메뉴 건너뛰기




Volumn 1859, Issue 4, 2017, Pages 561-576

Helix-helix interactions in membrane domains of bitopic proteins: Specificity and role of lipid environment

Author keywords

bitopic membrane protein; lipid density fluctuations; protein lipid and protein protein interactions; receptor tyrosine kinase; signal transduction; transmembrane domain

Indexed keywords

BITOPIC PROTEIN; CELL RECEPTOR; LIPID; MEMBRANE PROTEIN; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG; LIPID BILAYER; MEMBRANE LIPID;

EID: 85007369942     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2016.10.024     Document Type: Review
Times cited : (72)

References (187)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • [1] Singer, S.J., Nicolson, G.L., The fluid mosaic model of the structure of cell membranes. Science 175 (1972), 720–731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 84899444997 scopus 로고    scopus 로고
    • The Fluid-Mosaic Model of Membrane Structure: still relevant to understanding the structure, function and dynamics of biological membranes after >�40 years
    • [2] Nicolson, G.L., The Fluid-Mosaic Model of Membrane Structure: still relevant to understanding the structure, function and dynamics of biological membranes after >�40 years. Biochim. Biophys. Acta 1838 (2014), 1451–1466, 10.1016/j.bbamem.2013.10.019.
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 1451-1466
    • Nicolson, G.L.1
  • 3
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • [3] Simons, K., Ikonen, E., Functional rafts in cell membranes. Nature 387 (1997), 569–572, 10.1038/42408.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 4
    • 0034859215 scopus 로고    scopus 로고
    • Characterization of cholesterol-sphingomyelin domains and their dynamics in bilayer membranes
    • [4] Samsonov, A.V., Mihalyov, I., Cohen, F.S., Characterization of cholesterol-sphingomyelin domains and their dynamics in bilayer membranes. Biophys. J. 81 (2001), 1486–1500, 10.1016/S0006-3495(01)75803-1.
    • (2001) Biophys. J. , vol.81 , pp. 1486-1500
    • Samsonov, A.V.1    Mihalyov, I.2    Cohen, F.S.3
  • 5
    • 0242331729 scopus 로고    scopus 로고
    • Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension
    • [5] Baumgart, T., Hess, S.T., Webb, W.W., Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension. Nature 425 (2003), 821–824, 10.1038/nature02013.
    • (2003) Nature , vol.425 , pp. 821-824
    • Baumgart, T.1    Hess, S.T.2    Webb, W.W.3
  • 6
    • 29144531904 scopus 로고    scopus 로고
    • Seeing spots: complex phase behavior in simple membranes
    • [6] Veatch, S.L., Keller, S.L., Seeing spots: complex phase behavior in simple membranes. Biochim. Biophys. Acta 1746 (2005), 172–185, 10.1016/j.bbamcr.2005.06.010.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 172-185
    • Veatch, S.L.1    Keller, S.L.2
  • 7
    • 33748476306 scopus 로고    scopus 로고
    • Lipid peroxides promote large rafts: effects of excitation of probes in fluorescence microscopy and electrochemical reactions during vesicle formation
    • [7] Ayuyan, A.G., Cohen, F.S., Lipid peroxides promote large rafts: effects of excitation of probes in fluorescence microscopy and electrochemical reactions during vesicle formation. Biophys. J. 91 (2006), 2172–2183, 10.1529/biophysj.106.087387.
    • (2006) Biophys. J. , vol.91 , pp. 2172-2183
    • Ayuyan, A.G.1    Cohen, F.S.2
  • 9
    • 0030771336 scopus 로고    scopus 로고
    • Wetting and capillary condensation as means of protein organization in membranes
    • [9] Gil, T., Sabra, M.C., Ipsen, J.H., Mouritsen, O.G., Wetting and capillary condensation as means of protein organization in membranes. Biophys. J. 73 (1997), 1728–1741, 10.1016/S0006-3495(97)78204-3.
    • (1997) Biophys. J. , vol.73 , pp. 1728-1741
    • Gil, T.1    Sabra, M.C.2    Ipsen, J.H.3    Mouritsen, O.G.4
  • 11
    • 84960157108 scopus 로고    scopus 로고
    • Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations
    • [11] Hedger, G., Sansom, M.S.P., Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations. Biochim. Biophys. Acta 1858 (2016), 2390–2400.
    • (2016) Biochim. Biophys. Acta , vol.1858 , pp. 2390-2400
    • Hedger, G.1    Sansom, M.S.P.2
  • 12
    • 84874644958 scopus 로고    scopus 로고
    • Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells
    • [12] Hulce, J.J., Cognetta, A.B., Niphakis, M.J., Tully, S.E., Cravatt, B.F., Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells. Nat. Methods 10 (2013), 259–264, 10.1038/nmeth.2368.
    • (2013) Nat. Methods , vol.10 , pp. 259-264
    • Hulce, J.J.1    Cognetta, A.B.2    Niphakis, M.J.3    Tully, S.E.4    Cravatt, B.F.5
  • 14
    • 84936892311 scopus 로고    scopus 로고
    • The influence of cholesterol on membrane protein structure, function, and dynamics studied by molecular dynamics simulations
    • [14] Grouleff, J., Irudayam, S.J., Skeby, K.K., Schi�tt, B., The influence of cholesterol on membrane protein structure, function, and dynamics studied by molecular dynamics simulations. Biochim. Biophys. Acta 1848 (2015), 1783–1795, 10.1016/j.bbamem.2015.03.029.
    • (2015) Biochim. Biophys. Acta , vol.1848 , pp. 1783-1795
    • Grouleff, J.1    Irudayam, S.J.2    Skeby, K.K.3    Schi�tt, B.4
  • 15
    • 84936891731 scopus 로고    scopus 로고
    • Functional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization
    • [15] Stangl, M., Schneider, D., Functional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization. Biochim. Biophys. Acta 1848 (2015), 1886–1896, 10.1016/j.bbamem.2015.03.011.
    • (2015) Biochim. Biophys. Acta , vol.1848 , pp. 1886-1896
    • Stangl, M.1    Schneider, D.2
  • 18
    • 0001751245 scopus 로고    scopus 로고
    • A requirement for lipid rafts in B cell receptor induced Ca(2�+) flux
    • [18] Aman, M.J., Ravichandran, K.S., A requirement for lipid rafts in B cell receptor induced Ca(2�+) flux. Curr. Biol. 10 (2000), 393–396, 10.1016/S0960-9822(00)00415-2.
    • (2000) Curr. Biol. , vol.10 , pp. 393-396
    • Aman, M.J.1    Ravichandran, K.S.2
  • 19
    • 0036695812 scopus 로고    scopus 로고
    • Influence of gangliosides on the IL-2- and IL-4-dependent cell proliferation
    • [19] Molotkovskaya, I.M., Kholodenko, R.V., Molotkovsky, J.G., Influence of gangliosides on the IL-2- and IL-4-dependent cell proliferation. Neurochem. Res. 27 (2002), 761–770, 10.1023/A:1020248722282.
    • (2002) Neurochem. Res. , vol.27 , pp. 761-770
    • Molotkovskaya, I.M.1    Kholodenko, R.V.2    Molotkovsky, J.G.3
  • 20
    • 84948695261 scopus 로고    scopus 로고
    • Structure of Full-Length Human PDGFRβ Bound to Its Activating Ligand PDGF-B as Determined by Negative-Stain Electron Microscopy
    • [20] Chen, P.-H., Unger, V., He, X., Structure of Full-Length Human PDGFRβ Bound to Its Activating Ligand PDGF-B as Determined by Negative-Stain Electron Microscopy. J. Mol. Biol. 427 (2015), 3921–3934, 10.1016/j.jmb.2015.10.003.
    • (2015) J. Mol. Biol. , vol.427 , pp. 3921-3934
    • Chen, P.-H.1    Unger, V.2    He, X.3
  • 21
    • 84952815577 scopus 로고    scopus 로고
    • Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase
    • [21] Trenker, R., Call, M.E., Call, M.J., Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase. J. Am. Chem. Soc. 137 (2015), 15676–15679, 10.1021/jacs.5b11354.
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 15676-15679
    • Trenker, R.1    Call, M.E.2    Call, M.J.3
  • 22
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • [22] Ullrich, A., Schlessinger, J., Signal transduction by receptors with tyrosine kinase activity. Cell 61 (1990), 203–212, 10.1016/0092-8674(90)90801-K.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 23
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • [23] Heldin, C.H., Dimerization of cell surface receptors in signal transduction. Cell 80 (1995), 213–223, 10.1016/0092-8674(95)90404-2.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 25
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • [25] Lemmon, M.A., Schlessinger, J., Cell signaling by receptor tyrosine kinases. Cell 141 (2010), 1117–1134, 10.1016/j.cell.2010.06.011.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 26
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • [26] Shi, Y., Massagu�, J., Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 113 (2003), 685–700, 10.1016/S0092-8674(03)00432-X.
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massagu�, J.2
  • 27
    • 72849114709 scopus 로고    scopus 로고
    • Modulation of the Bioactive Conformation of Transforming Growth Factor β: Possible Implications of Cation Binding for Biological Function
    • [27] Bocharov, E.V., Pavlov, K.V., Blommers, M.J.J., Arvinte, T., Arseniev, A.S., Modulation of the Bioactive Conformation of Transforming Growth Factor β: Possible Implications of Cation Binding for Biological Function. Top. Curr. Chem. 273 (2008), 155–181, 10.1007/128_2007_17.
    • (2008) Top. Curr. Chem. , vol.273 , pp. 155-181
    • Bocharov, E.V.1    Pavlov, K.V.2    Blommers, M.J.J.3    Arvinte, T.4    Arseniev, A.S.5
  • 28
    • 9944246020 scopus 로고    scopus 로고
    • A Putative Mechanism for Downregulation of the Catalytic Activity of the EGF Receptor via Direct Contact between Its Kinase and C-Terminal Domains
    • [28] Landau, M., Fleishman, S.J., Ben-Tal, N., A Putative Mechanism for Downregulation of the Catalytic Activity of the EGF Receptor via Direct Contact between Its Kinase and C-Terminal Domains. Structure 12 (2004), 2265–2275, 10.1016/j.str.2004.10.006.
    • (2004) Structure , vol.12 , pp. 2265-2275
    • Landau, M.1    Fleishman, S.J.2    Ben-Tal, N.3
  • 30
    • 62649159075 scopus 로고    scopus 로고
    • Ligand-induced ErbB receptor dimerization
    • [30] Lemmon, M.A., Ligand-induced ErbB receptor dimerization. Exp. Cell Res. 315 (2009), 638–648, 10.1016/j.yexcr.2008.10.024.
    • (2009) Exp. Cell Res. , vol.315 , pp. 638-648
    • Lemmon, M.A.1
  • 31
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • [31] Schlessinger, J., Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 110 (2002), 669–672, 10.1016/S0092-8674(02)00966-2.
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 33
    • 55449102296 scopus 로고    scopus 로고
    • All EGF(ErbB) receptors have preformed homo- and heterodimeric structures in living cells
    • [33] Tao, R.-H., Maruyama, I.N., All EGF(ErbB) receptors have preformed homo- and heterodimeric structures in living cells. J. Cell Sci. 121 (2008), 3207–3217, 10.1242/jcs.033399.
    • (2008) J. Cell Sci. , vol.121 , pp. 3207-3217
    • Tao, R.-H.1    Maruyama, I.N.2
  • 35
    • 33847619358 scopus 로고    scopus 로고
    • The insulin and EGF receptor structures: new insights into ligand-induced receptor activation
    • [35] Ward, C.W., Lawrence, M.C., Streltsov, V.A., Adams, T.E., McKern, N.M., The insulin and EGF receptor structures: new insights into ligand-induced receptor activation. Trends Biochem. Sci. 32 (2007), 129–137, 10.1016/j.tibs.2007.01.001.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 129-137
    • Ward, C.W.1    Lawrence, M.C.2    Streltsov, V.A.3    Adams, T.E.4    McKern, N.M.5
  • 36
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • [36] Moriki, T., Maruyama, H., Maruyama, I.N., Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J. Mol. Biol. 311 (2001), 1011–1026, 10.1006/jmbi.2001.4923.
    • (2001) J. Mol. Biol. , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 37
    • 0036225144 scopus 로고    scopus 로고
    • Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling
    • [37] Martin-Fernandez, M., Clarke, D.T., Tobin, M.J., Jones, S.V., Jones, G.R., Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling. Biophys. J. 82 (2002), 2415–2427, 10.1016/S0006-3495(02)75585-9.
    • (2002) Biophys. J. , vol.82 , pp. 2415-2427
    • Martin-Fernandez, M.1    Clarke, D.T.2    Tobin, M.J.3    Jones, S.V.4    Jones, G.R.5
  • 38
    • 24044436190 scopus 로고    scopus 로고
    • Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis
    • [38] Clayton, A.H.A., Walker, F., Orchard, S.G., Henderson, C., Fuchs, D., Rothacker, J., Nice, E.C., Burgess, A.W., Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis. J. Biol. Chem. 280 (2005), 30392–30399, 10.1074/jbc.M504770200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30392-30399
    • Clayton, A.H.A.1    Walker, F.2    Orchard, S.G.3    Henderson, C.4    Fuchs, D.5    Rothacker, J.6    Nice, E.C.7    Burgess, A.W.8
  • 39
    • 34447299688 scopus 로고    scopus 로고
    • Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy
    • [39] Liu, P., Sudhaharan, T., Koh, R.M.L., Hwang, L.C., Ahmed, S., Maruyama, I.N., Wohland, T., Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy. Biophys. J. 93 (2007), 684–698, 10.1529/biophysj.106.102087.
    • (2007) Biophys. J. , vol.93 , pp. 684-698
    • Liu, P.1    Sudhaharan, T.2    Koh, R.M.L.3    Hwang, L.C.4    Ahmed, S.5    Maruyama, I.N.6    Wohland, T.7
  • 40
    • 34447313361 scopus 로고    scopus 로고
    • Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis
    • [40] Saffarian, S., Li, Y., Elson, E.L., Pike, L.J., Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis. Biophys. J. 93 (2007), 1021–1031, 10.1529/biophysj.107.105494.
    • (2007) Biophys. J. , vol.93 , pp. 1021-1031
    • Saffarian, S.1    Li, Y.2    Elson, E.L.3    Pike, L.J.4
  • 41
    • 79957820213 scopus 로고    scopus 로고
    • EGFR activation monitored by SW-FCCS in live cells
    • [41] Ma, X., Ahmed, S., Wohland, T., EGFR activation monitored by SW-FCCS in live cells. Front. Biosci. Elite Ed. 3 (2011), 22–32.
    • (2011) Front. Biosci. Elite Ed. , vol.3 , pp. 22-32
    • Ma, X.1    Ahmed, S.2    Wohland, T.3
  • 42
    • 0033786730 scopus 로고    scopus 로고
    • Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase
    • [42] Bell, C.A., Tynan, J.A., Hart, K.C., Meyer, A.N., Robertson, S.C., Donoghue, D.J., Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase. Mol. Biol. Cell 11 (2000), 3589–3599, 10.1091/mbc.11.10.3589.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3589-3599
    • Bell, C.A.1    Tynan, J.A.2    Hart, K.C.3    Meyer, A.N.4    Robertson, S.C.5    Donoghue, D.J.6
  • 43
    • 33748939242 scopus 로고    scopus 로고
    • Single-molecule analysis of epidermal growth factor binding on the surface of living cells
    • [43] Teramura, Y., Ichinose, J., Takagi, H., Nishida, K., Yanagida, T., Sako, Y., Single-molecule analysis of epidermal growth factor binding on the surface of living cells. EMBO J. 25 (2006), 4215–4222, 10.1038/sj.emboj.7601308.
    • (2006) EMBO J. , vol.25 , pp. 4215-4222
    • Teramura, Y.1    Ichinose, J.2    Takagi, H.3    Nishida, K.4    Yanagida, T.5    Sako, Y.6
  • 44
    • 84886907697 scopus 로고    scopus 로고
    • Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging
    • [44] Macdonald-Obermann, J.L., Adak, S., Landgraf, R., Piwnica-Worms, D., Pike, L.J., Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging. J. Biol. Chem. 288 (2013), 30773–30784, 10.1074/jbc.M113.489534.
    • (2013) J. Biol. Chem. , vol.288 , pp. 30773-30784
    • Macdonald-Obermann, J.L.1    Adak, S.2    Landgraf, R.3    Piwnica-Worms, D.4    Pike, L.J.5
  • 45
    • 65549138069 scopus 로고    scopus 로고
    • Luciferase fragment complementation imaging of conformational changes in the epidermal growth factor receptor
    • [45] Yang, K.S., Ilagan, M.X.G., Piwnica-Worms, D., Pike, L.J., Luciferase fragment complementation imaging of conformational changes in the epidermal growth factor receptor. J. Biol. Chem. 284 (2009), 7474–7482, 10.1074/jbc.M808041200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7474-7482
    • Yang, K.S.1    Ilagan, M.X.G.2    Piwnica-Worms, D.3    Pike, L.J.4
  • 46
    • 84925424845 scopus 로고    scopus 로고
    • Oligomerization-function relationship of EGFR on living cells detected by the coiled-coil labeling and FRET microscopy
    • [46] Yamashita, H., Yano, Y., Kawano, K., Matsuzaki, K., Oligomerization-function relationship of EGFR on living cells detected by the coiled-coil labeling and FRET microscopy. Biochim. Biophys. Acta 1848 (2015), 1359–1366, 10.1016/j.bbamem.2015.03.004.
    • (2015) Biochim. Biophys. Acta , vol.1848 , pp. 1359-1366
    • Yamashita, H.1    Yano, Y.2    Kawano, K.3    Matsuzaki, K.4
  • 48
    • 84856072855 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor receptor TrkB exists as a preformed dimer in living cells
    • [48] Shen, J., Maruyama, I.N., Brain-derived neurotrophic factor receptor TrkB exists as a preformed dimer in living cells. J. Mol. Signal., 7, 2012, 2, 10.1186/1750-2187-7-2.
    • (2012) J. Mol. Signal. , vol.7 , pp. 2
    • Shen, J.1    Maruyama, I.N.2
  • 50
    • 84964501391 scopus 로고    scopus 로고
    • VEGFR-2 conformational switch in response to ligand binding
    • [50] Sarabipour, S., Ballmer-Hofer, K., Hristova, K., VEGFR-2 conformational switch in response to ligand binding. eLife, 5, 2016, 10.7554/eLife.13876.
    • (2016) eLife , vol.5
    • Sarabipour, S.1    Ballmer-Hofer, K.2    Hristova, K.3
  • 52
    • 33646381647 scopus 로고    scopus 로고
    • Active conformation of the erythropoietin receptor: random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains
    • [52] Lu, X., Gross, A.W., Lodish, H.F., Active conformation of the erythropoietin receptor: random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains. J. Biol. Chem. 281 (2006), 7002–7011, 10.1074/jbc.M512638200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7002-7011
    • Lu, X.1    Gross, A.W.2    Lodish, H.F.3
  • 53
    • 0033615077 scopus 로고    scopus 로고
    • Receptor signaling: When dimerization is not enough
    • [53] Jiang, G., Hunter, T., Receptor signaling: When dimerization is not enough. Curr. Biol. 9 (1999), R568–R571, 10.1016/S0960-9822(99)80357-1.
    • (1999) Curr. Biol. , vol.9 , pp. R568-R571
    • Jiang, G.1    Hunter, T.2
  • 54
    • 18744378545 scopus 로고    scopus 로고
    • A putative molecular-activation switch in the transmembrane domain of erbB2
    • [54] Fleishman, S.J., Schlessinger, J., Ben-Tal, N., A putative molecular-activation switch in the transmembrane domain of erbB2. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 15937–15940, 10.1073/pnas.252640799.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 15937-15940
    • Fleishman, S.J.1    Schlessinger, J.2    Ben-Tal, N.3
  • 55
    • 84964595928 scopus 로고    scopus 로고
    • Type I Interferon Signaling Is Decoupled from Specific Receptor Orientation through Lenient Requirements of the Transmembrane Domain
    • [55] Sharma, N., Longjam, G., Schreiber, G., Type I Interferon Signaling Is Decoupled from Specific Receptor Orientation through Lenient Requirements of the Transmembrane Domain. J. Biol. Chem. 291 (2016), 3371–3384, 10.1074/jbc.M115.686071.
    • (2016) J. Biol. Chem. , vol.291 , pp. 3371-3384
    • Sharma, N.1    Longjam, G.2    Schreiber, G.3
  • 56
    • 0028788339 scopus 로고
    • Activation of the EGF receptor by insertional mutations in its juxtamembrane regions
    • [56] Sorokin, A., Activation of the EGF receptor by insertional mutations in its juxtamembrane regions. Oncogene 11 (1995), 1531–1540.
    • (1995) Oncogene , vol.11 , pp. 1531-1540
    • Sorokin, A.1
  • 58
    • 78649548465 scopus 로고    scopus 로고
    • Structural Evidence for Loose Linkage between Ligand Binding and Kinase Activation in the Epidermal Growth Factor Receptor
    • [58] Lu, C., Mi, L.-Z., Grey, M.J., Zhu, J., Graef, E., Yokoyama, S., Springer, T.A., Structural Evidence for Loose Linkage between Ligand Binding and Kinase Activation in the Epidermal Growth Factor Receptor. Mol. Cell. Biol. 30 (2010), 5432–5443, 10.1128/MCB.00742-10.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 5432-5443
    • Lu, C.1    Mi, L.-Z.2    Grey, M.J.3    Zhu, J.4    Graef, E.5    Yokoyama, S.6    Springer, T.A.7
  • 59
    • 84868323253 scopus 로고    scopus 로고
    • Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor
    • [59] Lu, C., Mi, L.-Z., Sch�rpf, T., Walz, T., Springer, T.A., Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor. J. Biol. Chem. 287 (2012), 38244–38253, 10.1074/jbc.M112.414391.
    • (2012) J. Biol. Chem. , vol.287 , pp. 38244-38253
    • Lu, C.1    Mi, L.-Z.2    Sch�rpf, T.3    Walz, T.4    Springer, T.A.5
  • 60
    • 84912114619 scopus 로고    scopus 로고
    • Complex relationship between ligand binding and dimerization in the epidermal growth factor receptor
    • [60] Bessman, N.J., Bagchi, A., Ferguson, K.M., Lemmon, M.A., Complex relationship between ligand binding and dimerization in the epidermal growth factor receptor. Cell Rep. 9 (2014), 1306–1317, 10.1016/j.celrep.2014.10.010.
    • (2014) Cell Rep. , vol.9 , pp. 1306-1317
    • Bessman, N.J.1    Bagchi, A.2    Ferguson, K.M.3    Lemmon, M.A.4
  • 61
    • 14844355538 scopus 로고    scopus 로고
    • The Transmembrane Domains of ErbB Receptors do not Dimerize Strongly in Micelles
    • [61] Stanley, A.M., Fleming, K.G., The Transmembrane Domains of ErbB Receptors do not Dimerize Strongly in Micelles. J. Mol. Biol. 347 (2005), 759–772, 10.1016/j.jmb.2005.01.059.
    • (2005) J. Mol. Biol. , vol.347 , pp. 759-772
    • Stanley, A.M.1    Fleming, K.G.2
  • 62
    • 0036408542 scopus 로고    scopus 로고
    • Standardizing the Free Energy Change of Transmembrane Helix–Helix Interactions
    • [62] Fleming, K.G., Standardizing the Free Energy Change of Transmembrane Helix–Helix Interactions. J. Mol. Biol. 323 (2002), 563–571, 10.1016/S0022-2836(02)00920-8.
    • (2002) J. Mol. Biol. , vol.323 , pp. 563-571
    • Fleming, K.G.1
  • 64
    • 33847118661 scopus 로고    scopus 로고
    • A dimerization hierarchy in the transmembrane domains of the HER receptor family
    • [64] Duneau, J.-P., Vegh, A.P., Sturgis, J.N., A dimerization hierarchy in the transmembrane domains of the HER receptor family. Biochemistry 46 (2007), 2010–2019, 10.1021/bi061436f.
    • (2007) Biochemistry , vol.46 , pp. 2010-2019
    • Duneau, J.-P.1    Vegh, A.P.2    Sturgis, J.N.3
  • 65
    • 68949110276 scopus 로고    scopus 로고
    • Energetics of ErbB1 transmembrane domain dimerization in lipid bilayers
    • [65] Chen, L., Merzlyakov, M., Cohen, T., Shai, Y., Hristova, K., Energetics of ErbB1 transmembrane domain dimerization in lipid bilayers. Biophys. J. 96 (2009), 4622–4630, 10.1016/j.bpj.2009.03.004.
    • (2009) Biophys. J. , vol.96 , pp. 4622-4630
    • Chen, L.1    Merzlyakov, M.2    Cohen, T.3    Shai, Y.4    Hristova, K.5
  • 66
    • 11844249905 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and forster resonance energy transfer suggest weak interactions between fibroblast growth factor receptor 3 (FGFR3) transmembrane domains in the absence of extracellular domains and ligands
    • [66] Li, E., You, M., Hristova, K., Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and forster resonance energy transfer suggest weak interactions between fibroblast growth factor receptor 3 (FGFR3) transmembrane domains in the absence of extracellular domains and ligands. Biochemistry 44 (2005), 352–360, 10.1021/bi048480k.
    • (2005) Biochemistry , vol.44 , pp. 352-360
    • Li, E.1    You, M.2    Hristova, K.3
  • 67
    • 84867327158 scopus 로고    scopus 로고
    • Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET
    • [67] Placone, J., Hristova, K., Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET. PLoS One, 7, 2012, e46678, 10.1371/journal.pone.0046678.
    • (2012) PLoS One , vol.7
    • Placone, J.1    Hristova, K.2
  • 68
    • 33645096586 scopus 로고    scopus 로고
    • Transmembrane helix heterodimerization in lipid bilayers: probing the energetics behind autosomal dominant growth disorders
    • [68] Merzlyakov, M., You, M., Li, E., Hristova, K., Transmembrane helix heterodimerization in lipid bilayers: probing the energetics behind autosomal dominant growth disorders. J. Mol. Biol. 358 (2006), 1–7, 10.1016/j.jmb.2006.01.086.
    • (2006) J. Mol. Biol. , vol.358 , pp. 1-7
    • Merzlyakov, M.1    You, M.2    Li, E.3    Hristova, K.4
  • 69
    • 34548013094 scopus 로고    scopus 로고
    • Studies of Receptor Tyrosine Kinase Transmembrane Domain Interactions: The EmEx-FRET Method
    • [69] Merzlyakov, M., Chen, L., Hristova, K., Studies of Receptor Tyrosine Kinase Transmembrane Domain Interactions: The EmEx-FRET Method. J. Membr. Biol. 215 (2007), 93–103, 10.1007/s00232-007-9009-0.
    • (2007) J. Membr. Biol. , vol.215 , pp. 93-103
    • Merzlyakov, M.1    Chen, L.2    Hristova, K.3
  • 70
    • 77949371562 scopus 로고    scopus 로고
    • Measuring the energetics of membrane protein dimerization in mammalian membranes
    • [70] Chen, L., Novicky, L., Merzlyakov, M., Hristov, T., Hristova, K., Measuring the energetics of membrane protein dimerization in mammalian membranes. J. Am. Chem. Soc. 132 (2010), 3628–3635, 10.1021/ja910692u.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3628-3635
    • Chen, L.1    Novicky, L.2    Merzlyakov, M.3    Hristov, T.4    Hristova, K.5
  • 71
    • 84877024051 scopus 로고    scopus 로고
    • Glycophorin A transmembrane domain dimerization in plasma membrane vesicles derived from CHO, HEK 293�T, and A431 cells
    • [71] Sarabipour, S., Hristova, K., Glycophorin A transmembrane domain dimerization in plasma membrane vesicles derived from CHO, HEK 293�T, and A431 cells. Biochim. Biophys. Acta 1828 (2013), 1829–1833, 10.1016/j.bbamem.2013.03.022.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1829-1833
    • Sarabipour, S.1    Hristova, K.2
  • 72
    • 84964330961 scopus 로고    scopus 로고
    • Effect of the achondroplasia mutation on FGFR3 dimerization and FGFR3 structural response to fgf1 and fgf2: A quantitative FRET study in osmotically derived plasma membrane vesicles
    • [72] Sarabipour, S., Hristova, K., Effect of the achondroplasia mutation on FGFR3 dimerization and FGFR3 structural response to fgf1 and fgf2: A quantitative FRET study in osmotically derived plasma membrane vesicles. Biochim. Biophys. Acta 1858 (2016), 1436–1442, 10.1016/j.bbamem.2016.03.027.
    • (2016) Biochim. Biophys. Acta , vol.1858 , pp. 1436-1442
    • Sarabipour, S.1    Hristova, K.2
  • 73
    • 73349087177 scopus 로고    scopus 로고
    • The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions
    • (ra56-ra56)
    • [73] Finger, C., Escher, C., Schneider, D., The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions. Sci. Signal., 2, 2009, 10.1126/scisignal.2000547 (ra56-ra56).
    • (2009) Sci. Signal. , vol.2
    • Finger, C.1    Escher, C.2    Schneider, D.3
  • 74
    • 84869105188 scopus 로고    scopus 로고
    • Isolated Toll-like Receptor Transmembrane Domains Are Capable of Oligomerization
    • [74] Godfroy, J.I., Roostan, M., Moroz, Y.S., Korendovych, I.V., Yin, H., Isolated Toll-like Receptor Transmembrane Domains Are Capable of Oligomerization. PLoS One, 7, 2012, e48875, 10.1371/journal.pone.0048875.
    • (2012) PLoS One , vol.7
    • Godfroy, J.I.1    Roostan, M.2    Moroz, Y.S.3    Korendovych, I.V.4    Yin, H.5
  • 75
    • 67549145398 scopus 로고    scopus 로고
    • Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment
    • [75] Jura, N., Endres, N.F., Engel, K., Deindl, S., Das, R., Lamers, M.H., Wemmer, D.E., Zhang, X., Kuriyan, J., Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment. Cell 137 (2009), 1293–1307, 10.1016/j.cell.2009.04.025.
    • (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    Wemmer, D.E.7    Zhang, X.8    Kuriyan, J.9
  • 77
    • 0022485548 scopus 로고
    • Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
    • [77] Bargmann, C.I., Hung, M.C., Weinberg, R.A., Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell 45 (1986), 649–657.
    • (1986) Cell , vol.45 , pp. 649-657
    • Bargmann, C.I.1    Hung, M.C.2    Weinberg, R.A.3
  • 78
    • 84859204549 scopus 로고    scopus 로고
    • Effects of the oncogenic V(664)E mutation on membrane insertion, structure, and sequence-dependent interactions of the Neu transmembrane domain in micelles and model membranes: an integrated biophysical and simulation study
    • [78] Beevers, A.J., Nash, A., Salazar-Cancino, M., Scott, D.J., Notman, R., Dixon, A.M., Effects of the oncogenic V(664)E mutation on membrane insertion, structure, and sequence-dependent interactions of the Neu transmembrane domain in micelles and model membranes: an integrated biophysical and simulation study. Biochemistry 51 (2012), 2558–2568, 10.1021/bi201269w.
    • (2012) Biochemistry , vol.51 , pp. 2558-2568
    • Beevers, A.J.1    Nash, A.2    Salazar-Cancino, M.3    Scott, D.J.4    Notman, R.5    Dixon, A.M.6
  • 79
    • 84901433916 scopus 로고    scopus 로고
    • Point mutations in dimerization motifs of the transmembrane domain stabilize active or inactive state of the EphA2 receptor tyrosine kinase
    • [79] Sharonov, G.V., Bocharov, E.V., Kolosov, P.M., Astapova, M.V., Arseniev, A.S., Feofanov, A.V., Point mutations in dimerization motifs of the transmembrane domain stabilize active or inactive state of the EphA2 receptor tyrosine kinase. J. Biol. Chem. 289 (2014), 14955–14964, 10.1074/jbc.M114.558783.
    • (2014) J. Biol. Chem. , vol.289 , pp. 14955-14964
    • Sharonov, G.V.1    Bocharov, E.V.2    Kolosov, P.M.3    Astapova, M.V.4    Arseniev, A.S.5    Feofanov, A.V.6
  • 80
    • 84890041471 scopus 로고    scopus 로고
    • The ErbB/HER family of protein-tyrosine kinases and cancer
    • [80] Roskoski, R., The ErbB/HER family of protein-tyrosine kinases and cancer. Pharmacol. Res. 79 (2014), 34–74, 10.1016/j.phrs.2013.11.002.
    • (2014) Pharmacol. Res. , vol.79 , pp. 34-74
    • Roskoski, R.1
  • 82
    • 84857640514 scopus 로고    scopus 로고
    • Physical-chemical principles underlying RTK activation, and their implications for human disease
    • [82] He, L., Hristova, K., Physical-chemical principles underlying RTK activation, and their implications for human disease. Biochim. Biophys. Acta 1818 (2012), 995–1005, 10.1016/j.bbamem.2011.07.044.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 995-1005
    • He, L.1    Hristova, K.2
  • 84
    • 36549085536 scopus 로고    scopus 로고
    • Dynamic equilibrium between multiple active and inactive conformations explains regulation and oncogenic mutations in ErbB receptors
    • [84] Landau, M., Ben-Tal, N., Dynamic equilibrium between multiple active and inactive conformations explains regulation and oncogenic mutations in ErbB receptors. Biochim. Biophys. Acta 1785 (2008), 12–31, 10.1016/j.bbcan.2007.08.001.
    • (2008) Biochim. Biophys. Acta , vol.1785 , pp. 12-31
    • Landau, M.1    Ben-Tal, N.2
  • 85
    • 84921463220 scopus 로고    scopus 로고
    • Effect of thanatophoric dysplasia type I mutations on FGFR3 dimerization
    • [85] Del Piccolo, N., Placone, J., Hristova, K., Effect of thanatophoric dysplasia type I mutations on FGFR3 dimerization. Biophys. J. 108 (2015), 272–278, 10.1016/j.bpj.2014.11.3460.
    • (2015) Biophys. J. , vol.108 , pp. 272-278
    • Del Piccolo, N.1    Placone, J.2    Hristova, K.3
  • 86
    • 0034163421 scopus 로고    scopus 로고
    • Population-based, case-control study of HER2 genetic polymorphism and breast cancer risk
    • [86] Xie, D., Shu, X.O., Deng, Z., Wen, W.Q., Creek, K.E., Dai, Q., Gao, Y.T., Jin, F., Zheng, W., Population-based, case-control study of HER2 genetic polymorphism and breast cancer risk. J. Natl. Cancer Inst. 92 (2000), 412–417, 10.1093/jnci/92.5.412.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 412-417
    • Xie, D.1    Shu, X.O.2    Deng, Z.3    Wen, W.Q.4    Creek, K.E.5    Dai, Q.6    Gao, Y.T.7    Jin, F.8    Zheng, W.9
  • 87
    • 75149176738 scopus 로고    scopus 로고
    • Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers
    • [87] Dosch, D.D., Ballmer-Hofer, K., Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers. FASEB J. 24 (2010), 32–38, 10.1096/fj.09-132670.
    • (2010) FASEB J. , vol.24 , pp. 32-38
    • Dosch, D.D.1    Ballmer-Hofer, K.2
  • 88
    • 32344449064 scopus 로고    scopus 로고
    • Ligand-independent oligomerization of TLR4 regulated by a short hydrophobic region adjacent to the transmembrane domain
    • [88] Nishiya, T., Kajita, E., Miwa, S., Ligand-independent oligomerization of TLR4 regulated by a short hydrophobic region adjacent to the transmembrane domain. Biochem. Biophys. Res. Commun. 341 (2006), 1128–1134, 10.1016/j.bbrc.2006.01.074.
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 1128-1134
    • Nishiya, T.1    Kajita, E.2    Miwa, S.3
  • 89
    • 0034730639 scopus 로고    scopus 로고
    • Chopper, a new death domain of the p75 neurotrophin receptor that mediates rapid neuronal cell death
    • [89] Coulson, E.J., Reid, K., Baca, M., Shipham, K.A., Hulett, S.M., Kilpatrick, T.J., Bartlett, P.F., Chopper, a new death domain of the p75 neurotrophin receptor that mediates rapid neuronal cell death. J. Biol. Chem. 275 (2000), 30537–30545, 10.1074/jbc.M005214200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30537-30545
    • Coulson, E.J.1    Reid, K.2    Baca, M.3    Shipham, K.A.4    Hulett, S.M.5    Kilpatrick, T.J.6    Bartlett, P.F.7
  • 90
    • 0347480307 scopus 로고    scopus 로고
    • The role of neurotransmission and the Chopper domain in p75 neurotrophin receptor death signaling
    • [90] Coulson, E.J., Reid, K., Shipham, K.M., Morley, S., Kilpatrick, T.J., Bartlett, P.F., The role of neurotransmission and the Chopper domain in p75 neurotrophin receptor death signaling. Prog. Brain Res. 146 (2004), 41–62, 10.1016/S0079-6123(03)46003-2.
    • (2004) Prog. Brain Res. , vol.146 , pp. 41-62
    • Coulson, E.J.1    Reid, K.2    Shipham, K.M.3    Morley, S.4    Kilpatrick, T.J.5    Bartlett, P.F.6
  • 91
    • 67449146917 scopus 로고    scopus 로고
    • The juxtamembrane region of the EGF receptor functions as an activation domain
    • [91] Red Brewer, M., Choi, S.H., Alvarado, D., Moravcevic, K., Pozzi, A., Lemmon, M.A., Carpenter, G., The juxtamembrane region of the EGF receptor functions as an activation domain. Mol. Cell 34 (2009), 641–651, 10.1016/j.molcel.2009.04.034.
    • (2009) Mol. Cell , vol.34 , pp. 641-651
    • Red Brewer, M.1    Choi, S.H.2    Alvarado, D.3    Moravcevic, K.4    Pozzi, A.5    Lemmon, M.A.6    Carpenter, G.7
  • 92
    • 21244446728 scopus 로고    scopus 로고
    • A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor
    • [92] Choowongkomon, K., Carlin, C.R., S�nnichsen, F.D., A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor. J. Biol. Chem. 280 (2005), 24043–24052, 10.1074/jbc.M502698200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24043-24052
    • Choowongkomon, K.1    Carlin, C.R.2    S�nnichsen, F.D.3
  • 93
    • 84961299369 scopus 로고    scopus 로고
    • HER2 Transmembrane Domain Dimerization Coupled with Self-Association of Membrane-Embedded Cytoplasmic Juxtamembrane Regions
    • [93] Bragin, P.E., Mineev, K.S., Bocharova, O.V., Volynsky, P.E., Bocharov, E.V., Arseniev, A.S., HER2 Transmembrane Domain Dimerization Coupled with Self-Association of Membrane-Embedded Cytoplasmic Juxtamembrane Regions. J. Mol. Biol. 428 (2016), 52–61, 10.1016/j.jmb.2015.11.007.
    • (2016) J. Mol. Biol. , vol.428 , pp. 52-61
    • Bragin, P.E.1    Mineev, K.S.2    Bocharova, O.V.3    Volynsky, P.E.4    Bocharov, E.V.5    Arseniev, A.S.6
  • 94
    • 84945382992 scopus 로고    scopus 로고
    • The Membrane Mimetic Affects the Spatial Structure and Mobility of EGFR Transmembrane and Juxtamembrane Domains
    • [94] Mineev, K.S., Panova, S.V., Bocharova, O.V., Bocharov, E.V., Arseniev, A.S., The Membrane Mimetic Affects the Spatial Structure and Mobility of EGFR Transmembrane and Juxtamembrane Domains. Biochemistry 54 (2015), 6295–6298, 10.1021/acs.biochem.5b00851.
    • (2015) Biochemistry , vol.54 , pp. 6295-6298
    • Mineev, K.S.1    Panova, S.V.2    Bocharova, O.V.3    Bocharov, E.V.4    Arseniev, A.S.5
  • 95
    • 84873181474 scopus 로고    scopus 로고
    • Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides
    • [95] Matsushita, C., Tamagaki, H., Miyazawa, Y., Aimoto, S., Smith, S.O., Sato, T., Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides. Proc. Natl. Acad. Sci. 110 (2013), 1646–1651, 10.1073/pnas.1215207110.
    • (2013) Proc. Natl. Acad. Sci. , vol.110 , pp. 1646-1651
    • Matsushita, C.1    Tamagaki, H.2    Miyazawa, Y.3    Aimoto, S.4    Smith, S.O.5    Sato, T.6
  • 96
    • 84905686652 scopus 로고    scopus 로고
    • Coupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3
    • [96] Tamagaki, H., Furukawa, Y., Yamaguchi, R., Hojo, H., Aimoto, S., Smith, S.O., Sato, T., Coupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3. Biochemistry 53 (2014), 5000–5007, 10.1021/bi500327q.
    • (2014) Biochemistry , vol.53 , pp. 5000-5007
    • Tamagaki, H.1    Furukawa, Y.2    Yamaguchi, R.3    Hojo, H.4    Aimoto, S.5    Smith, S.O.6    Sato, T.7
  • 97
    • 85012024491 scopus 로고    scopus 로고
    • Juxtamembrane contribution to transmembrane signaling
    • [97] Deng, W., Li, R., Juxtamembrane contribution to transmembrane signaling. Biopolymers 104 (2015), 317–322, 10.1002/bip.22651.
    • (2015) Biopolymers , vol.104 , pp. 317-322
    • Deng, W.1    Li, R.2
  • 99
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: a framework for transmembrane helix-helix association
    • [99] Russ, W.P., Engelman, D.M., The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296 (2000), 911–919, 10.1006/jmbi.1999.3489.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 100
    • 84939600856 scopus 로고    scopus 로고
    • Role of GxxxG Motifs in Transmembrane Domain Interactions
    • [100] Teese, M.G., Langosch, D., Role of GxxxG Motifs in Transmembrane Domain Interactions. Biochemistry 54 (2015), 5125–5135, 10.1021/acs.biochem.5b00495.
    • (2015) Biochemistry , vol.54 , pp. 5125-5135
    • Teese, M.G.1    Langosch, D.2
  • 101
    • 0345802999 scopus 로고    scopus 로고
    • Sequence-specific dimerization of the transmembrane domain of the “BH3-only” protein BNIP3 in membranes and detergent
    • [101] Sulistijo, E.S., Jaszewski, T.M., MacKenzie, K.R., Sequence-specific dimerization of the transmembrane domain of the “BH3-only” protein BNIP3 in membranes and detergent. J. Biol. Chem. 278 (2003), 51950–51956, 10.1074/jbc.M308429200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51950-51956
    • Sulistijo, E.S.1    Jaszewski, T.M.2    MacKenzie, K.R.3
  • 102
    • 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
    • [102] Sulistijo, E.S., MacKenzie, K.R., 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. 364 (2006), 974–990, 10.1016/j.jmb.2006.09.065.
    • (2006) J. Mol. Biol. , vol.364 , pp. 974-990
    • Sulistijo, E.S.1    MacKenzie, K.R.2
  • 103
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: structure and implications
    • [103] MacKenzie, K.R., Prestegard, J.H., Engelman, D.M., A transmembrane helix dimer: structure and implications. Science 276 (1997), 131–133, 10.1126/science.276.5309.131.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 105
    • 0035811042 scopus 로고    scopus 로고
    • Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers
    • [105] Smith, S.O., Song, D., Shekar, S., Groesbeek, M., Ziliox, M., Aimoto, S., Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers. Biochemistry 40 (2001), 6553–6558, 10.1021/bi010357v.
    • (2001) Biochemistry , vol.40 , pp. 6553-6558
    • Smith, S.O.1    Song, D.2    Shekar, S.3    Groesbeek, M.4    Ziliox, M.5    Aimoto, S.6
  • 107
    • 67049171187 scopus 로고    scopus 로고
    • Structural basis for dimerization of the BNIP3 transmembrane domain
    • [107] Sulistijo, E.S., Mackenzie, K.R., Structural basis for dimerization of the BNIP3 transmembrane domain. Biochemistry 48 (2009), 5106–5120, 10.1021/bi802245u.
    • (2009) Biochemistry , vol.48 , pp. 5106-5120
    • Sulistijo, E.S.1    Mackenzie, K.R.2
  • 109
    • 84861837644 scopus 로고    scopus 로고
    • Structural and thermodynamic insight into the process of “weak” dimerization of the ErbB4 transmembrane domain by solution NMR
    • [109] Bocharov, E.V., Mineev, K.S., Goncharuk, M.V., Arseniev, A.S., Structural and thermodynamic insight into the process of “weak” dimerization of the ErbB4 transmembrane domain by solution NMR. Biochim. Biophys. Acta 1818 (2012), 2158–2170, 10.1016/j.bbamem.2012.05.001.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2158-2170
    • Bocharov, E.V.1    Mineev, K.S.2    Goncharuk, M.V.3    Arseniev, A.S.4
  • 110
    • 77953810629 scopus 로고    scopus 로고
    • Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases
    • [110] Mineev, K.S., Bocharov, E.V., Pustovalova, Y.E., Bocharova, O.V., Chupin, V.V., Arseniev, A.S., Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases. J. Mol. Biol. 400 (2010), 231–243, 10.1016/j.jmb.2010.05.016.
    • (2010) J. Mol. Biol. , vol.400 , pp. 231-243
    • Mineev, K.S.1    Bocharov, E.V.2    Pustovalova, Y.E.3    Bocharova, O.V.4    Chupin, V.V.5    Arseniev, A.S.6
  • 112
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • [112] Lau, T.-L., Kim, C., Ginsberg, M.H., Ulmer, T.S., The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. EMBO J. 28 (2009), 1351–1361, 10.1038/emboj.2009.63.
    • (2009) EMBO J. , vol.28 , pp. 1351-1361
    • Lau, T.-L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 113
    • 70449566822 scopus 로고    scopus 로고
    • Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation
    • [113] Yang, J., Ma, Y.-Q., Page, R.C., Misra, S., Plow, E.F., Qin, J., Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 17729–17734, 10.1073/pnas.0909589106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 17729-17734
    • Yang, J.1    Ma, Y.-Q.2    Page, R.C.3    Misra, S.4    Plow, E.F.5    Qin, J.6
  • 114
    • 58949085677 scopus 로고    scopus 로고
    • Lipophobicity and the residue environments of the transmembrane alpha-helical bundle
    • [114] Mokrab, Y., Stevens, T.J., Mizuguchi, K., Lipophobicity and the residue environments of the transmembrane alpha-helical bundle. Proteins 74 (2009), 32–49, 10.1002/prot.22130.
    • (2009) Proteins , vol.74 , pp. 32-49
    • Mokrab, Y.1    Stevens, T.J.2    Mizuguchi, K.3
  • 115
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • [115] Wimley, W.C., White, S.H., Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3 (1996), 842–848, 10.1038/nsb1096-842.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 116
    • 0035979146 scopus 로고    scopus 로고
    • The Calpha –-H…O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions
    • [116] Senes, A., Ubarretxena-Belandia, I., Engelman, D.M., The Calpha –-H…O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 9056–9061, 10.1073/pnas.161280798.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 117
    • 4043082646 scopus 로고    scopus 로고
    • The occurrence of C–H…O hydrogen bonds in alpha-helices and helix termini in globular proteins
    • [117] Manikandan, K., Ramakumar, S., The occurrence of C–H…O hydrogen bonds in alpha-helices and helix termini in globular proteins. Proteins 56 (2004), 768–781, 10.1002/prot.20152.
    • (2004) Proteins , vol.56 , pp. 768-781
    • Manikandan, K.1    Ramakumar, S.2
  • 118
    • 38949159124 scopus 로고    scopus 로고
    • Strength of Calpha-H…O�=�C hydrogen bonds in transmembrane proteins
    • [118] Park, H., Yoon, J., Seok, C., Strength of Calpha-H…O�=�C hydrogen bonds in transmembrane proteins. J. Phys. Chem. B 112 (2008), 1041–1048, 10.1021/jp077285n.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 1041-1048
    • Park, H.1    Yoon, J.2    Seok, C.3
  • 119
    • 13444279948 scopus 로고    scopus 로고
    • The contribution of C alpha-H…O hydrogen bonds to membrane protein stability depends on the position of the amide
    • [119] Mottamal, M., Lazaridis, T., The contribution of C alpha-H…O hydrogen bonds to membrane protein stability depends on the position of the amide. Biochemistry (Mosc) 44 (2005), 1607–1613, 10.1021/bi048065s.
    • (2005) Biochemistry (Mosc) , vol.44 , pp. 1607-1613
    • Mottamal, M.1    Lazaridis, T.2
  • 120
    • 0347625831 scopus 로고    scopus 로고
    • Direct observation of Calpha-Halpha…O�=�C hydrogen bonds in proteins by interresidue h3JCalphaC’ scalar couplings
    • [120] Cordier, F., Barfield, M., Grzesiek, S., Direct observation of Calpha-Halpha…O�=�C hydrogen bonds in proteins by interresidue h3JCalphaC’ scalar couplings. J. Am. Chem. Soc. 125 (2003), 15750–15751, 10.1021/ja038616m.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 15750-15751
    • Cordier, F.1    Barfield, M.2    Grzesiek, S.3
  • 121
    • 84908318473 scopus 로고    scopus 로고
    • Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study
    • [121] Mineev, K.S., Goncharuk, S.A., Arseniev, A.S., Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study. FEBS Lett. 588 (2014), 3802–3807, 10.1016/j.febslet.2014.08.031.
    • (2014) FEBS Lett. , vol.588 , pp. 3802-3807
    • Mineev, K.S.1    Goncharuk, S.A.2    Arseniev, A.S.3
  • 122
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: a measure of transmembrane helix association in a biological membrane
    • [122] Russ, W.P., Engelman, D.M., TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl. Acad. Sci. U. S. A. 96 (1999), 863–868, 10.1073/pnas.96.3.863.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 123
    • 0035956884 scopus 로고    scopus 로고
    • Polar residues drive association of polyleucine transmembrane helices
    • [123] Zhou, F.X., Merianos, H.J., Brunger, A.T., Engelman, D.M., Polar residues drive association of polyleucine transmembrane helices. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 2250–2255, 10.1073/pnas.041593698.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2250-2255
    • Zhou, F.X.1    Merianos, H.J.2    Brunger, A.T.3    Engelman, D.M.4
  • 124
    • 33748791763 scopus 로고    scopus 로고
    • Helix-packing motifs in membrane proteins
    • [124] Walters, R.F.S., DeGrado, W.F., Helix-packing motifs in membrane proteins. Proc. Natl. Acad. Sci. 103 (2006), 13658–13663, 10.1073/pnas.0605878103.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 13658-13663
    • Walters, R.F.S.1    DeGrado, W.F.2
  • 125
    • 84923882811 scopus 로고    scopus 로고
    • The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions
    • [125] Zhang, S.-Q., Kulp, D.W., Schramm, C.A., Mravic, M., Samish, I., DeGrado, W.F., The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions. Structure 1993:23 (2015), 527–541, 10.1016/j.str.2015.01.009.
    • (2015) Structure , vol.1993 , Issue.23 , pp. 527-541
    • Zhang, S.-Q.1    Kulp, D.W.2    Schramm, C.A.3    Mravic, M.4    Samish, I.5    DeGrado, W.F.6
  • 126
    • 77749318504 scopus 로고    scopus 로고
    • Left-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine Kinases
    • [126] Bocharov, E., Mayzel, M., Volynsky, P., Mineev, K., Tkach, E., Ermolyuk, Y., Schulga, A., Efremov, R., Arseniev, A., Left-Handed Dimer of EphA2 Transmembrane Domain: Helix Packing Diversity among Receptor Tyrosine Kinases. Biophys. J. 98 (2010), 881–889, 10.1016/j.bpj.2009.11.008.
    • (2010) Biophys. J. , vol.98 , pp. 881-889
    • Bocharov, E.1    Mayzel, M.2    Volynsky, P.3    Mineev, K.4    Tkach, E.5    Ermolyuk, Y.6    Schulga, A.7    Efremov, R.8    Arseniev, A.9
  • 127
    • 84864387267 scopus 로고    scopus 로고
    • Hydrophobic Matching Controls the Tilt and Stability of the Dimeric Platelet-derived Growth Factor Receptor (PDGFR) Transmembrane Segment
    • [127] Muhle-Goll, C., Hoffmann, S., Afonin, S., Grage, S.L., Polyansky, A.A., Windisch, D., Zeitler, M., Burck, J., Ulrich, A.S., Hydrophobic Matching Controls the Tilt and Stability of the Dimeric Platelet-derived Growth Factor Receptor (PDGFR) Transmembrane Segment. J. Biol. Chem. 287 (2012), 26178–26186, 10.1074/jbc.M111.325555.
    • (2012) J. Biol. Chem. , vol.287 , pp. 26178-26186
    • Muhle-Goll, C.1    Hoffmann, S.2    Afonin, S.3    Grage, S.L.4    Polyansky, A.A.5    Windisch, D.6    Zeitler, M.7    Burck, J.8    Ulrich, A.S.9
  • 128
    • 84887406746 scopus 로고    scopus 로고
    • Structure of FGFR3 transmembrane domain dimer: implications for signaling and human pathologies
    • [128] Bocharov, E.V., Lesovoy, D.M., Goncharuk, S.A., Goncharuk, M.V., Hristova, K., Arseniev, A.S., Structure of FGFR3 transmembrane domain dimer: implications for signaling and human pathologies. Structure 1993:21 (2013), 2087–2093, 10.1016/j.str.2013.08.026.
    • (2013) Structure , vol.1993 , Issue.21 , pp. 2087-2093
    • Bocharov, E.V.1    Lesovoy, D.M.2    Goncharuk, S.A.3    Goncharuk, M.V.4    Hristova, K.5    Arseniev, A.S.6
  • 129
    • 33750022623 scopus 로고    scopus 로고
    • The Structure of the ζζ Transmembrane Dimer Reveals Features Essential for Its Assembly with the T Cell Receptor
    • [129] Call, M.E., Schnell, J.R., Xu, C., Lutz, R.A., Chou, J.J., Wucherpfennig, K.W., The Structure of the ζζ Transmembrane Dimer Reveals Features Essential for Its Assembly with the T Cell Receptor. Cell 127 (2006), 355–368, 10.1016/j.cell.2006.08.044.
    • (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
  • 130
    • 77958153191 scopus 로고    scopus 로고
    • The structural basis for intramembrane assembly of an activating immunoreceptor complex
    • [130] Call, M.E., Wucherpfennig, K.W., Chou, J.J., The structural basis for intramembrane assembly of an activating immunoreceptor complex. Nat. Immunol. 11 (2010), 1023–1029, 10.1038/ni.1943.
    • (2010) Nat. Immunol. , vol.11 , pp. 1023-1029
    • Call, M.E.1    Wucherpfennig, K.W.2    Chou, J.J.3
  • 131
    • 67749120188 scopus 로고    scopus 로고
    • Helical extension of the neuronal SNARE complex into the membrane
    • [131] Stein, A., Weber, G., Wahl, M.C., Jahn, R., Helical extension of the neuronal SNARE complex into the membrane. Nature 460 (2009), 525–528, 10.1038/nature08156.
    • (2009) Nature , vol.460 , pp. 525-528
    • Stein, A.1    Weber, G.2    Wahl, M.C.3    Jahn, R.4
  • 132
    • 84953331204 scopus 로고    scopus 로고
    • Mechanism of FGF receptor dimerization and activation
    • [132] Sarabipour, S., Hristova, K., Mechanism of FGF receptor dimerization and activation. Nat. Commun., 7, 2016, 10262, 10.1038/ncomms10262.
    • (2016) Nat. Commun. , vol.7 , pp. 10262
    • Sarabipour, S.1    Hristova, K.2
  • 133
    • 84986268684 scopus 로고    scopus 로고
    • Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein
    • [133] Dominguez, L., Foster, L., Straub, J.E., Thirumalai, D., Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein. Proc. Natl. Acad. Sci. 113 (2016), E5281–E5287, 10.1073/pnas.1606482113.
    • (2016) Proc. Natl. Acad. Sci. , vol.113 , pp. E5281-E5287
    • Dominguez, L.1    Foster, L.2    Straub, J.E.3    Thirumalai, D.4
  • 134
    • 84962568117 scopus 로고    scopus 로고
    • Alternative packing of EGFR transmembrane domain suggests that protein-lipid interactions underlie signal conduction across membrane
    • [134] Bocharov, E.V., Lesovoy, D.M., Pavlov, K.V., Pustovalova, Y.E., Bocharova, O.V., Arseniev, A.S., Alternative packing of EGFR transmembrane domain suggests that protein-lipid interactions underlie signal conduction across membrane. Biochim. Biophys. Acta 1858 (2016), 1254–1261, 10.1016/j.bbamem.2016.02.023.
    • (2016) Biochim. Biophys. Acta , vol.1858 , pp. 1254-1261
    • Bocharov, E.V.1    Lesovoy, D.M.2    Pavlov, K.V.3    Pustovalova, Y.E.4    Bocharova, O.V.5    Arseniev, A.S.6
  • 137
    • 84861971120 scopus 로고    scopus 로고
    • Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment
    • [137] Nadezhdin, K.D., Bocharova, O.V., Bocharov, E.V., Arseniev, A.S., Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment. FEBS Lett. 586 (2012), 1687–1692, 10.1016/j.febslet.2012.04.062.
    • (2012) FEBS Lett. , vol.586 , pp. 1687-1692
    • Nadezhdin, K.D.1    Bocharova, O.V.2    Bocharov, E.V.3    Arseniev, A.S.4
  • 138
    • 84878665725 scopus 로고    scopus 로고
    • Role of dimerization efficiency of transmembrane domains in activation of fibroblast growth factor receptor 3
    • [138] Volynsky, P.E., Polyansky, A.A., Fakhrutdinova, G.N., Bocharov, E.V., Efremov, R.G., Role of dimerization efficiency of transmembrane domains in activation of fibroblast growth factor receptor 3. J. Am. Chem. Soc. 135 (2013), 8105–8108, 10.1021/ja4011942.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8105-8108
    • Volynsky, P.E.1    Polyansky, A.A.2    Fakhrutdinova, G.N.3    Bocharov, E.V.4    Efremov, R.G.5
  • 139
    • 67349094494 scopus 로고    scopus 로고
    • Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains
    • [139] Escher, C., Cymer, F., Schneider, D., Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains. J. Mol. Biol. 389 (2009), 10–16, 10.1016/j.jmb.2009.04.002.
    • (2009) J. Mol. Biol. , vol.389 , pp. 10-16
    • Escher, C.1    Cymer, F.2    Schneider, D.3
  • 140
    • 84941039568 scopus 로고    scopus 로고
    • NMR Dynamics of Transmembrane and Intracellular Domains of p75NTR in Lipid-Protein Nanodiscs
    • [140] Mineev, K.S., Goncharuk, S.A., Kuzmichev, P.K., Vilar, M., Arseniev, A.S., NMR Dynamics of Transmembrane and Intracellular Domains of p75NTR in Lipid-Protein Nanodiscs. Biophys. J. 109 (2015), 772–782, 10.1016/j.bpj.2015.07.009.
    • (2015) Biophys. J. , vol.109 , pp. 772-782
    • Mineev, K.S.1    Goncharuk, S.A.2    Kuzmichev, P.K.3    Vilar, M.4    Arseniev, A.S.5
  • 141
    • 77955656071 scopus 로고    scopus 로고
    • The membrane environment modulates self-association of the human GpA TM domain—Implications for membrane protein folding and transmembrane signaling
    • [141] Anbazhagan, V., Schneider, D., The membrane environment modulates self-association of the human GpA TM domain—Implications for membrane protein folding and transmembrane signaling. Biochim. Biophys. Acta Biomembr. 1798 (2010), 1899–1907, 10.1016/j.bbamem.2010.06.027.
    • (2010) Biochim. Biophys. Acta Biomembr. , vol.1798 , pp. 1899-1907
    • Anbazhagan, V.1    Schneider, D.2
  • 142
    • 0035899991 scopus 로고    scopus 로고
    • Self-association of model transmembrane alpha-helices is modulated by lipid structure
    • [142] Mall, S., Broadbridge, R., Sharma, R.P., East, J.M., Lee, A.G., Self-association of model transmembrane alpha-helices is modulated by lipid structure. Biochemistry 40 (2001), 12379–12386, 10.1021/bi011075y.
    • (2001) Biochemistry , vol.40 , pp. 12379-12386
    • Mall, S.1    Broadbridge, R.2    Sharma, R.P.3    East, J.M.4    Lee, A.G.5
  • 143
    • 0345598917 scopus 로고    scopus 로고
    • Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers
    • [143] Cristian, L., Lear, J.D., DeGrado, W.F., Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 14772–14777, 10.1073/pnas.2536751100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14772-14777
    • Cristian, L.1    Lear, J.D.2    DeGrado, W.F.3
  • 145
    • 84867697719 scopus 로고    scopus 로고
    • Base-Mediated Carboxylation of Unprotected Indole Derivatives with Carbon Dioxide
    • [145] Yoo, W.-J., Capdevila, M.G., Du, X., Kobayashi, S., Base-Mediated Carboxylation of Unprotected Indole Derivatives with Carbon Dioxide. Org. Lett. 14 (2012), 5326–5329, 10.1021/ol3025082.
    • (2012) Org. Lett. , vol.14 , pp. 5326-5329
    • Yoo, W.-J.1    Capdevila, M.G.2    Du, X.3    Kobayashi, S.4
  • 146
    • 84876934637 scopus 로고    scopus 로고
    • Formation of raft-like assemblies within clusters of influenza hemagglutinin observed by MD simulations
    • [146] Parton, D.L., Tek, A., Baaden, M., Sansom, M.S.P., Formation of raft-like assemblies within clusters of influenza hemagglutinin observed by MD simulations. PLoS Comput. Biol., 9, 2013, e1003034, 10.1371/journal.pcbi.1003034.
    • (2013) PLoS Comput. Biol. , vol.9
    • Parton, D.L.1    Tek, A.2    Baaden, M.3    Sansom, M.S.P.4
  • 147
    • 77957901688 scopus 로고    scopus 로고
    • Lipid-mediated interactions tune the association of glycophorin A helix and its disruptive mutants in membranes
    • [147] Sengupta, D., Marrink, S.J., Lipid-mediated interactions tune the association of glycophorin A helix and its disruptive mutants in membranes. Phys. Chem. Chem. Phys. 12 (2010), 12987–12996, 10.1039/c0cp00101e.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 12987-12996
    • Sengupta, D.1    Marrink, S.J.2
  • 148
    • 84951985271 scopus 로고    scopus 로고
    • Role of the Lipid Environment in the Dimerization of Transmembrane Domains of Glycophorin A
    • ()
    • [148] Kuznetsov, A.S., Volynsky, P.E., Efremov, R.G., Role of the Lipid Environment in the Dimerization of Transmembrane Domains of Glycophorin A. Acta Nat. 7 (2015), 122–127 ( https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4717257).
    • (2015) Acta Nat. , vol.7 , pp. 122-127
    • Kuznetsov, A.S.1    Volynsky, P.E.2    Efremov, R.G.3
  • 149
    • 84871217969 scopus 로고    scopus 로고
    • Dynamic clustering of lipids in hydrated two-component membranes: results of computer modeling and putative biological impact
    • [149] Pyrkova, D.V., Tarasova, N.K., Krylov, N.A., Nolde, D.E., Pentkovsky, V.M., Efremov, R.G., Dynamic clustering of lipids in hydrated two-component membranes: results of computer modeling and putative biological impact. J. Biomol. Struct. Dyn. 31 (2013), 87–95, 10.1080/07391102.2012.691365.
    • (2013) J. Biomol. Struct. Dyn. , vol.31 , pp. 87-95
    • Pyrkova, D.V.1    Tarasova, N.K.2    Krylov, N.A.3    Nolde, D.E.4    Pentkovsky, V.M.5    Efremov, R.G.6
  • 150
    • 84914165385 scopus 로고    scopus 로고
    • Toward understanding driving forces in membrane protein folding
    • [150] Hong, H., Toward understanding driving forces in membrane protein folding. Arch. Biochem. Biophys. 564 (2014), 297–313, 10.1016/j.abb.2014.07.031.
    • (2014) Arch. Biochem. Biophys. , vol.564 , pp. 297-313
    • Hong, H.1
  • 151
    • 0000717364 scopus 로고
    • Hydrophobic Nature of Membrane-Spanning.alpha.-Helical Peptides as Revealed by Monte Carlo Simulations and Molecular Hydrophobicity Potential Analysis
    • [151] Efremov, R.G., Vergoten, G., Hydrophobic Nature of Membrane-Spanning.alpha.-Helical Peptides as Revealed by Monte Carlo Simulations and Molecular Hydrophobicity Potential Analysis. J. Phys. Chem. 99 (1995), 10658–10666, 10.1021/j100026a033.
    • (1995) J. Phys. Chem. , vol.99 , pp. 10658-10666
    • Efremov, R.G.1    Vergoten, G.2
  • 152
    • 84865748404 scopus 로고    scopus 로고
    • Multistate organization of transmembrane helical protein dimers governed by the host membrane
    • [152] Polyansky, A.A., Volynsky, P.E., Efremov, R.G., Multistate organization of transmembrane helical protein dimers governed by the host membrane. J. Am. Chem. Soc. 134 (2012), 14390–14400, 10.1021/ja303483k.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 14390-14400
    • Polyansky, A.A.1    Volynsky, P.E.2    Efremov, R.G.3
  • 153
    • 84857648415 scopus 로고    scopus 로고
    • Transmembrane helices can induce domain formation in crowded model membranes
    • [153] Domański, J., Marrink, S.J., Sch�fer, L.V., Transmembrane helices can induce domain formation in crowded model membranes. Biochim. Biophys. Acta 1818 (2012), 984–994, 10.1016/j.bbamem.2011.08.021.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 984-994
    • Domański, J.1    Marrink, S.J.2    Sch�fer, L.V.3
  • 154
    • 78649833557 scopus 로고    scopus 로고
    • Molecular simulation of the effect of cholesterol on lipid-mediated protein-protein interactions
    • [154] de Meyer, F.J.-M., Rodgers, J.M., Willems, T.F., Smit, B., Molecular simulation of the effect of cholesterol on lipid-mediated protein-protein interactions. Biophys. J. 99 (2010), 3629–3638, 10.1016/j.bpj.2010.09.030.
    • (2010) Biophys. J. , vol.99 , pp. 3629-3638
    • de Meyer, F.J.-M.1    Rodgers, J.M.2    Willems, T.F.3    Smit, B.4
  • 155
    • 84924956027 scopus 로고    scopus 로고
    • The juxtamembrane regions of human receptor tyrosine kinases exhibit conserved interaction sites with anionic lipids
    • [155] Hedger, G., Sansom, M.S.P., Kolds�, H., The juxtamembrane regions of human receptor tyrosine kinases exhibit conserved interaction sites with anionic lipids. Sci. Rep., 5, 2015, 9198, 10.1038/srep09198.
    • (2015) Sci. Rep. , vol.5 , pp. 9198
    • Hedger, G.1    Sansom, M.S.P.2    Kolds�, H.3
  • 156
    • 84860832684 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus interacts with EphrinA2 receptor to amplify signaling essential for productive infection
    • [156] Chakraborty, S., Veettil, M.V., Bottero, V., Chandran, B., Kaposi's sarcoma-associated herpesvirus interacts with EphrinA2 receptor to amplify signaling essential for productive infection. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), E1163–E1172, 10.1073/pnas.1119592109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. E1163-E1172
    • Chakraborty, S.1    Veettil, M.V.2    Bottero, V.3    Chandran, B.4
  • 157
    • 84869096283 scopus 로고    scopus 로고
    • Ligand-independent activation of EphA2 by arachidonic acid induces metastasis-like behaviour in prostate cancer cells
    • [157] Tawadros, T., Brown, M.D., Hart, C.A., Clarke, N.W., Ligand-independent activation of EphA2 by arachidonic acid induces metastasis-like behaviour in prostate cancer cells. Br. J. Cancer 107 (2012), 1737–1744, 10.1038/bjc.2012.457.
    • (2012) Br. J. Cancer , vol.107 , pp. 1737-1744
    • Tawadros, T.1    Brown, M.D.2    Hart, C.A.3    Clarke, N.W.4
  • 158
    • 84951770185 scopus 로고    scopus 로고
    • Structures of the EphA2 Receptor at the Membrane: Role of Lipid Interactions
    • [158] Chavent, M., Seiradake, E., Jones, E.Y., Sansom, M.S.P., Structures of the EphA2 Receptor at the Membrane: Role of Lipid Interactions. Structure 24 (2016), 337–347, 10.1016/j.str.2015.11.008.
    • (2016) Structure , vol.24 , pp. 337-347
    • Chavent, M.1    Seiradake, E.2    Jones, E.Y.3    Sansom, M.S.P.4
  • 160
    • 0034703270 scopus 로고    scopus 로고
    • Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations
    • [160] Petrache, H.I., Grossfield, A., MacKenzie, K.R., Engelman, D.M., Woolf, T.B., Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations. J. Mol. Biol. 302 (2000), 727–746, 10.1006/jmbi.2000.4072.
    • (2000) J. Mol. Biol. , vol.302 , pp. 727-746
    • Petrache, H.I.1    Grossfield, A.2    MacKenzie, K.R.3    Engelman, D.M.4    Woolf, T.B.5
  • 161
    • 84941651018 scopus 로고    scopus 로고
    • Dynamics of the Glycophorin A Dimer in Membranes of Native-Like Composition Uncovered by Coarse-Grained Molecular Dynamics Simulations
    • [161] Flinner, N., Schleiff, E., Dynamics of the Glycophorin A Dimer in Membranes of Native-Like Composition Uncovered by Coarse-Grained Molecular Dynamics Simulations. PLoS One, 10, 2015, e0133999, 10.1371/journal.pone.0133999.
    • (2015) PLoS One , vol.10
    • Flinner, N.1    Schleiff, E.2
  • 162
    • 79960590320 scopus 로고    scopus 로고
    • Dramatic destabilization of transmembrane helix interactions by features of natural membrane environments
    • [162] Hong, H., Bowie, J.U., Dramatic destabilization of transmembrane helix interactions by features of natural membrane environments. J. Am. Chem. Soc. 133 (2011), 11389–11398, 10.1021/ja204524c.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 11389-11398
    • Hong, H.1    Bowie, J.U.2
  • 163
    • 84968626588 scopus 로고    scopus 로고
    • Revealing the mechanism of passive transport in lipid bilayers via phonon-mediated nanometre-scale density fluctuations
    • [163] Zhernenkov, M., Bolmatov, D., Soloviov, D., Zhernenkov, K., Toperverg, B.P., Cunsolo, A., Bosak, A., Cai, Y.Q., Revealing the mechanism of passive transport in lipid bilayers via phonon-mediated nanometre-scale density fluctuations. Nat. Commun., 7, 2016, 11575, 10.1038/ncomms11575.
    • (2016) Nat. Commun. , vol.7 , pp. 11575
    • Zhernenkov, M.1    Bolmatov, D.2    Soloviov, D.3    Zhernenkov, K.4    Toperverg, B.P.5    Cunsolo, A.6    Bosak, A.7    Cai, Y.Q.8
  • 164
    • 38349184772 scopus 로고    scopus 로고
    • Tuning lipid mixtures to induce or suppress domain formation across leaflets of unsupported asymmetric bilayers
    • [164] Collins, M.D., Keller, S.L., Tuning lipid mixtures to induce or suppress domain formation across leaflets of unsupported asymmetric bilayers. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 124–128, 10.1073/pnas.0702970105.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 124-128
    • Collins, M.D.1    Keller, S.L.2
  • 165
    • 84949215763 scopus 로고    scopus 로고
    • Transbilayer Colocalization of Lipid Domains Explained via Measurement of Strong Coupling Parameters
    • [165] Blosser, M.C., Honerkamp-Smith, A.R., Han, T., Haataja, M., Keller, S.L., Transbilayer Colocalization of Lipid Domains Explained via Measurement of Strong Coupling Parameters. Biophys. J. 109 (2015), 2317–2327, 10.1016/j.bpj.2015.10.031.
    • (2015) Biophys. J. , vol.109 , pp. 2317-2327
    • Blosser, M.C.1    Honerkamp-Smith, A.R.2    Han, T.3    Haataja, M.4    Keller, S.L.5
  • 166
    • 84879465010 scopus 로고    scopus 로고
    • Long and short lipid molecules experience the same interleaflet drag in lipid bilayers
    • [166] Horner, A., Akimov, S.A., Pohl, P., Long and short lipid molecules experience the same interleaflet drag in lipid bilayers. Phys. Rev. Lett., 110, 2013, 268101, 10.1103/PhysRevLett.110.268101.
    • (2013) Phys. Rev. Lett. , vol.110 , pp. 268101
    • Horner, A.1    Akimov, S.A.2    Pohl, P.3
  • 167
    • 67649322141 scopus 로고    scopus 로고
    • Coupled diffusion of peripherally bound peptides along the outer and inner membrane leaflets
    • [167] Horner, A., Antonenko, Y.N., Pohl, P., Coupled diffusion of peripherally bound peptides along the outer and inner membrane leaflets. Biophys. J. 96 (2009), 2689–2695, 10.1016/j.bpj.2008.12.3931.
    • (2009) Biophys. J. , vol.96 , pp. 2689-2695
    • Horner, A.1    Antonenko, Y.N.2    Pohl, P.3
  • 168
    • 0034810547 scopus 로고    scopus 로고
    • Cholesterol organization in membranes at low concentrations: effects of curvature stress and membrane thickness
    • [168] Rukmini, R., Rawat, S.S., Biswas, S.C., Chattopadhyay, A., Cholesterol organization in membranes at low concentrations: effects of curvature stress and membrane thickness. Biophys. J. 81 (2001), 2122–2134, 10.1016/S0006-3495(01)75860-2.
    • (2001) Biophys. J. , vol.81 , pp. 2122-2134
    • Rukmini, R.1    Rawat, S.S.2    Biswas, S.C.3    Chattopadhyay, A.4
  • 169
    • 80052550711 scopus 로고    scopus 로고
    • Raft registration across bilayers in a molecularly detailed model
    • [169] Pantano, D.A., Moore, P.B., Klein, M.L., Discher, D.E., Raft registration across bilayers in a molecularly detailed model. Soft Matter, 7, 2011, 8182, 10.1039/c1sm05490b.
    • (2011) Soft Matter , vol.7 , pp. 8182
    • Pantano, D.A.1    Moore, P.B.2    Klein, M.L.3    Discher, D.E.4
  • 171
    • 56249119219 scopus 로고    scopus 로고
    • The molecular face of lipid rafts in model membranes
    • [171] Risselada, H.J., Marrink, S.J., The molecular face of lipid rafts in model membranes. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 17367–17372, 10.1073/pnas.0807527105.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 17367-17372
    • Risselada, H.J.1    Marrink, S.J.2
  • 172
    • 79955451530 scopus 로고    scopus 로고
    • Interleaflet interaction and asymmetry in phase separated lipid bilayers: molecular dynamics simulations
    • [172] Perlmutter, J.D., Sachs, J.N., Interleaflet interaction and asymmetry in phase separated lipid bilayers: molecular dynamics simulations. J. Am. Chem. Soc. 133 (2011), 6563–6577, 10.1021/ja106626r.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 6563-6577
    • Perlmutter, J.D.1    Sachs, J.N.2
  • 173
    • 84959377769 scopus 로고    scopus 로고
    • Elastic deformations of bolalipid membranes
    • [173] Galimzyanov, T.R., Kuzmin, P.I., Pohl, P., Akimov, S.A., Elastic deformations of bolalipid membranes. Soft Matter 12 (2016), 2357–2364, 10.1039/c5sm02635k.
    • (2016) Soft Matter , vol.12 , pp. 2357-2364
    • Galimzyanov, T.R.1    Kuzmin, P.I.2    Pohl, P.3    Akimov, S.A.4
  • 175
    • 23244446181 scopus 로고    scopus 로고
    • Membrane elasticity in giant vesicles with fluid phase coexistence
    • [175] Baumgart, T., Das, S., Webb, W.W., Jenkins, J.T., Membrane elasticity in giant vesicles with fluid phase coexistence. Biophys. J. 89 (2005), 1067–1080, 10.1529/biophysj.104.049692.
    • (2005) Biophys. J. , vol.89 , pp. 1067-1080
    • Baumgart, T.1    Das, S.2    Webb, W.W.3    Jenkins, J.T.4
  • 176
    • 65549094949 scopus 로고    scopus 로고
    • Alamethicin in lipid bilayers: combined use of X-ray scattering and MD simulations
    • [176] Pan, J., Tieleman, D.P., Nagle, J.F., Kucerka, N., Tristram-Nagle, S., Alamethicin in lipid bilayers: combined use of X-ray scattering and MD simulations. Biochim. Biophys. Acta 1788 (2009), 1387–1397, 10.1016/j.bbamem.2009.02.013.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1387-1397
    • Pan, J.1    Tieleman, D.P.2    Nagle, J.F.3    Kucerka, N.4    Tristram-Nagle, S.5
  • 177
    • 70349153375 scopus 로고    scopus 로고
    • Effect of cholesterol on structural and mechanical properties of membranes depends on lipid chain saturation
    • [177] Pan, J., Tristram-Nagle, S., Nagle, J.F., Effect of cholesterol on structural and mechanical properties of membranes depends on lipid chain saturation. Phys. Rev. E Stat. Nonlinear Soft Matter Phys., 80, 2009, 21931, 10.1103/PhysRevE.80.021931.
    • (2009) Phys. Rev. E Stat. Nonlinear Soft Matter Phys. , vol.80 , pp. 21931
    • Pan, J.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 178
    • 27644520001 scopus 로고    scopus 로고
    • Effect of lipid composition on the “membrane response” induced by a fusion peptide
    • [178] Volynsky, P.E., Polyansky, A.A., Simakov, N.A., Arseniev, A.S., Efremov, R.G., Effect of lipid composition on the “membrane response” induced by a fusion peptide. Biochemistry 44 (2005), 14626–14637, 10.1021/bi0514562.
    • (2005) Biochemistry , vol.44 , pp. 14626-14637
    • Volynsky, P.E.1    Polyansky, A.A.2    Simakov, N.A.3    Arseniev, A.S.4    Efremov, R.G.5
  • 179
    • 52049109183 scopus 로고    scopus 로고
    • Toroidal pores formed by antimicrobial peptides show significant disorder
    • [179] Sengupta, D., Leontiadou, H., Mark, A.E., Marrink, S.-J., Toroidal pores formed by antimicrobial peptides show significant disorder. Biochim. Biophys. Acta 1778 (2008), 2308–2317, 10.1016/j.bbamem.2008.06.007.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2308-2317
    • Sengupta, D.1    Leontiadou, H.2    Mark, A.E.3    Marrink, S.-J.4
  • 180
    • 61949310466 scopus 로고    scopus 로고
    • Adaptation of a membrane-active peptide to heterogeneous environment. II. The role of mosaic nature of the membrane surface
    • [180] Polyansky, A.A., Volynsky, P.E., Arseniev, A.S., Efremov, R.G., Adaptation of a membrane-active peptide to heterogeneous environment. II. The role of mosaic nature of the membrane surface. J. Phys. Chem. B 113 (2009), 1120–1126, 10.1021/jp803641x.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 1120-1126
    • Polyansky, A.A.1    Volynsky, P.E.2    Arseniev, A.S.3    Efremov, R.G.4
  • 181
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • [181] Nguyen, L.T., Haney, E.F., Vogel, H.J., The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol. 29 (2011), 464–472, 10.1016/j.tibtech.2011.05.001.
    • (2011) Trends Biotechnol. , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 182
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • [182] Simons, K., Toomre, D., Lipid rafts and signal transduction. Nat. Rev. Mol. Cell Biol. 1 (2000), 31–39, 10.1038/35036052.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 183
    • 22244449320 scopus 로고    scopus 로고
    • An Electrostatic Engine Model for Autoinhibition and Activation of the Epidermal Growth Factor Receptor (EGFR/ErbB) Family
    • [183] McLaughlin, S., Smith, S.O., Hayman, M.J., Murray, D., An Electrostatic Engine Model for Autoinhibition and Activation of the Epidermal Growth Factor Receptor (EGFR/ErbB) Family. J. Gen. Physiol. 126 (2005), 41–53, 10.1085/jgp.200509274.
    • (2005) J. Gen. Physiol. , vol.126 , pp. 41-53
    • McLaughlin, S.1    Smith, S.O.2    Hayman, M.J.3    Murray, D.4
  • 184
    • 84921425147 scopus 로고    scopus 로고
    • The EGFR family: not so prototypical receptor tyrosine kinases
    • [184] Lemmon, M.A., Schlessinger, J., Ferguson, K.M., The EGFR family: not so prototypical receptor tyrosine kinases. Cold Spring Harb. Perspect. Biol., 6, 2014, a020768, 10.1101/cshperspect.a020768.
    • (2014) Cold Spring Harb. Perspect. Biol. , vol.6 , pp. a020768
    • Lemmon, M.A.1    Schlessinger, J.2    Ferguson, K.M.3
  • 185
    • 84930714069 scopus 로고    scopus 로고
    • A structural perspective on the regulation of the epidermal growth factor receptor
    • [185] Kovacs, E., Zorn, J.A., Huang, Y., Barros, T., Kuriyan, J., A structural perspective on the regulation of the epidermal growth factor receptor. Annu. Rev. Biochem. 84 (2015), 739–764, 10.1146/annurev-biochem-060614-034402.
    • (2015) Annu. Rev. Biochem. , vol.84 , pp. 739-764
    • Kovacs, E.1    Zorn, J.A.2    Huang, Y.3    Barros, T.4    Kuriyan, J.5
  • 186
    • 84889045199 scopus 로고    scopus 로고
    • Structural and dynamic study of the transmembrane domain of the amyloid precursor protein
    • ()
    • [186] Nadezhdin, K.D., Bocharova, O.V., Bocharov, E.V., Arseniev, A.S., Structural and dynamic study of the transmembrane domain of the amyloid precursor protein. Acta Nat. 3 (2011), 69–76 ( http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347594).
    • (2011) Acta Nat. , vol.3 , pp. 69-76
    • Nadezhdin, K.D.1    Bocharova, O.V.2    Bocharov, E.V.3    Arseniev, A.S.4
  • 187
    • 79959336760 scopus 로고    scopus 로고
    • Regulation of human EGF receptor by lipids
    • [187] Coskun, U., Grzybek, M., Drechsel, D., Simons, K., Regulation of human EGF receptor by lipids. Proc. Natl. Acad. Sci. 108 (2011), 9044–9048, 10.1073/pnas.1105666108.
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 9044-9048
    • Coskun, U.1    Grzybek, M.2    Drechsel, D.3    Simons, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.