메뉴 건너뛰기




Volumn 51, Issue 1, 2012, Pages 90-99

Structural characterization of the caveolin scaffolding domain in association with cholesterol-rich membranes

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLAE; CAVEOLIN; CAVEOLIN PROTEIN; CAVEOLIN-1; COMPUTATIONAL ANALYSIS; CRITICAL FUNCTIONS; EXPERIMENTAL DATA; FTIR; HELICAL HAIRPINS; HELICAL STRUCTURES; MEMBRANE BINDING; MEMBRANE-BOUND; PRIMARY SEQUENCES; PROTEIN RECOGNITION; SECONDARY STRUCTURE PREFERENCES; SIGNALING PATHWAYS; SOLID STATE NMR; SPECTROSCOPIC METHOD; STRUCTURAL CHARACTERIZATION; STRUCTURAL DATA;

EID: 84856932972     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201356v     Document Type: Article
Times cited : (71)

References (61)
  • 1
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: From cell biology to animal physiology
    • Razani, B., Woodman, S. E., and Lisanti, M. P. (2002) Caveolae: from cell biology to animal physiology. Pharmacol. Rev. 54, 431-467.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 2
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • DOI 10.1146/annurev.biochem.67.1.199
    • Anderson, R. G. W. (1998) The caveolae membrane system. Annu. Rev. Biochem. 67, 199-225. (Pubitemid 28411129)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 4
    • 33645216741 scopus 로고    scopus 로고
    • Biogenesis of caveolae: A structural model for caveolin-induced domain formation
    • Parton, R. G., Hanzal-Bayer, M., and Hancock, J. F. (2006) Biogenesis of caveolae: a structural model for caveolin-induced domain formation. J. Cell Sci. 119, 787-796.
    • (2006) J. Cell Sci. , vol.119 , pp. 787-796
    • Parton, R.G.1    Hanzal-Bayer, M.2    Hancock, J.F.3
  • 6
    • 0347122967 scopus 로고    scopus 로고
    • Role of the hydrophobic domain in targeting caveolin-1 to lipid droplets
    • DOI 10.1083/jcb.200303037
    • Ostermeyer, A. G., Ramcharan, L. T., Zeng, Y., Lublin, D. M., and Brown, D. A. (2004) Role of the hydrophobic domain in targeting caveolin-1 to lipid droplets. J. Cell Biol. 164, 69-78. (Pubitemid 38082458)
    • (2004) Journal of Cell Biology , vol.164 , Issue.1 , pp. 69-78
    • Ostermeyer, A.G.1    Ramcharan, L.T.2    Zeng, Y.3    Lublin, D.M.4    Brown, D.A.5
  • 7
    • 77958502200 scopus 로고    scopus 로고
    • The role of proline in the membrane re-entrant helix of caveolin-1
    • Aoki, S., Thomas, A., Decaffmeyer, M., Brasseur, R., and Epand, R. M. (2010) The role of proline in the membrane re-entrant helix of caveolin-1. J. Biol. Chem. 285, 33371-33380.
    • (2010) J. Biol. Chem. , vol.285 , pp. 33371-33380
    • Aoki, S.1    Thomas, A.2    Decaffmeyer, M.3    Brasseur, R.4    Epand, R.M.5
  • 8
    • 0030027901 scopus 로고    scopus 로고
    • Expression and characterization of recombinant caveolin Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes
    • Li, S., Song, K. S., and Lisanti, M. P. (1996) Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes. J. Biol. Chem. 271, 568-573.
    • (1996) J. Biol. Chem. , vol.271 , pp. 568-573
    • Li, S.1    Song, K.S.2    Lisanti, M.P.3
  • 9
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues Palmitoylation is not necessary for localization of caveolin to caveolae
    • Dietzen, D. J., Hastings, W. R., and Lublin, D. M. (1995) Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae. J. Biol. Chem. 270, 6838-6842.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 10
    • 0034682847 scopus 로고    scopus 로고
    • Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae
    • Uittenbogaard, A., and Smart, E. J. (2000) Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae. J. Biol. Chem. 275, 25595-25599.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25595-25599
    • Uittenbogaard, A.1    Smart, E.J.2
  • 11
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, G(α) subunits, and H-Ras share a common membrane- anchored scaffolding protein, caveolin: Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • DOI 10.1074/jbc.271.46.29182
    • Li, S., Couet, J., and Lisanti, M. P. (1996) Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. J. Biol. Chem. 271, 29182-29190. (Pubitemid 26382628)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.46 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 12
    • 0033529643 scopus 로고    scopus 로고
    • A role for the caveolin scaffolding domain in mediating the membrane attachment of caveolin-1. The caveolin scaffolding domain is both necessary and sufficient for membrane binding in vitro
    • Schlegel, A., Schwab, R. B., Scherer, P. E., and Lisanti, M. P. (1999) A role for the caveolin scaffolding domain in mediating the membrane attachment of caveolin-1. The caveolin scaffolding domain is both necessary and sufficient for membrane binding in vitro. J. Biol. Chem. 274, 22660-22667.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22660-22667
    • Schlegel, A.1    Schwab, R.B.2    Scherer, P.E.3    Lisanti, M.P.4
  • 13
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin- scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins
    • DOI 10.1074/jbc.272.10.6525
    • Couet, J., Li, S., Okamoto, T., Ikezu, T., and Lisanti, M. P. (1997) Identification of peptide and protein ligands for the caveolinscaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J. Biol. Chem. 272, 6525-6533. (Pubitemid 27118133)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.10 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 14
    • 0030731231 scopus 로고    scopus 로고
    • Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities
    • DOI 10.1074/jbc.272.48.30429
    • Couet, J., Sargiacomo, M., and Lisanti, M. P. (1997) Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities. J. Biol. Chem. 272, 30429-30438. (Pubitemid 27512253)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.48 , pp. 30429-30438
    • Couet, J.1    Sargiacomo, M.2    Lisanti, M.P.3
  • 16
    • 9644281567 scopus 로고    scopus 로고
    • Caveolin scaffolding region and cholesterol-rich domains in membranes
    • DOI 10.1016/j.jmb.2004.10.064, PII S0022283604013701
    • Epand, R. M., Sayer, B. G., and Epand, R. F. (2005) Caveolin scaffolding region and cholesterol-rich domains in membranes. J. Mol. Biol. 345, 339-350. (Pubitemid 39574855)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.2 , pp. 339-350
    • Epand, R.M.1    Sayer, B.G.2    Epand, R.F.3
  • 17
    • 33748766106 scopus 로고    scopus 로고
    • Role of the membrane interface on the conformation of the caveolin scaffolding domain: A CD and NMR study
    • DOI 10.1016/j.febslet.2006.08.075, PII S0014579306010659
    • Le Lan, C., Neumann, J. M., and Jamin, N. (2006) Role of the membrane interface on the conformation of the caveolin scaffolding domain: a CD and NMR study. FEBS Lett. 580, 5301-5305. (Pubitemid 44415808)
    • (2006) FEBS Letters , vol.580 , Issue.22 , pp. 5301-5305
    • Lan, C.L.1    Neumann, J.-M.2    Jamin, N.3
  • 18
    • 33644502902 scopus 로고    scopus 로고
    • Exploring the interaction between the protein kinase A catalytic subunit and caveolin-1 scaffolding domain with shotgun scanning, oligomer complementation, NMR, and docking
    • Levin, A. M., Coroneus, J. G., Cocco, M. J., and Weiss, G. A. (2006) Exploring the interaction between the protein kinase A catalytic subunit and caveolin-1 scaffolding domain with shotgun scanning, oligomer complementation, NMR, and docking. Protein Sci. 15, 478-486.
    • (2006) Protein Sci. , vol.15 , pp. 478-486
    • Levin, A.M.1    Coroneus, J.G.2    Cocco, M.J.3    Weiss, G.A.4
  • 20
    • 73649086865 scopus 로고    scopus 로고
    • Structural and dynamic properties of juxtamembrane segments of caveolin-1 and caveolin-2 at the membrane interface
    • Le Lan, C., Gallay, J., Vincent, M., Neumann, J. M., de Foresta, B., and Jamin, N. (2010) Structural and dynamic properties of juxtamembrane segments of caveolin-1 and caveolin-2 at the membrane interface. Eur. Biophys. J. 39, 307-325.
    • (2010) Eur. Biophys. J. , vol.39 , pp. 307-325
    • Le Lan, C.1    Gallay, J.2    Vincent, M.3    Neumann, J.M.4    De Foresta, B.5    Jamin, N.6
  • 25
    • 67650285019 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR
    • McDermott, A. (2009) Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR. Annu. Rev. Biophys. 38, 385-403.
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 385-403
    • McDermott, A.1
  • 26
    • 33845217043 scopus 로고    scopus 로고
    • Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR
    • DOI 10.1016/j.str.2006.10.002, PII S0969212606004011
    • Hong, M. (2006) Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR. Structure 14, 1731-1740. (Pubitemid 44855624)
    • (2006) Structure , vol.14 , Issue.12 , pp. 1731-1740
    • Hong, M.1
  • 27
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella, S. J., and Marassi, F. M. (2004) Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev. 104, 3587-3606.
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 30
    • 77749267718 scopus 로고    scopus 로고
    • Conformational changes of an ion channel detected through water-protein interactions using solidstate NMR spectroscopy
    • Luo, W., and Hong, M. (2010) Conformational changes of an ion channel detected through water-protein interactions using solidstate NMR spectroscopy. J. Am. Chem. Soc. 132, 2378-2384.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2378-2384
    • Luo, W.1    Hong, M.2
  • 31
    • 0000953276 scopus 로고    scopus 로고
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR
    • DOI 10.1016/S0009-2614(01)00791-6, PII S0009261401007916
    • Takegoshi, K., Nakamura, S., and Terao, T. (2001) C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR. Chem. Phys. Lett. 344, 631-637. (Pubitemid 33628408)
    • (2001) Chemical Physics Letters , vol.344 , Issue.5-6 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 32
    • 0001501402 scopus 로고
    • Some new developments in solid-state nuclear magnetic resonance spectroscopic studies of lipids and biological membranes, including the effects of cholesterol in model and natural systems
    • Forbes, J., Bowers, J., Shan, X., Moran, L., Oldfield, E., and Moscarello, M. A. (1988) Some new developments in solid-state nuclear magnetic resonance spectroscopic studies of lipids and biological membranes, including the effects of cholesterol in model and natural systems. J. Chem. Soc., Faraday Trans. 1 84, 3821-3849.
    • (1988) J. Chem. Soc., Faraday Trans. , vol.184 , pp. 3821-3849
    • Forbes, J.1    Bowers, J.2    Shan, X.3    Moran, L.4    Oldfield, E.5    Moscarello, M.A.6
  • 33
    • 0029657776 scopus 로고    scopus 로고
    • 13C MAS NMR studies of crystalline cholesterol and lipid mixtures modeling atherosclerotic plaques
    • Guo, W., and Hamilton, J. A. (1996) 13C MAS NMR studies of crystalline cholesterol and lipid mixtures modeling atherosclerotic plaques. Biophys. J. 71, 2857-2868. (Pubitemid 26367748)
    • (1996) Biophysical Journal , vol.71 , Issue.5 , pp. 2857-2868
    • Guo, W.1    Hamilton, J.A.2
  • 34
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 38
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • DOI 10.1006/jmbi.1999.3091
    • Jones, D. T. (1999) Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292, 195-202. (Pubitemid 29435759)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 39
    • 3242885293 scopus 로고    scopus 로고
    • The PredictProtein server
    • DOI 10.1093/nar/gkh377
    • Rost, B., Yachdav, G., and Liu, J. (2004) The PredictProtein server. Nucleic Acids Res. 32, W321-326. (Pubitemid 39004075)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Rost, B.1    Yachdav, G.2    Liu, J.3
  • 41
    • 0026511937 scopus 로고
    • Dynamics of phosphate head groups in biomembranes. Comprehensive analysis using phosphorus-31 nuclear magnetic resonance lineshape and relaxation time measurements
    • Dufourc, E. J., Mayer, C., Stohrer, J., Althoff, G., and Kothe, G. (1992) Dynamics of phosphate head groups in biomembranes. Comprehensive analysis using phosphorus-31 nuclear magnetic resonance lineshape and relaxation time measurements. Biophys. J. 61, 42-57.
    • (1992) Biophys. J. , vol.61 , pp. 42-57
    • Dufourc, E.J.1    Mayer, C.2    Stohrer, J.3    Althoff, G.4    Kothe, G.5
  • 42
    • 0034696524 scopus 로고    scopus 로고
    • Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatch- dependent manner
    • DOI 10.1021/bi9922594
    • Van der Wel, P. C. A., Pott, T., Morein, S., Greathouse, D. V., Koeppe, R., and Killian, J. (2000) Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatchdependent manner. Biochemistry 39, 3124-3133. (Pubitemid 30159419)
    • (2000) Biochemistry , vol.39 , Issue.11 , pp. 3124-3133
    • Van Der Wel, P.C.A.1    Pott, T.2    Morein, S.3    Greathouse, D.V.4    Koeppe II, R.E.5    Killian, J.A.6
  • 43
    • 77954219657 scopus 로고    scopus 로고
    • Investigating the impact of cholesterol on magnetically aligned sphingomyelin/cholesterol multilamellar vesicles using static (31)P NMR
    • Costello, A. L., and Alam, T. M. (2010) Investigating the impact of cholesterol on magnetically aligned sphingomyelin/cholesterol multilamellar vesicles using static (31)P NMR. Chem. Phys. Lipids 163, 506-513.
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 506-513
    • Costello, A.L.1    Alam, T.M.2
  • 44
    • 33744900851 scopus 로고    scopus 로고
    • 31P MAS NMR
    • DOI 10.1529/biophysj.105.077289
    • Holland, G. P., McIntyre, S. K., and Alam, T. M. (2006) Distinguishing individual lipid headgroup mobility and phase transitions in raft-forming lipid mixtures with 31P MAS NMR. Biophys. J. 90, 4248-4260. (Pubitemid 43846139)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 4248-4260
    • Holland, G.P.1    McIntyre, S.K.2    Alam, T.M.3
  • 45
    • 0033065591 scopus 로고    scopus 로고
    • A microscopic interaction model of maximum solubility of cholesterol in lipid bilayers
    • Huang, J., and Feigenson, G. W. (1999) A microscopic interaction model of maximum solubility of cholesterol in lipid bilayers. Biophys. J. 76, 2142-2157. (Pubitemid 29266367)
    • (1999) Biophysical Journal , vol.76 , Issue.4 , pp. 2142-2157
    • Huang, J.1    Feigenson, G.W.2
  • 46
    • 18244392671 scopus 로고    scopus 로고
    • 31P NMR multilamellar bilayer broadlines in the absence and presence of the bioactive dipeptide β-Ala-Tyr or Glu
    • DOI 10.1016/j.chemphys.2005.01.028, PII S0301010405000315
    • Benetis, N., Kyrikou, I., Zervou, M., and Mavromoustakos, T. (2005) Static CP P-31 NMR multilamellar bilayer broadlines in the absence and presence of the bioactive dipeptide beta-Ala-Tyr or Glu. Chem. Phys. 314, 57-72. (Pubitemid 40630999)
    • (2005) Chemical Physics , vol.314 , Issue.1-3 , pp. 57-72
    • Benetis, N.-P.1    Kyrikou, I.2    Zervou, M.3    Mavromoustakos, T.4
  • 47
    • 0017902280 scopus 로고
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes
    • Seelig, J. (1978) P-31 nuclear magnetic-resonance and head group structure of phospholipids in membranes. Biochim. Biophys. Acta 515, 105-140. (Pubitemid 8398025)
    • (1978) Biochimica et Biophysica Acta , vol.515 , Issue.2 , pp. 105-140
    • Seelig, J.1
  • 48
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • DOI 10.1111/j.1745-7270.2007.00320.x
    • Kong, J., and Yu, S. (2007) Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim. Biophys. Sin. 39, 549-559. (Pubitemid 47293710)
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.8 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 49
    • 0030021044 scopus 로고    scopus 로고
    • The effect of high external pressure on DPPC-cholesterol multilamellar vesicles: A pressure-tuning Fourier transform infrared spectroscopy study
    • DOI 10.1016/0005-2736(95)00233-2
    • Reis, O., Winter, R., and Zerda, T. W. (1996) The effect of high external pressure on DPPC-cholesterol multilamellar vesicles: a pressure-tuning Fourier transform infrared spectroscopy study. Biochim. Biophys. Acta 1279, 5-16. (Pubitemid 26067411)
    • (1996) Biochimica et Biophysica Acta - Biomembranes , vol.1279 , Issue.1 , pp. 5-16
    • Reis, O.1    Winter, R.2    Zerda, T.W.3
  • 50
    • 0028393784 scopus 로고
    • The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart, D. S., and Sykes, B. D. (1994) The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 4, 171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 51
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: A database of uniformly referenced protein chemical shifts
    • DOI 10.1023/A:1022836027055
    • Zhang, H., Neal, S., and Wishart, D. S. (2003) RefDB: a database of uniformly referenced protein chemical shifts. J. Biomol. NMR 25, 173-195. (Pubitemid 36410583)
    • (2003) Journal of Biomolecular NMR , vol.25 , Issue.3 , pp. 173-195
    • Zhang, H.1    Neal, S.2    Wishart, D.S.3
  • 52
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: The role of polar, GxxxG-like and proline motifs
    • DOI 10.1016/j.sbi.2004.07.007, PII S0959440X04001149
    • Senes, A., Engel, D. E., and DeGrado, W. F. (2004) Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol. 14, 465-479. (Pubitemid 39094354)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.4 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    Degrado, W.F.3
  • 53
    • 7444227630 scopus 로고    scopus 로고
    • Rafts, little caves and large potholes: How lipid structure interacts with membrane proteins to create functionally diverse membrane environments
    • Morris, R., Cox, H., Mombelli, E., and Quinn, P. J. (2004) Rafts, little caves and large potholes: how lipid structure interacts with membrane proteins to create functionally diverse membrane environments. Subcell. Biochem. 37, 35-118.
    • (2004) Subcell. Biochem. , vol.37 , pp. 35-118
    • Morris, R.1    Cox, H.2    Mombelli, E.3    Quinn, P.J.4
  • 54
    • 73849147582 scopus 로고    scopus 로고
    • Inhibition of thioredoxin reductase 1 by caveolin 1 promotes stress-induced premature senescence
    • Volonte, D., and Galbiati, F. (2009) Inhibition of thioredoxin reductase 1 by caveolin 1 promotes stress-induced premature senescence. EMBO Rep. 10, 1334-1340.
    • (2009) EMBO Rep. , vol.10 , pp. 1334-1340
    • Volonte, D.1    Galbiati, F.2
  • 55
    • 0031733584 scopus 로고    scopus 로고
    • Inhibition of adenylyl cyclase by caveolin peptides
    • Toya, Y., Schwencke, C., Couet, J., Lisanti, M. P., and Ishikawa, Y. (1998) Inhibition of adenylyl cyclase by caveolin peptides. Endocrinology 139, 2025-2031. (Pubitemid 28513865)
    • (1998) Endocrinology , vol.139 , Issue.4 , pp. 2025-2031
    • Toya, Y.1    Schwencke, C.2    Couet, J.3    Lisanti, M.P.4    Ishikawa, Y.5
  • 57
    • 80051673604 scopus 로고    scopus 로고
    • Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions
    • Li, J., Hoop, C. L., Kodali, R., Sivanandam, V. N., and van der Wel, P. C. A. (2011) Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions. J. Biol. Chem. 286, 28988-28995.
    • (2011) J. Biol. Chem. , vol.286 , pp. 28988-28995
    • Li, J.1    Hoop, C.L.2    Kodali, R.3    Sivanandam, V.N.4    Van Der Wel, P.C.A.5
  • 58
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • Li, H., and Papadopoulos, V. (1998) Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology 139, 4991-4997. (Pubitemid 28533447)
    • (1998) Endocrinology , vol.139 , Issue.12 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 59
    • 77958086064 scopus 로고    scopus 로고
    • Interaction of mammalian seminal plasma protein PDC-109 with cholesterol-Implications for a putative CRAC domain
    • Scolari, S., Müller, K., Bittman, R., Herrmann, A., and Müller, P. (2010) Interaction of mammalian seminal plasma protein PDC-109 with cholesterol-Implications for a putative CRAC domain. Biochemistry 49, 9027-9031.
    • (2010) Biochemistry , vol.49 , pp. 9027-9031
    • Scolari, S.1    Müller, K.2    Bittman, R.3    Herrmann, A.4    Müller, P.5
  • 60
    • 45449105538 scopus 로고    scopus 로고
    • Proteins and cholesterol-rich domains
    • Epand, R. M. (2008) Proteins and cholesterol-rich domains. Biochim. Biophys. Acta 1778, 1576-1582.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1576-1582
    • Epand, R.M.1
  • 61
    • 0036223099 scopus 로고    scopus 로고
    • Sperm coating mechanism from the 1.8 Å crystal structure of PDC-109-phosphorylcholine complex
    • DOI 10.1016/S0969-2126(02)00751-7, PII S0969212602007517
    • Wah, D. A., Fernández-Tornero, C., Sanz, L., Romero, A., and Calvete, J. J. (2002) Sperm coating mechanism from the 1.8 A crystal structure of PDC-109-phosphorylcholine complex. Structure 10, 505-514. (Pubitemid 34304229)
    • (2002) Structure , vol.10 , Issue.4 , pp. 505-514
    • Wah, D.A.1    Fernandez-Tornero, C.2    Sanz, L.3    Romero, A.4    Calvete, J.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.