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Volumn 60, Issue 8, 2003, Pages 1575-1580

Lipid interactions with transmembrane proteins

Author keywords

Chain conformation; Crystal structures; Cytochrome oxidase; Order parameter; Phosphatidylethanolamine; trans gauche isomerism

Indexed keywords

CARBON; HYDROGEN; LIPID; MEMBRANE PROTEIN; PHOSPHOLIPID;

EID: 0042377402     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3171-z     Document Type: Short Survey
Times cited : (18)

References (22)
  • 4
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
    • Marsh D. and Horváth L. I. (1998) Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling. Biochim. Biophys. Acta 1376: 267-296
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 267-296
    • Marsh, D.1    Horváth, L.I.2
  • 6
    • 0035424669 scopus 로고    scopus 로고
    • High-resolution structures and dynamics of membrane protein-lipid complexes: A critique
    • Pebay-Peyroula E. and Rosenbusch J. P. (2001) High-resolution structures and dynamics of membrane protein-lipid complexes: a critique. Curr. Opin. Struct. Biol. 11: 427-432
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 427-432
    • Pebay-Peyroula, E.1    Rosenbusch, J.P.2
  • 9
    • 0016278896 scopus 로고
    • Statistical mechanics of the fluidity of phospholipid bilayers and membranes
    • Marsh D. (1974) Statistical mechanics of the fluidity of phospholipid bilayers and membranes. J. Membrane Biol. 18: 145-162
    • (1974) J. Membrane Biol. , vol.18 , pp. 145-162
    • Marsh, D.1
  • 10
    • 0024502680 scopus 로고
    • Chain configuration and flexibility gradient in phospholipid membranes. Comparison between spin-label electron spin resonance and deuteron nuclear magnetic resonance, and identification of new conformations
    • Moser M., Marsh D., Meier P., Wassmer K.-H., and Kothe G. (1989) Chain configuration and flexibility gradient in phospholipid membranes. Comparison between spin-label electron spin resonance and deuteron nuclear magnetic resonance, and identification of new conformations. Biophys. J. 55: 111-123
    • (1989) Biophys. J. , vol.55 , pp. 111-123
    • Moser, M.1    Marsh, D.2    Meier, P.3    Wassmer, K.-H.4    Kothe, G.5
  • 11
    • 0842297635 scopus 로고
    • Integral membrane proteins significantly decrease the molecular motion in lipid bilayers: A deuteron NMR relaxation study of membranes containing myelin proteolipid apoprotein
    • Meier P., Sachse J.-H., Brophy P. J., Marsh D., and Kothe G. (1987) Integral membrane proteins significantly decrease the molecular motion in lipid bilayers: a deuteron NMR relaxation study of membranes containing myelin proteolipid apoprotein. Proc. Natl. Acad. Sci. USA 84: 3704-3708
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3704-3708
    • Meier, P.1    Sachse, J.-H.2    Brophy, P.J.3    Marsh, D.4    Kothe, G.5
  • 12
    • 0041664782 scopus 로고
    • Spin label answers to lipid-protein interactions
    • Marsh D. (1983) Spin label answers to lipid-protein interactions. Trends Biochem. Sci. 8: 330-333
    • (1983) Trends Biochem. Sci. , vol.8 , pp. 330-333
    • Marsh, D.1
  • 13
    • 0023096158 scopus 로고
    • Lipid mobility and order in bovine rod outer segment disk membranes. A spin-label study of lipid-protein interactions
    • Pates R. D. and Marsh D. (1987) Lipid mobility and order in bovine rod outer segment disk membranes. A spin-label study of lipid-protein interactions. Biochemistry 26: 29-39
    • (1987) Biochemistry , vol.26 , pp. 29-39
    • Pates, R.D.1    Marsh, D.2
  • 14
    • 0027280812 scopus 로고
    • Exchange rates at the lipid-protein interface of the myelin proteolipid protein determined by saturation transfer electron spin resonance and continuous wave saturation studies
    • Horváth L. I., Brophy P. J., and Marsh D. (1993) Exchange rates at the lipid-protein interface of the myelin proteolipid protein determined by saturation transfer electron spin resonance and continuous wave saturation studies. Biophys. J. 64: 622-631
    • (1993) Biophys. J. , vol.64 , pp. 622-631
    • Horváth, L.I.1    Brophy, P.J.2    Marsh, D.3
  • 15
    • 0005674602 scopus 로고
    • Nuclear magnetic resonance and lipid-protein interactions
    • Jost P. C. and Griffith O. H. (eds), John Wiley, New York
    • Seelig J., Seelig A., and Tamm L. (1982) Nuclear magnetic resonance and lipid-protein interactions. In: Lipid-Protein Interactions, vol. 2, pp. 127-148, Jost P. C. and Griffith O. H. (eds), John Wiley, New York
    • (1982) Lipid-Protein Interactions , vol.2 , pp. 127-148
    • Seelig, J.1    Seelig, A.2    Tamm, L.3
  • 16
    • 0001889988 scopus 로고
    • Manifestations of lipid-protein interactions in deuterium NMR
    • Watts A. and de Pont J. J. H. H. M. (eds), Elsevier, Amsterdam
    • Bloom M. and Smith I. C. P. (1985) Manifestations of lipid-protein interactions in deuterium NMR. In: Progress in Protein-Lipid Interactions, vol. 1, pp. 61-88, Watts A. and de Pont J. J. H. H. M. (eds), Elsevier, Amsterdam
    • (1985) Progress in Protein-Lipid Interactions , vol.1 , pp. 61-88
    • Bloom, M.1    Smith, I.C.P.2
  • 17
    • 0020490463 scopus 로고
    • Evidence for protein-associated lipids from deuterium nuclear magnetic resonance studies of rhodopsin-dimyristoyl-phosphatidylcholine recombinants
    • Bienvenue A., Bloom M., Davis J. H., and Devaux P. F. (1982) Evidence for protein-associated lipids from deuterium nuclear magnetic resonance studies of rhodopsin-dimyristoyl-phosphatidylcholine recombinants. J. Biol. Chem. 257: 3032-3038
    • (1982) J. Biol. Chem. , vol.257 , pp. 3032-3038
    • Bienvenue, A.1    Bloom, M.2    Davis, J.H.3    Devaux, P.F.4
  • 19
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • Svensson-Ek M., Abramson J., Larsson G., Törnroth S., Brzezinski P., and Iwata S. (2002) The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321: 329-339
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Törnroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 20
    • 0028922586 scopus 로고
    • LIGPLOT - A program to generate schematic diagrams of protein ligand interactions
    • Wallace A. C., Laskowski R. A., and Thornton J. M. (1995) LIGPLOT - a program to generate schematic diagrams of protein ligand interactions. Prot. Engin. 8: 127-134
    • (1995) Prot. Engin. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 22
    • 0034805275 scopus 로고    scopus 로고
    • Cholesterol effects on the phosphatidylcholine bilayer nonpolar region: A molecular simulation study
    • Róg T. and Pasenkiewicz-Gierula M. (2001) Cholesterol effects on the phosphatidylcholine bilayer nonpolar region: a molecular simulation study. Biophys. J. 81: 2190-2202
    • (2001) Biophys. J. , vol.81 , pp. 2190-2202
    • Róg, T.1    Pasenkiewicz-Gierula, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.