phase NaAOT reverse micelles: Formation, encapsulation of glycine and collision induced dissociation
    • Fang Y, Bennett A, Liu J. 2010. Multiply charged gas-phase NaAOT reverse micelles: formation, encapsulation of glycine and collision induced dissociation. Int. J. Mass Spectrom. 293:12-22.
    • (2010) Int. J. Mass Spectrom. , vol.293 , pp. 12-22
    • Fang, Y.1    Bennett, A.2    Liu, J.3
  • 35
    • 47249106965 scopus 로고    scopus 로고
    • Micelles protect membrane complexes from solution to vacuum
    • DOI 10.1126/science.1159292
    • Barrera NP, Di Bartolo N, Booth PJ, Robinson CV. 2008. Micelles protect membrane complexes from solution to vacuum. Science 321:243-246. (Pubitemid 351989094)
    • (2008) Science , vol.321 , Issue.5886 , pp. 243-246
    • Barrera, N.P.1    Di Bartolo, N.2    Booth, P.J.3    Robinson, C.V.4
  • 37
    • 28844474910 scopus 로고    scopus 로고
    • Biochemistry: Evidence for macromolecular protein rings in the absence of bulk water
    • DOI 10.1126/science.1120177
    • Ruotolo BT, Giles K, Campuzano I, Sandercock AM, Bateman RH, Robinson CV. 2005. Evidence for macromolecular protein rings in the absence of bulk water. Science 310:1658-661. (Pubitemid 41780783)
    • (2005) Science , vol.310 , Issue.5754 , pp. 1658-1661
    • Ruotolo, B.T.1    Giles, K.2    Campuzano, I.3    Sandercock, A.M.4    Bateman, R.H.5    Robinson, C.V.6
  • 43
    • 77349098524 scopus 로고    scopus 로고
    • Exploring the membrane proteome-challenges and analytical strategies
    • Helbig AO, Heck AJ, Slijper M. 2010. Exploring the membrane proteome-challenges and analytical strategies. J. Proteomics 73:868-878.
    • (2010) J. Proteomics , vol.73 , pp. 868-878
    • Helbig, A.O.1    Heck, A.J.2    Slijper, M.3
  • 44
    • 79953192195 scopus 로고    scopus 로고
    • Overcoming key technological challenges in using mass spectrometry for mapping cell surfaces in tissues
    • Griffin NM, Schnitzer JE. 2011. Overcoming key technological challenges in using mass spectrometry for mapping cell surfaces in tissues. Mol. Cell. Proteomics 10:R110.000935.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Griffin, N.M.1    Schnitzer, J.E.2
  • 45
    • 77953773474 scopus 로고    scopus 로고
    • A simple and effectivemethod to analyze membrane proteins by SDS-PAGE andMALDI mass spectrometry
    • Di Girolamo F, Ponzi M, CrescenziM, Alessandroni J, Guadagni F. 2010. A simple and effectivemethod to analyze membrane proteins by SDS-PAGE andMALDI mass spectrometry. Anticancer Res. 30:1121-29.
    • (2010) Anticancer Res. , vol.30 , pp. 1121-1129
    • Di Girolamo, F.1    Ponzi, M.2    Crescenzi, M.3    Alessandroni, J.4    Guadagni, F.5
  • 46
    • 77954458497 scopus 로고    scopus 로고
    • Gel absorption-based sample preparation for the analysis of membrane proteome by mass spectrometry
    • Zhou J, Xiong J, Li J, Huang S, Zhang H, et al. 2010. Gel absorption-based sample preparation for the analysis of membrane proteome by mass spectrometry. Anal. Biochem. 404:204-210.
    • (2010) Anal. Biochem. , vol.404 , pp. 204-210
    • Zhou, J.1    Xiong, J.2    Li, J.3    Huang, S.4    Zhang, H.5
  • 49
    • 77149165069 scopus 로고    scopus 로고
    • Technologies for plasma membrane proteomics
    • Cordwell SJ, Thingholm TE. 2010. Technologies for plasma membrane proteomics. Proteomics 10:611-27.
    • (2010) Proteomics , vol.10 , pp. 611-27
    • Cordwell, S.J.1    Thingholm, T.E.2
  • 50
    • 34347234182 scopus 로고    scopus 로고
    • Shotgun analysis of integral membrane proteins facilitated by elevated temperature
    • DOI 10.1021/ac0700225
    • Speers AE, Blackler AR, Wu CC. 2007. Shotgun analysis of integral membrane proteins facilitated by elevated temperature. Anal. Chem. 79:4613-620. (Pubitemid 46999578)
    • (2007) Analytical Chemistry , vol.79 , Issue.12 , pp. 4613-4620
    • Speers, A.E.1    Blackler, A.R.2    Wu, C.C.3
  • 51
    • 77951786429 scopus 로고    scopus 로고
    • Quantitative improvements in peptide recovery at elevated chromatographic temperatures from microcapillary liquid chromatography-mass spectrometry analyses of brain using selected reaction monitoring
    • Farias SE, Kline KG, Klepacki J, Wu CC. 2010. Quantitative improvements in peptide recovery at elevated chromatographic temperatures from microcapillary liquid chromatography-mass spectrometry analyses of brain using selected reaction monitoring. Anal. Chem. 82:3435-440.
    • (2010) Anal. Chem. , vol.82 , pp. 3435-3440
    • Farias, S.E.1    Kline, K.G.2    Klepacki, J.3    Wu, C.C.4
  • 52
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, HCD and ETD-MS applied to the N-linked glycoproteome of Campylobacter jejuni
    • Scott NE, Parker BL, Connolly AM, Paulech J, Edwards AV, et al. 2011. Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, HCD and ETD-MS applied to the N-linked glycoproteome of Campylobacter jejuni. Mol. Cell. Proteomics 10(2):M000031MCP201.
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.2
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4    Edwards, A.V.5
  • 53
    • 70350235044 scopus 로고    scopus 로고
    • A three-way proteomics strategy allows differential analysis of yeast mitochondrial membrane protein complexes under anaerobic and aerobic conditions
    • Helbig AO, de Groot MJ, van Gestel RA, Mohammed S, de Hulster EA, et al. 2009. A three-way proteomics strategy allows differential analysis of yeast mitochondrial membrane protein complexes under anaerobic and aerobic conditions. Proteomics 9:4787-798.
    • (2009) Proteomics , vol.9 , pp. 4787-4798
    • Helbig, A.O.1    De Groot, M.J.2    Van Gestel, R.A.3    Mohammed, S.4    De Hulster, E.A.5
  • 54
    • 73349136580 scopus 로고    scopus 로고
    • Differential proteomics identifies protein biomarkers that predict local relapse of head and neck squamous cell carcinomas
    • Schaaij-Visser TB, Graveland AP, Gauci S, Braakhuis BJ, Buijze M, et al. 2009. Differential proteomics identifies protein biomarkers that predict local relapse of head and neck squamous cell carcinomas. Clin. Cancer Res. 15:7666-675.
    • (2009) Clin. Cancer Res. , vol.15 , pp. 7666-7675
    • Schaaij-Visser, T.B.1    Graveland, A.P.2    Gauci, S.3    Braakhuis, B.J.4    Buijze, M.5
  • 55
    • 77149125260 scopus 로고    scopus 로고
    • Hydrophobic fractionation enhances novel protein detection by mass spectrometry in triple negative breast cancer
    • Lu M, Whitelegge JP, Whelan SA, He J, Saxton RE, et al. 2010. Hydrophobic fractionation enhances novel protein detection by mass spectrometry in triple negative breast cancer. J. Proteomics Bioinform. 3:1-10.
    • (2010) J. Proteomics Bioinform. , vol.3 , pp. 1-10
    • Lu, M.1    Whitelegge, J.P.2    Whelan, S.A.3    He, J.4    Saxton, R.E.5
  • 57
    • 77958008719 scopus 로고    scopus 로고
    • The subunit composition of mitochondrial NADH:ubiquinone oxidoreductase (complex I) from Pichia pastoris
    • Bridges HR, Fearnley IM, Hirst J. 2010. The subunit composition of mitochondrial NADH:ubiquinone oxidoreductase (complex I) from Pichia pastoris. Mol. Cell. Proteomics 9:2318-326.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2318-2326
    • Bridges, H.R.1    Fearnley, I.M.2    Hirst, J.3
  • 59
    • 77950685492 scopus 로고    scopus 로고
    • Laser-induced liquid bead ion desorption-MS of protein complexes from blue-native gels, a sensitive top-down proteomic approach
    • Sokolova L, Wittig I, Barth HD, SchaggerH, Brutschy B, BrandtU. 2010. Laser-induced liquid bead ion desorption-MS of protein complexes from blue-native gels, a sensitive top-down proteomic approach. Proteomics 10:1401-7.
    • (2010) Proteomics , vol.10 , pp. 1401-1407
    • Sokolova, L.1    Wittig, I.2    Barth, H.D.3    Schagger, H.4    Brutschy, B.5    Brandt, U.6
  • 60
    • 33845909817 scopus 로고    scopus 로고
    • Top-down mass spectrometry of integral membrane proteins
    • DOI 10.1586/14789450.3.6.585
    • Whitelegge J, Halgand F, Souda P, Zabrouskov V. 2006. Top-down mass spectrometry of integral membrane proteins. Expert Rev. Proteomics 3:585-596. (Pubitemid 46021197)
    • (2006) Expert Review of Proteomics , vol.3 , Issue.6 , pp. 585-596
    • Whitelegge, J.1    Halgand, F.2    Souda, P.3    Zabrouskov, V.4
  • 61
    • 58549118993 scopus 로고    scopus 로고
    • Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface
    • Gubbens J, Ruijter E, de Fays LE, Damen JM, de Kruijff B, et al. 2009. Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface. Chem. Biol. 16:3-14.
    • (2009) Chem. Biol. , vol.16 , pp. 3-14
    • Gubbens, J.1    Ruijter, E.2    De Fays, L.E.3    Damen, J.M.4    De Kruijff, B.5
  • 62
    • 77956516299 scopus 로고    scopus 로고
    • Proteome-wide detection of phospholipid-protein interactions in mitochondria by photocrosslinking and click chemistry
    • Gubbens J, de Kroon AI. 2010. Proteome-wide detection of phospholipid-protein interactions in mitochondria by photocrosslinking and click chemistry. Mol. Biosyst. 6:1751-759.
    • (2010) Mol. Biosyst. , vol.6 , pp. 1751-1759
    • Gubbens, J.1    De Kroon, A.I.2
  • 63
    • 70349440924 scopus 로고    scopus 로고
    • Protein-lipid interactions: Paparazzi hunting for snap-shots
    • Haberkant P, van Meer G. 2009. Protein-lipid interactions: paparazzi hunting for snap-shots. Biol. Chem. 390:795-803.
    • (2009) Biol. Chem. , vol.390 , pp. 795-803
    • Haberkant, P.1    Van Meer, G.2
  • 64
    • 58149399828 scopus 로고    scopus 로고
    • Biochemical characterization of membrane fractions in murine sperm: Identification of three distinct sub-types of membrane rafts
    • Asano A, Selvaraj V, Buttke DE, Nelson JL, Green KM, et al. 2009. Biochemical characterization of membrane fractions in murine sperm: identification of three distinct sub-types of membrane rafts. J. Cell Physiol. 218:537-548.
    • (2009) J. Cell Physiol. , vol.218 , pp. 537-548
    • Asano, A.1    Selvaraj, V.2    Buttke, D.E.3    Nelson, J.L.4    Green, K.M.5
  • 65
    • 77957202484 scopus 로고    scopus 로고
    • Characterization of the proteomes associating with three distinct membrane raft sub-types in murine sperm
    • Asano A, Nelson JL, Zhang S, Travis AJ. 2010. Characterization of the proteomes associating with three distinct membrane raft sub-types in murine sperm. Proteomics 10:3494-505.
    • (2010) Proteomics , vol.10 , pp. 3494-3505
    • Asano, A.1    Nelson, J.L.2    Zhang, S.3    Travis, A.J.4
  • 66
    • 70449687854 scopus 로고    scopus 로고
    • Mapping the structure of an integral membrane protein under semi-denaturing conditions by laser-induced oxidative labeling and mass spectrometry
    • Pan Y, Brown L, Konermann L. 2009. Mapping the structure of an integral membrane protein under semi-denaturing conditions by laser-induced oxidative labeling and mass spectrometry. J. Mol. Biol. 394:968-981.
    • (2009) J. Mol. Biol. , vol.394 , pp. 968-981
    • Pan, Y.1    Brown, L.2    Konermann, L.3
  • 67
    • 58149473115 scopus 로고    scopus 로고
    • Structural characterization of an integral membrane protein in its natural lipid environment by oxidative methionine labeling and mass spectrometry
    • Pan Y, Stocks BB, Brown L, Konermann L. 2009. Structural characterization of an integral membrane protein in its natural lipid environment by oxidative methionine labeling and mass spectrometry. Anal. Chem. 81:28-35.
    • (2009) Anal. Chem. , vol.81 , pp. 28-35
    • Pan, Y.1    Stocks, B.B.2    Brown, L.3    Konermann, L.4
  • 69
    • 66649096395 scopus 로고    scopus 로고
    • Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors
    • Angel TE, Chance MR, Palczewski K. 2009. Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors. Proc. Natl. Acad. Sci. USA 106:8555-560.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8555-8560
    • Angel, T.E.1    Chance, M.R.2    Palczewski, K.3
  • 70
    • 74249114010 scopus 로고    scopus 로고
    • Defining topological features of membrane proteins by nanoelectrospray ionisation mass spectrometry
    • Jones LN, Baldwin SA, Henderson PJ, Ashcroft AE. 2010. Defining topological features of membrane proteins by nanoelectrospray ionisation mass spectrometry. Rapid Commun. Mass Spectrom. 24:276-284.
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 276-284
    • Jones, L.N.1    Baldwin, S.A.2    Henderson, P.J.3    Ashcroft, A.E.4
  • 71
    • 77953594657 scopus 로고    scopus 로고
    • Effective removal of nonionic detergents in protein mass spectrometry, hydrogen/deuterium exchange, and proteomics
    • ReyM, Mŕazek H, Pompach P, Nov́ak P, Pelosi L, et al. 2010. Effective removal of nonionic detergents in protein mass spectrometry, hydrogen/deuterium exchange, and proteomics. Anal. Chem. 82:5107-116.
    • (2010) Anal. Chem. , vol.82 , pp. 5107-5116
    • Rey, M.1    Mŕazek, H.2    Pompach, P.3    Nov́ak, P.4    Pelosi, L.5
  • 72
    • 61449085729 scopus 로고    scopus 로고
    • Encapsulation ofmyoglobin in a cetyl trimethylammonium bromide micelle in vacuo: A simulation study
    • Wang Y, Larsson DS, van der SpoelD. 2009. Encapsulation ofmyoglobin in a cetyl trimethylammonium bromide micelle in vacuo: a simulation study. Biochemistry 48:1006-015.
    • (2009) Biochemistry , vol.48 , pp. 1006-1015
    • Wang, Y.1    Larsson, D.S.2    Van Der Spoel, D.3
  • 74
    • 1842728364 scopus 로고    scopus 로고
    • Observation of an Intact Noncovalent Homotrimer of Detergent-solubilized Rat Microsomal Glutathione Transferase-1 by Electrospray Mass Spectrometry
    • DOI 10.1074/jbc.M310958200
    • Lengqvist J, Svensson R, Evergren E, Morgenstern R, Griffiths WJ. 2004. Observation of an intact noncovalent homotrimer of detergent-solubilized rat microsomal glutathione transferase-1 by electrospray mass spectrometry. J. Biol. Chem. 279:13311-316. (Pubitemid 38468853)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 13311-13316
    • Lengqvist, J.1    Svensson, R.2    Evergren, E.3    Morgenstern, R.4    Griffiths, W.J.5
  • 75
    • 41449111510 scopus 로고    scopus 로고
    • Stoichiometry and localization of the stator subunits e and G in Thermus thermophilus H+-ATPase/synthase
    • Esteban O, Bernal RA, DonohoeM, Videler H, SharonM, et al. 2008. Stoichiometry and localization of the stator subunits E and G in Thermus thermophilus H+-ATPase/synthase. J. Biol. Chem. 283:2595-603.
    • (2008) J. Biol. Chem. , vol.283 , pp. 2595-2603
    • Esteban, O.1    Bernal, R.A.2    Donohoe, M.3    Videler, H.4    Sharon, M.5
  • 76
    • 41249097135 scopus 로고    scopus 로고
    • Stoichiometry of the peripheral stalk subunits e and G of yeast V1-ATPase determined by mass spectrometry
    • Kitagawa N, Mazon H, Heck AJ, Wilkens S. 2008. Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry. J. Biol. Chem. 283:3329-337.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3329-3337
    • Kitagawa, N.1    Mazon, H.2    Heck, A.J.3    Wilkens, S.4
  • 77
    • 68349086900 scopus 로고    scopus 로고
    • Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions
    • Barrera NP, Isaacson SC, Zhou M, Bavro VN, Welch A, et al. 2009. Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions. Nat. Methods 6:585-587.
    • (2009) Nat. Methods , vol.6 , pp. 585-587
    • Barrera, N.P.1    Isaacson, S.C.2    Zhou, M.3    Bavro, V.N.4    Welch, A.5
  • 78
    • 65449155090 scopus 로고    scopus 로고
    • Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa
    • Sennhauser G, Bukowska MA, Briand C, Grutter MG. 2009. Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa. J. Mol. Biol. 389:134-145.
    • (2009) J. Mol. Biol. , vol.389 , pp. 134-145
    • Sennhauser, G.1    Bukowska, M.A.2    Briand, C.3    Grutter, M.G.4
  • 79
    • 59449104154 scopus 로고    scopus 로고
    • MacB ABC transporter is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA
    • Lin HT, Bavro VN, Barrera NP, Frankish HM, Velamakanni S, et al. 2009. MacB ABC transporter is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA. J. Biol. Chem. 284:1145-154.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1145-1154
    • Lin, H.T.1    Bavro, V.N.2    Barrera, N.P.3    Frankish, H.M.4    Velamakanni, S.5
  • 81
    • 70450162014 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a membrane protein-micelle complex in vacuo
    • Friemann R, Larsson DS, Wang Y, van der Spoel D. 2009. Molecular dynamics simulations of a membrane protein-micelle complex in vacuo. J. Am. Chem. Soc. 131:16606-7.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16606-7
    • Friemann, R.1    Larsson, D.S.2    Wang, Y.3    Van Der Spoel, D.4
  • 82
    • 57449113443 scopus 로고    scopus 로고
    • Stepwise evolution of protein native structure with electrospray into the gas phase, 10?12 to 102 s
    • Breuker K, McLafferty FW. 2008. Stepwise evolution of protein native structure with electrospray into the gas phase, 10?12 to 102 s. Proc. Natl. Acad. Sci. USA 105:18145-152.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 18145-18152
    • Breuker, K.1    McLafferty, F.W.2
  • 84
    • 71449084024 scopus 로고    scopus 로고
    • Biological chemistry: Dehydrated but unharmed
    • Benesch JL, Robinson CV. 2009. Biological chemistry: dehydrated but unharmed. Nature 462:576-577.
    • (2009) Nature , vol.462 , pp. 576-577
    • Benesch, J.L.1    Robinson, C.V.2
  • 85
    • 78649748259 scopus 로고    scopus 로고
    • Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing
    • Wang SC, Politis A, Di Bartolo N, Bavro VN, Tucker SJ, et al. 2010. Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing. J. Am. Chem. Soc. 132:15468-470.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15468-15470
    • Wang, S.C.1    Politis, A.2    Di Bartolo, N.3    Bavro, V.N.4    Tucker, S.J.5
  • 86
    • 53449098815 scopus 로고    scopus 로고
    • LILBID-mass spectrometry applied to the mass analysis of RNA polymerase II and an F1F0-ATP synthase
    • MorgnerN, Hoffmann J, Barth HD, Meier T, Brutschy B. 2008. LILBID-mass spectrometry applied to the mass analysis of RNA polymerase II and an F1F0-ATP synthase. Int. J. Mass Spectrom. 277:309-313.
    • (2008) Int. J. Mass Spectrom. , vol.277 , pp. 309-313
    • Morgner, N.1    Hoffmann, J.2    Barth, H.D.3    Meier, T.4    Brutschy, B.5
  • 88
    • 46349107838 scopus 로고    scopus 로고
    • Three-dimensional structure of respiratory complex i from Escherichia coli in ice in the presence of nucleotides
    • Morgan DJ, Sazanov LA. 2008. Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochim. Biophys. Acta 1777:711-718.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 711-718
    • Morgan, D.J.1    Sazanov, L.A.2
  • 89
    • 77950283310 scopus 로고    scopus 로고
    • Studying the stoichiometries of membrane proteins by mass spectrometry: Microbial rhodopsins and a potassium ion channel
    • Hoffmann J, Aslimovska L, Bamann C, Glaubitz C, Bamberg E, Brutschy B. 2010. Studying the stoichiometries of membrane proteins by mass spectrometry: microbial rhodopsins and a potassium ion channel. Phys. Chem. Chem. Phys. 12:3480-485.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 3480-3485
    • Hoffmann, J.1    Aslimovska, L.2    Bamann, C.3    Glaubitz, C.4    Bamberg, E.5    Brutschy, B.6
  • 90
    • 77954615206 scopus 로고    scopus 로고
    • Analytical ultracentrifugation sedimentation velocity for the characterization of detergent-solubilized membrane proteins Ca++-ATPase and ExbB
    • Salvay AG, Santamaria M, le Maire M, Ebel C. 2007. Analytical ultracentrifugation sedimentation velocity for the characterization of detergent-solubilized membrane proteins Ca++-ATPase and ExbB. J. Biol. Phys. 33:399-419.
    • (2007) J. Biol. Phys. , vol.33 , pp. 399-419
    • Salvay, A.G.1    Santamaria, M.2    Le Maire, M.3    Ebel, C.4
  • 91
    • 55249091365 scopus 로고    scopus 로고
    • Determination of membrane protein molecular weight using sedimentation equilibrium analytical ultracentrifugation
    • Chapter 7:Unit 7.12.1-7.12.13
    • Fleming KG. 2008. Determination of membrane protein molecular weight using sedimentation equilibrium analytical ultracentrifugation. Curr. Protoc. Protein Sci. Chapter 7:Unit 7.12.1-7.12.13.
    • (2008) Curr. Protoc. Protein Sci.
    • Fleming, K.G.1
  • 92
    • 76749116310 scopus 로고    scopus 로고
    • Multimeric forms of the small multidrug resistance protein EmrE in anionic detergent
    • Bay DC, Budiman RA, Nieh MP, Turner RJ. 2010. Multimeric forms of the small multidrug resistance protein EmrE in anionic detergent. Biochim. Biophys. Acta 1798:526-535.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 526-535
    • Bay, D.C.1    Budiman, R.A.2    Nieh, M.P.3    Turner, R.J.4
  • 94
    • 78049281844 scopus 로고    scopus 로고
    • Oligomeric forms of G protein-coupled receptors (GPCRs)
    • Palczewski K. 2010. Oligomeric forms of G protein-coupled receptors (GPCRs). Trends Biochem. Sci. 35:595-600.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 595-600
    • Palczewski, K.1
  • 96
    • 34548530597 scopus 로고    scopus 로고
    • Functional relevance of neurotransmitter receptor heteromers in the central nervous system
    • DOI 10.1016/j.tins.2007.07.001, PII S0166223607001762
    • Ferre S, Ciruela F, Woods AS, Lluis C, Franco R. 2007. Functional relevance of neurotransmitter receptor heteromers in the central nervous system. Trends Neurosci. 30:440-446. (Pubitemid 47381459)
    • (2007) Trends in Neurosciences , vol.30 , Issue.9 , pp. 440-446
    • Ferre, S.1    Ciruela, F.2    Woods, A.S.3    Lluis, C.4    Franco, R.5
  • 97
    • 77955981439 scopus 로고    scopus 로고
    • Nonmicellar systems for solutionNMR spectroscopy of membrane proteins
    • Raschle T, Hiller S, Etzkorn M, Wagner G. 2010. Nonmicellar systems for solutionNMR spectroscopy of membrane proteins. Curr. Opin. Struct. Biol. 20:471-479.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 471-479
    • Raschle, T.1    Hiller, S.2    Etzkorn, M.3    Wagner, G.4
  • 98
    • 38949113132 scopus 로고    scopus 로고
    • Providing Unique Insight into Cell Biology via Atomic Force Microscopy
    • DOI 10.1016/S0074-7696(07)65006-2, PII S0074769607650062, A Survey of Cell Biology
    • Shahin V, Barrera NP. 2008. Providing unique insight into cell biology via atomic force microscopy. Int. Rev. Cytol. 265:227-252. (Pubitemid 351215990)
    • (2008) International Review of Cytology , vol.265 , pp. 227-252
    • Shahin, V.1    Barrera, N.P.2
  • 99
    • 50649125304 scopus 로고    scopus 로고
    • Structure and mechanics of membrane proteins
    • Engel A, GaubHE. 2008. Structure and mechanics of membrane proteins. Annu. Rev Biochem. 77:127-148.
    • (2008) Annu. Rev Biochem. , vol.77 , pp. 127-148
    • Engel, A.1    Gaub, H.E.2
  • 100
    • 51349168500 scopus 로고    scopus 로고
    • What transmission electron microscopes can visualize now and in the future
    • M̈uller SA, Aebi U, Engel A. 2008. What transmission electron microscopes can visualize now and in the future. J. Struct. Biol. 163:235-245.
    • (2008) J. Struct. Biol. , vol.163 , pp. 235-245
    • M̈uller, S.A.1    Aebi, U.2    Engel, A.3
  • 101
    • 54249148893 scopus 로고    scopus 로고
    • The subunit arrangement and assembly of ionotropic receptors
    • Barrera NP, Edwardson JM. 2008. The subunit arrangement and assembly of ionotropic receptors. Trends Neurosci. 31:569-576.
    • (2008) Trends Neurosci. , vol.31 , pp. 569-576
    • Barrera, N.P.1    Edwardson, J.M.2
  • 102
    • 77957931285 scopus 로고    scopus 로고
    • Separating and visualising protein assemblies bymeans of preparativemass spectrometry and microscopy
    • Benesch JL, Ruotolo BT, Simmons DA, Barrera NP, Morgner N, et al. 2010. Separating and visualising protein assemblies bymeans of preparativemass spectrometry and microscopy. J. Struct. Biol. 172:161-168.
    • (2010) J. Struct. Biol. , vol.172 , pp. 161-168
    • Benesch, J.L.1    Ruotolo, B.T.2    Simmons, D.A.3    Barrera, N.P.4    Morgner, N.5
  • 103
    • 77957784477 scopus 로고    scopus 로고
    • Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes
    • Politis A, Park AY, Hyung SJ, Barsky D, Ruotolo BT, Robinson CV. 2010. Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes. PLoS ONE 5:e12080.
    • (2010) PLoS ONE , vol.5
    • Politis, A.1    Park, A.Y.2    Hyung, S.J.3    Barsky, D.4    Ruotolo, B.T.5    Robinson, C.V.6
  • 104
    • 79953702800 scopus 로고    scopus 로고
    • Production of membrane proteins without cells or detergents
    • In press
    • Rajesh S, Knowles T, OverduinM. 2011. Production of membrane proteins without cells or detergents. N. Biotechnol. In press.
    • (2011) N. Biotechnol.
    • Rajesh, S.1    Knowles, T.2    Overduin, M.3
  • 105
    • 77954193701 scopus 로고    scopus 로고
    • Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry
    • Hebling CM, Morgan CR, Stafford DW, Jorgenson JW, Rand KD, Engen JR. 2010. Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry. Anal. Chem. 82:5415-419.
    • (2010) Anal. Chem. , vol.82 , pp. 5415-5419
    • Hebling, C.M.1    Morgan, C.R.2    Stafford, D.W.3    Jorgenson, J.W.4    Rand, K.D.5    Engen, J.R.6
  • 107
    • 2142825695 scopus 로고    scopus 로고
    • Crystal structures of artificial metalloproteins: Tight binding of FeIII(Schiff-Base) by mutation of Ala71 to Gly in apo-myoglobin
    • Ueno T, Ohashi M, Kono M, Kondo K, Suzuki A, et al. 2004. Crystal structures of artificial metalloproteins: tight binding of FeIII(Schiff-Base) by mutation of Ala71 to Gly in apo-myoglobin. Inorg. Chem. 43:2852-858.
    • (2004) Inorg. Chem. , vol.43 , pp. 2852-2858
    • Ueno, T.1    Ohashi, M.2    Kono, M.3    Kondo, K.4    Suzuki, A.5
  • 108
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali A, Blundell TL. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815. (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 109
    • 67049159916 scopus 로고    scopus 로고
    • Crystal structure of the periplasmic region of MacB, a noncanonic ABC transporter
    • Xu Y, Sim SH, Nam KH, Jin XL, Kim HM, et al. 2009. Crystal structure of the periplasmic region of MacB, a noncanonic ABC transporter. Biochemistry 48:5218-225.
    • (2009) Biochemistry , vol.48 , pp. 5218-5225
    • Xu, Y.1    Sim, S.H.2    Nam, K.H.3    Jin, X.L.4    Kim, H.M.5
  • 110
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • DOI 10.1016/S1097-2765(02)00576-2
    • Smith PC, Karpowich N, Millen L, Moody JE, Rosen J, et al. 2002. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10:139-149. (Pubitemid 34876568)
    • (2002) Molecular Cell , vol.10 , Issue.1 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 111
    • 70350625080 scopus 로고    scopus 로고
    • Protein binding and the electronic properties of Iron(II) complexes: An electrochemical and optical investigation of outer sphere effects
    • Barker KD, Eckermann AL, Sazinsky MH, Hartings MR, Abajian C, et al. 2009. Protein binding and the electronic properties of Iron(II) complexes: an electrochemical and optical investigation of outer sphere effects. Bioconjug. Chem. 20:1930-939.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 1930-1939
    • Barker, K.D.1    Eckermann, A.L.2    Sazinsky, M.H.3    Hartings, M.R.4    Abajian, C.5
  • 112
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • DOI 10.1126/science.282.5397.2220
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC. 1998. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282:2220-226. (Pubitemid 29004063)
    • (1998) Science , vol.282 , Issue.5397 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 115
    • 70350309481 scopus 로고    scopus 로고
    • Use of thallium to identify monovalent cation binding sites in GroEL
    • Kiser PD, Lorimer GH, Palczewski K. 2009. Use of thallium to identify monovalent cation binding sites in GroEL. Acta Crystallogr. F 65:967-971.
    • (2009) Acta Crystallogr. , vol.F 65 , pp. 967-971
    • Kiser, P.D.1    Lorimer, G.H.2    Palczewski, K.3
  • 116
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • DOI 10.1126/science.1071142
    • Locher KP, Lee AT, Rees DC. 2002. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296:1091-098. (Pubitemid 34517120)
    • (2002) Science , vol.296 , Issue.5570 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 117
    • 4644290116 scopus 로고    scopus 로고
    • +-ATPase/synthase by electron microscopy
    • DOI 10.1016/j.str.2004.07.017, PII S0969212604002862
    • Bernal RA, Stock D. 2004. Three-dimensional structure of the intact Thermus thermophilus H+- ATPase/synthase by electron microscopy. Structure 12:1789-798. (Pubitemid 39298963)
    • (2004) Structure , vol.12 , Issue.10 , pp. 1789-1798
    • Bernal, R.A.1    Stock, D.2
  • 119
    • 33744490360 scopus 로고    scopus 로고
    • Positioning of proteins in membranes: A computational approach
    • DOI 10.1110/ps.062126106
    • Lomize AL, Pogozheva ID, Lomize MA, Mosberg HI. 2006. Positioning of proteins in membranes: a computational approach. Protein Sci. 15:1318-333. (Pubitemid 43800004)
    • (2006) Protein Science , vol.15 , Issue.6 , pp. 1318-1333
    • Lomize, A.L.1    Pogozheva, I.D.2    Lomize, M.A.3    Mosberg, H.I.4
  • 120
    • 77954948765 scopus 로고    scopus 로고
    • Three-dimensional structure of recombinant type 1 inositol 1, 4, 5-trisphosphate receptor
    • Wolfram F, Morris E, Taylor CW. 2010. Three-dimensional structure of recombinant type 1 inositol 1, 4, 5-trisphosphate receptor. Biochem. J. 428:483-489.
    • (2010) Biochem. J. , vol.428 , pp. 483-489
    • Wolfram, F.1    Morris, E.2    Taylor, C.W.3
  • 122
    • 33748310520 scopus 로고    scopus 로고
    • Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
    • DOI 10.1126/science.1131542
    • Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM. 2006. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313:1295-298. (Pubitemid 44330954)
    • (2006) Science , vol.313 , Issue.5791 , pp. 1295-1298
    • Seeger, M.A.1    Schiefner, A.2    Eicher, T.3    Verrey, F.4    Diederichs, K.5    Pos, K.M.6
  • 123
    • 50649121583 scopus 로고    scopus 로고
    • Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
    • Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G. 2008. Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science 321:1206-10
    • (2008) Science , vol.321 , pp. 1206-1210
    • Hiller, S.1    Garces, R.G.2    Malia, T.J.3    Orekhov, V.Y.4    Colombini, M.5    Wagner, G.6


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