메뉴 건너뛰기




Volumn 16, Issue 9, 2010, Pages 1055-1062

Development of agents that modulate protein-protein interactions in membranes

Author keywords

Integral membrane proteins; Peptide; Protein protein interactions; Rational drug design; Transmembrane domains

Indexed keywords

AMINO ACID DERIVATIVE; MEMBRANE PROTEIN;

EID: 77950262907     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161210790963878     Document Type: Review
Times cited : (7)

References (94)
  • 1
    • 0035987407 scopus 로고    scopus 로고
    • The post-genomic era of interactive proteomics: Facts and perspectives
    • Auerbach D, Thaminy S, Hottiger MO, Stagljar I. The post-genomic era of interactive proteomics: facts and perspectives. Proteomics 2002; 2: 611-623
    • (2002) Proteomics , vol.2 , pp. 611-623
    • Auerbach, D.1    Thaminy, S.2    Hottiger, M.O.3    Stagljar, I.4
  • 2
    • 0037810425 scopus 로고    scopus 로고
    • Identification of novel ErbB3-interacting factors using the split-ubiquitin membrane yeast two-hybrid system
    • Thaminy S, Auerbach D, Arnoldo A, Stagljar I. Identification of novel ErbB3-interacting factors using the split-ubiquitin membrane yeast two-hybrid system. Genome Res 2003; 13: 1744-1753
    • (2003) Genome Res , vol.13 , pp. 1744-1753
    • Thaminy, S.1    Auerbach, D.2    Arnoldo, A.3    Stagljar, I.4
  • 4
    • 33846399142 scopus 로고    scopus 로고
    • E(z), A depth-dependent potential for assessing the energies of insertion of amino acid side-chains into membranes: Derivation and applications to determining the orientation of transmembrane and interfacial helices
    • Senes A, Chadi DC, Law PB, Walters RF, Nanda V, Degrado WF. E(z), a depth-dependent potential for assessing the energies of insertion of amino acid side-chains into membranes: derivation and applications to determining the orientation of transmembrane and interfacial helices. J Mol Biol 2007; 366: 436-448
    • (2007) J Mol Biol , vol.366 , pp. 436-448
    • Senes, A.1    Chadi, D.C.2    Law, P.B.3    Walters, R.F.4    Nanda, V.5    Degrado, W.F.6
  • 5
    • 23044512120 scopus 로고    scopus 로고
    • Rational combinatorial design of pore-forming beta-sheet peptides
    • Rausch JM, Marks JR, Wimley WC. Rational combinatorial design of pore-forming beta-sheet peptides. Proc Natl Acad Sci USA 2005; 102: 10511-10515
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10511-10515
    • Rausch, J.M.1    Marks, J.R.2    Wimley, W.C.3
  • 6
    • 35649005895 scopus 로고    scopus 로고
    • β-sheet pore-forming peptides selected from a rational combinatorial library: Mechanism of pore formation in lipid vesicles and activity in biological membranes
    • Rausch JM, Marks JR, Rathinakumar R, Wimley WC. β-sheet pore-forming peptides selected from a rational combinatorial library: mechanism of pore formation in lipid vesicles and activity in biological membranes. Biochemistry 2007; 46: 12124-12139
    • (2007) Biochemistry , vol.46 , pp. 12124-12139
    • Rausch, J.M.1    Marks, J.R.2    Rathinakumar, R.3    Wimley, W.C.4
  • 7
    • 2142762954 scopus 로고    scopus 로고
    • Selection and characterization of small random transmembrane proteins that bind and activate the platelet-derived growth factor beta receptor
    • Freeman-Cook LL, Dixon AM, Frank JB, Xia Y, Ely L, Gerstein M, et al. Selection and characterization of small random transmembrane proteins that bind and activate the platelet-derived growth factor beta receptor. J Mol Biol 2004; 338: 907-920
    • (2004) J Mol Biol , vol.338 , pp. 907-920
    • Freeman-Cook, L.L.1    Dixon, A.M.2    Frank, J.B.3    Xia, Y.4    Ely, L.5    Gerstein, M.6
  • 8
    • 1642570286 scopus 로고    scopus 로고
    • Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol
    • Mitra K, Ubarretxena-Belandia I, Taguchi T, Warren G, Engelman DM. Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol. Proc Natl Acad Sci USA 2004; 101: 4083-4088
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4083-4088
    • Mitra, K.1    Ubarretxena-Belandia, I.2    Taguchi, T.3    Warren, G.4    Engelman, D.M.5
  • 9
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membranes
    • Mouritsen OG, Bloom M. Mattress model of lipid-protein interactions in membranes. Biophys J 1984; 46: 141-153
    • (1984) Biophys J , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Bloom, M.2
  • 10
    • 0032863720 scopus 로고    scopus 로고
    • Structure of dipalmitoylphosphatidylcholine/cholesterol bilayer at low and high cholesterol concentrations: Molecular dynamics simulation
    • Smondyrev AM, Berkowitz ML. Structure of dipalmitoylphosphatidylcholine/ cholesterol bilayer at low and high cholesterol concentrations: molecular dynamics simulation. Biophys J 1999; 77: 2075-2089
    • (1999) Biophys J , vol.77 , pp. 2075-2089
    • Smondyrev, A.M.1    Berkowitz, M.L.2
  • 11
    • 0026704101 scopus 로고
    • Combined influence of cholesterol and synthetic amphiphillic peptides upon bilayer thickness in model membranes
    • Nezil FA, Bloom M. Combined influence of cholesterol and synthetic amphiphillic peptides upon bilayer thickness in model membranes. Biophys J 1992; 61: 1176-1183
    • (1992) Biophys J , vol.61 , pp. 1176-1183
    • Nezil, F.A.1    Bloom, M.2
  • 12
    • 0020724172 scopus 로고
    • Molecular organization in cholesterol-lecithin bilayers by X-ray and electron diffraction measurements
    • Hui SW, He NB. Molecular organization in cholesterol-lecithin bilayers by X-ray and electron diffraction measurements. Biochemistry 1983; 22: 1159-1164
    • (1983) Biochemistry , vol.22 , pp. 1159-1164
    • Hui, S.W.1    He, N.B.2
  • 13
    • 0015243222 scopus 로고
    • Lipid bilayer structure in the membrane of Mycoplasma laidlawii
    • Engelman DM. Lipid bilayer structure in the membrane of Mycoplasma laidlawii. J Mol Biol 1971; 58: 153-165
    • (1971) J Mol Biol , vol.58 , pp. 153-165
    • Engelman, D.M.1
  • 14
    • 0021104058 scopus 로고
    • Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
    • Lewis BA, Engelman DM. Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles. J Mol Biol 1983; 166: 211-217
    • (1983) J Mol Biol , vol.166 , pp. 211-217
    • Lewis, B.A.1    Engelman, D.M.2
  • 15
    • 0025990802 scopus 로고
    • Sequences within and adjacent to the transmembrane segment of α-2,6-sialyltransferase specify Golgi retention
    • Munro S. Sequences within and adjacent to the transmembrane segment of α-2,6-sialyltransferase specify Golgi retention. EMBO J 1991; 10: 3577-3588
    • (1991) EMBO J , vol.10 , pp. 3577-3588
    • Munro, S.1
  • 16
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro S. An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J 1995; 14: 4695-4704
    • (1995) EMBO J , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 17
    • 0000064076 scopus 로고
    • Evaluation of methods for the prediction of membrane protein secondary structures
    • Wallace BA, Cascio M, Mielke DL. Evaluation of methods for the prediction of membrane protein secondary structures. Proc Natl Acad Sci USA 1986; 83: 9423-9427
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 9423-9427
    • Wallace, B.A.1    Cascio, M.2    Mielke, D.L.3
  • 18
    • 0028458257 scopus 로고
    • A measure of helical propensity for amino acids in membrane environments
    • Li SC, Deber CM. A measure of helical propensity for amino acids in membrane environments. Nat Struct Biol 1994; 1: 368-373
    • (1994) Nat Struct Biol , vol.1 , pp. 368-373
    • Li, S.C.1    Deber, C.M.2
  • 19
    • 0027438289 scopus 로고
    • Peptide environment specifies conformation. Helicity of hydrophobic segments compared in aqueous, organic, and membrane environments
    • Li SC, Deber CM. Peptide environment specifies conformation. Helicity of hydrophobic segments compared in aqueous, organic, and membrane environments. J Biol Chem 1993; 268: 22975-22978
    • (1993) J Biol Chem , vol.268 , pp. 22975-22978
    • Li, S.C.1    Deber, C.M.2
  • 20
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White SH, Wimley WC. Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct 1999; 28: 319-365
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 21
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • Hessa T, Kim H, Bihlmaier K, Lundin C, Boekel J, Andersson H, et al. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 2005; 433: 377-381
    • (2005) Nature , vol.433 , pp. 377-381
    • Hessa, T.1    Kim, H.2    Bihlmaier, K.3    Lundin, C.4    Boekel, J.5    Andersson, H.6
  • 22
    • 33748791763 scopus 로고    scopus 로고
    • Helix-packing motifs in membrane proteins
    • Walters RF, DeGrado WF. Helix-packing motifs in membrane proteins. Proc Natl Acad Sci USA 2006; 103: 13658-13663
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13658-13663
    • Walters, R.F.1    Degrado, W.F.2
  • 24
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ WP, Engelman DM. The GxxxG motif: a framework for transmembrane helix-helix association. J Mol Biol 2000; 296: 911-919
    • (2000) J Mol Biol , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 25
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie JU. Solving the membrane protein folding problem. Nature 2005; 438: 581-589
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 26
    • 0037379072 scopus 로고    scopus 로고
    • How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles
    • DeGrado WF, Gratkowski H, Lear JD. How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles. Protein Sci 2003; 12: 647-665
    • (2003) Protein Sci , vol.12 , pp. 647-665
    • Degrado, W.F.1    Gratkowski, H.2    Lear, J.D.3
  • 27
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: The role of polar, GxxxG-like and proline motifs
    • Senes A, Engel DE, DeGrado WF. Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr Opin Struct Biol 2004; 14: 465-479
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 28
    • 0036568229 scopus 로고    scopus 로고
    • Interhelical hydrogen bonds and spatial motifs in membrane proteins: Polar clamps and serine zippers
    • Adamian L, Liang J. Interhelical hydrogen bonds and spatial motifs in membrane proteins: polar clamps and serine zippers. Proteins 2002; 47: 209-218
    • (2002) Proteins , vol.47 , pp. 209-218
    • Adamian, L.1    Liang, J.2
  • 29
    • 26444611461 scopus 로고    scopus 로고
    • Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins
    • Kim S, Jeon TJ, Oberai A, Yang D, Schmidt JJ, Bowie JU. Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. Proc Natl Acad Sci USA 2005; 102: 14278-14283
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14278-14283
    • Kim, S.1    Jeon, T.J.2    Oberai, A.3    Yang, D.4    Schmidt, J.J.5    Bowie, J.U.6
  • 31
    • 0035979146 scopus 로고    scopus 로고
    • The Cα - H...O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • Senes A, Ubarretxena-Belandia I, Engelman DM. The Cα - H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions. Proc Natl Acad Sci USA 2001; 98: 9056-9061
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 32
    • 0032817780 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: Role of glycine in transmembrane helix association
    • Javadpour MM, Eilers M, Groesbeek M, Smith SO. Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association. Biophys J 1999; 77: 1609-1618
    • (1999) Biophys J , vol.77 , pp. 1609-1618
    • Javadpour, M.M.1    Eilers, M.2    Groesbeek, M.3    Smith, S.O.4
  • 33
    • 0032584233 scopus 로고    scopus 로고
    • Structure-based prediction of the stability of transmembrane helix-helix interactions: The sequence dependence of glycophorin A dimerization
    • MacKenzie KR, Engelman DM. Structure-based prediction of the stability of transmembrane helix-helix interactions: the sequence dependence of glycophorin A dimerization. Proc Natl Acad Sci USA 1998; 95: 3583-3590
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3583-3590
    • MacKenzie, K.R.1    Engelman, D.M.2
  • 34
    • 0024346677 scopus 로고
    • Hydrophobic organization of membrane proteins
    • Rees DC, DeAntonio L, Eisenberg D. Hydrophobic organization of membrane proteins. Science 1989; 245: 510-513
    • (1989) Science , vol.245 , pp. 510-513
    • Rees, D.C.1    Deantonio, L.2    Eisenberg, D.3
  • 36
    • 0037414434 scopus 로고    scopus 로고
    • Functional role of C(α)-H...O hydrogen bonds between transmembrane α-helices in photosystem I
    • Loll B, Raszewski G, Saenger W, Biesiadka J. Functional role of C(α)-H...O hydrogen bonds between transmembrane α-helices in photosystem I. J Mol Biol 2003; 328: 737-747
    • (2003) J Mol Biol , vol.328 , pp. 737-747
    • Loll, B.1    Raszewski, G.2    Saenger, W.3    Biesiadka, J.4
  • 38
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski H, Lear JD, DeGrado WF. Polar side chains drive the association of model transmembrane peptides. Proc Natl Acad Sci USA 2001; 98: 880-885
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    Degrado, W.F.3
  • 40
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • Russ WP, Engelman DM. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc Natl Acad Sci USA 1999; 96: 863-868
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 41
    • 0036301006 scopus 로고    scopus 로고
    • Motifs of serine and threonine can drive association of transmembrane helices
    • Dawson JP, Weinger JS, Engelman DM. Motifs of serine and threonine can drive association of transmembrane helices. J Mol Biol 2002; 316: 799-805.
    • (2002) J Mol Biol , vol.316 , pp. 799-805
    • Dawson, J.P.1    Weinger, J.S.2    Engelman, D.M.3
  • 42
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 43
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 2003; 55: 27-55.
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 44
    • 0041428149 scopus 로고    scopus 로고
    • The versatile β-barrel membrane protein
    • Wimley WC. The versatile β-barrel membrane protein. Curr Opin Struct Biol 2003; 13: 404-411
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 45
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley WC, White SH. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat Struct Biol 1996; 3: 842-848
    • (1996) Nat Struct Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 46
    • 0030000062 scopus 로고    scopus 로고
    • Using self-assembled monolayers to understand the interactions of man-made surfaces with proteins and cells
    • Mrksich M, Whitesides GM. Using self-assembled monolayers to understand the interactions of man-made surfaces with proteins and cells. Annu Rev Biophys Biomol Struct 1996; 25: 55-78.
    • (1996) Annu Rev Biophys Biomol Struct , vol.25 , pp. 55-78
    • Mrksich, M.1    Whitesides, G.M.2
  • 47
    • 0346216990 scopus 로고    scopus 로고
    • Synthesis and screening of "one-bead one-compound" combinatorial peptide libraries
    • Lam KS, Lehman AL, Song A, Doan N, Enstrom AM, Maxwell J, et al. Synthesis and screening of "one-bead one-compound" combinatorial peptide libraries. Methods Enzymol 2003; 369: 298-322.
    • (2003) Methods Enzymol , vol.369 , pp. 298-322
    • Lam, K.S.1    Lehman, A.L.2    Song, A.3    Doan, N.4    Enstrom, A.M.5    Maxwell, J.6
  • 48
    • 0035876283 scopus 로고    scopus 로고
    • A high-throughput screen for identifying transmembrane pore-forming peptides
    • Rausch JM, Wimley WC. A high-throughput screen for identifying transmembrane pore-forming peptides. Anal Biochem 2001; 293: 258-263
    • (2001) Anal Biochem , vol.293 , pp. 258-263
    • Rausch, J.M.1    Wimley, W.C.2
  • 49
    • 0347755460 scopus 로고    scopus 로고
    • APD: The antimicrobial peptide database
    • Wang Z, Wang G. APD: the antimicrobial peptide database. Nucleic Acids Res 2004; 32: D590-2.
    • (2004) Nucleic Acids Res , vol.32
    • Wang, Z.1    Wang, G.2
  • 51
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S, Song O. A novel genetic system to detect protein-protein interactions. Nature 1989; 340: 245-246
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 52
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz P, Giot L, Cagney G, Mansfield TA, Judson RS, Knight JR, et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 2000; 403: 623-627
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.A.4    Judson, R.S.5    Knight, J.R.6
  • 54
    • 0032574840 scopus 로고    scopus 로고
    • A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
    • Stagljar I, Korostensky C, Johnsson N, te Heesen S. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc Natl Acad Sci USA 1998; 95: 5187-5192
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5187-5192
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    Te Heesen, S.4
  • 55
    • 0036849482 scopus 로고    scopus 로고
    • Analysis of membrane protein interactions using yeast-based technologies
    • Stagljar I, Fields S. Analysis of membrane protein interactions using yeast-based technologies. Trends Biochem Sci 2002; 27: 559-563
    • (2002) Trends Biochem Sci , vol.27 , pp. 559-563
    • Stagljar, I.1    Fields, S.2
  • 56
    • 0033515557 scopus 로고    scopus 로고
    • A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments
    • Gurezka R, Laage R, Brosig B, Langosch D. A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments. J Biol Chem 1999; 274: 9265-9270
    • (1999) J Biol Chem , vol.274 , pp. 9265-9270
    • Gurezka, R.1    Laage, R.2    Brosig, B.3    Langosch, D.4
  • 57
    • 2342477732 scopus 로고    scopus 로고
    • Structural adaptation of the glycophorin A transmembrane homodimer to D-amino acid modifications
    • Gerber D, Sal-Man N, Shai Y. Structural adaptation of the glycophorin A transmembrane homodimer to D-amino acid modifications. J Mol Biol 2004; 339: 243-250
    • (2004) J Mol Biol , vol.339 , pp. 243-250
    • Gerber, D.1    Sal-Man, N.2    Shai, Y.3
  • 58
    • 68649098555 scopus 로고    scopus 로고
    • Hill coefficient analysis of transmembrane helix dimerization
    • Soong R, Merzlyakov M, Hristova K. Hill coefficient analysis of transmembrane helix dimerization. J Membr Biol 2009; 230: 49-55.
    • (2009) J Membr Biol , vol.230 , pp. 49-55
    • Soong, R.1    Merzlyakov, M.2    Hristova, K.3
  • 59
    • 58249091559 scopus 로고    scopus 로고
    • Forster resonance energy transfer measurements of transmembrane helix dimerization energetics
    • Merzlyakov M, Hristova K. Forster resonance energy transfer measurements of transmembrane helix dimerization energetics. Methods Enzymol 2008; 450: 107-127
    • (2008) Methods Enzymol , vol.450 , pp. 107-127
    • Merzlyakov, M.1    Hristova, K.2
  • 60
    • 0023082137 scopus 로고
    • Receptors for epidermal growth factor and other polypeptide mitogens
    • Carpenter G. Receptors for epidermal growth factor and other polypeptide mitogens. Annu Rev Biochem 1987; 56: 881-914.
    • (1987) Annu Rev Biochem , vol.56 , pp. 881-914
    • Carpenter, G.1
  • 61
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin CH. Dimerization of cell surface receptors in signal transduction. Cell 1995; 80: 213-223
    • (1995) Cell , vol.80 , pp. 213-223
    • Ch, H.1
  • 62
    • 0031726412 scopus 로고    scopus 로고
    • Virocrine transformation: The intersection between viral transforming proteins and cellular signal transduction pathways
    • DiMaio D, Lai CC, Klein O. Virocrine transformation: the intersection between viral transforming proteins and cellular signal transduction pathways. Annu Rev Microbiol 1998; 52: 397-421.
    • (1998) Annu Rev Microbiol , vol.52 , pp. 397-421
    • Dimaio, D.1    Lai, C.C.2    Klein, O.3
  • 63
    • 0022539283 scopus 로고
    • The E5 transforming gene of bovine papillomavirus encodes a small, hydrophobic polypeptide
    • Schlegel R, Wade-Glass M, Rabson MS, Yang YC. The E5 transforming gene of bovine papillomavirus encodes a small, hydrophobic polypeptide. Science 1986; 233: 464-467
    • (1986) Science , vol.233 , pp. 464-467
    • Schlegel, R.1    Wade-Glass, M.2    Rabson, M.S.3    Yang, Y.C.4
  • 64
    • 0035963317 scopus 로고    scopus 로고
    • Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein
    • Mattoon D, Gupta K, Doyon J, Loll PJ, DiMaio D. Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein. Oncogene 2001; 20: 3824-3834
    • (2001) Oncogene , vol.20 , pp. 3824-3834
    • Mattoon, D.1    Gupta, K.2    Doyon, J.3    Loll, P.J.4    Dimaio, D.5
  • 65
    • 0028338904 scopus 로고
    • Cellular transformation by a transmembrane peptide: Structural requirements for the bovine papillomavirus E5 oncoprotein
    • Meyer AN, Xu YF, Webster MK, Smith AE, Donoghue DJ. Cellular transformation by a transmembrane peptide: structural requirements for the bovine papillomavirus E5 oncoprotein. Proc Natl Acad Sci USA 1994; 91: 4634-4638
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4634-4638
    • Meyer, A.N.1    Xu, Y.F.2    Webster, M.K.3    Smith, A.E.4    Donoghue, D.J.5
  • 66
    • 2442647912 scopus 로고    scopus 로고
    • Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization
    • Gerber D, Sal-Man N, Shai Y. Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization. J Biol Chem 2004; 279: 21177-21182
    • (2004) J Biol Chem , vol.279 , pp. 21177-21182
    • Gerber, D.1    Sal-Man, N.2    Shai, Y.3
  • 67
    • 0037085373 scopus 로고    scopus 로고
    • The single transmembrane domains of ErbB receptors self-associate in cell membranes
    • Mendrola JM, Berger MB, King MC, Lemmon MA. The single transmembrane domains of ErbB receptors self-associate in cell membranes. J Biol Chem 2002; 277: 4704-4712
    • (2002) J Biol Chem , vol.277 , pp. 4704-4712
    • Mendrola, J.M.1    Berger, M.B.2    King, M.C.3    Ma, L.4
  • 68
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch D, Brosig B, Kolmar H, Fritz HJ. Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J Mol Biol 1996; 263: 525-530
    • (1996) J Mol Biol , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.J.4
  • 69
    • 0035903168 scopus 로고    scopus 로고
    • In vivo detection of hetero-association of glycophorin-A and its mutants within the membrane
    • Gerber D, Shai Y. In vivo detection of hetero-association of glycophorin-A and its mutants within the membrane. J Biol Chem 2001; 276: 31229-31232
    • (2001) J Biol Chem , vol.276 , pp. 31229-31232
    • Gerber, D.1    Shai, Y.2
  • 70
    • 0036385727 scopus 로고    scopus 로고
    • Chirality-independent protein-protein recognition between transmembrane domains in vivo
    • Gerber D, Shai Y. Chirality-independent protein-protein recognition between transmembrane domains in vivo. J Mol Biol 2002; 322: 491-495
    • (2002) J Mol Biol , vol.322 , pp. 491-495
    • Gerber, D.1    Shai, Y.2
  • 71
    • 0026686793 scopus 로고
    • Glycophorin A dimerization is driven by specific interactions between transmembrane α-helices
    • Lemmon MA, Flanagan JM, Hunt JF, Adair BD, Bormann BJ, Dempsey CE, et al. Glycophorin A dimerization is driven by specific interactions between transmembrane α-helices. J Biol Chem 1992; 267: 7683-7689
    • (1992) J Biol Chem , vol.267 , pp. 7683-7689
    • Lemmon, M.A.1    Flanagan, J.M.2    Hunt, J.F.3    Adair, B.D.4    Bormann, B.J.5    Dempsey, C.E.6
  • 72
    • 0030959114 scopus 로고    scopus 로고
    • A subclass of tumor-inhibitory monoclonal antibodies to ErbB-2/HER2 blocks crosstalk with growth factor receptors
    • Klapper LN, Vaisman N, Hurwitz E, Pinkas-Kramarski R, Yarden Y, Sela M. A subclass of tumor-inhibitory monoclonal antibodies to ErbB-2/HER2 blocks crosstalk with growth factor receptors. Oncogene 1997; 14: 2099-2109
    • (1997) Oncogene , vol.14 , pp. 2099-2109
    • Klapper, L.N.1    Vaisman, N.2    Hurwitz, E.3    Pinkas-Kramarski, R.4    Yarden, Y.5    Sela, M.6
  • 73
    • 0033944158 scopus 로고    scopus 로고
    • Inhibition of tumor growth by poly(ethylene glycol) derivatives of anti-ErbB2 antibodies
    • Hurwitz E, Klapper LN, Wilchek M, Yarden Y, Sela M. Inhibition of tumor growth by poly(ethylene glycol) derivatives of anti-ErbB2 antibodies. Cancer Immunol Immunother 2000; 49: 226-234
    • (2000) Cancer Immunol Immunother , vol.49 , pp. 226-234
    • Hurwitz, E.1    Klapper, L.N.2    Wilchek, M.3    Yarden, Y.4    Sela, M.5
  • 75
    • 0033521097 scopus 로고    scopus 로고
    • Inhibition of G-protein-coupled receptor function by disruption of transmembrane domain interactions
    • Tarasova NI, Rice WG, Michejda CJ. Inhibition of G-protein-coupled receptor function by disruption of transmembrane domain interactions. J Biol Chem 1999; 274: 34911-34915
    • (1999) J Biol Chem , vol.274 , pp. 34911-34915
    • Tarasova, N.I.1    Rice, W.G.2    Michejda, C.J.3
  • 76
    • 0028012561 scopus 로고
    • Cloning of a human seven-transmembrane domain receptor, LESTR, that is highly expressed in leukocytes
    • Loetscher M, Geiser T, O'Reilly T, Zwahlen R, Baggiolini M, Moser B. Cloning of a human seven-transmembrane domain receptor, LESTR, that is highly expressed in leukocytes. J Biol Chem 1994; 269: 232-237
    • (1994) J Biol Chem , vol.269 , pp. 232-237
    • Loetscher, M.1    Geiser, T.2    O'Reilly, T.3    Zwahlen, R.4    Baggiolini, M.5    Moser, B.6
  • 77
    • 0032566739 scopus 로고    scopus 로고
    • Testing the charge difference hypothesis for the assembly of a eucaryotic multispanning membrane protein
    • Sato M, Hresko R, Mueckler M. Testing the charge difference hypothesis for the assembly of a eucaryotic multispanning membrane protein. J Biol Chem 1998; 273: 25203-25208
    • (1998) J Biol Chem , vol.273 , pp. 25203-25208
    • Sato, M.1    Hresko, R.2    Mueckler, M.3
  • 78
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger EA, Murphy PM, Farber JM. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu Rev Immunol 1999; 17: 657-700.
    • (1999) Annu Rev Immunol , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 80
    • 0031013825 scopus 로고    scopus 로고
    • T-cell antigen receptor transmembrane peptides modulate T-cell function and T cell-mediated disease
    • Manolios N, Collier S, Taylor J, Pollard J, Harrison LC, Bender V. T-cell antigen receptor transmembrane peptides modulate T-cell function and T cell-mediated disease. Nat Med 1997; 3: 84-88
    • (1997) Nat Med , vol.3 , pp. 84-88
    • Manolios, N.1    Collier, S.2    Taylor, J.3    Pollard, J.4    Harrison, L.C.5    Bender, V.6
  • 81
    • 0027955305 scopus 로고
    • The T cell antigen receptor alpha and beta chains interact via distinct regions with CD3 chains
    • Manolios N, Kemp O, Li ZG. The T cell antigen receptor alpha and beta chains interact via distinct regions with CD3 chains. Eur J Immunol 1994; 24: 84-92.
    • (1994) Eur J Immunol , vol.24 , pp. 84-92
    • Manolios, N.1    Kemp, O.2    Li, Z.G.3
  • 82
    • 0027600318 scopus 로고
    • A gentle method for linking Tris to amino acids and peptides
    • Whittaker RG, Hayes PJ, Bender VJ. A gentle method for linking Tris to amino acids and peptides. Pept Res 1993; 6: 125-128
    • (1993) Pept Res , vol.6 , pp. 125-128
    • Whittaker, R.G.1    Hayes, P.J.2    Bender, V.J.3
  • 83
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • Senes A, Gerstein M, Engelman DM. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions. J Mol Biol 2000; 296: 921-936
    • (2000) J Mol Biol , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 84
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang Y, Lemieux MJ, Song J, Auer M, Wang DN. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 2003; 301: 616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 85
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 a resolution
    • Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, Krauss N. Three-dimensional structure of cyanobacterial photosystem I at 2.5 A resolution. Nature 2001; 411: 909-917
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 86
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: The role of polar, GXXXG-like and proline motifs
    • Senes A, Engel DE, DeGrado WF. Folding of helical membrane proteins: the role of polar, GXXXG-like and proline motifs. Curr Opin Struc Biol 2004; 14: 465-479
    • (2004) Curr Opin Struc Biol , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    Degrado, W.F.3
  • 87
    • 33847668295 scopus 로고    scopus 로고
    • A structurally altered D,L-amino acid TCRα transmembrane peptide interacts with the TCRα and inhibits T-cell activation in vitro and in an animal model
    • Quintana FJ, Gerber D, Bloch I, Cohen IR, Shai Y. A structurally altered D,L-amino acid TCRα transmembrane peptide interacts with the TCRα and inhibits T-cell activation in vitro and in an animal model. Biochemistry 2007; 46: 2317-2325
    • (2007) Biochemistry , vol.46 , pp. 2317-2325
    • Quintana, F.J.1    Gerber, D.2    Bloch, I.3    Cohen, I.R.4    Shai, Y.5
  • 88
    • 7944224560 scopus 로고    scopus 로고
    • Hetero-assembly between all-L- and all-D-amino acid transmembrane domains: Forces involved and implication for inactivation of membrane proteins
    • Sal-Man N, Gerber D, Shai Y. Hetero-assembly between all-L- and all-D-amino acid transmembrane domains: forces involved and implication for inactivation of membrane proteins. J Mol Biol 2004; 344: 855-864
    • (2004) J Mol Biol , vol.344 , pp. 855-864
    • Sal-Man, N.1    Gerber, D.2    Shai, Y.3
  • 90
    • 0031013825 scopus 로고    scopus 로고
    • T-cell antigen receptor transmembrane peptides modulate T-cell function and T cell-mediated disease
    • Manolios N, Collier S, Taylor J, Pollard J, Harrison LC, Bender V. T-cell antigen receptor transmembrane peptides modulate T-cell function and T cell-mediated disease. Nat Med 1997; 3: 84-88
    • (1997) Nat Med , vol.3 , pp. 84-88
    • Manolios, N.1    Collier, S.2    Taylor, J.3    Pollard, J.4    Harrison, L.C.5    Bender, V.6
  • 91
    • 21744458728 scopus 로고    scopus 로고
    • D-enantiomer peptide of the TCR α transmembrane domain inhibits T-cell activation in vitro and in vivo
    • Gerber D, Quintana FJ, Bloch I, Cohen IR, Shai Y. D-enantiomer peptide of the TCR α transmembrane domain inhibits T-cell activation in vitro and in vivo. FASEB J 2005; 19: 1190-1192
    • (2005) FASEB J , vol.19 , pp. 1190-1192
    • Gerber, D.1    Quintana, F.J.2    Bloch, I.3    Cohen, I.R.4    Shai, Y.5
  • 92
    • 70649088038 scopus 로고    scopus 로고
    • Kinases as upstream regulators of the HIF system: Their emerging potential as anti-cancer drug targets
    • Dimova EY, Michiels C, Kietzmann T. Kinases as upstream regulators of the HIF system: their emerging potential as anti-cancer drug targets. Curr Pharm Des 2009; 15(33): 3867-3877
    • (2009) Curr Pharm Des , vol.15 , Issue.33 , pp. 3867-3877
    • Dimova, E.Y.1    Michiels, C.2    Kietzmann, T.3
  • 93
    • 69249115278 scopus 로고    scopus 로고
    • Peptides as signaling inhibitors for mammalian MAP kinase cascades
    • Gaestel M, Kracht M. Peptides as signaling inhibitors for mammalian MAP kinase cascades. Curr Pharm Des 2009; 15(21): 2471-2480
    • (2009) Curr Pharm Des , vol.15 , Issue.21 , pp. 2471-2480
    • Gaestel, M.1    Kracht, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.