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Volumn 4, Issue 2, 2010, Pages 313-324

Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?

Author keywords

Bitopic membrane proteins; Helix helix interactions; Receptors; Transmembrane domains; Transmembrane signaling

Indexed keywords

BITOPIC PROTEIN; GLYCOPHORIN A; MEMBRANE PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 77953584951     PISSN: 19336918     EISSN: 19336926     Source Type: Journal    
DOI: 10.4161/cam.4.2.12430     Document Type: Review
Times cited : (72)

References (178)
  • 1
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • Stevens TJ, Arkin IT. Do more complex organisms have a greater proportion of membrane proteins in their genomes? Proteins 2000; 39:417-20.
    • (2000) Proteins , vol.39 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 3
    • 71749104018 scopus 로고    scopus 로고
    • Computational analysis of membrane proteins: The largest class of drug targets
    • Arinaminpathy Y, Khurana E, Engelman DM, Gerstein MB. Computational analysis of membrane proteins: the largest class of drug targets. Drug Discov Today 2009; 14:1130-5.
    • (2009) Drug Discov Today , vol.14 , pp. 1130-1135
    • Arinaminpathy, Y.1    Khurana, E.2    Engelman, D.M.3    Gerstein, M.B.4
  • 4
    • 34848885103 scopus 로고    scopus 로고
    • A monomeric membrane peptide that lives in three worlds: In solution, attached to and inserted across lipid bilayers
    • Reshetnyak YK, Segala M, Andreev OA, Engelman DM. A monomeric membrane peptide that lives in three worlds: in solution, attached to and inserted across lipid bilayers. Biophys J 2007; 93:2363-72.
    • (2007) Biophys J , vol.93 , pp. 2363-2372
    • Reshetnyak, Y.K.1    Segala, M.2    Andreev, O.A.3    Engelman, D.M.4
  • 5
    • 47749118037 scopus 로고    scopus 로고
    • Membrane interactions of designed cationic antimicrobial peptides: The two thresholds
    • Glukhov E, Burrows LL, Deber CM. Membrane interactions of designed cationic antimicrobial peptides: The two thresholds. Biopolymers 2008; 89:360-71.
    • (2008) Biopolymers , vol.89 , pp. 360-371
    • Glukhov, E.1    Burrows, L.L.2    Deber, C.M.3
  • 6
    • 67649274356 scopus 로고    scopus 로고
    • Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: Lessons from temporins B and L
    • Mahalka AK, Kinnunen PK. Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L. Biochim Biophys Acta 2009; 1788:1600-9.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1600-1609
    • Mahalka, A.K.1    Kinnunen, P.K.2
  • 7
    • 53049090332 scopus 로고    scopus 로고
    • A dynamic view of peptides and proteins in membranes
    • Bechinger B. A dynamic view of peptides and proteins in membranes. Cell Mol Life Sci 2008; 65:3028-39.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3028-3039
    • Bechinger, B.1
  • 8
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer SJ, Nicolson GL. The fluid mosaic model of the structure of cell membranes. Science 1972; 175:720-31.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 9
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman DM. Membranes are more mosaic than fluid. Nature 2005; 438:578-80.
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 11
    • 33750459691 scopus 로고    scopus 로고
    • Dynamic helix interactions in transmembrane signaling
    • Matthews EE, Zoonens M, Engelman DM. Dynamic helix interactions in transmembrane signaling. Cell 2006; 127:447-50.
    • (2006) Cell , vol.127 , pp. 447-450
    • Matthews, E.E.1    Zoonens, M.2    Engelman, D.M.3
  • 12
    • 67650069254 scopus 로고    scopus 로고
    • Interaction and conformational dynamics of membrane-spanning protein helices
    • Langosch D, Arkin IT. Interaction and conformational dynamics of membrane-spanning protein helices. Protein Sci 2009; 18:1343-58.
    • (2009) Protein Sci , vol.18 , pp. 1343-1358
    • Langosch, D.1    Arkin, I.T.2
  • 13
    • 70349469585 scopus 로고    scopus 로고
    • Domains in biological membranes
    • Lindner R, Naim HY. Domains in biological membranes. Exp Cell Res 2009; 315:2871-8.
    • (2009) Exp Cell Res , vol.315 , pp. 2871-2878
    • Lindner, R.1    Naim, H.Y.2
  • 14
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D, Simons K. Lipid rafts as a membrane-organizing principle. Science 2010; 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 15
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot JL, Engelman DM. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 1990; 29:4031-7.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 17
    • 76649135799 scopus 로고    scopus 로고
    • Signalling complexes and clusters: Functional advantages and methodological hurdles
    • Cebecauer M, Spitaler M, Serge A, Magee AI. Signalling complexes and clusters: functional advantages and methodological hurdles. J Cell Sci 2010; 123:309-20.
    • (2010) J Cell Sci , vol.123 , pp. 309-320
    • Cebecauer, M.1    Spitaler, M.2    Serge, A.3    Magee, A.I.4
  • 18
    • 33745936562 scopus 로고    scopus 로고
    • Structure and function of photosystems I and II
    • Nelson N, Yocum CF. Structure and function of photosystems I and II. Annu Rev Plant Biol 2006; 57:521-65.
    • (2006) Annu Rev Plant Biol , vol.57 , pp. 521-565
    • Nelson, N.1    Yocum, C.F.2
  • 19
    • 48949095741 scopus 로고    scopus 로고
    • The structure and function of mitochondrial F1F0-ATP synthases
    • Devenish RJ, Prescott M, Rodgers AJ. The structure and function of mitochondrial F1F0-ATP synthases. Int Rev Cell Mol Biol 2008; 267:1-58.
    • (2008) Int Rev Cell Mol Biol , vol.267 , pp. 1-58
    • Devenish, R.J.1    Prescott, M.2    Rodgers, A.J.3
  • 22
    • 58149361853 scopus 로고    scopus 로고
    • SCHOOL model and new targeting strategies
    • Sigalov AB. SCHOOL model and new targeting strategies. Adv Exp Med Biol 2008; 640:268-311.
    • (2008) Adv Exp Med Biol , vol.640 , pp. 268-311
    • Sigalov, A.B.1
  • 23
    • 33644663445 scopus 로고    scopus 로고
    • The role of supramolecular protein complexes and membrane potential in transmembrane signaling processes of lymphocytes
    • DOI 10.1016/j.imlet.2005.11.014, PII S0165247805003597, Signal and Signaling Processing in the Immune System
    • Vamosi G, Bodnar A, Damjanovich S, Nagy P, Varga Z, Damjanovich L. The role of supramolecular protein complexes and membrane potential in transmembrane signaling processes of lymphocytes. Immunol Lett 2006; 104:53-8. (Pubitemid 43330709)
    • (2006) Immunology Letters , vol.104 , Issue.1-2 , pp. 53-58
    • Vamosi, G.1    Bodnar, A.2    Damjanovich, S.3    Nagy, P.4    Varga, Z.5    Damjanovich, L.6
  • 24
    • 69249206623 scopus 로고    scopus 로고
    • G protein-coupled receptor heterodimerization contribution to pharmacology and function
    • Milligan G. G protein-coupled receptor heterodimerization: contribution to pharmacology and function. Br J Pharmacol 2009; 158:5-14.
    • (2009) Br J Pharmacol , vol.158 , pp. 5-14
    • Milligan, G.1
  • 25
    • 77649096828 scopus 로고    scopus 로고
    • Receptor heteromerization and drug discovery
    • Rozenfeld R, Devi LA. Receptor heteromerization and drug discovery. Trends Pharmacol Sci 2010; 31:124-30.
    • (2010) Trends Pharmacol Sci , vol.31 , pp. 124-130
    • Rozenfeld, R.1    Devi, L.A.2
  • 26
    • 71649092717 scopus 로고    scopus 로고
    • Alpha-helical transmembrane peptides: A "divide and conquer" approach to membrane proteins
    • Bordag N, Keller S. Alpha-helical transmembrane peptides: a "divide and conquer" approach to membrane proteins. Chem Phys Lipids 2010; 163:1-26.
    • (2010) Chem Phys Lipids , vol.163 , pp. 1-26
    • Bordag, N.1    Keller, S.2
  • 27
    • 66249121383 scopus 로고    scopus 로고
    • Biophysical dissection of membrane proteins
    • White SH. Biophysical dissection of membrane proteins. Nature 2009; 459:344-6.
    • (2009) Nature , vol.459 , pp. 344-346
    • White, S.H.1
  • 28
    • 65249114173 scopus 로고    scopus 로고
    • Peptide models of membrane protein folding
    • Rath A, Tulumello DV, Deber CM. Peptide models of membrane protein folding. Biochemistry 2009; 48:3036-45.
    • (2009) Biochemistry , vol.48 , pp. 3036-3045
    • Rath, A.1    Tulumello, D.V.2    Deber, C.M.3
  • 29
    • 68149170743 scopus 로고    scopus 로고
    • Structural determinants of transmembrane helical proteins
    • Harrington SE, Ben-Tal N. Structural determinants of transmembrane helical proteins. Structure 2009; 17:1092-103.
    • (2009) Structure , vol.17 , pp. 1092-1103
    • Harrington, S.E.1    Ben-Tal, N.2
  • 30
    • 70349786938 scopus 로고    scopus 로고
    • Dissecting membrane protein architecture: An annotation of structural complexity
    • Arce J, Sturgis JN, Duneau JP. Dissecting membrane protein architecture: An annotation of structural complexity. Biopolymers 2009; 91:815-29.
    • (2009) Biopolymers , vol.91 , pp. 815-829
    • Arce, J.1    Sturgis, J.N.2    Duneau, J.P.3
  • 31
    • 46049088691 scopus 로고    scopus 로고
    • Protein-Protein Interactions in the Membrane: Sequence, Structural and Biological Motifs
    • Moore DT, Berger BW, DeGrado WF. Protein-Protein Interactions in the Membrane: Sequence, Structural and Biological Motifs. Structure 2008; 16:991-1001.
    • (2008) Structure , vol.16 , pp. 991-1001
    • Moore, D.T.1    Berger, B.W.2    DeGrado, W.F.3
  • 32
    • 45449105164 scopus 로고    scopus 로고
    • Protein modulation of lipids and viceversa, in membranes
    • Marsh D. Protein modulation of lipids and viceversa, in membranes. Biochim Biophys Acta 2008; 1778:1545-75.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1545-1575
    • Marsh, D.1
  • 33
    • 49549088809 scopus 로고    scopus 로고
    • Association energetics of membrane spanning alpha-helices
    • Mackenzie KR, Fleming KG. Association energetics of membrane spanning alpha-helices. Curr Opin Struct Biol 2008; 18:412-19.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 412-419
    • Mackenzie, K.R.1    Fleming, K.G.2
  • 34
    • 33847233683 scopus 로고    scopus 로고
    • How important are transmembrane helices of bitopic membrane proteins?
    • Zviling M, Kochva U, Arkin IT. How important are transmembrane helices of bitopic membrane proteins? Biochim Biophys Acta 2007; 1768:387-92.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 387-392
    • Zviling, M.1    Kochva, U.2    Arkin, I.T.3
  • 35
    • 34249739711 scopus 로고    scopus 로고
    • The membrane protein universe: What's out there and why bother?
    • von Heijne G. The membrane protein universe: what's out there and why bother? J Intern Med 2007; 261:543-57.
    • (2007) J Intern Med , vol.261 , pp. 543-557
    • Von Heijne, G.1
  • 36
    • 33847270649 scopus 로고    scopus 로고
    • From interactions of single transmembrane helices to folding of alpha-helical membrane proteins: Analyzing transmembrane helix-helix interactions in bacteria
    • Schneider D, Finger C, Prodohl A, Volkmer T. From interactions of single transmembrane helices to folding of alpha-helical membrane proteins: analyzing transmembrane helix-helix interactions in bacteria. Curr Protein Pept Sci 2007; 8:45-61.
    • (2007) Curr Protein Pept Sci , vol.8 , pp. 45-61
    • Schneider, D.1    Finger, C.2    Prodohl, A.3    Volkmer, T.4
  • 37
    • 34247476788 scopus 로고    scopus 로고
    • Peptides as transmembrane segments: Decrypting the determinants for helix-helix interactions in membrane proteins
    • Rath A, Johnson RM, Deber CM. Peptides as transmembrane segments: decrypting the determinants for helix-helix interactions in membrane proteins. Biopolymers 2007; 88:217-32.
    • (2007) Biopolymers , vol.88 , pp. 217-232
    • Rath, A.1    Johnson, R.M.2    Deber, C.M.3
  • 38
    • 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; 103:13658-63.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13658-13663
    • Walters, R.F.1    DeGrado, W.F.2
  • 39
    • 33746358793 scopus 로고    scopus 로고
    • Introduction to the membrane protein reviews: The interplay of structure, dynamics and environment in membrane protein function
    • Sachs JN, Engelman DM. Introduction to the membrane protein reviews: the interplay of structure, dynamics and environment in membrane protein function. Annu Rev Biochem 2006; 75:707-12.
    • (2006) Annu Rev Biochem , vol.75 , pp. 707-712
    • Sachs, J.N.1    Engelman, D.M.2
  • 40
    • 33646902110 scopus 로고    scopus 로고
    • Folding and stability of alpha-helical integral membrane proteins
    • Mackenzie KR. Folding and stability of alpha-helical integral membrane proteins. Chem Rev 2006; 106:1931-77.
    • (2006) Chem Rev , vol.106 , pp. 1931-1977
    • Mackenzie, K.R.1
  • 41
    • 34247580102 scopus 로고    scopus 로고
    • Membrane protein insertion the biology-physics nexus
    • White SH. Membrane protein insertion: the biology-physics nexus. J Gen Physiol 2007; 129:363-9.
    • (2007) J Gen Physiol , vol.129 , pp. 363-369
    • White, S.H.1
  • 42
    • 0028153788 scopus 로고
    • A mutation data matrix for transmembrane proteins
    • Jones DT, Taylor WR, Thornton JM. A mutation data matrix for transmembrane proteins. FEBS Lett 1994; 339:269-75.
    • (1994) FEBS Lett , vol.339 , pp. 269-275
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 43
    • 58149117450 scopus 로고    scopus 로고
    • Complex patterns of histidine hydroxylated amino acids and the GxxxG motif mediate high-affinity transmembrane domain interactions
    • Herrmann JR, Panitz JC, Unterreitmeier S, Fuchs A, Frishman D, Langosch D. Complex patterns of histidine, hydroxylated amino acids and the GxxxG motif mediate high-affinity transmembrane domain interactions. J Mol Biol 2009; 385:912-23.
    • (2009) J Mol Biol , vol.385 , pp. 912-923
    • Herrmann, J.R.1    Panitz, J.C.2    Unterreitmeier, S.3    Fuchs, A.4    Frishman, D.5    Langosch, D.6
  • 44
    • 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; 14:465-79.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 45
    • 0038499536 scopus 로고    scopus 로고
    • Sequence context strongly modulates association of polar residues in transmembrane helices
    • Dawson JP, Melnyk RA, Deber CM, Engelman DM. Sequence context strongly modulates association of polar residues in transmembrane helices. J Mol Biol 2003; 331:255-62.
    • (2003) J Mol Biol , vol.331 , pp. 255-262
    • Dawson, J.P.1    Melnyk, R.A.2    Deber, C.M.3    Engelman, D.M.4
  • 46
    • 77449104569 scopus 로고    scopus 로고
    • Ionic Interactions Promote Transmembrane Helix-Helix Association Depending on Sequence Context
    • Herrmann JR, Fuchs A, Panitz JC, Eckert T, Unterreitmeier S, Frishman D, et al. Ionic Interactions Promote Transmembrane Helix-Helix Association Depending on Sequence Context. J Mol Biol 2010; 396:452-61.
    • (2010) J Mol Biol , vol.396 , pp. 452-461
    • Herrmann, J.R.1    Fuchs, A.2    Panitz, J.C.3    Eckert, T.4    Unterreitmeier, S.5    Frishman, D.6
  • 47
    • 1942469334 scopus 로고    scopus 로고
    • The affinity of GXXXG motifs in transmembrane helix-helix interactions is modulated by long-range communication
    • Melnyk RA, Kim S, Curran AR, Engelman DM, Bowie JU, Deber CM. The affinity of GXXXG motifs in transmembrane helix-helix interactions is modulated by long-range communication. J Biol Chem 2004; 279:16591-7.
    • (2004) J Biol Chem , vol.279 , pp. 16591-16597
    • Melnyk, R.A.1    Kim, S.2    Curran, A.R.3    Engelman, D.M.4    Bowie, J.U.5    Deber, C.M.6
  • 48
    • 68949142901 scopus 로고    scopus 로고
    • Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues
    • Zhang J, Lazaridis T. Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues. Biophys J 2009; 96:4418-27.
    • (2009) Biophys J , vol.96 , pp. 4418-4427
    • Zhang, J.1    Lazaridis, T.2
  • 49
    • 0026694442 scopus 로고
    • Intramembrane helix-helix association in oligomerization and transmembrane signaling
    • Bormann BJ, Engelman DM. Intramembrane helix-helix association in oligomerization and transmembrane signaling. Annu Rev Biophys Biomol Struct 1992; 21:223-42.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 223-242
    • Bormann, B.J.1    Engelman, D.M.2
  • 50
    • 0032570779 scopus 로고    scopus 로고
    • Do transmembrane protein superfolds exist?
    • Jones DT. Do transmembrane protein superfolds exist? FEBS Lett 1998; 423:281-5.
    • (1998) FEBS Lett , vol.423 , pp. 281-285
    • Jones, D.T.1
  • 51
    • 0034808117 scopus 로고    scopus 로고
    • Comparing function and structure between entire proteomes
    • Liu J, Rost B. Comparing function and structure between entire proteomes. Protein Sci 2001; 10:1970-9.
    • (2001) Protein Sci , vol.10 , pp. 1970-1979
    • Liu, J.1    Rost, B.2
  • 52
    • 17944394278 scopus 로고    scopus 로고
    • Signaling receptome: A genomic and evolutionary perspective of plasma membrane receptors involved in signal transduction
    • Ben-Shlomo I, Yu Hsu S, Rauch R, Kowalski HW, Hsueh AJ. Signaling receptome: a genomic and evolutionary perspective of plasma membrane receptors involved in signal transduction. Sci STKE 2003; RE9.
    • (2003) Sci STKE
    • Ben-Shlomo, I.1    Yu Hsu, S.2    Rauch, R.3    Kowalski, H.W.4    Hsueh, A.J.5
  • 53
    • 56849105342 scopus 로고    scopus 로고
    • Adhesion proteins meet receptors: A common theme?
    • Orian-Rousseau V, Ponta H. Adhesion proteins meet receptors: a common theme? Adv Cancer Res 2008; 101:63-92.
    • (2008) Adv Cancer Res , vol.101 , pp. 63-92
    • Orian-Rousseau, V.1    Ponta, H.2
  • 54
    • 0028235050 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • Lemmon MA, Engelman DM. Specificity and promiscuity in membrane helix interactions. FEBS Lett 1994; 346:17-20.
    • (1994) FEBS Lett , vol.346 , pp. 17-20
    • Lemmon, M.A.1    Engelman, D.M.2
  • 55
    • 0032584233 scopus 로고    scopus 로고
    • Structure-based prediction of the stability of transmembrane helix-ìhelix interactions: The sequence dependence of glycophorin a dimerization
    • MacKenzie KR, Engelman DM. Structure-based prediction of the stability of transmembrane helix-ìhelix interactions: The sequence dependence of glycophorin A dimerization. Proc Natl Acad Sci USA 1998; 95:3583-90.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3583-3590
    • MacKenzie, K.R.1    Engelman, D.M.2
  • 56
    • 77952093470 scopus 로고    scopus 로고
    • Orientation and dynamics of transmembrane peptides: The power of simple models
    • Holt A, Killian JA. Orientation and dynamics of transmembrane peptides: the power of simple models. Eur Biophys J 2010; 39:609-21.
    • (2010) Eur Biophys J , vol.39 , pp. 609-621
    • Holt, A.1    Killian, J.A.2
  • 57
    • 33746647787 scopus 로고    scopus 로고
    • Peptides in lipid bilayers: The power of simple models
    • Killian JA, Nyholm TK. Peptides in lipid bilayers: the power of simple models. Curr Opin Struct Biol 2006; 16:473-9.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 473-479
    • Killian, J.A.1    Nyholm, T.K.2
  • 58
    • 42049090110 scopus 로고    scopus 로고
    • Lessons from viruses: Controlling the function of transmembrane proteins by interfering transmembrane helices
    • Cymer F, Schneider D. Lessons from viruses: controlling the function of transmembrane proteins by interfering transmembrane helices. Curr Med Chem 2008; 15:779-85.
    • (2008) Curr Med Chem , vol.15 , pp. 779-785
    • Cymer, F.1    Schneider, D.2
  • 59
    • 59349092349 scopus 로고    scopus 로고
    • The bovine papillomavirus E5 protein and the PDGF beta receptor: It takes two to tango
    • Talbert-Slagle K, DiMaio D. The bovine papillomavirus E5 protein and the PDGF beta receptor: it takes two to tango. Virology 2009; 384:345-51.
    • (2009) Virology , vol.384 , pp. 345-351
    • Talbert-Slagle, K.1    DiMaio, D.2
  • 60
    • 50149103930 scopus 로고    scopus 로고
    • In vitro dimerization of the bovine papillomavirus E5 protein transmembrane domain
    • Oates J, Hicks M, Dafforn TR, DiMaio D, Dixon AM. In vitro dimerization of the bovine papillomavirus E5 protein transmembrane domain. Biochemistry 2008; 47:8985-92.
    • (2008) Biochemistry , vol.47 , pp. 8985-8992
    • Oates, J.1    Hicks, M.2    Dafforn, T.R.3    DiMaio, D.4    Dixon, A.M.5
  • 61
    • 76749147499 scopus 로고    scopus 로고
    • Strong oligomerization behavior of PDGFbeta receptor transmembrane domain and its regulation by the juxtamembrane regions
    • Oates J, King G, Dixon AM. Strong oligomerization behavior of PDGFbeta receptor transmembrane domain and its regulation by the juxtamembrane regions. Biochim Biophys Acta 2010; 1798:605-15.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 605-615
    • Oates, J.1    King, G.2    Dixon, A.M.3
  • 62
    • 77649247830 scopus 로고    scopus 로고
    • Construction and genetic selection of small transmembrane proteins that activate the human erythropoietin receptor
    • Cammett TJ, Jun SJ, Cohen EB, Barrera FN, Engelman DM, Dimaio D. Construction and genetic selection of small transmembrane proteins that activate the human erythropoietin receptor. Proc Natl Acad Sci USA 2010; 107:3447-52.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3447-3452
    • Cammett, T.J.1    Jun, S.J.2    Cohen, E.B.3    Barrera, F.N.4    Engelman, D.M.5    Dimaio, D.6
  • 63
    • 0034213931 scopus 로고    scopus 로고
    • RTK mutations and human syndromeswhen good receptors turn bad
    • Robertson SC, Tynan JA, Donoghue DJ. RTK mutations and human syndromeswhen good receptors turn bad. Trends Genet 2000; 16:265-71.
    • (2000) Trends Genet , vol.16 , pp. 265-271
    • Robertson, S.C.1    Tynan, J.A.2    Donoghue, D.J.3
  • 64
    • 33646889068 scopus 로고    scopus 로고
    • Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies
    • Li E, Hristova K. Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies. Biochemistry 2006; 45:6241-51.
    • (2006) Biochemistry , vol.45 , pp. 6241-6251
    • Li, E.1    Hristova, K.2
  • 65
    • 1542376209 scopus 로고    scopus 로고
    • Missense mutations in transmembrane domains of proteins: Phenotypic propensity of polar residues for human disease
    • Partridge AW, Therien AG, Deber CM. Missense mutations in transmembrane domains of proteins: phenotypic propensity of polar residues for human disease. Proteins 2004; 54:648-56.
    • (2004) Proteins , vol.54 , pp. 648-656
    • Partridge, A.W.1    Therien, A.G.2    Deber, C.M.3
  • 67
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie KR, Prestegard JH, Engelman DM. A transmembrane helix dimer: structure and implications. Science 1997; 276:131-3.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 68
    • 43749091771 scopus 로고    scopus 로고
    • Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state
    • Bocharov EV, Mineev KS, Volynsky PE, Ermolyuk YS, Tkach EN, Sobol AG, et al. Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state. J Biol Chem 2008; 283:6950-6.
    • (2008) J Biol Chem , vol.283 , pp. 6950-6956
    • Bocharov, E.V.1    Mineev, K.S.2    Volynsky, P.E.3    Ermolyuk, Y.S.4    Tkach, E.N.5    Sobol, A.G.6
  • 69
    • 57649221018 scopus 로고    scopus 로고
    • Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1
    • Bocharov EV, Mayzel ML, Volynsky PE, Goncharuk MV, Ermolyuk YS, Schulga AA, et al. Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1. J Biol Chem 2008; 283:29385-95.
    • (2008) J Biol Chem , vol.283 , pp. 29385-29395
    • Bocharov, E.V.1    Mayzel, M.L.2    Volynsky, P.E.3    Goncharuk, M.V.4    Ermolyuk, Y.S.5    Schulga, A.A.6
  • 71
    • 33750022623 scopus 로고    scopus 로고
    • The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor
    • Call ME, Schnell JR, Xu C, Lutz RA, Chou JJ, Wucherpfennig KW. The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor. Cell 2006; 127:355-68.
    • (2006) Cell , vol.127 , pp. 355-368
    • Call, M.E.1    Schnell, J.R.2    Xu, C.3    Lutz, R.A.4    Chou, J.J.5    Wucherpfennig, K.W.6
  • 72
    • 67049171187 scopus 로고    scopus 로고
    • Structural basis for dimerization of the BNIP3 transmembrane domain
    • Sulistijo ES, Mackenzie KR. Structural basis for dimerization of the BNIP3 transmembrane domain. Biochemistry 2009; 48:5106-20.
    • (2009) Biochemistry , vol.48 , pp. 5106-5120
    • Sulistijo, E.S.1    Mackenzie, K.R.2
  • 73
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • Lau TL, Kim C, Ginsberg MH, Ulmer TS. The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. EMBO J 2009; 28:1351-61.
    • (2009) EMBO J , vol.28 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 74
    • 77950405050 scopus 로고    scopus 로고
    • Sequence Dependent Oligomerization of the Neu Transmembrane Domain Suggests Inhibition of Conformational Switching' by Oncogenic Mutant
    • Beevers AJ, Damianoglou A, Oates JE, Rodger A, Dixon AM. Sequence Dependent Oligomerization of the Neu Transmembrane Domain Suggests Inhibition of Conformational Switching' by Oncogenic Mutant. Biochemistry 2010; 49:2811-20.
    • (2010) Biochemistry , vol.49 , pp. 2811-2820
    • Beevers, A.J.1    Damianoglou, A.2    Oates, J.E.3    Rodger, A.4    Dixon, A.M.5
  • 75
    • 67349094494 scopus 로고    scopus 로고
    • Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains
    • Escher C, Cymer F, Schneider D. Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains. J Mol Biol 2009; 389:10-6.
    • (2009) J Mol Biol , vol.389 , pp. 10-16
    • Escher, C.1    Cymer, F.2    Schneider, D.3
  • 76
    • 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; 279:21177-82.
    • (2004) J Biol Chem , vol.279 , pp. 21177-21182
    • Gerber, D.1    Sal-Man, N.2    Shai, Y.3
  • 77
    • 1442287309 scopus 로고    scopus 로고
    • Comparisons of force fields for proteins by generalized-ensemble simulations
    • Yoda T, Sugita Y, Okamoto Y. Comparisons of force fields for proteins by generalized-ensemble simulations. Chem Phys Lett 2004; 386:460-7.
    • (2004) Chem Phys Lett , vol.386 , pp. 460-467
    • Yoda, T.1    Sugita, Y.2    Okamoto, Y.3
  • 78
    • 12844258934 scopus 로고    scopus 로고
    • Ptuba: A tool for the visualization of helix surfaces in proteins
    • Lopera JA, Sturgis JN, Duneau JP. Ptuba: a tool for the visualization of helix surfaces in proteins. J Mol Graph Model 2005; 23:305-15.
    • (2005) J Mol Graph Model , vol.23 , pp. 305-315
    • Lopera, J.A.1    Sturgis, J.N.2    Duneau, J.P.3
  • 79
    • 33847118661 scopus 로고    scopus 로고
    • A dimerization hierarchy in the transmembrane domains of the HER receptor family
    • Duneau JP, Vegh AP, Sturgis JN. A dimerization hierarchy in the transmembrane domains of the HER receptor family. Biochemistry 2007; 46:2010-9.
    • (2007) Biochemistry , vol.46 , pp. 2010-2019
    • Duneau, J.P.1    Vegh, A.P.2    Sturgis, J.N.3
  • 80
    • 14844355538 scopus 로고    scopus 로고
    • The transmembrane domains of ErbB receptors do not dimerize strongly in micelles
    • Stanley AM, Fleming KG. The transmembrane domains of ErbB receptors do not dimerize strongly in micelles. J Mol Biol 2005; 347:759-72.
    • (2005) J Mol Biol , vol.347 , pp. 759-772
    • Stanley, A.M.1    Fleming, K.G.2
  • 82
    • 73449095502 scopus 로고    scopus 로고
    • Bioinformatic approaches for the structure and function of membrane proteins
    • Nam HJ, Jeon J, Kim S. Bioinformatic approaches for the structure and function of membrane proteins. BMB Rep 2009; 42:697-704.
    • (2009) BMB Rep , vol.42 , pp. 697-704
    • Nam, H.J.1    Jeon, J.2    Kim, S.3
  • 83
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 2001; 305:567-80. (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 84
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins at 86% accuracy
    • Rost B, Fariselli P, Casadio R. Topology prediction for helical transmembrane proteins at 86% accuracy. Protein Sci 1996; 5:1704-18. (Pubitemid 26257233)
    • (1996) Protein Science , vol.5 , Issue.8 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 86
    • 34547584314 scopus 로고    scopus 로고
    • Advantages of combined transmembrane topology and signal peptide prediction - The Phobius web server
    • Kall L, Krogh A, Sonnhammer EL. Advantages of combined transmembrane topology and signal peptide prediction - the Phobius web server. Nucleic Acids Res 2007; 35:429-32.
    • (2007) Nucleic Acids Res , vol.35 , pp. 429-432
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 87
    • 0033167996 scopus 로고    scopus 로고
    • Are membrane proteins "insideout" proteins?
    • Stevens TJ, Arkin IT. Are membrane proteins "insideout" proteins? Proteins 1999; 36:135-43.
    • (1999) Proteins , vol.36 , pp. 135-143
    • Stevens, T.J.1    Arkin, I.T.2
  • 88
    • 33747184794 scopus 로고    scopus 로고
    • Prediction of transmembrane helix orientation in polytopic membrane proteins
    • Adamian L, Liang J. Prediction of transmembrane helix orientation in polytopic membrane proteins. BMC Struct Biol 2006; 6:13.
    • (2006) BMC Struct Biol , vol.6 , pp. 13
    • Adamian, L.1    Liang, J.2
  • 90
    • 64549119506 scopus 로고    scopus 로고
    • Predicting helix-helix interactions from residue contacts in membrane proteins
    • Lo A, Chiu YY, Rodland EA, Lyu PC, Sung TY, Hsu WL. Predicting helix-helix interactions from residue contacts in membrane proteins. Bioinformatics 2009; 25:996-1003.
    • (2009) Bioinformatics , vol.25 , pp. 996-1003
    • Lo, A.1    Chiu, Y.Y.2    Rodland, E.A.3    Lyu, P.C.4    Sung, T.Y.5    Hsu, W.L.6
  • 91
    • 77949509024 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of the Dimerization of Transmembrane alpha-Helices
    • Psachoulia E, Marshall DP, Sansom MS. Molecular Dynamics Simulations of the Dimerization of Transmembrane alpha-Helices. Acc Chem Res 2010; 43:388-96.
    • (2010) Acc Chem Res , vol.43 , pp. 388-396
    • Psachoulia, E.1    Marshall, D.P.2    Sansom, M.S.3
  • 92
    • 35748947251 scopus 로고    scopus 로고
    • Molecular dynamics simulation approach for the prediction of transmembrane helix-helix heterodimers assembly
    • Samna Soumana O, Garnier N, Genest M. Molecular dynamics simulation approach for the prediction of transmembrane helix-helix heterodimers assembly. Eur Biophys J 2007; 36:1071-82.
    • (2007) Eur Biophys J , vol.36 , pp. 1071-1082
    • Samna Soumana, O.1    Garnier, N.2    Genest, M.3
  • 94
    • 67549145398 scopus 로고    scopus 로고
    • Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment
    • Jura N, Endres NF, Engel K, Deindl S, Das R, Lamers MH, et al. Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Cell 2009; 137:1293-307.
    • (2009) Cell , vol.137 , pp. 1293-1307
    • Jura, N.1    Endres, N.F.2    Engel, K.3    Deindl, S.4    Das, R.5    Lamers, M.H.6
  • 95
    • 62649159075 scopus 로고    scopus 로고
    • Ligand-induced ErbB receptor dimerization
    • Lemmon MA. Ligand-induced ErbB receptor dimerization. Exp Cell Res 2009; 315:638-48.
    • (2009) Exp Cell Res , vol.315 , pp. 638-648
    • Lemmon, M.A.1
  • 96
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki T, Maruyama H, Maruyama IN. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J Mol Biol 2001; 311:1011-26.
    • (2001) J Mol Biol , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 97
    • 55449102296 scopus 로고    scopus 로고
    • All EGF(ErbB) receptors have preformed homo- And heterodimeric structures in living cells
    • Tao RH, Maruyama IN. All EGF(ErbB) receptors have preformed homo- and heterodimeric structures in living cells. J Cell Sci 2008; 121:3207-17.
    • (2008) J Cell Sci , vol.121 , pp. 3207-3217
    • Tao, R.H.1    Maruyama, I.N.2
  • 98
    • 50349083489 scopus 로고    scopus 로고
    • Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements
    • Szabo A, Horvath G, Szollosi J, Nagy P. Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements. Biophys J 2008; 95:2086-96.
    • (2008) Biophys J , vol.95 , pp. 2086-2096
    • Szabo, A.1    Horvath, G.2    Szollosi, J.3    Nagy, P.4
  • 99
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin MR, Wells JA. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 2004; 3:301-17.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 100
    • 0142241304 scopus 로고    scopus 로고
    • Blockade of G protein-coupled receptors and the dopamine transporter by a transmembrane domain peptide novel strategy for functional inhibition of membrane proteins in vivo
    • George SR, Ng GY, Lee SP, Fan T, Varghese G, Wang C, et al. Blockade of G protein-coupled receptors and the dopamine transporter by a transmembrane domain peptide: novel strategy for functional inhibition of membrane proteins in vivo. J Pharmacol Exp Ther 2003; 307:481-9.
    • (2003) J Pharmacol Exp Ther , vol.307 , pp. 481-489
    • George, S.R.1    Ng, G.Y.2    Lee, S.P.3    Fan, T.4    Varghese, G.5    Wang, C.6
  • 101
    • 0027203585 scopus 로고
    • Specific short transmembrane sequences can inhibit transformation by the mutant neu growth factor receptor in vitro and in vivo
    • Lofts FJ, Hurst HC, Sternberg MJ, Gullick WJ. Specific short transmembrane sequences can inhibit transformation by the mutant neu growth factor receptor in vitro and in vivo. Oncogene 1993; 8:2813-20.
    • (1993) Oncogene , vol.8 , pp. 2813-2820
    • Lofts, F.J.1    Hurst, H.C.2    Sternberg, M.J.3    Gullick, W.J.4
  • 102
    • 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; 3:84-8.
    • (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
  • 103
    • 77951622512 scopus 로고    scopus 로고
    • Peptide-based interference of the transmembrane domain of neuropilin-1 inhibits glioma growth in vivo
    • Nasarre C, Roth M, Jacob L, Roth L, Koncina E, Thien A, et al. Peptide-based interference of the transmembrane domain of neuropilin-1 inhibits glioma growth in vivo. Oncogene 2010; 29:2381-92.
    • (2010) Oncogene , vol.29 , pp. 2381-2392
    • Nasarre, C.1    Roth, M.2    Jacob, L.3    Roth, L.4    Koncina, E.5    Thien, A.6
  • 104
    • 33847668295 scopus 로고    scopus 로고
    • A structurally altered D,L-amino acid TCRalpha transmembrane peptide interacts with the TCRalpha 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 TCRalpha transmembrane peptide interacts with the TCRalpha and inhibits T-cell activation in vitro and in an animal model. Biochemistry 2007; 46:2317-25.
    • (2007) Biochemistry , vol.46 , pp. 2317-2325
    • Quintana, F.J.1    Gerber, D.2    Bloch, I.3    Cohen, I.R.4    Shai, Y.5
  • 105
    • 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; 344:855-64.
    • (2004) J Mol Biol , vol.344 , pp. 855-864
    • Sal-Man, N.1    Gerber, D.2    Shai, Y.3
  • 106
    • 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; 322:491-5.
    • (2002) J Mol Biol , vol.322 , pp. 491-495
    • Gerber, D.1    Shai, Y.2
  • 107
    • 33747036119 scopus 로고    scopus 로고
    • Lipidation and glycosylation of a T cell antigen receptor (TCR) transmembrane hydrophobic peptide dramatically enhances in vitro and in vivo function
    • Amon MA, Ali M, Bender V, Chan YN, Toth I, Manolios N. Lipidation and glycosylation of a T cell antigen receptor (TCR) transmembrane hydrophobic peptide dramatically enhances in vitro and in vivo function. Biochim Biophys Acta 2006; 1763:879-88.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 879-888
    • Amon, M.A.1    Ali, M.2    Bender, V.3    Chan, Y.N.4    Toth, I.5    Manolios, N.6
  • 108
    • 73349087177 scopus 로고    scopus 로고
    • The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions
    • Finger C, Escher C, Schneider D. The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions. Sci Signal 2009; 2:ra56.
    • (2009) Sci Signal , vol.2
    • Finger, C.1    Escher, C.2    Schneider, D.3
  • 109
    • 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; 277:4704-12.
    • (2002) J Biol Chem , vol.277 , pp. 4704-4712
    • Mendrola, J.M.1    Berger, M.B.2    King, M.C.3    Lemmon, M.A.4
  • 110
    • 56949102246 scopus 로고    scopus 로고
    • Pathogenic activation of receptor tyrosine kinases in mammalian membranes
    • He L, Hristova K. Pathogenic activation of receptor tyrosine kinases in mammalian membranes. J Mol Biol 2008; 384:1130-42.
    • (2008) J Mol Biol , vol.384 , pp. 1130-1142
    • He, L.1    Hristova, K.2
  • 111
    • 0022485548 scopus 로고
    • Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
    • Bargmann CI, Hung MC, Weinberg RA. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell 1986; 45:649-57.
    • (1986) Cell , vol.45 , pp. 649-657
    • Bargmann, C.I.1    Hung, M.C.2    Weinberg, R.A.3
  • 112
    • 0030614530 scopus 로고    scopus 로고
    • Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
    • Burke CL, Lemmon MA, Coren BA, Engelman DM, Stern DF. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene 1997; 14:687-96.
    • (1997) Oncogene , vol.14 , pp. 687-696
    • Burke, C.L.1    Lemmon, M.A.2    Coren, B.A.3    Engelman, D.M.4    Stern, D.F.5
  • 114
    • 0030064347 scopus 로고    scopus 로고
    • Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia
    • Webster MK, Donoghue DJ. Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia. EMBO Journal 1996; 15:520-7.
    • (1996) EMBO Journal , vol.15 , pp. 520-527
    • Webster, M.K.1    Donoghue, D.J.2
  • 115
    • 0030941036 scopus 로고    scopus 로고
    • Activation of FGF receptors by mutations in the transmembrane domain
    • Li Y, Mangasarian K, Mansukhani A, Basilico C. Activation of FGF receptors by mutations in the transmembrane domain. Oncogene 1997; 14:1397-406. (Pubitemid 27182429)
    • (1997) Oncogene , vol.14 , Issue.12 , pp. 1397-1406
    • Li, Y.1    Mangasarian, K.2    Mansukhani, A.3    Basilico, C.4
  • 116
    • 0035858985 scopus 로고    scopus 로고
    • Deregulated FGFR3 mutants in multiple myeloma cell lines with t(4;14): Comparative analysis of Y373C, K650E and the novel G384D mutations
    • Ronchetti D, Greco A, Compasso S, Colombo G, Dell'Era P, Otsuki T, et al. Deregulated FGFR3 mutants in multiple myeloma cell lines with t(4;14): comparative analysis of Y373C, K650E and the novel G384D mutations. Oncogene 2001; 20:3553-62.
    • (2001) Oncogene , vol.20 , pp. 3553-3562
    • Ronchetti, D.1    Greco, A.2    Compasso, S.3    Colombo, G.4    Dell'Era, P.5    Otsuki, T.6
  • 117
    • 14544292898 scopus 로고    scopus 로고
    • Synthesis and initial characterization of FGFR3 transmembrane domain: Consequences of sequence modifications
    • Iwamoto T, You M, Li E, Spangler J, Tomich JM, Hristova K. Synthesis and initial characterization of FGFR3 transmembrane domain: consequences of sequence modifications. Biochim Biophys Acta 2005; 1668:240-7.
    • (2005) Biochim Biophys Acta , vol.1668 , pp. 240-247
    • Iwamoto, T.1    You, M.2    Li, E.3    Spangler, J.4    Tomich, J.M.5    Hristova, K.6
  • 118
    • 31344468061 scopus 로고    scopus 로고
    • FGFR3 dimer stabilization due to a single amino acid pathogenic mutation
    • Li E, You M, Hristova K. FGFR3 dimer stabilization due to a single amino acid pathogenic mutation. J Mol Biol 2006; 356:600-12.
    • (2006) J Mol Biol , vol.356 , pp. 600-612
    • Li, E.1    You, M.2    Hristova, K.3
  • 119
    • 34548013094 scopus 로고    scopus 로고
    • Studies of receptor tyrosine kinase transmembrane domain interactions the EmEx-FRET method
    • Merzlyakov M, Chen L, Hristova K. Studies of receptor tyrosine kinase transmembrane domain interactions: the EmEx-FRET method. J Membr Biol 2007; 215:93-103.
    • (2007) J Membr Biol , vol.215 , pp. 93-103
    • Merzlyakov, M.1    Chen, L.2    Hristova, K.3
  • 120
    • 34848865082 scopus 로고    scopus 로고
    • Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers
    • You M, Spangler J, Li E, Han X, Ghosh P, Hristova K. Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers. Biochemistry 2007; 46:11039-46.
    • (2007) Biochemistry , vol.46 , pp. 11039-11046
    • You, M.1    Spangler, J.2    Li, E.3    Han, X.4    Ghosh, P.5    Hristova, K.6
  • 121
    • 59949089096 scopus 로고    scopus 로고
    • The strong dimerization of the transmembrane domain of the fibroblast growth factor receptor (FGFR) is modulated by C-terminal juxtamembrane residues
    • Peng WC, Lin X, Torres J. The strong dimerization of the transmembrane domain of the fibroblast growth factor receptor (FGFR) is modulated by C-terminal juxtamembrane residues. Protein Sci 2009; 18:450-9.
    • (2009) Protein Sci , vol.18 , pp. 450-459
    • Peng, W.C.1    Lin, X.2    Torres, J.3
  • 122
    • 75149176738 scopus 로고    scopus 로고
    • Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers
    • Dosch DD, Ballmer-Hofer K. Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers. Faseb Journal 2010; 24:32-8.
    • (2010) Faseb Journal , vol.24 , pp. 32-38
    • Dosch, D.D.1    Ballmer-Hofer, K.2
  • 123
    • 70349279951 scopus 로고    scopus 로고
    • Artificial transmembrane oncoproteins smaller than the bovine papillomavirus E5 protein redefine sequence requirements for activation of the platelet-derived growth factor beta receptor
    • Talbert-Slagle K, Marlatt S, Barrera FN, Khurana E, Oates J, Gerstein M, et al. Artificial transmembrane oncoproteins smaller than the bovine papillomavirus E5 protein redefine sequence requirements for activation of the platelet-derived growth factor beta receptor. J Virol 2009; 83:9773-85.
    • (2009) J Virol , vol.83 , pp. 9773-9785
    • Talbert-Slagle, K.1    Marlatt, S.2    Barrera, F.N.3    Khurana, E.4    Oates, J.5    Gerstein, M.6
  • 124
    • 33750876850 scopus 로고    scopus 로고
    • Self-association of the transmembrane domain of RET underlies oncogenic activation by MEN2A mutations
    • Kjaer S, Kurokawa K, Perrinjaquet M, Abrescia C, Ibanez CF. Self-association of the transmembrane domain of RET underlies oncogenic activation by MEN2A mutations. Oncogene 2006; 25:7086-95.
    • (2006) Oncogene , vol.25 , pp. 7086-7095
    • Kjaer, S.1    Kurokawa, K.2    Perrinjaquet, M.3    Abrescia, C.4    Ibanez, C.F.5
  • 125
    • 0033564715 scopus 로고    scopus 로고
    • Activation of the erythropoietin receptor by the gp55-P viral envelope protein is determined by a single amino acid in its transmembrane domain
    • Constantinescu SN, Liu X, Beyer W, Fallon A, Shekar S, Henis YI, et al. Activation of the erythropoietin receptor by the gp55-P viral envelope protein is determined by a single amino acid in its transmembrane domain. EMBO J 1999; 18:3334-47.
    • (1999) EMBO J , vol.18 , pp. 3334-3347
    • Constantinescu, S.N.1    Liu, X.2    Beyer, W.3    Fallon, A.4    Shekar, S.5    Henis, Y.I.6
  • 126
    • 0035936596 scopus 로고    scopus 로고
    • Self assembly of the transmembrane domain promotes signal transduction through the erythropoietin receptor
    • Kubatzky KF, Ruan W, Gurezka R, Cohen J, Ketteler R, Watowich SS, et al. Self assembly of the transmembrane domain promotes signal transduction through the erythropoietin receptor. Curr Biol 2001; 11:110-5.
    • (2001) Curr Biol , vol.11 , pp. 110-115
    • Kubatzky, K.F.1    Ruan, W.2    Gurezka, R.3    Cohen, J.4    Ketteler, R.5    Watowich, S.S.6
  • 127
    • 0344413478 scopus 로고    scopus 로고
    • Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer
    • Seubert N, Royer Y, Staerk J, Kubatzky KF, Moucadel V, Krishnakumar S, et al. Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer. Mol Cell 2003; 12:1239-50.
    • (2003) Mol Cell , vol.12 , pp. 1239-1250
    • Seubert, N.1    Royer, Y.2    Staerk, J.3    Kubatzky, K.F.4    Moucadel, V.5    Krishnakumar, S.6
  • 128
    • 33846390316 scopus 로고    scopus 로고
    • Dimerization of the erythropoietin receptor transmembrane domain in micelles
    • Ebie AZ, Fleming KG. Dimerization of the erythropoietin receptor transmembrane domain in micelles. J Mol Biol 2007; 366:517-24.
    • (2007) J Mol Biol , vol.366 , pp. 517-524
    • Ebie, A.Z.1    Fleming, K.G.2
  • 129
    • 55849089247 scopus 로고    scopus 로고
    • Packing density of the erythropoietin receptor transmembrane domain correlates with amplification of biological responses
    • Becker V, Sengupta D, Ketteler R, Ullmann GM, Smith JC, Klingmuller U. Packing density of the erythropoietin receptor transmembrane domain correlates with amplification of biological responses. Biochemistry 2008; 47:11771-82.
    • (2008) Biochemistry , vol.47 , pp. 11771-11782
    • Becker, V.1    Sengupta, D.2    Ketteler, R.3    Ullmann, G.M.4    Smith, J.C.5    Klingmuller, U.6
  • 130
    • 33751526473 scopus 로고    scopus 로고
    • Ligand-Independent Dimerization of the Human Prolactin Receptor Isoforms: Functional Implications
    • Gadd SL, Clevenger CV. Ligand-Independent Dimerization of the Human Prolactin Receptor Isoforms: Functional Implications. Mol Endocrinol 2006; 20:2734-46.
    • (2006) Mol Endocrinol , vol.20 , pp. 2734-2746
    • Gadd, S.L.1    Clevenger, C.V.2
  • 131
  • 132
    • 0027186439 scopus 로고
    • Substitution of the erbB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1
    • Cheatham B, Shoelson SE, Yamada K, Goncalves E, Kahn CR. Substitution of the erbB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1. Proc Natl Acad Sci USA 1993; 90:7336-40.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7336-7340
    • Cheatham, B.1    Shoelson, S.E.2    Yamada, K.3    Goncalves, E.4    Kahn, C.R.5
  • 133
    • 0031031464 scopus 로고    scopus 로고
    • Effect of dimerization on signal transduction and biological function of oncogenic Ros, insulin and insulin-like growth factor I receptors
    • Chan JLK, Lai M, Wang LH. Effect of dimerization on signal transduction and biological function of oncogenic Ros, insulin and insulin-like growth factor I receptors. Journal of Biological Chemistry 1997; 272:146-53.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 146-153
    • Chan, J.L.K.1    Lai, M.2    Wang, L.H.3
  • 134
    • 0032815374 scopus 로고    scopus 로고
    • Substitution of the insulin receptor transmembrane domain with that of glycophorin a inhibits insulin action
    • Gardin A, Auzan C, Clauser E, Malherbe T, Aunis D, Cremel G, et al. Substitution of the insulin receptor transmembrane domain with that of glycophorin A inhibits insulin action. Faseb J 1999; 13:1347-57.
    • (1999) Faseb J , vol.13 , pp. 1347-1357
    • Gardin, A.1    Auzan, C.2    Clauser, E.3    Malherbe, T.4    Aunis, D.5    Cremel, G.6
  • 135
    • 21244460002 scopus 로고    scopus 로고
    • Transmembrane homodimerization of receptor-like protein tyrosine phosphatases
    • Chin CN, Sachs JN, Engelman DM. Transmembrane homodimerization of receptor-like protein tyrosine phosphatases. FEBS Lett 2005; 579:3855-8.
    • (2005) FEBS Lett , vol.579 , pp. 3855-3858
    • Chin, C.N.1    Sachs, J.N.2    Engelman, D.M.3
  • 136
  • 137
    • 0025108858 scopus 로고
    • Assembly and function of the T cell antigen receptor Requirement of either the lysine or arginine residues in the transmembrane region of the alpha chain
    • Blumberg RS, Alarcon B, Sancho J, McDermott FV, Lopez P, Breitmeyer J, et al. Assembly and function of the T cell antigen receptor. Requirement of either the lysine or arginine residues in the transmembrane region of the alpha chain. J Biol Chem 1990; 265:14036-43.
    • (1990) J Biol Chem , vol.265 , pp. 14036-14043
    • Blumberg, R.S.1    Alarcon, B.2    Sancho, J.3    McDermott, F.V.4    Lopez, P.5    Breitmeyer, J.6
  • 138
    • 0026782498 scopus 로고
    • Transmembrane helical interactions: Zeta chain dimerization and functional association with the T cell antigen receptor
    • Rutledge T, Cosson P, Manolios N, Bonifacino JS, Klausner RD. Transmembrane helical interactions: zeta chain dimerization and functional association with the T cell antigen receptor. EMBO J 1992; 11:3245-54.
    • (1992) EMBO J , vol.11 , pp. 3245-3254
    • Rutledge, T.1    Cosson, P.2    Manolios, N.3    Bonifacino, J.S.4    Klausner, R.D.5
  • 140
    • 0026485306 scopus 로고
    • Role of transmembrane domain interactions in the assembly of class II MHC molecules
    • Cosson P, Bonifacino JS. Role of transmembrane domain interactions in the assembly of class II MHC molecules. Science 1992; 258:659-62.
    • (1992) Science , vol.258 , pp. 659-662
    • Cosson, P.1    Bonifacino, J.S.2
  • 141
    • 0035940359 scopus 로고    scopus 로고
    • Oligomerization of the integrin alphaIIbbeta3: Roles of the transmembrane and cytoplasmic domains
    • Li R, Babu CR, Lear JD, Wand AJ, Bennett JS, DeGrado WF. Oligomerization of the integrin alphaIIbbeta3: roles of the transmembrane and cytoplasmic domains. Proc Natl Acad Sci USA 2001; 98:12462-7.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12462-12467
    • Li, R.1    Babu, C.R.2    Lear, J.D.3    Wand, A.J.4    Bennett, J.S.5    DeGrado, W.F.6
  • 142
    • 1642396353 scopus 로고    scopus 로고
    • Involvement of transmembrane domain interactions in signal transduction by alpha/beta integrins
    • Schneider D, Engelman DM. Involvement of transmembrane domain interactions in signal transduction by alpha/beta integrins. J Biol Chem 2004; 279:9840-6.
    • (2004) J Biol Chem , vol.279 , pp. 9840-9846
    • Schneider, D.1    Engelman, D.M.2
  • 143
  • 144
    • 33645020555 scopus 로고    scopus 로고
    • Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved
    • Lin X, Tan SM, Law SK, Torres J. Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved. Proteins 2006; 63:16-23.
    • (2006) Proteins , vol.63 , pp. 16-23
    • Lin, X.1    Tan, S.M.2    Law, S.K.3    Torres, J.4
  • 145
    • 33645913831 scopus 로고    scopus 로고
    • Activation of individual alphaIIbbeta3 integrin molecules by disruption of transmembrane domain interactions in the absence of clustering
    • Litvinov RI, Vilaire G, Li W, DeGrado WF, Weisel JW, Bennett JS. Activation of individual alphaIIbbeta3 integrin molecules by disruption of transmembrane domain interactions in the absence of clustering. Biochemistry 2006; 45:4957-64.
    • (2006) Biochemistry , vol.45 , pp. 4957-4964
    • Litvinov, R.I.1    Vilaire, G.2    Li, W.3    DeGrado, W.F.4    Weisel, J.W.5    Bennett, J.S.6
  • 146
    • 33845995843 scopus 로고    scopus 로고
    • Activation of platelet alphaIIbbeta3 by an exogenous peptide corresponding to the transmembrane domain of alphaIIb
    • Yin H, Litvinov RI, Vilaire G, Zhu H, Li W, Caputo GA, et al. Activation of platelet alphaIIbbeta3 by an exogenous peptide corresponding to the transmembrane domain of alphaIIb. J Biol Chem 2006; 281:36732-41.
    • (2006) J Biol Chem , vol.281 , pp. 36732-36741
    • Yin, H.1    Litvinov, R.I.2    Vilaire, G.3    Zhu, H.4    Li, W.5    Caputo, G.A.6
  • 147
    • 38049174634 scopus 로고    scopus 로고
    • Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions
    • Dews IC, Mackenzie KR. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proc Natl Acad Sci USA 2007; 104:20782-7.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20782-20787
    • Dews, I.C.1    Mackenzie, K.R.2
  • 148
    • 30044440012 scopus 로고    scopus 로고
    • Transmembrane domain-induced oligomerization is crucial for the functions of syndecan-2 and syndecan-4
    • Choi S, Lee E, Kwon S, Park H, Yi JY, Kim S, et al. Transmembrane domain-induced oligomerization is crucial for the functions of syndecan-2 and syndecan-4. J Biol Chem 2005; 280:42573-9.
    • (2005) J Biol Chem , vol.280 , pp. 42573-42579
    • Choi, S.1    Lee, E.2    Kwon, S.3    Park, H.4    Yi, J.Y.5    Kim, S.6
  • 149
    • 35648932886 scopus 로고    scopus 로고
    • Transmembrane domain of myelin protein zero can form dimers: Possible implications for myelin construction
    • Plotkowski ML, Kim S, Phillips ML, Partridge AW, Deber CM, Bowie JU. Transmembrane domain of myelin protein zero can form dimers: possible implications for myelin construction. Biochemistry 2007; 46:12164-73.
    • (2007) Biochemistry , vol.46 , pp. 12164-12173
    • Plotkowski, M.L.1    Kim, S.2    Phillips, M.L.3    Partridge, A.W.4    Deber, C.M.5    Bowie, J.U.6
  • 150
    • 0033490984 scopus 로고    scopus 로고
    • Mutations affecting transmembrane segment interactions impair adhesiveness of E-cadherin
    • Huber O, Kemler R, Langosch D. Mutations affecting transmembrane segment interactions impair adhesiveness of E-cadherin. J Cell Sci 1999; 112:4415-23. (Pubitemid 30122033)
    • (1999) Journal of Cell Science , vol.112 , Issue.23 , pp. 4415-4423
    • Huber, O.1    Kemler, R.2    Langosch, D.3
  • 151
    • 33747778354 scopus 로고    scopus 로고
    • The variable transmembrane domain of Drosophila N-cadherin regulates adhesive activity
    • Yonekura S, Ting CY, Neves G, Hung K, Hsu SN, Chiba A, et al. The variable transmembrane domain of Drosophila N-cadherin regulates adhesive activity. Mol Cell Biol 2006; 26:6598-608.
    • (2006) Mol Cell Biol , vol.26 , pp. 6598-6608
    • Yonekura, S.1    Ting, C.Y.2    Neves, G.3    Hung, K.4    Hsu, S.N.5    Chiba, A.6
  • 152
    • 0037207101 scopus 로고    scopus 로고
    • Mutational analysis of synaptobrevin transmembrane domain oligomerization
    • Bowen ME, Engelman DM, Brunger AT. Mutational analysis of synaptobrevin transmembrane domain oligomerization. Biochemistry 2002; 41:15861-6.
    • (2002) Biochemistry , vol.41 , pp. 15861-15866
    • Bowen, M.E.1    Engelman, D.M.2    Brunger, A.T.3
  • 153
    • 0030661912 scopus 로고    scopus 로고
    • Dimerization of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein) II depends on specific residues within the transmembrane segment
    • Laage R, Langosch D. Dimerization of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein) II depends on specific residues within the transmembrane segment. European Journal of Biochemistry 1997; 249:540-6. (Pubitemid 27455798)
    • (1997) European Journal of Biochemistry , vol.249 , Issue.2 , pp. 540-546
    • Laage, R.1    Langosch, D.2
  • 154
    • 0026686793 scopus 로고
    • Glycophorin a dimerization is driven by specific interactions between transmembrane alpha-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 alpha-helices. J Biol Chem 1992; 267:7683-9.
    • (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
  • 155
    • 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; 95:3583-90.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3583-3590
    • MacKenzie, K.R.1    Engelman, D.M.2
  • 156
    • 0032732426 scopus 로고    scopus 로고
    • Detergents modulate dimerization, but not helicity of the glycophorin a transmembrane domain
    • Fisher LE, Engelman DM, Sturgis JN. Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain. J Mol Biol 1999; 293:639-51.
    • (1999) J Mol Biol , vol.293 , pp. 639-651
    • Fisher, L.E.1    Engelman, D.M.2    Sturgis, J.N.3
  • 157
    • 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; 96:863-8.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 158
    • 33751088317 scopus 로고    scopus 로고
    • Sequence dependence of BNIP3 transmembrane domain dimerization implicates side-chain hydrogen bonding and a tandem GxxxG motif in specific helix-helix interactions
    • Sulistijo ES, MacKenzie KR. Sequence dependence of BNIP3 transmembrane domain dimerization implicates side-chain hydrogen bonding and a tandem GxxxG motif in specific helix-helix interactions. J Mol Biol 2006; 364:974-90.
    • (2006) J Mol Biol , vol.364 , pp. 974-990
    • Sulistijo, E.S.1    MacKenzie, K.R.2
  • 159
    • 21544465581 scopus 로고    scopus 로고
    • An alternative interpretation of the amyloid Abeta hypothesis with regard to the pathogenesis of Alzheimer's disease
    • Marchesi VT. An alternative interpretation of the amyloid Abeta hypothesis with regard to the pathogenesis of Alzheimer's disease. Proc Natl Acad Sci USA 2005; 102:9093-8.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9093-9098
    • Marchesi, V.T.1
  • 160
    • 43149088724 scopus 로고    scopus 로고
    • Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs
    • Kienlen-Campard P, Tasiaux B, Van Hees J, Li M, Huysseune S, Sato T, et al. Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs. J Biol Chem 2008; 283:7733-44.
    • (2008) J Biol Chem , vol.283 , pp. 7733-7744
    • Kienlen-Campard, P.1    Tasiaux, B.2    Van Hees, J.3    Li, M.4    Huysseune, S.5    Sato, T.6
  • 161
    • 60849131737 scopus 로고    scopus 로고
    • A helix-to-coil transition at the epsilon-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis
    • Sato T, Tang TC, Reubins G, Fei JZ, Fujimoto T, Kienlen-Campard P, et al. A helix-to-coil transition at the epsilon-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis. Proc Natl Acad Sci USA 2009; 106:1421-6.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1421-1426
    • Sato, T.1    Tang, T.C.2    Reubins, G.3    Fei, J.Z.4    Fujimoto, T.5    Kienlen-Campard, P.6
  • 162
    • 33947597857 scopus 로고    scopus 로고
    • GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42
    • Munter LM, Voigt P, Harmeier A, Kaden D, Gottschalk KE, Weise C, et al. GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42. EMBO J 2007; 26:1702-12.
    • (2007) EMBO J , vol.26 , pp. 1702-1712
    • Munter, L.M.1    Voigt, P.2    Harmeier, A.3    Kaden, D.4    Gottschalk, K.E.5    Weise, C.6
  • 163
    • 0012597802 scopus 로고
    • Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene
    • Bargmann CI, Weinberg RA. Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene. Proc Natl Acad Sci USA 1988; 85:5394-8.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5394-5398
    • Bargmann, C.I.1    Weinberg, R.A.2
  • 165
    • 19944430581 scopus 로고    scopus 로고
    • Mutations that cause osteoglophonic dysplasia define novel roles for FGFR1 in bone elongation
    • White KE, Cabral JM, Davis SI, Fishburn T, Evans WE, Ichikawa S, et al. Mutations that cause osteoglophonic dysplasia define novel roles for FGFR1 in bone elongation. Am J Hum Genet 2005; 76:361-7.
    • (2005) Am J Hum Genet , vol.76 , pp. 361-367
    • White, K.E.1    Cabral, J.M.2    Davis, S.I.3    Fishburn, T.4    Evans, W.E.5    Ichikawa, S.6
  • 166
    • 15844388219 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor 2 mutations in Beare-Stevenson Cutis gyrata syndrome
    • Przylepa KA, Paznekas W, Zhang M, Golabi M, Bias W, Bamshad MJ, et al. Fibroblast growth factor receptor 2 mutations in Beare-Stevenson Cutis gyrata syndrome. Nat Genet 1996; 13:492-4.
    • (1996) Nat Genet , vol.13 , pp. 492-494
    • Przylepa, K.A.1    Paznekas, W.2    Zhang, M.3    Golabi, M.4    Bias, W.5    Bamshad, M.J.6
  • 167
    • 0028793472 scopus 로고
    • Fibroblast growth factor receptor 3 (FGFR3) transmembrane mutation in Crouzon syndrome with Acanthosis nigricans
    • Meyers GA, Orlow SJ, Munro IR, Przylepa KA, Jabs EW. Fibroblast growth factor receptor 3 (FGFR3) transmembrane mutation in Crouzon syndrome with Acanthosis nigricans. Nat Genet 1995; 11:462-4.
    • (1995) Nat Genet , vol.11 , pp. 462-464
    • Meyers, G.A.1    Orlow, S.J.2    Munro, I.R.3    Przylepa, K.A.4    Jabs, E.W.5
  • 168
    • 0030485182 scopus 로고    scopus 로고
    • Common mutations in the gene encoding fibroblast growth factor receptor 3 account for achondroplasia, hypochondroplasia and thanatophoric dysplasia
    • Bonaventure J, Rousseau F, Legeai-Mallet L, Le Merrer M, Munnich A, Maroteaux P. Common mutations in the gene encoding fibroblast growth factor receptor 3 account for achondroplasia, hypochondroplasia and thanatophoric dysplasia. Acta Paediatr Suppl 1996; 417:33-8.
    • (1996) Acta Paediatr Suppl , vol.417 , pp. 33-38
    • Bonaventure, J.1    Rousseau, F.2    Legeai-Mallet, L.3    Le Merrer, M.4    Munnich, A.5    Maroteaux, P.6
  • 169
    • 0031005778 scopus 로고    scopus 로고
    • FGFR activation in skeletal disorders: Too much of a good thing
    • Webster MK, Donoghue DJ. FGFR activation in skeletal disorders: too much of a good thing. Trends Genet 1997; 13:178-82.
    • (1997) Trends Genet , vol.13 , pp. 178-182
    • Webster, M.K.1    Donoghue, D.J.2
  • 170
    • 0036468871 scopus 로고    scopus 로고
    • Cancer progression and tumor cell motility are associated with the FGFR4 Arg(388) allele
    • Bange J, Prechtl D, Cheburkin Y, Specht K, Harbeck N, Schmitt M, et al. Cancer progression and tumor cell motility are associated with the FGFR4 Arg(388) allele. Cancer Res 2002; 62:840-7.
    • (2002) Cancer Res , vol.62 , pp. 840-847
    • Bange, J.1    Prechtl, D.2    Cheburkin, Y.3    Specht, K.4    Harbeck, N.5    Schmitt, M.6
  • 171
    • 33846484813 scopus 로고    scopus 로고
    • Identification of a novel G245R polymorphism in the IL-2 receptor beta membrane proximal domain associated with human visceral leishmaniasis
    • Bucheton B, Argiro L, Chevillard C, Marquet S, Kheir MM, Mergani A, et al. Identification of a novel G245R polymorphism in the IL-2 receptor beta membrane proximal domain associated with human visceral leishmaniasis. Genes Immun 2007; 8:79-83.
    • (2007) Genes Immun , vol.8 , pp. 79-83
    • Bucheton, B.1    Argiro, L.2    Chevillard, C.3    Marquet, S.4    Kheir, M.M.5    Mergani, A.6
  • 172
    • 0027422165 scopus 로고
    • De novo mutation of the myelin P0 gene in Dejerine-Sottas disease (hereditary motor and sensory neuropathy type III)
    • Hayasaka K, Himoro M, Sawaishi Y, Nanao K, Takahashi T, Takada G, et al. De novo mutation of the myelin P0 gene in Dejerine-Sottas disease (hereditary motor and sensory neuropathy type III). Nat Genet 1993; 5:266-8.
    • (1993) Nat Genet , vol.5 , pp. 266-268
    • Hayasaka, K.1    Himoro, M.2    Sawaishi, Y.3    Nanao, K.4    Takahashi, T.5    Takada, G.6
  • 173
    • 0036157054 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease and related neuropathies: Mutation distribution and genotype-phenotype correlation
    • Boerkoel CF, Takashima H, Garcia CA, Olney RK, Johnson J, Berry K, et al. Charcot-Marie-Tooth disease and related neuropathies: mutation distribution and genotype-phenotype correlation. Ann Neurol 2002; 51:190-201.
    • (2002) Ann Neurol , vol.51 , pp. 190-201
    • Boerkoel, C.F.1    Takashima, H.2    Garcia, C.A.3    Olney, R.K.4    Johnson, J.5    Berry, K.6
  • 174
    • 2642510733 scopus 로고    scopus 로고
    • Clinical and genetic description of a family with Charcot-Marie-Tooth disease type 1B from a transmembrane MPZ mutation
    • Eggers SD, Keswani SC, Melli G, Cornblath DR. Clinical and genetic description of a family with Charcot-Marie-Tooth disease type 1B from a transmembrane MPZ mutation. Muscle Nerve 2004; 29:867-9.
    • (2004) Muscle Nerve , vol.29 , pp. 867-869
    • Eggers, S.D.1    Keswani, S.C.2    Melli, G.3    Cornblath, D.R.4
  • 176
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G. Global topology analysis of the Escherichia coli inner membrane proteome. Science 2005; 308:1321-3.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    Von Heijne, G.6
  • 177
    • 70350038016 scopus 로고    scopus 로고
    • Mapping the human membrane proteome: A majority of the human membrane proteins can be classified according to function and evolutionary origin
    • Almen MS, Nordstrom KJ, Fredriksson R, Schioth HB. Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin. BMC Biol 2009; 7:50.
    • (2009) BMC Biol , vol.7 , pp. 50
    • Almen, M.S.1    Nordstrom, K.J.2    Fredriksson, R.3    Schioth, H.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.