메뉴 건너뛰기




Volumn 7, Issue 4, 2008, Pages 1572-1583

The identification and characterization of membranome components

Author keywords

Con a; In gel digestion; LC MS MS; Lectin affinity; Membrane proteins; WGA

Indexed keywords

LECTIN; MEMBRANE PROTEIN; CONCANAVALIN A; GLYCOPROTEIN; WHEAT GERM AGGLUTININ;

EID: 45549091555     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr070509u     Document Type: Article
Times cited : (31)

References (60)
  • 1
    • 4944243849 scopus 로고    scopus 로고
    • Integrating mass spectrometry into membrane protein drug discovery
    • Weinglass, A. B.; Whitelegge, J.; Kaback, H. R. Integrating mass spectrometry into membrane protein drug discovery. Curr. Opin. Drug Discovery Dev. 2004, 7 (5), 589-599.
    • (2004) Curr. Opin. Drug Discovery Dev , vol.7 , Issue.5 , pp. 589-599
    • Weinglass, A.B.1    Whitelegge, J.2    Kaback, H.R.3
  • 2
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu, C. C; Yates, J. R. The application of mass spectrometry to membrane proteomics. Nat. Biotechnol. 2003, 21 (3), 262-267.
    • (2003) Nat. Biotechnol , vol.21 , Issue.3 , pp. 262-267
    • Wu, C.C.1    Yates, J.R.2
  • 3
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics, un amour impossible
    • Santoni, V.; Molloy, M.; Rabilloud, T. Membrane proteins and proteomics, un amour impossible. Electrophoresis 2000, 21 (6), 1054-1070.
    • (2000) Electrophoresis , vol.21 , Issue.6 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 4
    • 0020039866 scopus 로고    scopus 로고
    • Fujiki, Y; H, A.; Fowler, S.; Lazarow, P. B. Isolation of intracellular membranes by means of sodium carbonate treatment, application to endoplasmic reticulum. J. Cell Biol. 1982, 93 (1), 97-102.
    • Fujiki, Y; H, A.; Fowler, S.; Lazarow, P. B. Isolation of intracellular membranes by means of sodium carbonate treatment, application to endoplasmic reticulum. J. Cell Biol. 1982, 93 (1), 97-102.
  • 5
    • 0035135419 scopus 로고    scopus 로고
    • Ford, M. G.; Pearse, B.; Higgins, M. K.; Vallis, Y.; Owen, D. J.; Gibson, A.; Hopkins, C. R.; Evans, P. R.; McMahon, H. T. Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes. Science 2001, 291 (5506), 1051-1055.
    • Ford, M. G.; Pearse, B.; Higgins, M. K.; Vallis, Y.; Owen, D. J.; Gibson, A.; Hopkins, C. R.; Evans, P. R.; McMahon, H. T. Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes. Science 2001, 291 (5506), 1051-1055.
  • 7
    • 0017800488 scopus 로고
    • Specific release of plasma membrane enzymes by a phosphatidylinositol-specific phospholipase C
    • Low, M. G.; Finean, J. B. Specific release of plasma membrane enzymes by a phosphatidylinositol-specific phospholipase C. Biochim. Biophys. Acta 1978, 508 (3), 565-570.
    • (1978) Biochim. Biophys. Acta , vol.508 , Issue.3 , pp. 565-570
    • Low, M.G.1    Finean, J.B.2
  • 8
    • 0018859942 scopus 로고
    • Selective release of plasma-membrane enzymes from rat hepatocytes by a phosphatidylinositol-specific phospholipase C
    • Shukla, S. D.; Coleman, R.; Finean, J. B.; Michell, R. H. Selective release of plasma-membrane enzymes from rat hepatocytes by a phosphatidylinositol-specific phospholipase C. Biochem. J. 1980, 187 (1), 277-280.
    • (1980) Biochem. J , vol.187 , Issue.1 , pp. 277-280
    • Shukla, S.D.1    Coleman, R.2    Finean, J.B.3    Michell, R.H.4
  • 9
    • 26844473519 scopus 로고    scopus 로고
    • Lipid-modified proteins as biomarkers for cardiovascular disease, a review
    • Ferri, N. R.; Corsini, A. Lipid-modified proteins as biomarkers for cardiovascular disease, a review. Biomarkers 2005, 10 (4), 219-237.
    • (2005) Biomarkers , vol.10 , Issue.4 , pp. 219-237
    • Ferri, N.R.1    Corsini, A.2
  • 10
    • 0022777521 scopus 로고
    • The C terminus of penicillin-binding protein 5 is essential for localisation to the E. coli inner membrane
    • Pratt, J. M.; Jackson, M. E.; Holland, I. B. The C terminus of penicillin-binding protein 5 is essential for localisation to the E. coli inner membrane. EMBO J. 1986, 5 (9), 2399-2405.
    • (1986) EMBO J , vol.5 , Issue.9 , pp. 2399-2405
    • Pratt, J.M.1    Jackson, M.E.2    Holland, I.B.3
  • 12
    • 12344330612 scopus 로고    scopus 로고
    • Granseth, E.; von.Heijne, G.; Elofsson, A. A study of the membrane-water interface region of membrane proteins. J. Mol. Biol, 2005, 346 (1), 377-385.
    • Granseth, E.; von.Heijne, G.; Elofsson, A. A study of the membrane-water interface region of membrane proteins. J. Mol. Biol, 2005, 346 (1), 377-385.
  • 14
    • 33144486308 scopus 로고    scopus 로고
    • NMR structure and molecular dynamics of the in-plane membrane anchor of nonstructural protein 5A from bovine viral diarrhea virus
    • Sapay, N.; Montserret, R.; Chipot, C.; Brass, V.; Moradpour, D.; Deleage, G.; Penin, F. NMR structure and molecular dynamics of the in-plane membrane anchor of nonstructural protein 5A from bovine viral diarrhea virus. Biochemistry 2006, 45 (7), 2221-2233.
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2221-2233
    • Sapay, N.1    Montserret, R.2    Chipot, C.3    Brass, V.4    Moradpour, D.5    Deleage, G.6    Penin, F.7
  • 15
    • 0036280738 scopus 로고    scopus 로고
    • Interaction of cardiotoxins with membranes, a molecular modeling study
    • Efremov, R. G.; Volynsky, P. E.; Nolde, D. E.; Dubovskii, P. V.; Arseniev, A. S. Interaction of cardiotoxins with membranes, a molecular modeling study. Biophys. J. 2002, 83 (1), 144-153.
    • (2002) Biophys. J , vol.83 , Issue.1 , pp. 144-153
    • Efremov, R.G.1    Volynsky, P.E.2    Nolde, D.E.3    Dubovskii, P.V.4    Arseniev, A.S.5
  • 16
    • 0032409445 scopus 로고    scopus 로고
    • Sequence properties of GPI-anchored proteins near the omega-site, constraints for the polypeptide binding site of the putative transamidase
    • Eisenhaber, B. B.; Eisenhaber, F. Sequence properties of GPI-anchored proteins near the omega-site, constraints for the polypeptide binding site of the putative transamidase. Protein Eng. 1998, 11 (12), 1155-1161.
    • (1998) Protein Eng , vol.11 , Issue.12 , pp. 1155-1161
    • Eisenhaber, B.B.1    Eisenhaber, F.2
  • 17
    • 33747793145 scopus 로고    scopus 로고
    • Energetics of membrane protein folding and stability
    • Minetti, C. A.; Remeta, D. P. Energetics of membrane protein folding and stability. Arch. Biochem. Biophys. 2006, 453 (1), 32-53.
    • (2006) Arch. Biochem. Biophys , vol.453 , Issue.1 , pp. 32-53
    • Minetti, C.A.1    Remeta, D.P.2
  • 18
    • 0033342531 scopus 로고    scopus 로고
    • Recent advances in the understanding of membrane protein assembly and structure
    • von Heijne, G. Recent advances in the understanding of membrane protein assembly and structure. Q. Rev. Biophys. 1999, 32 (4), 285-307.
    • (1999) Q. Rev. Biophys , vol.32 , Issue.4 , pp. 285-307
    • von Heijne, G.1
  • 19
    • 0033178531 scopus 로고    scopus 로고
    • Beta-barrel proteins from bacterial outer membranes, structure, function and refolding
    • Buchanan, S. Beta-barrel proteins from bacterial outer membranes, structure, function and refolding. Curr. Opin. Struct. Biol. 1998, 9 (4), 455-461.
    • (1998) Curr. Opin. Struct. Biol , vol.9 , Issue.4 , pp. 455-461
    • Buchanan, S.1
  • 20
    • 7044247850 scopus 로고    scopus 로고
    • Folding and assembly of beta-barrel membrane proteins
    • Tamm, L. K.; Hong, H.; Liang, B. Folding and assembly of beta-barrel membrane proteins. Biochim. Biophys. Acta 2004, 1666, 1-2.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 1-2
    • Tamm, L.K.1    Hong, H.2    Liang, B.3
  • 21
    • 0033932639 scopus 로고    scopus 로고
    • Schulz, G. beta-Barrel membrane proteins. Curr. Opin. Struct. Biol. 2000, 10 (4), 443-447.
    • Schulz, G. beta-Barrel membrane proteins. Curr. Opin. Struct. Biol. 2000, 10 (4), 443-447.
  • 22
    • 0028229579 scopus 로고
    • Folding pattern diversity of integral membrane proteins
    • Cowan, S. W.; Rosenbusch, J. Folding pattern diversity of integral membrane proteins. Science 1994, 264 (5161), 914-916.
    • (1994) Science , vol.264 , Issue.5161 , pp. 914-916
    • Cowan, S.W.1    Rosenbusch, J.2
  • 23
    • 25144452723 scopus 로고    scopus 로고
    • Biogenesis of beta-barrel membrane proteins of mitochondria
    • Paschen, S. A.; Neupert, W.; Rapaport, D. Biogenesis of beta-barrel membrane proteins of mitochondria. Trends Biochem. Sci. 2005, 30 (10), 575-582.
    • (2005) Trends Biochem. Sci , vol.30 , Issue.10 , pp. 575-582
    • Paschen, S.A.1    Neupert, W.2    Rapaport, D.3
  • 24
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E.; von Heijne, G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 1998, 7 (A), 1029-1038.
    • (1998) Protein Sci , vol.7 , Issue.A , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 25
    • 24644450611 scopus 로고    scopus 로고
    • Donnes, P.; Hoglund, A. Predicting protein subcellular localization, past, present, and future. Genomics Proteomics Bioinf. 2004, 2(4), 209-215.
    • Donnes, P.; Hoglund, A. Predicting protein subcellular localization, past, present, and future. Genomics Proteomics Bioinf. 2004, 2(4), 209-215.
  • 26
    • 33645297088 scopus 로고    scopus 로고
    • The use of functional domains to improve transmembrane protein topology prediction
    • Xu, E. W.; Kearney, P.; Brown, D. G. The use of functional domains to improve transmembrane protein topology prediction. J. Bioinf. Comput. Biol. 2006, 4 (1), 109-123.
    • (2006) J. Bioinf. Comput. Biol , vol.4 , Issue.1 , pp. 109-123
    • Xu, E.W.1    Kearney, P.2    Brown, D.G.3
  • 27
    • 22744431807 scopus 로고    scopus 로고
    • An investigation into the ability to define transmembrane protein spans using the biophysical properties of amino acid residues
    • Daman, O.; Wallace, J.; Harris, F.; Phoenix, D. A. An investigation into the ability to define transmembrane protein spans using the biophysical properties of amino acid residues. Mol. Cell. Biochem. 2005, 275 (1-2), 189-197.
    • (2005) Mol. Cell. Biochem , vol.275 , Issue.1-2 , pp. 189-197
    • Daman, O.1    Wallace, J.2    Harris, F.3    Phoenix, D.A.4
  • 28
    • 11144310571 scopus 로고    scopus 로고
    • 2D LC/MS analysis of membrane proteins from breast cancer cell lines MCF7 and BT474
    • Xiang, R.; Shi, Y.; Dillon, D. A.; Negin, B.; Horváth, C.; Wilkins, J. A. 2D LC/MS analysis of membrane proteins from breast cancer cell lines MCF7 and BT474. J. Proteome Res. 2004, 3 (6), 1278-1283.
    • (2004) J. Proteome Res , vol.3 , Issue.6 , pp. 1278-1283
    • Xiang, R.1    Shi, Y.2    Dillon, D.A.3    Negin, B.4    Horváth, C.5    Wilkins, J.A.6
  • 29
    • 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.; Aebersold, R. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotechnol. 2001, 19 (10), 946-951.
    • (2001) Nat. Biotechnol , vol.19 , Issue.10 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 31
    • 1842529218 scopus 로고    scopus 로고
    • Proteomic analysis of integral plasma membrane proteins
    • Zhao, Y; Zhang, W.; Kho, Y.; Zhao, Y. Proteomic analysis of integral plasma membrane proteins. Anal. Chem. 2004, 76 (7), 1817-1823.
    • (2004) Anal. Chem , vol.76 , Issue.7 , pp. 1817-1823
    • Zhao, Y.1    Zhang, W.2    Kho, Y.3    Zhao, Y.4
  • 33
    • 11144320641 scopus 로고    scopus 로고
    • Open source system for analyzing, validating, and storing protein identification
    • Craig, R.; Cortens, J. P.; Beavis, R. C. Open source system for analyzing, validating, and storing protein identification. J. Proteome Res. 2004, 3 (6), 1234-1242.
    • (2004) J. Proteome Res , vol.3 , Issue.6 , pp. 1234-1242
    • Craig, R.1    Cortens, J.P.2    Beavis, R.C.3
  • 34
    • 0018651448 scopus 로고
    • Synthesis of intracellular membrane proteins in vitro. Relation between rough endoplasmic reticulum and mitochondrial outer membrane
    • Shore, G. Synthesis of intracellular membrane proteins in vitro. Relation between rough endoplasmic reticulum and mitochondrial outer membrane. J. Cell Sci. 1979, 38, 137-153.
    • (1979) J. Cell Sci , vol.38 , pp. 137-153
    • Shore, G.1
  • 35
    • 0016377705 scopus 로고
    • Isolation of rough and smooth microsomes
    • Fleischer, S, Packer, L, Eds, Academic Press: New York
    • Dallner, G. Isolation of rough and smooth microsomes. In Methods in Enzymology, Fleischer, S., Packer, L., Eds.; Academic Press: New York, 1974; Vol. 31, pp 191-201.
    • (1974) Methods in Enzymology , vol.31 , pp. 191-201
    • Dallner, G.1
  • 36
    • 0020039867 scopus 로고
    • Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes, comparison with endoplasmic reticulum and mitochondrial membranes
    • Fujiki, Y.; Fowler, S.; Shio, H.; Hubbard, A. L.; Lazarow, P. B. Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes, comparison with endoplasmic reticulum and mitochondrial membranes. J. Cell Biol. 1982, 93 (1), 103-110.
    • (1982) J. Cell Biol , vol.93 , Issue.1 , pp. 103-110
    • Fujiki, Y.1    Fowler, S.2    Shio, H.3    Hubbard, A.L.4    Lazarow, P.B.5
  • 37
    • 2642551423 scopus 로고    scopus 로고
    • The human erythrocyte proteome, analysis by ion trap mass spectrometry
    • Kakhniashvili, D. G.; Bulla, L. A.; Goodman, S. R. The human erythrocyte proteome, analysis by ion trap mass spectrometry. Mol. Cell. Proteomics 2004, 3 (5), 501-509.
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.5 , pp. 501-509
    • Kakhniashvili, D.G.1    Bulla, L.A.2    Goodman, S.R.3
  • 39
    • 0022395235 scopus 로고
    • Functional characterization of LFA-1 antigens in the interaction of human NK clones and target cells
    • Schmidt, R. E.; Bartley, G.; Levine, H.; Schlossman, S. F.; Ritz, J. Functional characterization of LFA-1 antigens in the interaction of human NK clones and target cells. J. Immunol. 1985, 135 (2), 1020-1025.
    • (1985) J. Immunol , vol.135 , Issue.2 , pp. 1020-1025
    • Schmidt, R.E.1    Bartley, G.2    Levine, H.3    Schlossman, S.F.4    Ritz, J.5
  • 40
    • 0021926120 scopus 로고
    • Effects of monoclonal antibodies to the alpha and beta chains of the human lymphocyte function-associated (H-LFA-1) antigen on T lymphocyte functions
    • Dongworth, D. W.; Gotch, F. M; Hildreth, J. E.; Morris, A.; McMichael, A. J. Effects of monoclonal antibodies to the alpha and beta chains of the human lymphocyte function-associated (H-LFA-1) antigen on T lymphocyte functions. Eur. J. Immunol. 1985, 15 (9), 888-892.
    • (1985) Eur. J. Immunol , vol.15 , Issue.9 , pp. 888-892
    • Dongworth, D.W.1    Gotch, F.M.2    Hildreth, J.E.3    Morris, A.4    McMichael, A.J.5
  • 41
    • 0020356801 scopus 로고
    • Purification and structural characterization of LFA-1, a lymphocyte function-associated antigen, and Mac-1, a related macrophage differentiation antigen associated with the type three complement receptor
    • Kürzinger, K.; Springer, T. A. Purification and structural characterization of LFA-1, a lymphocyte function-associated antigen, and Mac-1, a related macrophage differentiation antigen associated with the type three complement receptor. J. Biol. Chem. 1982, 257 (20), 12412-12418.
    • (1982) J. Biol. Chem , vol.257 , Issue.20 , pp. 12412-12418
    • Kürzinger, K.1    Springer, T.A.2
  • 42
    • 0027053032 scopus 로고
    • Induction of alpha v beta 3 integrin-mediated attachment to extracellular matrix in beta 1 integrin (CD29)-negative B cell lines
    • Stupack, D. G.; Shen, C; Wilkins, J. A. Induction of alpha v beta 3 integrin-mediated attachment to extracellular matrix in beta 1 integrin (CD29)-negative B cell lines. Exp. Cell Res. 1992, 203 (2), 443-448.
    • (1992) Exp. Cell Res , vol.203 , Issue.2 , pp. 443-448
    • Stupack, D.G.1    Shen, C.2    Wilkins, J.A.3
  • 44
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model, application to complete genomes
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model, application to complete genomes. J. Mol. Biol. 2001, 305 (3), 567-580.
    • (2001) J. Mol. Biol , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 45
    • 4444343944 scopus 로고    scopus 로고
    • Analysis of murine natural killer cell microsomal proteins using two-dimensional liquid chromatography coupled to tandem electrospray ionization mass spectrometry
    • Blonder, J; Rodriguez-Galan, M. C.; Chan, K.C.; Lucas,D.A.; Yu, L. R.; Conrads, T. P.; Issaq, H. J.; Young, H. A.; Veenstra, T. D. Analysis of murine natural killer cell microsomal proteins using two-dimensional liquid chromatography coupled to tandem electrospray ionization mass spectrometry. J. Proteome Res. 2004, 3 (4), 862-870.
    • (2004) J. Proteome Res , vol.3 , Issue.4 , pp. 862-870
    • Blonder, J.1    Rodriguez-Galan, M.C.2    Chan, K.C.3    Lucas, D.A.4    Yu, L.R.5    Conrads, T.P.6    Issaq, H.J.7    Young, H.A.8    Veenstra, T.D.9
  • 46
    • 16844373498 scopus 로고    scopus 로고
    • Targeting of Arf-1 to the early Golgi by membrin, an ER-Golgi SNARE. J
    • Honda, A.; Al-Awar, O. S.; Hay, J. C; Donaldson, J. G. Targeting of Arf-1 to the early Golgi by membrin, an ER-Golgi SNARE. J. Cell Biol. 2005, 168 (7), 1039-1051.
    • (2005) Cell Biol , vol.168 , Issue.7 , pp. 1039-1051
    • Honda, A.1    Al-Awar, O.S.2    Hay, J.C.3    Donaldson, J.G.4
  • 47
    • 33645795446 scopus 로고    scopus 로고
    • Modification-specific proteomics of plasma membrane proteins, identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment
    • Elortza, F.; Mohammed, S.; Bunkenborg, J.; Foster, L. J.; Nuhse, T. S.; Brodbeck, U.; Peck, S. C; Jensen, 0. N. Modification-specific proteomics of plasma membrane proteins, identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment. J. Proteome Res. 2006, 5 (4), 935-943.
    • (2006) J. Proteome Res , vol.5 , Issue.4 , pp. 935-943
    • Elortza, F.1    Mohammed, S.2    Bunkenborg, J.3    Foster, L.J.4    Nuhse, T.S.5    Brodbeck, U.6    Peck, S.C.7    Jensen, 0.N.8
  • 48
    • 30544447982 scopus 로고    scopus 로고
    • Analysis of glycosylphosphatidylinositol protein anchors, the prion protein
    • Baldwin, M. Analysis of glycosylphosphatidylinositol protein anchors, the prion protein. Methods Enzymol. 2005, 405, 172-187.
    • (2005) Methods Enzymol , vol.405 , pp. 172-187
    • Baldwin, M.1
  • 49
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes, simple physics, complicated biology
    • Murray, D.; Ben-Tal, N.; Honig, B.; McLaughlin, S. Electrostatic interaction of myristoylated proteins with membranes, simple physics, complicated biology. Structure. 1997, 5 (8), 985-989.
    • (1997) Structure , vol.5 , Issue.8 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 50
    • 0029098999 scopus 로고
    • Identification and characterization of a novel protein (pl37) which transcytoses bidirectionally in Caco-2 cells
    • Ellis, J. A.; Luzio, J. P. Identification and characterization of a novel protein (pl37) which transcytoses bidirectionally in Caco-2 cells. J. Biol. Chem. 1995, 270 (35), 20717-20723.
    • (1995) J. Biol. Chem , vol.270 , Issue.35 , pp. 20717-20723
    • Ellis, J.A.1    Luzio, J.P.2
  • 51
    • 33748579946 scopus 로고    scopus 로고
    • Morone, N.; Fujiwara, T.; Murase, K.; Kasai, R. S.; Ike, H.; Yuasa, S.; Usukura, J.; Kusumi, A. Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography. j. Cell Biol. 2006, 174 (6), 851-862.
    • Morone, N.; Fujiwara, T.; Murase, K.; Kasai, R. S.; Ike, H.; Yuasa, S.; Usukura, J.; Kusumi, A. Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography. j. Cell Biol. 2006, 174 (6), 851-862.
  • 52
    • 7444232710 scopus 로고    scopus 로고
    • Role of the membrane skeleton in creation of microdomains
    • Ritchie, K.; Kusumi, A. Role of the membrane skeleton in creation of microdomains. Subcell. Biochem. 2004, 37, 233-245.
    • (2004) Subcell. Biochem , vol.37 , pp. 233-245
    • Ritchie, K.1    Kusumi, A.2
  • 53
    • 0038491423 scopus 로고    scopus 로고
    • Nicolas, V.; Le Van Kim, C.; Gane, P.; Birkenmeier, C; Cartron, J. P.; Colin, Y.; Mouro-Chanteloup, I. Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation. J. Biol. Chem. 2003, 278 (28), 25526-25533.
    • Nicolas, V.; Le Van Kim, C.; Gane, P.; Birkenmeier, C; Cartron, J. P.; Colin, Y.; Mouro-Chanteloup, I. Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation. J. Biol. Chem. 2003, 278 (28), 25526-25533.
  • 54
    • 34249650761 scopus 로고    scopus 로고
    • The role of junctional adhesion molecules in vascular inflammation
    • Weber, C.; Fraemohs, L.; Dejana, E. The role of junctional adhesion molecules in vascular inflammation. Nat. Rev. Immunol. 2007, 7 (6), 467-177.
    • (2007) Nat. Rev. Immunol , vol.7 , Issue.6 , pp. 467-177
    • Weber, C.1    Fraemohs, L.2    Dejana, E.3
  • 55
    • 34249936024 scopus 로고    scopus 로고
    • Forces and bond dynamics in cell adhesion
    • Evans, E. A.; Calderwood, D. Forces and bond dynamics in cell adhesion. Science 2007, 316 (5828), 1148-1153.
    • (2007) Science , vol.316 , Issue.5828 , pp. 1148-1153
    • Evans, E.A.1    Calderwood, D.2
  • 56
    • 34249291950 scopus 로고    scopus 로고
    • The double role of the endoplasmic reticulum chaperone tapasin in peptide optimization of HLA class I molecules
    • Cabrera, C. M. The double role of the endoplasmic reticulum chaperone tapasin in peptide optimization of HLA class I molecules. Scand. J. Immunol. 2007, 65 (6), 487-493.
    • (2007) Scand. J. Immunol , vol.65 , Issue.6 , pp. 487-493
    • Cabrera, C.M.1
  • 57
    • 0033746295 scopus 로고    scopus 로고
    • Intracellular trafficking and regulation of canalicular ATP-binding cassette transporters
    • Kipp, H.; Arias, I. M. Intracellular trafficking and regulation of canalicular ATP-binding cassette transporters. Semin. Liver Dis. 2000, 20 (3), 339-351.
    • (2000) Semin. Liver Dis , vol.20 , Issue.3 , pp. 339-351
    • Kipp, H.1    Arias, I.M.2
  • 58
    • 0015540436 scopus 로고
    • An improved cell fractionation procedure for the preparation of rat liver membrane-bound ribosomes
    • Adelman, M. R.; Blobel, G.; Sabatini, D. D. An improved cell fractionation procedure for the preparation of rat liver membrane-bound ribosomes. J Cell Biol. 1973, 56 (1), 191-205.
    • (1973) J Cell Biol , vol.56 , Issue.1 , pp. 191-205
    • Adelman, M.R.1    Blobel, G.2    Sabatini, D.D.3
  • 59
    • 0028028022 scopus 로고
    • Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles
    • Kim, J.; Shishido, T.; Jiang, X.; Aderem, A.; McLaughlin, S. Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles. J. Biol. Chem. 1994, 269 (45), 28214-28219.
    • (1994) J. Biol. Chem , vol.269 , Issue.45 , pp. 28214-28219
    • Kim, J.1    Shishido, T.2    Jiang, X.3    Aderem, A.4    McLaughlin, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.