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Volumn 52, Issue 22, 2013, Pages 3807-3817

Mass spectrometry of membrane proteins: A focus on aquaporins

Author keywords

[No Author keywords available]

Indexed keywords

IMAGING MASS SPECTROMETRY; INTEGRAL MEMBRANE PROTEINS; MEMBRANE-ASSOCIATED PROTEINS; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN STRUCTURES; PROTEIN-PROTEIN INTERACTIONS; SAMPLE PREPARATION; TISSUE DISTRIBUTIONS;

EID: 84878659212     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301604j     Document Type: Article
Times cited : (35)

References (104)
  • 1
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • Stevens, T. J. and Arkin, I. T. (2000) Do more complex organisms have a greater proportion of membrane proteins in their genomes? Proteins 39, 417-420
    • (2000) Proteins , vol.39 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 2
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu, C. C. and Yates, J. R., III (2003) The application of mass spectrometry to membrane proteomics Nat. Biotechnol. 21, 262-267
    • (2003) Nat. Biotechnol. , vol.21 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 3
    • 85028098813 scopus 로고    scopus 로고
    • Exosomes/microvesicles: Mediators of cancer-associated immunosuppressive microenvironments
    • Taylor, D. D. and Gercel-Taylor, C. (2011) Exosomes/microvesicles: Mediators of cancer-associated immunosuppressive microenvironments Semin. Immunopathol. 33, 441-454
    • (2011) Semin. Immunopathol. , vol.33 , pp. 441-454
    • Taylor, D.D.1    Gercel-Taylor, C.2
  • 4
    • 84855573739 scopus 로고    scopus 로고
    • The roles of tumor-derived exosomes in cancer pathogenesis
    • Yang, C. and Robbins, P. D. (2011) The roles of tumor-derived exosomes in cancer pathogenesis Clin. Dev. Immunol. 2011, 842849
    • (2011) Clin. Dev. Immunol. , vol.2011 , pp. 842849
    • Yang, C.1    Robbins, P.D.2
  • 5
    • 81055157988 scopus 로고    scopus 로고
    • Exosome secretion: Molecular mechanisms and roles in immune responses
    • Bobrie, A., Colombo, M., Raposo, G., and Thery, C. (2011) Exosome secretion: Molecular mechanisms and roles in immune responses Traffic 12, 1659-1668
    • (2011) Traffic , vol.12 , pp. 1659-1668
    • Bobrie, A.1    Colombo, M.2    Raposo, G.3    Thery, C.4
  • 7
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C., MacCoss, M. J., Howell, K. E., and Yates, J. R., III (2003) A method for the comprehensive proteomic analysis of membrane proteins Nat. Biotechnol. 21, 532-538
    • (2003) Nat. Biotechnol. , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 9
    • 77957232334 scopus 로고    scopus 로고
    • Advances in shotgun proteomics and the analysis of membrane proteomes
    • Gilmore, J. M. and Washburn, M. P. (2010) Advances in shotgun proteomics and the analysis of membrane proteomes J. Proteomics 73, 2078-2091
    • (2010) J. Proteomics , vol.73 , pp. 2078-2091
    • Gilmore, J.M.1    Washburn, M.P.2
  • 10
    • 77349098524 scopus 로고    scopus 로고
    • Exploring the membrane proteome: Challenges and analytical strategies
    • Helbig, A. O., Heck, A. J., and 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
  • 11
    • 17444377003 scopus 로고    scopus 로고
    • Characterization and quantitation of membrane proteomes using multidimensional MS-based proteomic technologies
    • Blonder, J., Conrads, T. P., and Veenstra, T. D. (2004) Characterization and quantitation of membrane proteomes using multidimensional MS-based proteomic technologies Expert Rev. Proteomics 1, 153-163
    • (2004) Expert Rev. Proteomics , vol.1 , pp. 153-163
    • Blonder, J.1    Conrads, T.P.2    Veenstra, T.D.3
  • 12
    • 0027166358 scopus 로고
    • Analysis of hydrophobic proteins and peptides by electrospray ionization mass spectrometry
    • Schindler, P. A., Van Dorsselaer, A., and Falick, A. M. (1993) Analysis of hydrophobic proteins and peptides by electrospray ionization mass spectrometry Anal. Biochem. 213, 256-263
    • (1993) Anal. Biochem. , vol.213 , pp. 256-263
    • Schindler, P.A.1    Van Dorsselaer, A.2    Falick, A.M.3
  • 13
    • 0026723294 scopus 로고
    • Matrix-assisted laser desorption mass spectrometry of rhodopsin and bacteriorhodopsin
    • Schey, K. L., Papac, D. I., Knapp, D. R., and Crouch, R. K. (1992) Matrix-assisted laser desorption mass spectrometry of rhodopsin and bacteriorhodopsin Biophys. J. 63, 1240-1243
    • (1992) Biophys. J. , vol.63 , pp. 1240-1243
    • Schey, K.L.1    Papac, D.I.2    Knapp, D.R.3    Crouch, R.K.4
  • 14
    • 0034669677 scopus 로고    scopus 로고
    • A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins
    • Cadene, M. and Chait, B. T. (2000) A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins Anal. Chem. 72, 5655-5658
    • (2000) Anal. Chem. , vol.72 , pp. 5655-5658
    • Cadene, M.1    Chait, B.T.2
  • 15
    • 0942276251 scopus 로고    scopus 로고
    • A detergent- and cyanogen bromide-free method for integral membrane proteomics: Application to Halobacterium purple membranes and the human epidermal membrane proteome
    • Blonder, J., Conrads, T. P., Yu, L. R., Terunuma, A., Janini, G. M., Issaq, H. J., Vogel, J. C., and Veenstra, T. D. (2004) A detergent- and cyanogen bromide-free method for integral membrane proteomics: Application to Halobacterium purple membranes and the human epidermal membrane proteome Proteomics 4, 31-45
    • (2004) Proteomics , vol.4 , pp. 31-45
    • Blonder, J.1    Conrads, T.P.2    Yu, L.R.3    Terunuma, A.4    Janini, G.M.5    Issaq, H.J.6    Vogel, J.C.7    Veenstra, T.D.8
  • 16
    • 53549100778 scopus 로고    scopus 로고
    • Nonionic detergent phase extraction for the proteomic analysis of heart membrane proteins using label-free LC-MS
    • Donoghue, P. M., Hughes, C., Vissers, J. P., Langridge, J. I., and Dunn, M. J. (2008) Nonionic detergent phase extraction for the proteomic analysis of heart membrane proteins using label-free LC-MS Proteomics 8, 3895-3905
    • (2008) Proteomics , vol.8 , pp. 3895-3905
    • Donoghue, P.M.1    Hughes, C.2    Vissers, J.P.3    Langridge, J.I.4    Dunn, M.J.5
  • 17
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han, D. K., Eng, J., Zhou, H., and Aebersold, R. (2001) Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry Nat. Biotechnol. 19, 946-951
    • (2001) Nat. Biotechnol. , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 18
    • 0031776931 scopus 로고    scopus 로고
    • Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins
    • Whitelegge, J. P., Gundersen, C. B., and Faull, K. F. (1998) Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins Protein Sci. 7, 1423-1430
    • (1998) Protein Sci. , vol.7 , pp. 1423-1430
    • Whitelegge, J.P.1    Gundersen, C.B.2    Faull, K.F.3
  • 19
    • 84856005633 scopus 로고    scopus 로고
    • Profiling of integral membrane proteins and their post translational modifications using high-resolution mass spectrometry
    • Souda, P., Ryan, C. M., Cramer, W. A., and Whitelegge, J. (2011) Profiling of integral membrane proteins and their post translational modifications using high-resolution mass spectrometry Methods 55, 330-336
    • (2011) Methods , vol.55 , pp. 330-336
    • Souda, P.1    Ryan, C.M.2    Cramer, W.A.3    Whitelegge, J.4
  • 20
    • 4444320836 scopus 로고    scopus 로고
    • Proteolysis and mass spectrometric analysis of an integral membrane: Aquaporin 0
    • Han, J. and Schey, K. L. (2004) Proteolysis and mass spectrometric analysis of an integral membrane: Aquaporin 0 J. Proteome Res. 3, 807-812
    • (2004) J. Proteome Res. , vol.3 , pp. 807-812
    • Han, J.1    Schey, K.L.2
  • 22
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., and Yates, J. R., III (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat. Biotechnol. 19, 242-247
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 24
    • 84855549488 scopus 로고    scopus 로고
    • System-wide perturbation analysis with nearly complete coverage of the yeast proteome by single-shot ultra HPLC runs on a bench top Orbitrap
    • Nagaraj, N., Kulak, N. A., Cox, J., Neuhauser, N., Mayr, K., Hoerning, O., Vorm, O., and Mann, M. (2012) System-wide perturbation analysis with nearly complete coverage of the yeast proteome by single-shot ultra HPLC runs on a bench top Orbitrap Mol. Cell. Proteomics 11, M111.013722
    • (2012) Mol. Cell. Proteomics , vol.11
    • Nagaraj, N.1    Kulak, N.A.2    Cox, J.3    Neuhauser, N.4    Mayr, K.5    Hoerning, O.6    Vorm, O.7    Mann, M.8
  • 25
    • 55749085987 scopus 로고    scopus 로고
    • Proteomics of mitochondrial inner and outer membranes
    • Distler, A. M., Kerner, J., and Hoppel, C. L. (2008) Proteomics of mitochondrial inner and outer membranes Proteomics 8, 4066-4082
    • (2008) Proteomics , vol.8 , pp. 4066-4082
    • Distler, A.M.1    Kerner, J.2    Hoppel, C.L.3
  • 26
    • 55749096878 scopus 로고    scopus 로고
    • Sub-cellular localization of membrane proteins
    • Sadowski, P. G., Groen, A. J., Dupree, P., and Lilley, K. S. (2008) Sub-cellular localization of membrane proteins Proteomics 8, 3991-4011
    • (2008) Proteomics , vol.8 , pp. 3991-4011
    • Sadowski, P.G.1    Groen, A.J.2    Dupree, P.3    Lilley, K.S.4
  • 27
    • 25144491496 scopus 로고    scopus 로고
    • The nuclear membrane proteome: Extending the envelope
    • Schirmer, E. C. and Gerace, L. (2005) The nuclear membrane proteome: Extending the envelope Trends Biochem. Sci. 30, 551-558
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 551-558
    • Schirmer, E.C.1    Gerace, L.2
  • 28
    • 38449106913 scopus 로고    scopus 로고
    • Lipid raft proteomics: More than just detergent-resistant membranes
    • Foster, L. J. and Chan, Q. W. (2007) Lipid raft proteomics: More than just detergent-resistant membranes Subcell. Biochem. 43, 35-47
    • (2007) Subcell. Biochem. , vol.43 , pp. 35-47
    • Foster, L.J.1    Chan, Q.W.2
  • 29
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J. E., Coon, J. J., Schroeder, M. J., Shabanowitz, J., and Hunt, D. F. (2004) Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry Proc. Natl. Acad. Sci. U.S.A. 101, 9528-9533
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 30
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications
    • Wiesner, J., Premsler, T., and Sickmann, A. (2008) Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications Proteomics 8, 4466-4483
    • (2008) Proteomics , vol.8 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 31
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni
    • M000031.MCP000201
    • Scott, N. E., Parker, B. L., Connolly, A. M., Paulech, J., Edwards, A. V., Crossett, B., Falconer, L., Kolarich, D., Djordjevic, S. P., Hojrup, P., Packer, N. H., Larsen, M. R., and Cordwell, S. J. (2011) Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni Mol. Cell. Proteomics 10, M000031.MCP000201
    • (2011) Mol. Cell. Proteomics , vol.10
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4    Edwards, A.V.5    Crossett, B.6    Falconer, L.7    Kolarich, D.8    Djordjevic, S.P.9    Hojrup, P.10    Packer, N.H.11    Larsen, M.R.12    Cordwell, S.J.13
  • 34
    • 0036051481 scopus 로고    scopus 로고
    • The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry
    • Gomez, S. M., Nishio, J. N., Faull, K. F., and Whitelegge, J. P. (2002) The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry Mol. Cell. Proteomics 1, 46-59
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 46-59
    • Gomez, S.M.1    Nishio, J.N.2    Faull, K.F.3    Whitelegge, J.P.4
  • 36
    • 84862833364 scopus 로고    scopus 로고
    • Structural mass spectrometry of proteins using hydroxyl radical based protein footprinting
    • Wang, L. and Chance, M. R. (2011) Structural mass spectrometry of proteins using hydroxyl radical based protein footprinting Anal. Chem. 83, 7234-7241
    • (2011) Anal. Chem. , vol.83 , pp. 7234-7241
    • Wang, L.1    Chance, M.R.2
  • 37
    • 77952800825 scopus 로고    scopus 로고
    • Membrane protein structural insights from chemical labeling and mass spectrometry
    • Pan, Y. and Konermann, L. (2010) Membrane protein structural insights from chemical labeling and mass spectrometry Analyst 135, 1191-1200
    • (2010) Analyst , vol.135 , pp. 1191-1200
    • Pan, Y.1    Konermann, L.2
  • 38
    • 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., and 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
  • 39
    • 68849107091 scopus 로고    scopus 로고
    • Fast photochemical oxidation of protein footprints faster than protein unfolding
    • Gau, B. C., Sharp, J. S., Rempel, D. L., and Gross, M. L. (2009) Fast photochemical oxidation of protein footprints faster than protein unfolding Anal. Chem. 81, 6563-6571
    • (2009) Anal. Chem. , vol.81 , pp. 6563-6571
    • Gau, B.C.1    Sharp, J.S.2    Rempel, D.L.3    Gross, M.L.4
  • 40
    • 84869451240 scopus 로고    scopus 로고
    • Fast Photochemical Oxidation of Proteins and Mass Spectrometry Follow Submillisecond Protein Folding at the Amino-Acid Level
    • Chen, J., Rempel, D. L., Gau, B. C., and Gross, M. L. (2012) Fast Photochemical Oxidation of Proteins and Mass Spectrometry Follow Submillisecond Protein Folding at the Amino-Acid Level J. Am. Chem. Soc. 134, 18724-18731
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 18724-18731
    • Chen, J.1    Rempel, D.L.2    Gau, B.C.3    Gross, M.L.4
  • 41
    • 4444316044 scopus 로고    scopus 로고
    • Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1
    • Busenlehner, L. S., Codreanu, S. G., Holm, P. J., Bhakat, P., Hebert, H., Morgenstern, R., and Armstrong, R. N. (2004) Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1 Biochemistry 43, 11145-11152
    • (2004) Biochemistry , vol.43 , pp. 11145-11152
    • Busenlehner, L.S.1    Codreanu, S.G.2    Holm, P.J.3    Bhakat, P.4    Hebert, H.5    Morgenstern, R.6    Armstrong, R.N.7
  • 42
    • 38049091274 scopus 로고    scopus 로고
    • Structural elements involved in proton translocation by cytochrome c oxidase as revealed by backbone amide hydrogen-deuterium exchange of the E286H mutant
    • Busenlehner, L. S., Branden, G., Namslauer, I., Brzezinski, P., and Armstrong, R. N. (2008) Structural elements involved in proton translocation by cytochrome c oxidase as revealed by backbone amide hydrogen-deuterium exchange of the E286H mutant Biochemistry 47, 73-83
    • (2008) Biochemistry , vol.47 , pp. 73-83
    • Busenlehner, L.S.1    Branden, G.2    Namslauer, I.3    Brzezinski, P.4    Armstrong, R.N.5
  • 43
    • 83755169019 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry of bacteriorhodopsin reveals light-induced changes in the structural dynamics of a biomolecular machine
    • Pan, Y., Brown, L., and Konermann, L. (2011) Hydrogen exchange mass spectrometry of bacteriorhodopsin reveals light-induced changes in the structural dynamics of a biomolecular machine J. Am. Chem. Soc. 133, 20237-20244
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 20237-20244
    • Pan, Y.1    Brown, L.2    Konermann, L.3
  • 44
    • 46249089993 scopus 로고    scopus 로고
    • Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins
    • Joh, N. H., Min, A., Faham, S., Whitelegge, J. P., Yang, D., Woods, V. L., and Bowie, J. U. (2008) Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins Nature 453, 1266-1270
    • (2008) Nature , vol.453 , pp. 1266-1270
    • Joh, N.H.1    Min, A.2    Faham, S.3    Whitelegge, J.P.4    Yang, D.5    Woods, V.L.6    Bowie, J.U.7
  • 45
    • 84861079526 scopus 로고    scopus 로고
    • Conformational dynamics of activation for the pentameric complex of dimeric G protein-coupled receptor and heterotrimeric G protein
    • Orban, T., Jastrzebska, B., Gupta, S., Wang, B., Miyagi, M., Chance, M. R., and Palczewski, K. (2012) Conformational dynamics of activation for the pentameric complex of dimeric G protein-coupled receptor and heterotrimeric G protein Structure 20, 826-840
    • (2012) Structure , vol.20 , pp. 826-840
    • Orban, T.1    Jastrzebska, B.2    Gupta, S.3    Wang, B.4    Miyagi, M.5    Chance, M.R.6    Palczewski, K.7
  • 46
    • 77954193701 scopus 로고    scopus 로고
    • Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry
    • Hebling, C. M., Morgan, C. R., Stafford, D. W., Jorgenson, J. W., Rand, K. D., and Engen, J. R. (2010) Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry Anal. Chem. 82, 5415-5419
    • (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
  • 47
    • 4644327652 scopus 로고    scopus 로고
    • Native protein mass spectrometry: From intact oligomers to functional machineries
    • van den Heuvel, R. H. and Heck, A. J. (2004) Native protein mass spectrometry: From intact oligomers to functional machineries Curr. Opin. Chem. Biol. 8, 519-526
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 519-526
    • Van Den Heuvel, R.H.1    Heck, A.J.2
  • 48
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon, M. and Robinson, C. V. (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
  • 49
    • 79959456892 scopus 로고    scopus 로고
    • Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes
    • Barrera, N. P. and Robinson, C. V. (2011) Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes Annu. Rev. Biochem. 80, 247-271
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 247-271
    • Barrera, N.P.1    Robinson, C.V.2
  • 50
    • 47249106965 scopus 로고    scopus 로고
    • Micelles protect membrane complexes from solution to vacuum
    • Barrera, N. P., Di Bartolo, N., Booth, P. J., and Robinson, C. V. (2008) Micelles protect membrane complexes from solution to vacuum Science 321, 243-246
    • (2008) Science , vol.321 , pp. 243-246
    • Barrera, N.P.1    Di Bartolo, N.2    Booth, P.J.3    Robinson, C.V.4
  • 51
    • 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., and 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, 1429-1438
    • (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
  • 52
    • 65649105054 scopus 로고    scopus 로고
    • Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy
    • Vonck, J., Pisa, K. Y., Morgner, N., Brutschy, B., and Muller, V. (2009) Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy J. Biol. Chem. 284, 10110-10119
    • (2009) J. Biol. Chem. , vol.284 , pp. 10110-10119
    • Vonck, J.1    Pisa, K.Y.2    Morgner, N.3    Brutschy, B.4    Muller, V.5
  • 53
    • 4043141477 scopus 로고    scopus 로고
    • Quantitative cancer proteomics: Stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research
    • Everley, P. A., Krijgsveld, J., Zetter, B. R., and Gygi, S. P. (2004) Quantitative cancer proteomics: Stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research Mol. Cell. Proteomics 3, 729-735
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 729-735
    • Everley, P.A.1    Krijgsveld, J.2    Zetter, B.R.3    Gygi, S.P.4
  • 57
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., and Gygi, S. P. (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS Proc. Natl. Acad. Sci. U.S.A. 100, 6940-6945
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 58
    • 84862534271 scopus 로고    scopus 로고
    • Sample prefractionation for mass spectrometry quantification of low-abundance membrane proteins
    • Wang, M., Heo, G. Y., Omarova, S., Pikuleva, I. A., and Turko, I. V. (2012) Sample prefractionation for mass spectrometry quantification of low-abundance membrane proteins Anal. Chem. 84, 5186-5191
    • (2012) Anal. Chem. , vol.84 , pp. 5186-5191
    • Wang, M.1    Heo, G.Y.2    Omarova, S.3    Pikuleva, I.A.4    Turko, I.V.5
  • 59
    • 65249113798 scopus 로고    scopus 로고
    • Stable isotope dilution multidimensional liquid chromatography-tandem mass spectrometry for pancreatic cancer serum biomarker discovery
    • Yu, K. H., Barry, C. G., Austin, D., Busch, C. M., Sangar, V., Rustgi, A. K., and Blair, I. A. (2009) Stable isotope dilution multidimensional liquid chromatography-tandem mass spectrometry for pancreatic cancer serum biomarker discovery J. Proteome Res. 8, 1565-1576
    • (2009) J. Proteome Res. , vol.8 , pp. 1565-1576
    • Yu, K.H.1    Barry, C.G.2    Austin, D.3    Busch, C.M.4    Sangar, V.5    Rustgi, A.K.6    Blair, I.A.7
  • 60
    • 77954193702 scopus 로고    scopus 로고
    • Optimizing the conditions of a multiple reaction monitoring assay for membrane proteins: Quantification of cytochrome P450 11A1 and adrenodoxin reductase in bovine adrenal cortex and retina
    • Liao, W. L., Heo, G. Y., Dodder, N. G., Pikuleva, I. A., and Turko, I. V. (2010) Optimizing the conditions of a multiple reaction monitoring assay for membrane proteins: Quantification of cytochrome P450 11A1 and adrenodoxin reductase in bovine adrenal cortex and retina Anal. Chem. 82, 5760-5767
    • (2010) Anal. Chem. , vol.82 , pp. 5760-5767
    • Liao, W.L.1    Heo, G.Y.2    Dodder, N.G.3    Pikuleva, I.A.4    Turko, I.V.5
  • 62
    • 84934439747 scopus 로고    scopus 로고
    • Quantitative proteomic analysis to profile dynamic changes in the spatial distribution of cellular proteins
    • Yan, W., Hwang, D., and Aebersold, R. (2008) Quantitative proteomic analysis to profile dynamic changes in the spatial distribution of cellular proteins Methods Mol. Biol. 432, 389-401
    • (2008) Methods Mol. Biol. , vol.432 , pp. 389-401
    • Yan, W.1    Hwang, D.2    Aebersold, R.3
  • 63
    • 62449191490 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of pancreatic zymogen granule membrane proteins
    • Chen, X. and Andrews, P. C. (2009) Quantitative proteomics analysis of pancreatic zymogen granule membrane proteins Methods Mol. Biol. 528, 327-338
    • (2009) Methods Mol. Biol. , vol.528 , pp. 327-338
    • Chen, X.1    Andrews, P.C.2
  • 66
    • 0031304362 scopus 로고    scopus 로고
    • Molecular imaging of biological samples: Localization of peptides and proteins using MALDI-TOF MS
    • Caprioli, R. M., Farmer, T. B., and Gile, J. (1997) Molecular imaging of biological samples: Localization of peptides and proteins using MALDI-TOF MS Anal. Chem. 69, 4751-4760
    • (1997) Anal. Chem. , vol.69 , pp. 4751-4760
    • Caprioli, R.M.1    Farmer, T.B.2    Gile, J.3
  • 68
    • 67650360403 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry of integral membrane proteins from ocular lens and retinal tissue
    • Grey, A. C., Chaurand, P., Caprioli, R. M., and Schey, K. L. (2009) MALDI imaging mass spectrometry of integral membrane proteins from ocular lens and retinal tissue J. Proteome Res. 8, 3278-3283
    • (2009) J. Proteome Res. , vol.8 , pp. 3278-3283
    • Grey, A.C.1    Chaurand, P.2    Caprioli, R.M.3    Schey, K.L.4
  • 69
    • 78149421964 scopus 로고    scopus 로고
    • Novel fatty acid acylation of lens integral membrane protein aquaporin-0
    • Schey, K. L., Gutierrez, D. B., Wang, Z., Wei, J., and Grey, A. C. (2010) Novel fatty acid acylation of lens integral membrane protein aquaporin-0 Biochemistry 49, 9858-9865
    • (2010) Biochemistry , vol.49 , pp. 9858-9865
    • Schey, K.L.1    Gutierrez, D.B.2    Wang, Z.3    Wei, J.4    Grey, A.C.5
  • 70
    • 84855968394 scopus 로고    scopus 로고
    • Spatial analysis of human lens aquaporin-0 post-translational modifications by MALDI mass spectrometry tissue profiling
    • Gutierrez, D. B., Garland, D., and Schey, K. L. (2011) Spatial analysis of human lens aquaporin-0 post-translational modifications by MALDI mass spectrometry tissue profiling Exp. Eye Res. 93, 912-920
    • (2011) Exp. Eye Res. , vol.93 , pp. 912-920
    • Gutierrez, D.B.1    Garland, D.2    Schey, K.L.3
  • 71
    • 64849113023 scopus 로고    scopus 로고
    • Protein aging: Truncation of aquaporin 0 in human lens regions is a continuous age-dependent process
    • Korlimbinis, A., Berry, Y., Thibault, D., Schey, K. L., and Truscott, R. J. (2009) Protein aging: Truncation of aquaporin 0 in human lens regions is a continuous age-dependent process Exp. Eye Res. 88, 966-973
    • (2009) Exp. Eye Res. , vol.88 , pp. 966-973
    • Korlimbinis, A.1    Berry, Y.2    Thibault, D.3    Schey, K.L.4    Truscott, R.J.5
  • 72
    • 77956622324 scopus 로고    scopus 로고
    • Aquaporins: A family of highly regulated multifunctional channels
    • Hachez, C. and Chaumont, F. (2010) Aquaporins: A family of highly regulated multifunctional channels Adv. Exp. Med. Biol. 679, 1-17
    • (2010) Adv. Exp. Med. Biol. , vol.679 , pp. 1-17
    • Hachez, C.1    Chaumont, F.2
  • 73
    • 4544353285 scopus 로고    scopus 로고
    • Aquaporin water channels (Nobel Lecture)
    • Agre, P. (2004) Aquaporin water channels (Nobel Lecture) Angew. Chem., Int. Ed. 43, 4278-4290
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 4278-4290
    • Agre, P.1
  • 74
    • 84855932788 scopus 로고    scopus 로고
    • Aquaporins in clinical medicine
    • Verkman, A. S. (2012) Aquaporins in clinical medicine Annu. Rev. Med. 63, 303-316
    • (2012) Annu. Rev. Med. , vol.63 , pp. 303-316
    • Verkman, A.S.1
  • 78
    • 37849015874 scopus 로고    scopus 로고
    • Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation
    • Rose, K. M., Wang, Z., Magrath, G. N., Hazard, E. S., Hildebrandt, J. D., and Schey, K. L. (2008) Aquaporin 0-calmodulin interaction and the effect of aquaporin 0 phosphorylation Biochemistry 47, 339-347
    • (2008) Biochemistry , vol.47 , pp. 339-347
    • Rose, K.M.1    Wang, Z.2    Magrath, G.N.3    Hazard, E.S.4    Hildebrandt, J.D.5    Schey, K.L.6
  • 80
    • 50849097568 scopus 로고    scopus 로고
    • Noncanonical binding of calmodulin to aquaporin-0: Implications for channel regulation
    • Reichow, S. L. and Gonen, T. (2008) Noncanonical binding of calmodulin to aquaporin-0: Implications for channel regulation Structure 16, 1389-1398
    • (2008) Structure , vol.16 , pp. 1389-1398
    • Reichow, S.L.1    Gonen, T.2
  • 82
  • 84
    • 3342946768 scopus 로고    scopus 로고
    • Post-translational modifications of aquaporin 0 (AQP0) in the normal human lens: Spatial and temporal occurrence
    • Ball, L. E., Garland, D. L., Crouch, R. K., and Schey, K. L. (2004) Post-translational modifications of aquaporin 0 (AQP0) in the normal human lens: Spatial and temporal occurrence Biochemistry 43, 9856-9865
    • (2004) Biochemistry , vol.43 , pp. 9856-9865
    • Ball, L.E.1    Garland, D.L.2    Crouch, R.K.3    Schey, K.L.4
  • 85
    • 51649091442 scopus 로고    scopus 로고
    • Spatial differences in an integral membrane proteome detected in laser capture microdissected samples
    • Wang, Z., Han, J., and Schey, K. L. (2008) Spatial differences in an integral membrane proteome detected in laser capture microdissected samples J. Proteome Res. 7, 2696-2702
    • (2008) J. Proteome Res. , vol.7 , pp. 2696-2702
    • Wang, Z.1    Han, J.2    Schey, K.L.3
  • 86
    • 33646485094 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites
    • Hoffert, J. D., Pisitkun, T., Wang, G., Shen, R. F., and Knepper, M. A. (2006) Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites Proc. Natl. Acad. Sci. U.S.A. 103, 7159-7164
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7159-7164
    • Hoffert, J.D.1    Pisitkun, T.2    Wang, G.3    Shen, R.F.4    Knepper, M.A.5
  • 87
    • 84874976592 scopus 로고    scopus 로고
    • Proteomics and phosphoproteomics analysis of human lens fiber cell membranes
    • Wang, Z. and Schey, K. L. (2013) Proteomics and phosphoproteomics analysis of human lens fiber cell membranes Invest. Ophthalmol. Visual Sci. 54, 1135-1143
    • (2013) Invest. Ophthalmol. Visual Sci. , vol.54 , pp. 1135-1143
    • Wang, Z.1    Schey, K.L.2
  • 88
    • 0030825096 scopus 로고    scopus 로고
    • Reverse-phase HPLC of the hydrophobic pulmonary surfactant proteins: Detection of a surfactant protein C isoform containing Nε-palmitoyl-lysine
    • Gustafsson, M., Curstedt, T., Jornvall, H., and Johansson, J. (1997) Reverse-phase HPLC of the hydrophobic pulmonary surfactant proteins: Detection of a surfactant protein C isoform containing Nε-palmitoyl-lysine Biochem. J. 326 (Part 3) 799-806
    • (1997) Biochem. J. , vol.326 , Issue.PART 3 , pp. 799-806
    • Gustafsson, M.1    Curstedt, T.2    Jornvall, H.3    Johansson, J.4
  • 89
    • 40949164734 scopus 로고    scopus 로고
    • Formation of aquaporin-4 arrays is inhibited by palmitoylation of N-terminal cysteine residues
    • Suzuki, H., Nishikawa, K., Hiroaki, Y., and Fujiyoshi, Y. (2008) Formation of aquaporin-4 arrays is inhibited by palmitoylation of N-terminal cysteine residues Biochim. Biophys. Acta 1778, 1181-1189
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1181-1189
    • Suzuki, H.1    Nishikawa, K.2    Hiroaki, Y.3    Fujiyoshi, Y.4
  • 90
    • 33644503593 scopus 로고    scopus 로고
    • Isolation and characterization of lipid microdomains from apical and basolateral plasma membranes of rat hepatocytes
    • Mazzone, A., Tietz, P., Jefferson, J., Pagano, R., and LaRusso, N. F. (2006) Isolation and characterization of lipid microdomains from apical and basolateral plasma membranes of rat hepatocytes Hepatology 43, 287-296
    • (2006) Hepatology , vol.43 , pp. 287-296
    • Mazzone, A.1    Tietz, P.2    Jefferson, J.3    Pagano, R.4    Larusso, N.F.5
  • 91
    • 26844545317 scopus 로고    scopus 로고
    • Identification of AQP5 in lipid rafts and its translocation to apical membranes by activation of M3 mAChRs in interlobular ducts of rat parotid gland
    • Ishikawa, Y., Yuan, Z., Inoue, N., Skowronski, M. T., Nakae, Y., Shono, M., Cho, G., Yasui, M., Agre, P., and Nielsen, S. (2005) Identification of AQP5 in lipid rafts and its translocation to apical membranes by activation of M3 mAChRs in interlobular ducts of rat parotid gland Am. J. Physiol. 289, C1303-C1311
    • (2005) Am. J. Physiol. , vol.289
    • Ishikawa, Y.1    Yuan, Z.2    Inoue, N.3    Skowronski, M.T.4    Nakae, Y.5    Shono, M.6    Cho, G.7    Yasui, M.8    Agre, P.9    Nielsen, S.10
  • 92
    • 1642494672 scopus 로고    scopus 로고
    • Glycosylation is important for cell surface expression of the water channel aquaporin-2 but is not essential for tetramerization in the endoplasmic reticulum
    • Hendriks, G., Koudijs, M., van Balkom, B. W., Oorschot, V., Klumperman, J., Deen, P. M., and van der Sluijs, P. (2004) Glycosylation is important for cell surface expression of the water channel aquaporin-2 but is not essential for tetramerization in the endoplasmic reticulum J. Biol. Chem. 279, 2975-2983
    • (2004) J. Biol. Chem. , vol.279 , pp. 2975-2983
    • Hendriks, G.1    Koudijs, M.2    Van Balkom, B.W.3    Oorschot, V.4    Klumperman, J.5    Deen, P.M.6    Van Der Sluijs, P.7
  • 94
    • 4444382267 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions form upon proteolytic cleavage
    • Gonen, T., Cheng, Y., Kistler, J., and Walz, T. (2004) Aquaporin-0 membrane junctions form upon proteolytic cleavage J. Mol. Biol. 342, 1337-1345
    • (2004) J. Mol. Biol. , vol.342 , pp. 1337-1345
    • Gonen, T.1    Cheng, Y.2    Kistler, J.3    Walz, T.4
  • 95
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • Gonen, T., Sliz, P., Kistler, J., Cheng, Y., and Walz, T. (2004) Aquaporin-0 membrane junctions reveal the structure of a closed water pore Nature 429, 193-197
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 97
    • 17044377499 scopus 로고    scopus 로고
    • Identification of a multiprotein "motor" complex binding to water channel aquaporin-2
    • Noda, Y., Horikawa, S., Katayama, Y., and Sasaki, S. (2005) Identification of a multiprotein "motor" complex binding to water channel aquaporin-2 Biochem. Biophys. Res. Commun. 330, 1041-1047
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 1041-1047
    • Noda, Y.1    Horikawa, S.2    Katayama, Y.3    Sasaki, S.4
  • 98
    • 65249083361 scopus 로고    scopus 로고
    • Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry
    • Zwang, N. A., Hoffert, J. D., Pisitkun, T., Moeller, H. B., Fenton, R. A., and Knepper, M. A. (2009) Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry J. Proteome Res. 8, 1540-1554
    • (2009) J. Proteome Res. , vol.8 , pp. 1540-1554
    • Zwang, N.A.1    Hoffert, J.D.2    Pisitkun, T.3    Moeller, H.B.4    Fenton, R.A.5    Knepper, M.A.6
  • 99
    • 49549119977 scopus 로고    scopus 로고
    • Altered distribution of aquaporin 5 and its C-terminal binding protein in the lacrimal glands of a mouse model for Sjogren's syndrome
    • Ohashi, Y., Tsuzaka, K., Takeuchi, T., Sasaki, Y., and Tsubota, K. (2008) Altered distribution of aquaporin 5 and its C-terminal binding protein in the lacrimal glands of a mouse model for Sjogren's syndrome Curr. Eye Res. 33, 621-629
    • (2008) Curr. Eye Res. , vol.33 , pp. 621-629
    • Ohashi, Y.1    Tsuzaka, K.2    Takeuchi, T.3    Sasaki, Y.4    Tsubota, K.5
  • 101
    • 80052521522 scopus 로고    scopus 로고
    • Aquaporin-0 interacts with the FERM domain of ezrin/radixin/moesin proteins in the ocular lens
    • Wang, Z. and Schey, K. L. (2011) Aquaporin-0 interacts with the FERM domain of ezrin/radixin/moesin proteins in the ocular lens Invest. Ophthalmol. Visual Sci. 52, 5079-5087
    • (2011) Invest. Ophthalmol. Visual Sci. , vol.52 , pp. 5079-5087
    • Wang, Z.1    Schey, K.L.2
  • 104
    • 84856731634 scopus 로고    scopus 로고
    • Conformational dynamics of a membrane transport protein probed by H/D exchange and covalent labeling: The glycerol facilitator
    • Pan, Y., Piyadasa, H., O'Neil, J. D., and Konermann, L. (2012) Conformational dynamics of a membrane transport protein probed by H/D exchange and covalent labeling: The glycerol facilitator J. Mol. Biol. 416, 400-413
    • (2012) J. Mol. Biol. , vol.416 , pp. 400-413
    • Pan, Y.1    Piyadasa, H.2    O'Neil, J.D.3    Konermann, L.4


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