메뉴 건너뛰기




Volumn 8, Issue 11, 2013, Pages

Membrane orientation and binding determinants of G protein-coupled receptor kinase 5 as assessed by combined vibrational spectroscopic studies

Author keywords

[No Author keywords available]

Indexed keywords

BETA ADRENERGIC RECEPTOR; G PROTEIN COUPLED RECEPTOR KINASE 2; G PROTEIN COUPLED RECEPTOR KINASE 5;

EID: 84896740158     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0082072     Document Type: Article
Times cited : (24)

References (77)
  • 1
    • 83555168220 scopus 로고    scopus 로고
    • G protein-coupled receptor kinases: More than just kinases and not only for GPCRs
    • Gurevich EV, Tesmer JJ, Mushegian A, Gurevich VV (2012) G protein-coupled receptor kinases: More than just kinases and not only for GPCRs. Pharmacol Ther 113: 40-69.
    • (2012) Pharmacol Ther , vol.113 , pp. 40-69
    • Gurevich, E.V.1    Tesmer, J.J.2    Mushegian, A.3    Gurevich, V.V.4
  • 2
    • 84858611820 scopus 로고    scopus 로고
    • The Origin and Evolution of G Protein-Coupled Receptor Kinases
    • doi:10.1371/journal.pone.0033806. PubMed: 22442725
    • Mushegian A, Gurevich VV, Gurevich EV (2012) The Origin and Evolution of G Protein-Coupled Receptor Kinases. PLOS ONE 7: e33806. doi:10.1371/journal. pone.0033806. PubMed: 22442725.
    • (2012) PLOS ONE , vol.7
    • Mushegian, A.1    Gurevich, V.V.2    Gurevich, E.V.3
  • 3
    • 0026726050 scopus 로고
    • Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases
    • doi:10.1038/359147a0. PubMed: 1522899
    • Inglese J, Koch WJ, Caron MG, Lefkowitz RJ (1992) Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases. Nature 359: 147-150. doi:10.1038/359147a0. PubMed: 1522899.
    • (1992) Nature , vol.359 , pp. 147-150
    • Inglese, J.1    Koch, W.J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 4
    • 0026803164 scopus 로고
    • Role of βγ Subunits of G Proteins in Targeting the β-Adrenergic Receptor Kinase to Membrane-Bound Receptors
    • doi:10.1126/science.1325672. PubMed: 1325672
    • Pitcher JA, Inglese J, Higgins JB, Arriza JL, Casey PK et al. (1992) Role of βγ Subunits of G Proteins in Targeting the β-Adrenergic Receptor Kinase to Membrane-Bound Receptors. Science 257: 1264-1267. doi:10.1126/science.1325672. PubMed: 1325672.
    • (1992) Science , vol.257 , pp. 1264-1267
    • Pitcher, J.A.1    Inglese, J.2    Higgins, J.B.3    Arriza, J.L.4    Casey, P.K.5
  • 5
    • 80053089071 scopus 로고    scopus 로고
    • Heterotrimeric G protein β1γ2 Subunits Change Orientation upon Complex Formation with G Protein-coupled Receptor Kinase 2 (GRK2) on a Model
    • doi:10.1073/pnas.1108236108
    • Boughton AP, Yang P, Tesmer VM, Ding B, Tesmer JJ et al. (2011) Heterotrimeric G protein β1γ2 Subunits Change Orientation upon Complex Formation with G Protein-coupled Receptor Kinase 2 (GRK2) on a Model. Membr - Proc Natl Acad Sci U S A 108: E667-E673. doi:10.1073/pnas.1108236108.
    • (2011) Membr - Proc Natl Acad Sci U S A , vol.108
    • Boughton, A.P.1    Yang, P.2    Tesmer, V.M.3    Ding, B.4    Tesmer, J.J.5
  • 7
    • 0032553549 scopus 로고    scopus 로고
    • Structure-Function Analysis of G Protein-coupled Receptor Kinase-5
    • doi:10.1074/jbc.273.47.31510. PubMed: 9813065
    • Pronin AN, Carman CV, Benovic JL (1998) Structure-Function Analysis of G Protein-coupled Receptor Kinase-5. J Biol Chem 273: 31510-31518. doi:10.1074/jbc.273.47.31510. PubMed: 9813065.
    • (1998) J Biol Chem , vol.273 , pp. 31510-31518
    • Pronin, A.N.1    Carman, C.V.2    Benovic, J.L.3
  • 9
    • 0029915255 scopus 로고    scopus 로고
    • Characterization of the G Protein-coupled Receptor Kinase GRK4
    • doi:10.1074/jbc.271.11.6403. PubMed: 8626439
    • Premont RT, Macrae AD, Stoffel RH, Chung N, Pitcher JA (1996) Characterization of the G Protein-coupled Receptor Kinase GRK4. J Biol Chem 271: 6403-6410. doi:10.1074/jbc.271.11.6403. PubMed: 8626439.
    • (1996) J Biol Chem , vol.271 , pp. 6403-6410
    • Premont, R.T.1    Macrae, A.D.2    Stoffel, R.H.3    Chung, N.4    Pitcher, J.A.5
  • 11
    • 0028300574 scopus 로고
    • Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases
    • Premont RT, Walter JK, Inglese J, Lefkowitz RL (1994) Identification, Purification, and Characterization of GRK5, a Member of the Family of G Protein-coupled Receptor Kinase. J Biol Chem 269: 6832-6841. PubMed: 8120045. (Pubitemid 24191077)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.9 , pp. 6832-6841
    • Premont, R.T.1    Koch, W.J.2    Inglese, J.3    Lefkowitz, R.J.4
  • 12
    • 37249040944 scopus 로고    scopus 로고
    • 2-Adrenergic Receptor in Plasma Membranes by Intrinsic GRK5
    • doi:10.1021/bi700922h. PubMed: 18034461
    • 2-Adrenergic Receptor in Plasma Membranes by Intrinsic GRK5. Biochemistry 46: 14438-14449. doi:10.1021/bi700922h. PubMed: 18034461.
    • (2007) Biochemistry , vol.46 , pp. 14438-14449
    • Tran, T.M.1    Jorgensen, R.2    Clark, R.B.3
  • 13
    • 0031022334 scopus 로고    scopus 로고
    • Regulation of the G protein-coupled receptor kinase GRK5 by protein kinase C
    • DOI 10.1074/jbc.272.6.3806
    • Pronin AN, Benovic JL (1997) Regulation of the G Protein-coupled Receptor Kinase GRK5 by Protein Kinase C. J Biol Chem 272: 3806-3812. doi:10.1074/jbc.272.6.3806. PubMed: 9013639. (Pubitemid 27066891)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.6 , pp. 3806-3812
    • Pronin, A.N.1    Benovic, J.L.2
  • 14
    • 0028290815 scopus 로고
    • Phospholipid-stimulated Autophosphorylation Activates the G Protein-coupled Receptor Kinase GRK5
    • PubMed: 8144599
    • Kunapuli P, Gurevich VV, Benovic JL (1994) Phospholipid-stimulated Autophosphorylation Activates the G Protein-coupled Receptor Kinase GRK5. J Biol Chem 269: 10209-10212. PubMed: 8144599.
    • (1994) J Biol Chem , vol.269 , pp. 10209-10212
    • Kunapuli, P.1    Gurevich, V.V.2    Benovic, J.L.3
  • 15
    • 77957778459 scopus 로고    scopus 로고
    • Molecular basis for activation of G protein-coupled receptor kinases
    • doi:10.1038/emboj.2010.206. PubMed: 20729810
    • Boguth CA, Singh P, Huang CC, Tesmer JJG (2010) Molecular basis for activation of G protein-coupled receptor kinases. EMBO J 29: 3249-3259. doi:10.1038/emboj.2010.206. PubMed: 20729810.
    • (2010) EMBO J , vol.29 , pp. 3249-3259
    • Boguth, C.A.1    Singh, P.2    Huang, C.C.3    Tesmer, J.J.G.4
  • 16
    • 33745207354 scopus 로고    scopus 로고
    • The Structure of G Protein-coupled Receptor Kinase (GRK)-6 Defines a Second Lineage of GRKs
    • doi:10.1074/jbc.M601327200. PubMed: 16613860
    • Lodowski DT, Tesmer VM, Benovic JL, Tesmer JJG (2006) The Structure of G Protein-coupled Receptor Kinase (GRK)-6 Defines a Second Lineage of GRKs. J Biol Chem 281: 16785-16793. doi:10.1074/jbc.M601327200. PubMed: 16613860.
    • (2006) J Biol Chem , vol.281 , pp. 16785-16793
    • Lodowski, D.T.1    Tesmer, V.M.2    Benovic, J.L.3    Tesmer, J.J.G.4
  • 17
    • 66149178593 scopus 로고    scopus 로고
    • A Surface of the Kinase Domain Critical for the Allosteric Activation of G Protein-coupled Receptor Kinases
    • doi:10.1074/jbc.M809544200. PubMed: 19364770
    • Huang CC, Yoshino-Koh K, Tesmer JJG (2009) A Surface of the Kinase Domain Critical for the Allosteric Activation of G Protein-coupled Receptor Kinases. J Biol Chem 284: 17206-17215. doi:10.1074/jbc.M809544200. PubMed: 19364770.
    • (2009) J Biol Chem , vol.284 , pp. 17206-17215
    • Huang, C.C.1    Yoshino-Koh, K.2    Tesmer, J.J.G.3
  • 18
    • 79952796822 scopus 로고    scopus 로고
    • Activation of G Protein-Coupled Receptor Kinase 1 Involves Interactions between Its N-Terminal Region and Its Kinase Domain
    • doi:10.1021/bi101606e. PubMed: 21265573
    • Huang CC, Orban T, Jastrzebska B, Palczewski K, Tesmer JJG (2011) Activation of G Protein-Coupled Receptor Kinase 1 Involves Interactions between Its N-Terminal Region and Its Kinase Domain. Biochemistry 50: 1940-1949. doi:10.1021/bi101606e. PubMed: 21265573.
    • (2011) Biochemistry , vol.50 , pp. 1940-1949
    • Huang, C.C.1    Orban, T.2    Jastrzebska, B.3    Palczewski, K.4    Tesmer, J.J.G.5
  • 19
    • 79952784761 scopus 로고    scopus 로고
    • Recognition in the Face of Diversity: Interactions of Heterotrimeric G proteins and G Protein-coupled Receptor (GPCR) Kinases with Activated GPCRs
    • doi:10.1074/jbc.R109.051847. PubMed: 21199869
    • Huang CC, Tesmer JJG (2011) Recognition in the Face of Diversity: Interactions of Heterotrimeric G proteins and G Protein-coupled Receptor (GPCR) Kinases with Activated GPCRs. J Biol Chem 286: 7715-7721. doi:10.1074/jbc.R109. 051847. PubMed: 21199869.
    • (2011) J Biol Chem , vol.286 , pp. 7715-7721
    • Huang, C.C.1    Tesmer, J.J.G.2
  • 20
    • 84859768258 scopus 로고    scopus 로고
    • Structural Domains Required for Caenorhabditis elegans G Protein-coupled Receptor Kinase 2 (GRK-2) Function in Vivo
    • doi:10.1074/jbc.M111.336818. PubMed: 22375004
    • Wood JF, Wang J, Benovic JL, Ferkey DM (2012) Structural Domains Required for Caenorhabditis elegans G Protein-coupled Receptor Kinase 2 (GRK-2) Function in Vivo. J Biol Chem 287: 12634-12644. doi:10.1074/jbc.M111.336818. PubMed: 22375004.
    • (2012) J Biol Chem , vol.287 , pp. 12634-12644
    • Wood, J.F.1    Wang, J.2    Benovic, J.L.3    Ferkey, D.M.4
  • 21
    • 84857911676 scopus 로고    scopus 로고
    • GRK2: Multiple roles beyond G protein-coupled receptor desensitization
    • doi:10.1016/j.tips.2011.12.003. PubMed: 22277298
    • Evron T, Daigle TL, Caron MG (2012) GRK2: multiple roles beyond G protein-coupled receptor desensitization. Trends Pharmacol Sci 33: 154-164. doi:10.1016/j.tips.2011.12.003. PubMed: 22277298.
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 154-164
    • Evron, T.1    Daigle, T.L.2    Caron, M.G.3
  • 23
    • 84883137525 scopus 로고    scopus 로고
    • Lipid Fluid-Gel Phase Transition Induced Alamethicin Orientational Change Probed by Sum Frequency Generation
    • Yang P, Wu FG, Chen Z (2013) Lipid Fluid-Gel Phase Transition Induced Alamethicin Orientational Change Probed by Sum Frequency Generation. Vibrational Spectroscopy - J Phys Chem C 117: 17039-17049.
    • (2013) Vibrational Spectroscopy - J Phys Chem C , vol.117 , pp. 17039-17049
    • Yang, P.1    Wu, F.G.2    Chen, Z.3
  • 24
    • 35548947618 scopus 로고    scopus 로고
    • In situ investigation of heterotrimeric G protein βγ subunit binding and orientation on membrane bilayers
    • DOI 10.1021/ja075542w
    • Chen X, Boughton AP, Tesmer JJG, Chen Z (2007) In Situ Investigation of Heterotrimeric G Protein βγ Subunit Binding and Orientation on Membrane Bilayers. J Am Chem Soc 129: 12658-12659. doi:10.1021/ja075542w. PubMed: 17902674. (Pubitemid 350004464)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.42 , pp. 12658-12659
    • Chen, X.1    Boughton, A.P.2    Tesmer, J.J.G.3    Chen, Z.4
  • 25
    • 84875766760 scopus 로고    scopus 로고
    • Membrane Orientation of Gαiβ1γ2 and Gβ1γ2 Determined via Combined Vibrational Spectroscopic Studies
    • doi:10.1021/ja3116026
    • Yang P, Boughton AP, Homan KT, Tesmer JJG, Chen Z (2013) Membrane Orientation of Gαiβ1γ2 and Gβ1γ2 Determined via Combined Vibrational Spectroscopic Studies. J Am Chem Soc 135: 5044-5051. doi:10.1021/ja3116026.
    • (2013) J Am Chem Soc , vol.135 , pp. 5044-5051
    • Yang, P.1    Boughton, A.P.2    Homan, K.T.3    Tesmer, J.J.G.4    Chen, Z.5
  • 26
    • 79959211416 scopus 로고    scopus 로고
    • Membrane Orientation of MSI-78 Measured by Sum Frequency Generation Vibrational Spectroscopy
    • doi:10.1021/la201048t. PubMed: 21595453
    • Yang P, Ramamoorthy A, Chen Z (2011) Membrane Orientation of MSI-78 Measured by Sum Frequency Generation Vibrational Spectroscopy. Langmuir 27: 7760-7767. doi:10.1021/la201048t. PubMed: 21595453.
    • (2011) Langmuir , vol.27 , pp. 7760-7767
    • Yang, P.1    Ramamoorthy, A.2    Chen, Z.3
  • 27
    • 84859590055 scopus 로고    scopus 로고
    • Observing a Model Ion Channel Gating Action in Model Cell Membranes in Real Time in Situ: Membrane Potential Change Induced Alamethicin Orientation
    • doi:10.1021/ja2110784
    • Ye S, Li H, Wei F, Jasensky J, Boughton AP et al. (2012) Observing a Model Ion Channel Gating Action in Model Cell Membranes in Real Time in Situ: Membrane Potential Change Induced Alamethicin Orientation. Change - J Am Chem Soc 134: 6237-6243. doi:10.1021/ja2110784.
    • (2012) Change - J Am Chem Soc , vol.134 , pp. 6237-6243
    • Ye, S.1    Li, H.2    Wei, F.3    Jasensky, J.4    Boughton, A.P.5
  • 28
    • 79954589291 scopus 로고    scopus 로고
    • Single Lipid Bilayers Constructed on Polymer Cushion Studied by Sum Frequency Generation
    • Wang T, Li D, Lu X, Khmaladze A, Han X et al. (2011) Single Lipid Bilayers Constructed on Polymer Cushion Studied by Sum Frequency Generation. Vibrational Spectroscopy - J Phys Chem C 115: 7613-7620.
    • (2011) Vibrational Spectroscopy - J Phys Chem C , vol.115 , pp. 7613-7620
    • Wang, T.1    Li, D.2    Lu, X.3    Khmaladze, A.4    Han, X.5
  • 29
    • 78650348571 scopus 로고    scopus 로고
    • Limiting an Antimicrobial Peptide to the Lipid-Water Interface Enhances Its Bacterial Membrane Selectivity: A Case Study of MSI-367
    • doi:10.1021/bi101394r. PubMed: 21062093
    • Thennarasu S, Huang R, Lee DK, Yang P, Maloy L et al. (2010) Limiting an Antimicrobial Peptide to the Lipid-Water Interface Enhances Its Bacterial Membrane Selectivity: A Case Study of MSI-367. Biochemistry 49: 10595-10605. doi:10.1021/bi101394r. PubMed: 21062093.
    • (2010) Biochemistry , vol.49 , pp. 10595-10605
    • Thennarasu, S.1    Huang, R.2    Lee, D.K.3    Yang, P.4    Maloy, L.5
  • 30
    • 84874144367 scopus 로고    scopus 로고
    • Dependence of Alamethicin Membrane Orientation on the Solution Concentration
    • doi:10.1021/jp3099522. PubMed: 23565299
    • Yang P, Wu FG, Chen Z (2013) Dependence of Alamethicin Membrane Orientation on the Solution Concentration. J Phys Chem C Nanomater Interfaces 117: 3358-3365. doi:10.1021/jp3099522. PubMed: 23565299.
    • (2013) J Phys Chem C Nanomater Interfaces , vol.117 , pp. 3358-3365
    • Yang, P.1    Wu, F.G.2    Chen, Z.3
  • 31
    • 6744248168 scopus 로고
    • Surface Properties Probed by Second-Harmonic and Sum-Frequency Generation
    • doi:10.1038/337519a0
    • Shen YR (1989) Surface Properties Probed by Second-Harmonic and Sum-Frequency Generation. Nature 337: 519-525. doi:10.1038/337519a0.
    • (1989) Nature , vol.337 , pp. 519-525
    • Shen, Y.R.1
  • 32
    • 0042709672 scopus 로고    scopus 로고
    • Liquid Interfaces Probed by Second-Harmonic and Sum-Frequency
    • Eisenthal KB (1996) Liquid Interfaces Probed by Second-Harmonic and Sum-Frequency. Spectroscopy - Chem Rev 96: 1343-1360.
    • (1996) Spectroscopy - Chem Rev , vol.96 , pp. 1343-1360
    • Eisenthal, K.B.1
  • 33
    • 0037433596 scopus 로고    scopus 로고
    • Molecular packing of lysozyme, fibrinogen, and bovine serum albumin on hydrophilic and hydrophobic surfaces studied by infrared-visible sum frequency generation and fluorescence microscopy
    • DOI 10.1021/ja028987n
    • Kim J, Somorjai GA (2003) Molecular Packing of Lysozyme, Fibrinogen, and Bovine Serum Albumin on Hydrophilic and Hydrophobic Surfaces Studied by Infrared-Visible Sum Frequency Generation and Fluorescence. Journal of Microscopy - J Am Chem Soc 125: 3150-3158. doi:10.1021/ja028987n. (Pubitemid 36512540)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.10 , pp. 3150-3158
    • Kim, J.1    Somorjai, G.A.2
  • 34
    • 0036667303 scopus 로고    scopus 로고
    • Molecular Bonding and Interactions at Aqueous Surfaces as Probed by Vibrational Sum Frequency
    • Richmond GL (2002) Molecular Bonding and Interactions at Aqueous Surfaces as Probed by Vibrational Sum Frequency. Spectroscopy - Chem Rev 102: 2693-2724.
    • (2002) Spectroscopy - Chem Rev , vol.102 , pp. 2693-2724
    • Richmond, G.L.1
  • 35
    • 0035903262 scopus 로고    scopus 로고
    • Elucidating changes in interfacial water structure upon protein adsorption
    • Kim J, Cremer PS (2001) Elucidating Changes in Interfacial Water Structure upon Protein Adsorption. Chemphyschem 2: 543-546. doi:10.1002/1439- 7641(20010917)2:8/9. PubMed: 23686994. (Pubitemid 33725038)
    • (2001) ChemPhysChem , vol.2 , Issue.8-9 , pp. 543-546
    • Kim, J.1    Cremer, P.S.2
  • 36
    • 27444435192 scopus 로고    scopus 로고
    • Quantitative spectral and orientational analysis in surface sum frequency generation vibrational spectroscopy (SFG-VS)
    • DOI 10.1080/01442350500225894
    • Wang H, Gang W, Lu R, Rao Y, Wu B (2005) Quantitative Spectral and Orientational Analysis in Surface Sum Frequency Generation Vibrational Spectroscopy (SFG-VS). Int Rev Phys Chem 24: 191-256. doi:10.1080/ 01442350500225894. (Pubitemid 41532408)
    • (2005) International Reviews in Physical Chemistry , vol.24 , Issue.2 , pp. 191-256
    • Wang, H.-F.1    Gan, W.2    Lu, R.3    Rao, Y.4    Wu, B.-H.5
  • 37
    • 37049081310 scopus 로고
    • Sum-frequency Vibrational Spectroscopy of the Solid/Liquid Interface
    • doi:10.1039/ft9959101281
    • Bain CD (1995) Sum-frequency Vibrational Spectroscopy of the Solid/Liquid Interface. J Chem Soc Faraday Trans 91: 1281-1296. doi:10.1039/ft9959101281.
    • (1995) J Chem Soc Faraday Trans , vol.91 , pp. 1281-1296
    • Bain, C.D.1
  • 38
    • 67651055722 scopus 로고    scopus 로고
    • Chirality in Nonlinear
    • doi:10.1146/annurev.physchem.59.032607.093712
    • Haupert LM, Simpson GJ (2009) Chirality in Nonlinear. Journal of Optics - Annu Rev Phys Chem 60: 345-365. doi:10.1146/annurev.physchem.59.032607.093712.
    • (2009) Journal of Optics - Annu Rev Phys Chem , vol.60 , pp. 345-365
    • Haupert, L.M.1    Simpson, G.J.2
  • 39
    • 79957845982 scopus 로고    scopus 로고
    • Supported Phospholipid Monolayers. The Molecular Structure Investigated by Vibrational Sum Frequency
    • Liljeblad JFD, Bulone V, Rutland MW, Johnson CM (2011) Supported Phospholipid Monolayers. The Molecular Structure Investigated by Vibrational Sum Frequency. Spectroscopy - J Phys Chem C 115: 10617-10629.
    • (2011) Spectroscopy - J Phys Chem C , vol.115 , pp. 10617-10629
    • Liljeblad, J.F.D.1    Bulone, V.2    Rutland, M.W.3    Johnson, C.M.4
  • 40
    • 84861889644 scopus 로고    scopus 로고
    • Interkingdom Signaling: Integration, Conformation, and Orientation of N-Acyl-l-homoserine Lactones in Supported Lipid Bilayers
    • doi:10.1021/la301241s. PubMed: 22568488
    • Barth C, Jakubczyk D, Kubas A, Anastassacos F, Brenner-Weiss G et al. (2012) Interkingdom Signaling: Integration, Conformation, and Orientation of N-Acyl-l-homoserine Lactones in Supported Lipid Bilayers. Langmuir 28: 8456-8462. doi:10.1021/la301241s. PubMed: 22568488.
    • (2012) Langmuir , vol.28 , pp. 8456-8462
    • Barth, C.1    Jakubczyk, D.2    Kubas, A.3    Anastassacos, F.4    Brenner-Weiss, G.5
  • 41
    • 84861410132 scopus 로고    scopus 로고
    • Protein Adsorption at the Electrified Air-Water Interface: Implications on Foam Stability
    • doi:10.1021/la301368v. PubMed: 22530646
    • Engelhardt K, Rumpel A, Walter J, Dombrowski J, Kulozik U et al. (2012) Protein Adsorption at the Electrified Air-Water Interface: Implications on Foam Stability. Langmuir 28: 7780-7787. doi:10.1021/la301368v. PubMed: 22530646.
    • (2012) Langmuir , vol.28 , pp. 7780-7787
    • Engelhardt, K.1    Rumpel, A.2    Walter, J.3    Dombrowski, J.4    Kulozik, U.5
  • 42
    • 77953514565 scopus 로고    scopus 로고
    • Mechanistic Studies by Sum-Frequency Generation Spectroscopy: Hydrolysis of a Supported Phospholipid Bilayer by Phospholipase A2
    • Tong Y, Li N, Liu H, Ge A, Osawa M et al. (2010) Mechanistic Studies by Sum-Frequency Generation Spectroscopy: Hydrolysis of a Supported Phospholipid Bilayer by Phospholipase A2. Angew Chem - Int Ed 49: 2369-2373.
    • (2010) Angew Chem - Int Ed , vol.49 , pp. 2369-2373
    • Tong, Y.1    Li, N.2    Liu, H.3    Ge, A.4    Osawa, M.5
  • 43
    • 3242816081 scopus 로고    scopus 로고
    • Phase transition of a single lipid bilayer measured by sum-frequency vibrational spectroscopy
    • DOI 10.1021/ja031570c
    • Liu J, Conboy JC (2004) Phase Transition of a Single Lipid Bilayer Measured by Sum-Frequency. Vibrational Spectroscopy - J Am Chem Soc 126: 8894-8895. (Pubitemid 38971053)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.29 , pp. 8894-8895
    • Liu, J.1    Conboy, J.C.2
  • 44
    • 84862933522 scopus 로고    scopus 로고
    • (3) Contribution to Sum Frequency Generation Signal
    • doi:10.1021/la203690p. PubMed: 22149290
    • (3) Contribution to Sum Frequency Generation Signal. Langmuir 28: 1374-1380. doi:10.1021/la203690p. PubMed: 22149290.
    • (2012) Langmuir , vol.28 , pp. 1374-1380
    • Ye, S.1    Liu, G.2    Li, H.3    Chen, F.4    Wang, X.5
  • 45
    • 11144220823 scopus 로고    scopus 로고
    • Piperidine adsorption on hydrated α-alumina (0001) surface studied by vibrational sum frequency generation spectroscopy
    • DOI 10.1021/la0487343
    • Ma G, Liu DF, Allen HC (2004) Piperidine Adsorption on Hydrated α-Alumina (0001) Surface Studied by Vibrational Sum Frequency Generation Spectroscopy. Langmuir 20: 11620-11629. doi:10.1021/la0487343. PubMed: 15595791. (Pubitemid 40049635)
    • (2004) Langmuir , vol.20 , Issue.26 , pp. 11620-11629
    • Ma, G.1    Liu, D.2    Allen, H.C.3
  • 46
    • 77955786270 scopus 로고    scopus 로고
    • Sum Frequency Generation and Solid-state NMR Study of the Structure, Orientation, and Dynamics of Polystyrene-adsorbed
    • doi:10.1073/pnas.1003832107
    • Weidner T, Breen NF, Li K, Drohny GP, Castner DG (2010) Sum Frequency Generation and Solid-state NMR Study of the Structure, Orientation, and Dynamics of Polystyrene-adsorbed. Peptides - Proc Natl Acad Sci U S A 107: 13288-13293. doi:10.1073/pnas.1003832107.
    • (2010) Peptides - Proc Natl Acad Sci U S A , vol.107 , pp. 13288-13293
    • Weidner, T.1    Breen, N.F.2    Li, K.3    Drohny, G.P.4    Castner, D.G.5
  • 47
    • 84861590202 scopus 로고    scopus 로고
    • Direct Observation of Phenylalanine Orientations in Statherin Bound to Hydroxyapatite Surfaces
    • doi:10.1021/ja301711w. PubMed: 22563672
    • Weidner T, Dubey M, Breen NF, Ash J, Baio JE et al. (2012) Direct Observation of Phenylalanine Orientations in Statherin Bound to Hydroxyapatite Surfaces. J Am Chem Soc 134: 8750-8753. doi:10.1021/ja301711w. PubMed: 22563672.
    • (2012) J Am Chem Soc , vol.134 , pp. 8750-8753
    • Weidner, T.1    Dubey, M.2    Breen, N.F.3    Ash, J.4    Baio, J.E.5
  • 48
    • 77951026783 scopus 로고    scopus 로고
    • In Situ Misfolding of Human Islet Amyloid Polypeptide at Interfaces Probed by Vibrational Sum Frequency Generation
    • doi:10.1021/ja909546b. PubMed: 20337445
    • Fu L, Ma G, Yan EC (2010) In Situ Misfolding of Human Islet Amyloid Polypeptide at Interfaces Probed by Vibrational Sum Frequency Generation. J Am Chem Soc 132: 5405-5412. doi:10.1021/ja909546b. PubMed: 20337445.
    • (2010) J Am Chem Soc , vol.132 , pp. 5405-5412
    • Fu, L.1    Ma, G.2    Yan, E.C.3
  • 49
    • 79957725089 scopus 로고    scopus 로고
    • Chiral Sum Frequency Generation Spectroscopy for Characterizing Protein Secondary Structures at Interfaces
    • doi:10.1021/ja201575e. PubMed: 21534603
    • Fu L, Liu J, Yan EC (2011) Chiral Sum Frequency Generation Spectroscopy for Characterizing Protein Secondary Structures at Interfaces. J Am Chem Soc 133: 8094-8097. doi:10.1021/ja201575e. PubMed: 21534603.
    • (2011) J Am Chem Soc , vol.133 , pp. 8094-8097
    • Fu, L.1    Liu, J.2    Yan, E.C.3
  • 50
    • 35048862275 scopus 로고    scopus 로고
    • Specific ion effects on interfacial water structure near macromolecules
    • DOI 10.1021/ja073869r
    • Chen X, Yang T, Kataoka S, Cremer PS (2007) Specific Ion Effects on Interfacial Water Structure near Macromolecules. J Am Chem Soc 129: 12272-12279. doi:10.1021/ja073869r. PubMed: 17880076. (Pubitemid 47556862)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.40 , pp. 12272-12279
    • Chen, X.1    Yang, T.2    Kataoka, S.3    Cremer, P.S.4
  • 51
    • 78049283410 scopus 로고    scopus 로고
    • Specific Anion Effects on Water Structure Adjacent to Protein Monolayers
    • doi:10.1021/la1015862. PubMed: 20560589
    • Chen X, Flores SC, Lim SM, Zhang YJ, Yang TL et al. (2010) Specific Anion Effects on Water Structure Adjacent to Protein Monolayers. Langmuir 26: 16447-16454. doi:10.1021/la1015862. PubMed: 20560589.
    • (2010) Langmuir , vol.26 , pp. 16447-16454
    • Chen, X.1    Flores, S.C.2    Lim, S.M.3    Zhang, Y.J.4    Yang, T.L.5
  • 52
    • 77953314650 scopus 로고    scopus 로고
    • Molecular Restructuring of Water and Lipids upon the Interaction of DNA with Lipid Monolayers
    • doi:10.1021/ja100838q. PubMed: 20486664
    • Campen RK, Ngo TTM, Sovago M, Ruysschaert JM, Bonn M (2010) Molecular Restructuring of Water and Lipids upon the Interaction of DNA with Lipid Monolayers. J Am Chem Soc 132: 8037-8047. doi:10.1021/ja100838q. PubMed: 20486664.
    • (2010) J Am Chem Soc , vol.132 , pp. 8037-8047
    • Campen, R.K.1    Ngo, T.T.M.2    Sovago, M.3    Ruysschaert, J.M.4    Bonn, M.5
  • 53
    • 34447500475 scopus 로고    scopus 로고
    • Adsorption at a carbon black microparticle surface in aqueous colloids probed by optical second-harmonic generation
    • DOI 10.1021/jp066873i
    • Wang HF, Troxler T, Yeh AG, Dai HL (2007) Adsorption at a Carbon Black Microparticle Surface in Aqueous Colloids Probed by Optical Second-Harmonic Generation. J Phys Chem C 111: 8708-8715. doi:10.1021/jp066873i. (Pubitemid 47152579)
    • (2007) Journal of Physical Chemistry C , vol.111 , Issue.25 , pp. 8708-8715
    • Wang, H.-F.1    Troxler, T.2    Yeh, A.-G.3    Dai, H.-L.4
  • 54
    • 33846057446 scopus 로고    scopus 로고
    • Probing Molecules Adsorbed at the Surface of Nanometer Colloidal Particles by Optical Second-Harmonic Generation
    • doi:10.1021/jp0644762. PubMed: 17107136
    • Jen SH, Dai HL (2006) Probing Molecules Adsorbed at the Surface of Nanometer Colloidal Particles by Optical Second-Harmonic Generation. J Phys Chem B 110: 23000-23003. doi:10.1021/jp0644762. PubMed: 17107136.
    • (2006) J Phys Chem B , vol.110 , pp. 23000-23003
    • Jen, S.H.1    Dai, H.L.2
  • 55
    • 33644524108 scopus 로고    scopus 로고
    • Kinetics of Ultraviolet and Plasma Surface Modification of Poly(dimethylsiloxane) Probed by Sum Frequency Vibrational Spectroscopy
    • doi:10.1021/la052030r. PubMed: 16460119
    • Ye H, Gu Z, Gracias DH (2006) Kinetics of Ultraviolet and Plasma Surface Modification of Poly(dimethylsiloxane) Probed by Sum Frequency Vibrational Spectroscopy. Langmuir 22: 1863-1868. doi:10.1021/la052030r. PubMed: 16460119.
    • (2006) Langmuir , vol.22 , pp. 1863-1868
    • Ye, H.1    Gu, Z.2    Gracias, D.H.3
  • 56
    • 34648816719 scopus 로고    scopus 로고
    • Correlations between SFG spectra and electrical properties of organic field effect transistors
    • DOI 10.1021/jp072767k
    • Ye H, Huang J, Park JR, Katz HE, Gracias DH (2007) Correlations between SFG Spectra and Electrical Properties of Organic Field Effect Transistors. J Phys Chem C 111: 13250-13255. doi:10.1021/jp072767k. (Pubitemid 47459227)
    • (2007) Journal of Physical Chemistry C , vol.111 , Issue.35 , pp. 13250-13255
    • Ye, H.1    Huang, J.2    Park, J.-R.3    Katz, H.E.4    Gracias, D.H.5
  • 57
    • 65349196132 scopus 로고    scopus 로고
    • Surface-enhanced IR-visible sum frequency generation vibrational spectroscopy
    • doi:10.1039/b821045d. PubMed: 19421546
    • Li Q, Kuo CW, Yang Z, Chen P, Chou KC (2009) Surface-enhanced IR-visible sum frequency generation vibrational spectroscopy. Phys Chem Chem Phys 11: 3436-3442. doi:10.1039/b821045d. PubMed: 19421546.
    • (2009) Phys Chem Chem Phys , vol.11 , pp. 3436-3442
    • Li, Q.1    Kuo, C.W.2    Yang, Z.3    Chen, P.4    Chou, K.C.5
  • 58
    • 84859478198 scopus 로고    scopus 로고
    • Role of Interfacial Water on Protein Adsorption at Cross-Linked Polyethylene Oxide Interfaces
    • doi:10.1021/la204805x. PubMed: 22390193
    • Leung BO, Yang Z, Wu SSH, Chou KC (2012) Role of Interfacial Water on Protein Adsorption at Cross-Linked Polyethylene Oxide Interfaces. Langmuir 28: 5724-5728. doi:10.1021/la204805x. PubMed: 22390193.
    • (2012) Langmuir , vol.28 , pp. 5724-5728
    • Leung, B.O.1    Yang, Z.2    Wu, S.S.H.3    Chou, K.C.4
  • 59
    • 0025993413 scopus 로고
    • Orientation of Melittin in Phospholipid Bilayers
    • doi:10.1016/S0006-3495(91)82126-9. PubMed: 1742459
    • Frey S, Tamm LK (1991) Orientation of Melittin in Phospholipid Bilayers. Biophys J 60: 922-930. doi:10.1016/S0006-3495(91)82126-9. PubMed: 1742459.
    • (1991) Biophys J , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 60
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • DOI 10.1017/S0033583597003375
    • Tamm LK, Tatulian SA (1997) Infrared Spectroscopy of Proteins and Peptides in Lipid Bilayers. Quarterly Rev Biophys 30: 365-429. doi:10.1017/S0033583597003375. (Pubitemid 28260614)
    • (1997) Quarterly Reviews of Biophysics , vol.30 , Issue.4 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 61
    • 0030928208 scopus 로고    scopus 로고
    • Dichroic Ratios in Polarized Fourier Transform Infrared for Nonaxial Symmetry of β-Sheet Structures
    • doi:10.1016/S0006-3495(97)78914-8. PubMed: 9168046
    • Marsh D (1997) Dichroic Ratios in Polarized Fourier Transform Infrared for Nonaxial Symmetry of β-Sheet Structures. Biophys J 72: 2710-2718. doi:10.1016/S0006-3495(97)78914-8. PubMed: 9168046.
    • (1997) Biophys J , vol.72 , pp. 2710-2718
    • Marsh, D.1
  • 62
    • 14644398554 scopus 로고    scopus 로고
    • Orientation of β-barrel proteins OmpA and FhuA in lipid membranes. Chain length dependence from infrared dichroism
    • DOI 10.1021/bi047603y
    • Ramakrishnan M, Qu J, Pocanschi CL, Kleinschmidt JH, Marsh D (2005) Orientation of β-Barrel Proteins OmpA and FhuA in Lipid Membranes. Chain Length Dependence from Infrared Dichroism. Biochemistry 44: 3515-3523. doi:10.1021/bi047603y. PubMed: 15736961. (Pubitemid 40322021)
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3515-3523
    • Ramakrishnan, M.1    Qu, J.2    Pocanschi, C.L.3    Kleinschmidt, J.H.4    Marsh, D.5
  • 63
    • 0028986697 scopus 로고
    • Characterization of Two Membrane-Bound Forms of OmpA
    • doi:10.1021/bi00006a013. PubMed: 7849052
    • Rodionova NA, Tatulian SA, Surrey T, Jähnig F, Tamm LK (1995) Characterization of Two Membrane-Bound Forms of OmpA. Biochemistry 34: 1921-1929. doi:10.1021/bi00006a013. PubMed: 7849052.
    • (1995) Biochemistry , vol.34 , pp. 1921-1929
    • Rodionova, N.A.1    Tatulian, S.A.2    Surrey, T.3    Jähnig, F.4    Tamm, L.K.5
  • 64
    • 84883295607 scopus 로고    scopus 로고
    • Molecular Orientation of Enzymes Attached to Surfaces Through Defined Chemical Linkages at the Solid/Liquid Interface
    • doi:10.1021/ja403672s. PubMed: 23883344
    • Liu Y, Ogorzalek TL, Yang P, Schroeder MM, Marsh ENG et al. (2013) Molecular Orientation of Enzymes Attached to Surfaces Through Defined Chemical Linkages at the Solid/Liquid Interface. J Am Chem Soc 135: 12660-12669. doi:10.1021/ja403672s. PubMed: 23883344.
    • (2013) J Am Chem Soc , vol.135 , pp. 12660-12669
    • Liu, Y.1    Ogorzalek, T.L.2    Yang, P.3    Schroeder, M.M.4    Marsh, E.N.G.5
  • 65
    • 77953965202 scopus 로고    scopus 로고
    • Determination of Interfacial β-Sheet Structures in Situ
    • doi:10.1021/jp102343h. PubMed: 20504035
    • Nguyen KT, King JT, Chen Z (2010) Determination of Interfacial β-Sheet Structures in Situ. J Phys Chem B 114: 8291-8300. doi:10.1021/jp102343h. PubMed: 20504035.
    • (2010) J Phys Chem B , vol.114 , pp. 8291-8300
    • Nguyen, K.T.1    King, J.T.2    Chen, Z.3
  • 66
    • 69949168824 scopus 로고    scopus 로고
    • Orientation Determination of Protein Helical Secondary Structures Using Linear and Nonlinear
    • Nguyen KT, Le Clair SV, Ye S, Chen Z (2009) Orientation Determination of Protein Helical Secondary Structures Using Linear and Nonlinear. Vibrational Spectroscopy - J Phys Chem B 113: 12169-12180.
    • (2009) Vibrational Spectroscopy - J Phys Chem B , vol.113 , pp. 12169-12180
    • Nguyen, K.T.1    Le Clair, S.V.2    Ye, S.3    Chen, Z.4
  • 67
    • 69949187577 scopus 로고    scopus 로고
    • Molecular Interaction between Magainin 2 and Model Membranes in Situ
    • doi:10.1021/jp904154w. PubMed: 19728722
    • Nguyen KT, Le Clair SV, Ye S, Chen Z (2009) Molecular Interaction between Magainin 2 and Model Membranes in Situ. J Phys Chem B 113: 12358-12363. doi:10.1021/jp904154w. PubMed: 19728722.
    • (2009) J Phys Chem B , vol.113 , pp. 12358-12363
    • Nguyen, K.T.1    Le Clair, S.V.2    Ye, S.3    Chen, Z.4
  • 68
    • 84863232604 scopus 로고    scopus 로고
    • Molecular Interactions Between Cell Penetrating Peptide Pep-1 and Model Cell
    • doi:10.1021/jp209604m
    • Ding B, Chen Z (2012) Molecular Interactions Between Cell Penetrating Peptide Pep-1 and Model Cell. Membranes - J Phys Chem B 116: 2545-2552. doi:10.1021/jp209604m.
    • (2012) Membranes - J Phys Chem B , vol.116 , pp. 2545-2552
    • Ding, B.1    Chen, Z.2
  • 69
    • 79958018447 scopus 로고    scopus 로고
    • Solvent Effect and Time-Dependent Behavior of C-Terminus Cysteine Modified Cecropin P1 Chemically Immobilized onto Polymer Surface
    • doi:10.1021/la200388y. PubMed: 21553837
    • Han X, Soblosky L, Slutsky M, Mello CM, Chen Z (2011) Solvent Effect and Time-Dependent Behavior of C-Terminus Cysteine Modified Cecropin P1 Chemically Immobilized onto Polymer Surface. Langmuir 27: 7042-7051. doi:10.1021/la200388y. PubMed: 21553837.
    • (2011) Langmuir , vol.27 , pp. 7042-7051
    • Han, X.1    Soblosky, L.2    Slutsky, M.3    Mello, C.M.4    Chen, Z.5
  • 70
    • 0030800966 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor kinases by calmodulin and localization of the calmodulin binding domain
    • DOI 10.1074/jbc.272.29.18273
    • Pronin AN, Satpaev DK, Slepak VZ, Benovic JL (1997) Regulation of G Protein-coupled Receptor Kinases by Calmodulin and Localization of the Calmodulin Binding Domain. J Biol Chem 272: 18273-18280. doi:10.1074/jbc.272.29. 18273. PubMed: 9218466. (Pubitemid 27306417)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.29 , pp. 18273-18280
    • Pronin, A.N.1    Satpaev, D.K.2    Slepak, V.Z.3    Benovic, J.L.4
  • 72
    • 46649109793 scopus 로고    scopus 로고
    • Structures of Rhodopsin Kinase in Different Ligand States Reveal Key Elements Involved in G Protein-coupled Receptor Kinase Activation
    • doi:10.1074/jbc.M708974200. PubMed: 18339619
    • Singh P, Wang B, Maeda T, Palczewski K, Tesmer JJ (2008) Structures of Rhodopsin Kinase in Different Ligand States Reveal Key Elements Involved in G Protein-coupled Receptor Kinase Activation. J Biol Chem 283: 14053-14062. doi:10.1074/jbc.M708974200. PubMed: 18339619.
    • (2008) J Biol Chem , vol.283 , pp. 14053-14062
    • Singh, P.1    Wang, B.2    Maeda, T.3    Palczewski, K.4    Tesmer, J.J.5
  • 73
    • 8644290071 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase 5 contains a DNA-binding nuclear localization sequence
    • DOI 10.1128/MCB.24.23.10169-10179.2004
    • Johnson LR, Scott MG, Pitcher JA (2004) G Protein-Coupled Receptor Kinase 5 Contains a DNA-Binding Nuclear Localization Sequence. Mol Cell Biol 24: 10169-10179. doi:10.1128/MCB.24.23.10169-10179.2004. PubMed: 15542828. (Pubitemid 39507857)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.23 , pp. 10169-10179
    • Johnson, L.R.1    Scott, M.G.H.2    Pitcher, J.A.3
  • 74
    • 84872917955 scopus 로고    scopus 로고
    • Regulation of G Protein-Coupled Receptor Kinases by Phospholipids
    • PubMed: 23151001
    • Homan KT, Glukhova A, Tesmer JJG (2013) Regulation of G Protein-Coupled Receptor Kinases by Phospholipids. Curr Med Chem 20: 39-46. PubMed: 23151001.
    • (2013) Curr Med Chem , vol.20 , pp. 39-46
    • Homan, K.T.1    Glukhova, A.2    Tesmer, J.J.G.3
  • 75
    • 84874607739 scopus 로고    scopus 로고
    • Nuclear Translocation of Cardiac G Protein-Coupled Receptor Kinase 5 Downstream of Select Gq-Activating Hypertrophic Ligands Is a Calmodulin-Dependent Process
    • doi:10.1371/journal.pone.0057324. PubMed: 23472081
    • Gold JI, Martini JS, Hullmann J, Gao E, Chuprun JK et al. (2013) Nuclear Translocation of Cardiac G Protein-Coupled Receptor Kinase 5 Downstream of Select Gq-Activating Hypertrophic Ligands Is a Calmodulin-Dependent Process. PLOS ONE 8: e57324. doi:10.1371/journal.pone.0057324. PubMed: 23472081.
    • (2013) PLOS ONE , vol.8
    • Gold, J.I.1    Martini, J.S.2    Hullmann, J.3    Gao, E.4    Chuprun, J.K.5
  • 76
    • 50449087071 scopus 로고    scopus 로고
    • Uncovering G protein-coupled receptor kinase-5 as a histone deacetylase kinase in the nucleus of cardiomyocytes
    • doi:10.1073/pnas.0803153105. PubMed: 18711143
    • Martini JS, Raake P, Vinge LE, DeGeorge BR Jr, Chuprun JK et al. (2008) Uncovering G protein-coupled receptor kinase-5 as a histone deacetylase kinase in the nucleus of cardiomyocytes. Proc Natl Acad Sci U S A 105: 12457-12462. doi:10.1073/pnas.0803153105. PubMed: 18711143.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 12457-12462
    • Martini, J.S.1    Raake, P.2    Vinge, L.E.3    DeGeorge Jr., B.R.4    Chuprun, J.K.5
  • 77
    • 80051666683 scopus 로고    scopus 로고
    • A Myristoyl/Phosphoserine Switch Controls cAMP-Dependent Protein Kinase Association to Membranes
    • doi:10.1016/j.jmb.2011.06.034. PubMed: 21740913
    • Gaffarogullari EC, Masterson LR, Metcalfe EE, Traaseth NJ, Balatri E et al. (2011) A Myristoyl/Phosphoserine Switch Controls cAMP-Dependent Protein Kinase Association to Membranes. J Mol Biol 411: 823-836. doi:10.1016/j.jmb. 2011.06.034. PubMed: 21740913.
    • (2011) J Mol Biol , vol.411 , pp. 823-836
    • Gaffarogullari, E.C.1    Masterson, L.R.2    Metcalfe, E.E.3    Traaseth, N.J.4    Balatri, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.