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Volumn 1788, Issue 7, 2009, Pages 1474-1481

Interaction of the MARCKS peptide with PIP2 in phospholipid monolayers

Author keywords

Lateral organization; Peptide monolayer interaction; Structural parameter

Indexed keywords

DIPALMITOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLINOSITOL 4,5 DIPHOSPHATE; MARCKS PROTEIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPID; UNCLASSIFIED DRUG; MARCKS RELATED PEPTIDE; MARCKS-RELATED PEPTIDE; PEPTIDE FRAGMENT;

EID: 68149139721     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.04.001     Document Type: Article
Times cited : (30)

References (56)
  • 1
    • 0026639826 scopus 로고
    • Signal transduction and the actin cytoskeleton: the role of MARCKS and profilin
    • Aderem A. Signal transduction and the actin cytoskeleton: the role of MARCKS and profilin. TIBS 17 (1992) 438-443
    • (1992) TIBS , vol.17 , pp. 438-443
    • Aderem, A.1
  • 2
    • 0027392102 scopus 로고
    • The MARCKS Family of Cellular Protein Kinase C Substrates
    • Blackshear P.J. The MARCKS Family of Cellular Protein Kinase C Substrates. J. Biol. Chem. 268 (1993) 1501-1504
    • (1993) J. Biol. Chem. , vol.268 , pp. 1501-1504
    • Blackshear, P.J.1
  • 4
    • 0034617183 scopus 로고    scopus 로고
    • Interaction between Actin and the Effector Peptide of MARCKS-related Protein
    • Wohnsland F., Schmitz A.A.P., Steinmetz M.O., Aebi U., and Vergères G. Interaction between Actin and the Effector Peptide of MARCKS-related Protein. J. Biol. Chem. 275 (2000) 20873-20879
    • (2000) J. Biol. Chem. , vol.275 , pp. 20873-20879
    • Wohnsland, F.1    Schmitz, A.A.P.2    Steinmetz, M.O.3    Aebi, U.4    Vergères, G.5
  • 5
    • 0026513601 scopus 로고
    • MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin
    • Hartwig J.H., Thelen M., Rosen A., Janmey P.A., Nairn A.C., and Aderem A. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature 356 (1992) 618-622
    • (1992) Nature , vol.356 , pp. 618-622
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5    Aderem, A.6
  • 7
    • 0034702838 scopus 로고    scopus 로고
    • Membrane Binding of Peptides Containing Both Basic and Aromatic Residues. Experimental Studies with Peptides Corresponding to the Scaffolding Region of Caveolin and the Effector Region of MARCKS
    • Arbuzova A., Wang L., Wang J., Hangyás-Milháyné G., Murray D., Honig B., and McLaughlin S. Membrane Binding of Peptides Containing Both Basic and Aromatic Residues. Experimental Studies with Peptides Corresponding to the Scaffolding Region of Caveolin and the Effector Region of MARCKS. Biochemistry 39 (2000) 10330-10339
    • (2000) Biochemistry , vol.39 , pp. 10330-10339
    • Arbuzova, A.1    Wang, L.2    Wang, J.3    Hangyás-Milháyné, G.4    Murray, D.5    Honig, B.6    McLaughlin, S.7
  • 8
    • 0035895882 scopus 로고    scopus 로고
    • The Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Binds Strongly to Phosphatidylinositol 4,5-Biphosphate
    • Wang J., Arbuzova A., Hangás-Milháyné G., and McLaughlin S. The Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Binds Strongly to Phosphatidylinositol 4,5-Biphosphate. J. Biol. Chem. 276 (2001) 5012-5019
    • (2001) J. Biol. Chem. , vol.276 , pp. 5012-5019
    • Wang, J.1    Arbuzova, A.2    Hangás-Milháyné, G.3    McLaughlin, S.4
  • 9
    • 0030869425 scopus 로고    scopus 로고
    • Kinetics of Interaction of the Myristoylated Alanine-rich C Kinase Substrate, Membranes, and Calmodulin
    • Arbuzova A., Wang J., Murray D., Jacob J., Cafiso D.S., and McLaughlin S. Kinetics of Interaction of the Myristoylated Alanine-rich C Kinase Substrate, Membranes, and Calmodulin. J. Biol. Chem. 272 (1997) 27167-27177
    • (1997) J. Biol. Chem. , vol.272 , pp. 27167-27177
    • Arbuzova, A.1    Wang, J.2    Murray, D.3    Jacob, J.4    Cafiso, D.S.5    McLaughlin, S.6
  • 10
    • 0037072757 scopus 로고    scopus 로고
    • Lateral Sequestration of Phosphatidylinositol 4,5-Biphosphate by the Basic Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Is Due to Nonspecific Electrostatic Interactions
    • Wang J., Gambhir A., Hangyás-Mihályné G., Murray D., Golebiewska U., and McLaughlin S. Lateral Sequestration of Phosphatidylinositol 4,5-Biphosphate by the Basic Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Is Due to Nonspecific Electrostatic Interactions. J. Biol. Chem. 277 (2002) 34001-34412
    • (2002) J. Biol. Chem. , vol.277 , pp. 34001-34412
    • Wang, J.1    Gambhir, A.2    Hangyás-Mihályné, G.3    Murray, D.4    Golebiewska, U.5    McLaughlin, S.6
  • 12
    • 0034713935 scopus 로고    scopus 로고
    • Importance of Protein Kinase C Targeting for the Phosphorylation of Its Substrate, Myristoylated Alanine-rich C-kinase Substrate
    • Ohomori S., Sakai N., Shirai Y., Yamamoto H., Miyamoto E., Shimizu N., and Saito N. Importance of Protein Kinase C Targeting for the Phosphorylation of Its Substrate, Myristoylated Alanine-rich C-kinase Substrate. J. Biol. Chem. 275 (2000) 26449-26457
    • (2000) J. Biol. Chem. , vol.275 , pp. 26449-26457
    • Ohomori, S.1    Sakai, N.2    Shirai, Y.3    Yamamoto, H.4    Miyamoto, E.5    Shimizu, N.6    Saito, N.7
  • 13
    • 0028361026 scopus 로고
    • Phosphorylation Reverses the Membrane Association of Peptides that Correspond to the Basic Domains of MARCKS and Neuromodulin
    • Kim J., Blackshear P.J., Johnson J.D., and McLaughlin S. Phosphorylation Reverses the Membrane Association of Peptides that Correspond to the Basic Domains of MARCKS and Neuromodulin. Biophys. J. 67 (1994) 227-237
    • (1994) Biophys. J. , vol.67 , pp. 227-237
    • Kim, J.1    Blackshear, P.J.2    Johnson, J.D.3    McLaughlin, S.4
  • 14
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions
    • McLaughlin S., and Aderem A. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. TIBS 20 (1995) 272-276
    • (1995) TIBS , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 15
    • 0029780527 scopus 로고    scopus 로고
    • Molecular Determinants of the Myristoyl-electrostatic Switch of MARCKS
    • Seykora J.T., Myat M.M., Allen L.-A.H., Ravetch J.V., and Aderem A. Molecular Determinants of the Myristoyl-electrostatic Switch of MARCKS. J. Biol. Chem. 271 (1996) 18797-18802
    • (1996) J. Biol. Chem. , vol.271 , pp. 18797-18802
    • Seykora, J.T.1    Myat, M.M.2    Allen, L.-A.H.3    Ravetch, J.V.4    Aderem, A.5
  • 16
    • 0001704947 scopus 로고    scopus 로고
    • MARCKS regulates membrane ruffling and cell spreading
    • Myat M.M., Anderson S., Allen L.-A.H., and Aderem A. MARCKS regulates membrane ruffling and cell spreading. Curr. Biol. 7 (1997) 611-614
    • (1997) Curr. Biol. , vol.7 , pp. 611-614
    • Myat, M.M.1    Anderson, S.2    Allen, L.-A.H.3    Aderem, A.4
  • 17
    • 0031795796 scopus 로고    scopus 로고
    • MARCKS, membranes, and calmodulin: kinetics of their interaction
    • Arbuzova A., Murray D., and McLaughlin S. MARCKS, membranes, and calmodulin: kinetics of their interaction. Biochim. Biophys. Acta 1376 (1998) 369-379
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 369-379
    • Arbuzova, A.1    Murray, D.2    McLaughlin, S.3
  • 18
    • 35448979574 scopus 로고    scopus 로고
    • The Role of Electrostatic and Nonpolar Interactions in the Association of Peripheral Proteins with Membranes
    • Murray D., Arbuzova A., Honig B., and McLaughlin S. The Role of Electrostatic and Nonpolar Interactions in the Association of Peripheral Proteins with Membranes. Curr. Top. Membranes 52 (2002) 277-307
    • (2002) Curr. Top. Membranes , vol.52 , pp. 277-307
    • Murray, D.1    Arbuzova, A.2    Honig, B.3    McLaughlin, S.4
  • 19
    • 0037821876 scopus 로고    scopus 로고
    • Binding of Peptides with Basic and Aromatic Residues to Bilayer Membranes
    • Zhang W., Crocker E., McLaughlin S., and Smith S.O. Binding of Peptides with Basic and Aromatic Residues to Bilayer Membranes. J. Biol. Chem. 278 (2003) 21459-21466
    • (2003) J. Biol. Chem. , vol.278 , pp. 21459-21466
    • Zhang, W.1    Crocker, E.2    McLaughlin, S.3    Smith, S.O.4
  • 20
    • 0029921472 scopus 로고    scopus 로고
    • Membrane Structure of Protein Kinase C and Calmodulin Binding Domain of Myristoylated Alanine Rich C Kinase Substrate Determined by Site-Directed Spin Labeling
    • Qin Z., and Cafiso D.S. Membrane Structure of Protein Kinase C and Calmodulin Binding Domain of Myristoylated Alanine Rich C Kinase Substrate Determined by Site-Directed Spin Labeling. Biochemistry 35 (1996) 2917-2925
    • (1996) Biochemistry , vol.35 , pp. 2917-2925
    • Qin, Z.1    Cafiso, D.S.2
  • 21
    • 0039182142 scopus 로고    scopus 로고
    • Interactions Controlling the Membrane Binding of Basic Protein Domains: Phenylalanine and the Attachment of the Myristoylated Alanine-rich C-Kinase Substrate Protein to Interfaces
    • Victor K., Jacob J., and Cafiso D.S. Interactions Controlling the Membrane Binding of Basic Protein Domains: Phenylalanine and the Attachment of the Myristoylated Alanine-rich C-Kinase Substrate Protein to Interfaces. Biochemistry 38 (1999) 12527-12536
    • (1999) Biochemistry , vol.38 , pp. 12527-12536
    • Victor, K.1    Jacob, J.2    Cafiso, D.S.3
  • 22
    • 0037134540 scopus 로고    scopus 로고
    • Myristoylated Alanine Rich C Kinase Substrate (MARCKS) Sequesters spin-labeled Phosphatidylinositol 4,5-Biphosphate in Lipid Bilayers
    • Rauch M.E., Ferguson C.G., Prestwich G.D., and Cafiso D.S. Myristoylated Alanine Rich C Kinase Substrate (MARCKS) Sequesters spin-labeled Phosphatidylinositol 4,5-Biphosphate in Lipid Bilayers. J. Biol. Chem. 266 (2002) 14068-14076
    • (2002) J. Biol. Chem. , vol.266 , pp. 14068-14076
    • Rauch, M.E.1    Ferguson, C.G.2    Prestwich, G.D.3    Cafiso, D.S.4
  • 23
    • 0141754072 scopus 로고    scopus 로고
    • Location of the Myristoylated Alanine Rich C Kinase Substrate (MARCKS) Effector Domain in Negatively Charged Phospholipid Bicells
    • Ellena J.F., Burnitz M.C., and Cafiso D.S. Location of the Myristoylated Alanine Rich C Kinase Substrate (MARCKS) Effector Domain in Negatively Charged Phospholipid Bicells. Biophys. J. 85 (2003) 2442:2448
    • (2003) Biophys. J. , vol.85
    • Ellena, J.F.1    Burnitz, M.C.2    Cafiso, D.S.3
  • 25
    • 4143120995 scopus 로고    scopus 로고
    • Fluorescence Correlation Spectroscopy Studies of Peptide and Protein Binding to Phospholipid Vesicles
    • Rusu L., Gambhir A., McLaughlin S., and Rädler J. Fluorescence Correlation Spectroscopy Studies of Peptide and Protein Binding to Phospholipid Vesicles. Biophys. J. 87 (2004) 1044-1053
    • (2004) Biophys. J. , vol.87 , pp. 1044-1053
    • Rusu, L.1    Gambhir, A.2    McLaughlin, S.3    Rädler, J.4
  • 27
    • 77957063705 scopus 로고    scopus 로고
    • Structural Properties and Interactions of Thin Films at the Air-Liquid Interface Explored by Synchrotron X-ray Scattering
    • Jensen T.R., and Kjaer K. Structural Properties and Interactions of Thin Films at the Air-Liquid Interface Explored by Synchrotron X-ray Scattering. Studies in Interface Sci. 11 (2001) 205-254
    • (2001) Studies in Interface Sci. , vol.11 , pp. 205-254
    • Jensen, T.R.1    Kjaer, K.2
  • 28
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: a structural perspective
    • Lee A.G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta 1612 (2003) 1-40
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 29
    • 0032911920 scopus 로고    scopus 로고
    • Bacterial S-Layer Protein Coupling to Lipids: X-Ray Reflectivity and Gracing Incidence Diffraction Studies
    • Weygand M., Wetzer B., Pum D., Sleytr U.B., Cuvillier N., Kjaer K., Howes P.B., and Lösche M. Bacterial S-Layer Protein Coupling to Lipids: X-Ray Reflectivity and Gracing Incidence Diffraction Studies. Biophys. J. 76 (1999) 458-468
    • (1999) Biophys. J. , vol.76 , pp. 458-468
    • Weygand, M.1    Wetzer, B.2    Pum, D.3    Sleytr, U.B.4    Cuvillier, N.5    Kjaer, K.6    Howes, P.B.7    Lösche, M.8
  • 31
    • 0029757993 scopus 로고    scopus 로고
    • Hisactophilin-Mediated Binding of Actin to Lipid Lamellae: A Neutron Reflectivity Study of Protein Membrane Coupling
    • Naumann C., Dietrich C., Behrisch A., Bayerl T., Schleicher M., Bucknall D., and Sackmann E. Hisactophilin-Mediated Binding of Actin to Lipid Lamellae: A Neutron Reflectivity Study of Protein Membrane Coupling. Biophys. J. 71 (1996) 811-823
    • (1996) Biophys. J. , vol.71 , pp. 811-823
    • Naumann, C.1    Dietrich, C.2    Behrisch, A.3    Bayerl, T.4    Schleicher, M.5    Bucknall, D.6    Sackmann, E.7
  • 32
    • 0001010247 scopus 로고    scopus 로고
    • Structure of Phospholipid Monolayers Containing Poly(ethylene glycol) Lipids at the Air-Water Interface
    • Majewski J., Kuhl T.L., Gerstenberg M.C., Israelachvili J.N., and Smith G.S. Structure of Phospholipid Monolayers Containing Poly(ethylene glycol) Lipids at the Air-Water Interface. J. Phys. Chem. B 101 (1997) 3122-3129
    • (1997) J. Phys. Chem. B , vol.101 , pp. 3122-3129
    • Majewski, J.1    Kuhl, T.L.2    Gerstenberg, M.C.3    Israelachvili, J.N.4    Smith, G.S.5
  • 33
    • 0000638087 scopus 로고    scopus 로고
    • Neutron scattering for surface characterization
    • Penfold J. Neutron scattering for surface characterization. Curr. Sci. 78 (2000) 1458-1466
    • (2000) Curr. Sci. , vol.78 , pp. 1458-1466
    • Penfold, J.1
  • 34
    • 33751315453 scopus 로고    scopus 로고
    • Interaction of the Neurotransmitter, Neuropeptide Y, with Phospholipid Membranes: Film Balance and Fluorescence Microscopy Studies
    • Dyck M., and Lösche M. Interaction of the Neurotransmitter, Neuropeptide Y, with Phospholipid Membranes: Film Balance and Fluorescence Microscopy Studies. J. Phys. Chem. B 110 (2006) 22143-22151
    • (2006) J. Phys. Chem. B , vol.110 , pp. 22143-22151
    • Dyck, M.1    Lösche, M.2
  • 35
    • 0042222203 scopus 로고    scopus 로고
    • Effect of hydrophobic surfactant peptides SP-B and SP-C on binary phospholipid monolayers. I. Fluorescence and dark-field microscopy
    • Krüger P., Schalke M., Wang Z., Notter R.H., Dluhy R.A., and Lösche M. Effect of hydrophobic surfactant peptides SP-B and SP-C on binary phospholipid monolayers. I. Fluorescence and dark-field microscopy. Biophys. J. 77 (1999) 943-952
    • (1999) Biophys. J. , vol.77 , pp. 943-952
    • Krüger, P.1    Schalke, M.2    Wang, Z.3    Notter, R.H.4    Dluhy, R.A.5    Lösche, M.6
  • 38
    • 0343621506 scopus 로고    scopus 로고
    • Submolecular organization of DMPA in surface monolayers: beyond the two-layer model
    • Schalke M., Krüger P., Weygand M., and Lösche M. Submolecular organization of DMPA in surface monolayers: beyond the two-layer model. Biochim. Biophys. Acta 1464 (2000) 113-126
    • (2000) Biochim. Biophys. Acta , vol.1464 , pp. 113-126
    • Schalke, M.1    Krüger, P.2    Weygand, M.3    Lösche, M.4
  • 39
    • 0034353627 scopus 로고    scopus 로고
    • Structural models of lipid surface monolayers from x-ray and neutron reflectivity measurements
    • Schalke M., and Lösche M. Structural models of lipid surface monolayers from x-ray and neutron reflectivity measurements. Adv. Colloid Interface Sci. 88 (2000) 243-274
    • (2000) Adv. Colloid Interface Sci. , vol.88 , pp. 243-274
    • Schalke, M.1    Lösche, M.2
  • 40
    • 0031820877 scopus 로고    scopus 로고
    • Phospholipid Component Volumes: Determination and Application to Bilayer Structure Calculations
    • Armen R.S., Uitto O.D., and Feller S.E. Phospholipid Component Volumes: Determination and Application to Bilayer Structure Calculations. Biophys. J. 75 (1998) 734-744
    • (1998) Biophys. J. , vol.75 , pp. 734-744
    • Armen, R.S.1    Uitto, O.D.2    Feller, S.E.3
  • 42
    • 26144449160 scopus 로고
    • Surface studies of solids by total reflection of x-rays
    • Parratt L.G. Surface studies of solids by total reflection of x-rays. Phys. Rev. 95 (1954) 359-369
    • (1954) Phys. Rev. , vol.95 , pp. 359-369
    • Parratt, L.G.1
  • 43
    • 0025797495 scopus 로고
    • Structural properties of phosphatidylcholine in a monolayer at the air/water interface
    • Vaknin D., Kjaer K., Als-Nielsen J., and Lösche M. Structural properties of phosphatidylcholine in a monolayer at the air/water interface. Biophys. J. 59 (1991) 1325-1332
    • (1991) Biophys. J. , vol.59 , pp. 1325-1332
    • Vaknin, D.1    Kjaer, K.2    Als-Nielsen, J.3    Lösche, M.4
  • 44
    • 0032542056 scopus 로고    scopus 로고
    • Interaction of the Effector Domain of MARCKS and MARCKS-Related Protein with Lipid Membranes Revealed by Electric Potential Measurements
    • Bähr G., Diederich A., Vergères G., and Winterhalter M. Interaction of the Effector Domain of MARCKS and MARCKS-Related Protein with Lipid Membranes Revealed by Electric Potential Measurements. Biochemistry 37 (1998) 16252-16261
    • (1998) Biochemistry , vol.37 , pp. 16252-16261
    • Bähr, G.1    Diederich, A.2    Vergères, G.3    Winterhalter, M.4
  • 45
    • 51249114388 scopus 로고    scopus 로고
    • Electrostatic Contribution to the Surface Pressure of Charged Monolayers Containing Polyphosphoinositide
    • Levental I., Janmey P.A., and Cebers A. Electrostatic Contribution to the Surface Pressure of Charged Monolayers Containing Polyphosphoinositide. Biophys. J. 95 (2008) 1199-1205
    • (2008) Biophys. J. , vol.95 , pp. 1199-1205
    • Levental, I.1    Janmey, P.A.2    Cebers, A.3
  • 46
    • 1942455262 scopus 로고    scopus 로고
    • Increased Concentration of Polyvalent Phospholipids in the Adsorption Domain of a Charged Protein
    • Haleva E., Ben-Tal N., and Diamant H. Increased Concentration of Polyvalent Phospholipids in the Adsorption Domain of a Charged Protein. Biophys. J. 86 (2004) 2165-2178
    • (2004) Biophys. J. , vol.86 , pp. 2165-2178
    • Haleva, E.1    Ben-Tal, N.2    Diamant, H.3
  • 47
    • 0031456748 scopus 로고    scopus 로고
    • Short-Chain Phosphatidylinositol Conformation and Its Relevance to Phosphatidylinositol-Specific Phospholipase C
    • Zhou C., Garigapati V., and Robert M.F. Short-Chain Phosphatidylinositol Conformation and Its Relevance to Phosphatidylinositol-Specific Phospholipase C. Biochemistry 36 (1997) 15925-15931
    • (1997) Biochemistry , vol.36 , pp. 15925-15931
    • Zhou, C.1    Garigapati, V.2    Robert, M.F.3
  • 48
    • 0033614814 scopus 로고    scopus 로고
    • Orientation of the Headgroup of Phosphatidylinositol in a Model Biomembrane As Determined by Neutron Diffraction
    • Bradshaw J.P., Bushby R.J., Giles C.C.D., and Saunders M.R. Orientation of the Headgroup of Phosphatidylinositol in a Model Biomembrane As Determined by Neutron Diffraction. Biochemistry 38 (1999) 8393-8401
    • (1999) Biochemistry , vol.38 , pp. 8393-8401
    • Bradshaw, J.P.1    Bushby, R.J.2    Giles, C.C.D.3    Saunders, M.R.4
  • 51
    • 0033005969 scopus 로고    scopus 로고
    • Phase separation in phosphatidylinositol/phosphatidylcholine mixed monolayers
    • DeWolf C., Leporatti S., Kirsch C., Klinger R., and Brezesinski G. Phase separation in phosphatidylinositol/phosphatidylcholine mixed monolayers. Chem. Phys. Lip. 97 (1999) 129-138
    • (1999) Chem. Phys. Lip. , vol.97 , pp. 129-138
    • DeWolf, C.1    Leporatti, S.2    Kirsch, C.3    Klinger, R.4    Brezesinski, G.5
  • 52
    • 0035942978 scopus 로고    scopus 로고
    • The distribution of polyphosphoinositides in lipid films
    • Foster W.J., and Janmey P.A. The distribution of polyphosphoinositides in lipid films. Biophys. Chem. 91 (2001) 211-218
    • (2001) Biophys. Chem. , vol.91 , pp. 211-218
    • Foster, W.J.1    Janmey, P.A.2
  • 53
    • 33746058677 scopus 로고    scopus 로고
    • Absence of clustering of phosphatidylinositol-(4,5)-biphosphate in fluid phosphatidylcholine
    • Fernandes F., Loura L.M.S., Fedorov A., and Prieto M. Absence of clustering of phosphatidylinositol-(4,5)-biphosphate in fluid phosphatidylcholine. J. Lip. Res. 47 (2006) 1521-1525
    • (2006) J. Lip. Res. , vol.47 , pp. 1521-1525
    • Fernandes, F.1    Loura, L.M.S.2    Fedorov, A.3    Prieto, M.4
  • 54
    • 0018795945 scopus 로고
    • A Comparative Study of the Phase Transitions of Phospholipid Bilayers and Monolayers
    • Blume A. A Comparative Study of the Phase Transitions of Phospholipid Bilayers and Monolayers. Biochim. Biophys. Acta 557 (1979) 32-44
    • (1979) Biochim. Biophys. Acta , vol.557 , pp. 32-44
    • Blume, A.1
  • 55
    • 7044274626 scopus 로고    scopus 로고
    • Lipids in membrane protein structures
    • Palsdottir H., and Hunte C. Lipids in membrane protein structures. Biochim. Biophys. Acta 1666 (2004) 2-18
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 2-18
    • Palsdottir, H.1    Hunte, C.2
  • 56
    • 0029100115 scopus 로고
    • Interaction of Small Peptides with Lipid Bilayers
    • Damoran K.V., Merz K.M., and Gaber B.P. Interaction of Small Peptides with Lipid Bilayers. Biophys. J. 69 (1995) 1299-1308
    • (1995) Biophys. J. , vol.69 , pp. 1299-1308
    • Damoran, K.V.1    Merz, K.M.2    Gaber, B.P.3


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