메뉴 건너뛰기




Volumn 40, Issue 4, 2011, Pages 565-576

The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2

Author keywords

GCAP 2; Lipid modification; Membrane protein interaction; Order parameter

Indexed keywords

1-PALMITOYL-2-OLEOYLPHOSPHATIDYLCHOLINE; 2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; CALCIUM BINDING PROTEIN; GUANYLATE CYCLASE ACTIVATOR; LIPOSOME; MYRISTIC ACID; NERVE PROTEIN; PHOSPHATIDYLCHOLINE;

EID: 79956046910     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-011-0680-9     Document Type: Article
Times cited : (18)

References (61)
  • 1
    • 0030848464 scopus 로고    scopus 로고
    • Molecular mechanics of calcium-myristoyl switches
    • DOI 10.1038/38310
    • JB Ames R Ishima T Tanaka JI Gordon L Stryer M Ikura 1997 Molecular mechanics of calcium-myristoyl switches Nature 389 198 202 9296500 10.1038/38310 1:CAS:528:DyaK2sXmtVSqu74%3D (Pubitemid 27400604)
    • (1997) Nature , vol.389 , Issue.6647 , pp. 198-202
    • Ames, J.B.1    Ishima, R.2    Tanaka, T.3    Gordon, J.I.4    Stryer, L.5    Ikura, M.6
  • 2
    • 0033516487 scopus 로고    scopus 로고
    • Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases
    • DOI 10.1074/jbc.274.27.19329
    • JB Ames AM Dizhoor M Ikura K Palczewski L Stryer 1999 Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases J Biol Chem 274 19329 19337 10383444 10.1074/jbc.274.27.19329 1:CAS:528:DyaK1MXksVWltbs%3D (Pubitemid 29314138)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.27 , pp. 19329-19337
    • Ames, J.B.1    Dizhoor, A.M.2    Ikura, M.3    Palczewski, K.4    Stryer, L.5
  • 3
    • 0037035554 scopus 로고    scopus 로고
    • Structure and calcium-binding studies of a recoverin mutant (E85Q) in an allosteric intermediate state
    • DOI 10.1021/bi012153k
    • JB Ames N Hamasaki T Molchanova 2002 Structure and calcium-binding studies of a recoverin mutant (E85Q) in an allosteric intermediate state Biochemistry 41 5776 5787 11980481 10.1021/bi012153k 1:CAS:528: DC%2BD38XjtF2jsb4%3D (Pubitemid 34462698)
    • (2002) Biochemistry , vol.41 , Issue.18 , pp. 5776-5787
    • Ames, J.B.1    Hamasaki, N.2    Molchanova, T.3
  • 4
    • 33747790300 scopus 로고    scopus 로고
    • Folding of the Repeat Domain of Tau Upon Binding to Lipid Surfaces
    • DOI 10.1016/j.jmb.2006.07.018, PII S0022283606008709
    • P Barre D Eliezer 2006 Folding of the repeat domain of tau upon binding to lipid surfaces J Mol Biol 362 312 326 16908029 10.1016/j.jmb.2006.07.018 1:CAS:528:DC%2BD28XovVSrt70%3D (Pubitemid 44278850)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.2 , pp. 312-326
    • Barre, P.1    Eliezer, D.2
  • 5
    • 58149197889 scopus 로고    scopus 로고
    • Membrane binding of lipidated Ras peptides and proteins-the structural point of view
    • 18771652 10.1016/j.bbamem.2008.08.006 1:CAS:528:DC%2BD1MXksVWksw%3D%3D
    • L Brunsveld H Waldmann D Huster 2009 Membrane binding of lipidated Ras peptides and proteins-the structural point of view Biochim Biophys Acta 1788 273 288 18771652 10.1016/j.bbamem.2008.08.006 1:CAS:528:DC%2BD1MXksVWksw%3D%3D
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 273-288
    • Brunsveld, L.1    Waldmann, H.2    Huster, D.3
  • 6
    • 0035156560 scopus 로고    scopus 로고
    • 2+-binding proteins
    • DOI 10.1042/0264-6021:3530001
    • 2+-binding proteins Biochem J 353 1 12 11115393 10.1042/0264-6021: 3530001 1:CAS:528:DC%2BD3MXnslyhtw%3D%3D (Pubitemid 32094594)
    • (2001) Biochemical Journal , vol.353 , Issue.1 , pp. 1-12
    • Burgoyne, R.D.1    Weiss, J.L.2
  • 7
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • 7716512 10.1126/science.7716512 1:CAS:528:DyaK2MXltVCitLs%3D
    • PJ Casey 1995 Protein lipidation in cell signaling Science 268 221 225 7716512 10.1126/science.7716512 1:CAS:528:DyaK2MXltVCitLs%3D
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 8
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • 10.1021/ac60119a033 1:CAS:528:DyaG2sXitFSjug%3D%3D
    • PS Chen TY Toribara H Warner 1956 Microdetermination of phosphorus Anal Chem 28 1756 1758 10.1021/ac60119a033 1:CAS:528:DyaG2sXitFSjug%3D%3D
    • (1956) Anal Chem , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 9
    • 0000745176 scopus 로고
    • Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains
    • 10.1016/0009-2614(76)80392-2 1:CAS:528:DyaE2sXntFWjuw%3D%3D
    • JH Davis KR Jeffrey M Bloom MI Valic TP Higgs 1976 Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains Chem Phys Lett 42 390 394 10.1016/0009-2614(76)80392-2 1:CAS:528:DyaE2sXntFWjuw%3D%3D
    • (1976) Chem Phys Lett , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 10
    • 0029400480 scopus 로고
    • NMR pipe-a multidimensional spectral processing system based on Unix pipes
    • 8520220 10.1007/BF00197809 1:CAS:528:DyaK2MXhtVSmurfK
    • F Delaglio S Grzesiek GW Vuister G Zhu J Pfeifer A Bax 1995 NMR pipe-a multidimensional spectral processing system based on Unix pipes J Biomol NMR 6 277 293 8520220 10.1007/BF00197809 1:CAS:528:DyaK2MXhtVSmurfK
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 11
    • 0033035402 scopus 로고    scopus 로고
    • Heterogeneous N-terminal acylation of retinal proteins
    • DOI 10.1016/S0163-7827(98)00020-4, PII S0163782798000204
    • JC Demar DR Rundle TG Wensel RE Anderson 1999 Heterogeneous N-terminal acylation of retinal proteins Prog Lipid Res 38 49 90 10396602 10.1016/S0163-7827(98)00020-4 1:CAS:528:DyaK1MXitVertLw%3D (Pubitemid 29090113)
    • (1999) Progress in Lipid Research , vol.38 , Issue.1 , pp. 49-90
    • DeMar Jr., J.C.1    Rundle, D.R.2    Wensel, T.G.3    Anderson, R.E.4
  • 14
    • 0029870184 scopus 로고    scopus 로고
    • Functional characterization of a guanylyl cyclase-activating protein from vertebrate rods. Cloning, heterologous expression, and localization
    • DOI 10.1074/jbc.271.14.8022
    • S Frins W Bönigk F Müller R Kellner KW Koch 1996 Functional characterization of a guanylyl cyclase-activating protein from vertebrate rods-cloning, heterologous expression, and localization J Biol Chem 271 8022 8027 8626484 10.1074/jbc.271.14.8022 1:CAS:528:DyaK28XitFartr4%3D (Pubitemid 26108622)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.14 , pp. 8022-8027
    • Frins, S.1    Bonigk, W.2    Muller, F.3    Kellner, R.4    Koch, K.-W.5
  • 17
    • 38349008362 scopus 로고    scopus 로고
    • 2+ sensor
    • 18202676 10.1038/nchembio0208-90 1:CAS:528:DC%2BD1cXnt1Cmug%3D%3D
    • 2+ sensor Nat Chem Biol 4 90 91 18202676 10.1038/nchembio0208-90 1:CAS:528: DC%2BD1cXnt1Cmug%3D%3D
    • (2008) Nat Chem Biol , vol.4 , pp. 90-91
    • Haynes, L.P.1    Burgoyne, R.D.2
  • 18
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • DOI 10.1016/0005-2736(85)90521-8
    • MJ Hope MB Bally G Webb PR Cullis 1985 Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume, and ability to maintain a membrane potential Biochim Biophys Acta 812 55 65 10.1016/0005-2736(85)90521-8 1:CAS:528:DyaL2MXnsFagug%3D%3D (Pubitemid 15159822)
    • (1985) Biochimica et Biophysica Acta - Biomembranes , vol.812 , Issue.1 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 20
    • 0032497935 scopus 로고    scopus 로고
    • Influence of docosahexaenoic acid and cholesterol on lateral lipid organization in phospholipid mixtures
    • DOI 10.1021/bi980078g
    • D Huster K Arnold K Gawrisch 1998 Influence of docosahexaenoic acid and cholesterol on lateral lipid organization in phospholipid membranes Biochemistry 37 17299 17308 9860844 10.1021/bi980078g 1:CAS:528:DyaK1cXnt1Cluro%3D (Pubitemid 29013788)
    • (1998) Biochemistry , vol.37 , Issue.49 , pp. 17299-17308
    • Huster, D.1    Arnold, K.2    Gawrisch, K.3
  • 22
    • 0037195270 scopus 로고    scopus 로고
    • Calcium- and myristoyl-dependent properties of guanylate cyclase-activating protein-1 and protein-2
    • DOI 10.1021/bi026618y
    • JY Hwang KW Koch 2002 Calcium- and myristoyl-dependent properties of guanylate cyclase-activating protein-1 and protein-2 Biochemistry 41 13021 13028 12390029 10.1021/bi026618y 1:CAS:528:DC%2BD38XntlOrur8%3D (Pubitemid 35215786)
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 13021-13028
    • Hwang, J.-Y.1    Koch, K.-W.2
  • 23
    • 0037020681 scopus 로고    scopus 로고
    • 2+-sensors guanylate cyclase-activating protein 1 and 2
    • 12445466 1:CAS:528:DC%2BD38XoslChu70%3D
    • 2+-sensors guanylate cyclase-activating protein 1 and 2 Biochim Biophys Acta 1600 111 117 12445466 1:CAS:528:DC%2BD38XoslChu70%3D
    • (2002) Biochim Biophys Acta , vol.1600 , pp. 111-117
    • Hwang, J.Y.1    Koch, K.W.2
  • 24
    • 4344679413 scopus 로고    scopus 로고
    • Diversity of guanylate cyclase-activating proteins (GCAPs) in teleost fish: Characterization of three novel GCAPs (GCAP4, GCAP5, GCAP7) from zebrafish (Danio rerio) and prediction of eight GCAPs (GCAP1-8) in pufferfish (Fugu rubripes)
    • DOI 10.1007/s00239-004-2614-y
    • Y Imanishi L Yang I Sokal S Filipek K Palczewski W Baehr 2004 Diversity of guanylate cyclase-activating proteins (GCAPs) in teleost fish: characterization of three novel GCAPs (GCAP4, GCAP5, GCAP7) from zebrafish (Danio rerio) and prediction of eight GCAPs (GCAP1-8) in pufferfish (Fugu rubripes) J Mol Evol 59 204 217 15486694 10.1007/s00239-004-2614-y 1:CAS:528:DC%2BD2cXntlCkurk%3D (Pubitemid 39128343)
    • (2004) Journal of Molecular Evolution , vol.59 , Issue.2 , pp. 204-217
    • Imanishi, Y.1    Yang, L.2    Sokal, I.3    Filipek, S.4    Palczewski, K.5    Baehr, W.6
  • 25
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • 10.1021/ja00052a088 1:CAS:528:DyaK3sXjt1eg
    • LE Kay P Keifer T Saarinen 1992 Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J Am Chem Soc 114 10663 10665 10.1021/ja00052a088 1:CAS:528:DyaK3sXjt1eg
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 26
    • 0027319966 scopus 로고
    • Myristoylation of hippocalcin is linked to its calcium-dependent membrane association properties
    • M Kobayashi K Takamatsu S Saitoh T Noguchi 1993 Myristoylation of hippocalcin is linked to its calcium-dependent membrane association properties J Biol Chem 268 18898 18904 8360179 1:CAS:528:DyaK3sXlslKht70%3D (Pubitemid 23273837)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.25 , pp. 18898-18904
    • Kobayashi, M.1    Takamatsu, K.2    Saitoh, S.3    Noguchi, T.4
  • 27
    • 0029239706 scopus 로고
    • Simple fed-batch technique for high cell density cultivation of Escherichia coli
    • 7766011 10.1016/0168-1656(94)00143-Z 1:CAS:528:DyaK2MXjvVemtLk%3D
    • DJ Korz U Rinas K Hellmuth EA Sanders WD Deckwer 1995 Simple fed-batch technique for high cell density cultivation of Escherichia coli J Biotechnol 39 59 65 7766011 10.1016/0168-1656(94)00143-Z 1:CAS:528:DyaK2MXjvVemtLk%3D
    • (1995) J Biotechnol , vol.39 , pp. 59-65
    • Korz, D.J.1    Rinas, U.2    Hellmuth, K.3    Sanders, E.A.4    Deckwer, W.D.5
  • 28
    • 0028894334 scopus 로고
    • Calcium and membrane-binding properties of bovine neurocalcin-delta expressed in Escherichia coli
    • 7852401 1:CAS:528:DyaK2MXjslahuro%3D
    • D Ladant 1995 Calcium and membrane-binding properties of bovine neurocalcin-delta expressed in Escherichia coli J Biol Chem 270 3179 3185 7852401 1:CAS:528:DyaK2MXjslahuro%3D
    • (1995) J Biol Chem , vol.270 , pp. 3179-3185
    • Ladant, D.1
  • 29
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • 11017708 10.1006/abio.2000.4773 1:CAS:528:DC%2BD3cXmvFOksL0%3D
    • AS Ladokhin S Jayasinghe SH White 2000 How to measure and analyze tryptophan fluorescence in membranes properly, and why bother? Anal Biochem 285 235 245 11017708 10.1006/abio.2000.4773 1:CAS:528:DC%2BD3cXmvFOksL0%3D
    • (2000) Anal Biochem , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 30
    • 0024758461 scopus 로고
    • 2H-nuclear magnetic resonance
    • 2605294 10.1016/S0006-3495(89)82749-3 1:CAS:528:DyaK3cXjvVKm
    • 2H-nuclear magnetic resonance Biophys J 56 1037 1041 2605294 10.1016/S0006-3495(89)82749-3 1:CAS:528:DyaK3cXjvVKm
    • (1989) Biophys J , vol.56 , pp. 1037-1041
    • Lafleur, M.1    Fine, B.2    Sternin, E.3    Cullis, P.R.4    Bloom, M.5
  • 31
    • 0001909564 scopus 로고    scopus 로고
    • Improved Watergate Pulse Sequences for Solvent Suppression in NMR Spectroscopy
    • ML Liu XA Mao CH Ye H Huang JK Nicholson JC Lindon 1998 Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy J Magn Reson 132 125 129 10.1006/jmre.1998.1405 1:CAS:528:DyaK1cXjsFSjsbg%3D (Pubitemid 128450594)
    • (1998) Journal of Magnetic Resonance , vol.132 , Issue.1 , pp. 125-129
    • Liu, M.1    Mao, X.-A.2    Ye, C.3    Huang, H.4    Nicholson, J.K.5    Lindon, J.C.6
  • 33
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • 7667880 10.1016/S0968-0004(00)89042-8 1:CAS:528:DyaK2MXntFWrsrg%3D
    • S McLaughlin A Aderem 1995 The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions Trends Biochem Sci 20 272 276 7667880 10.1016/S0968-0004(00)89042-8 1:CAS:528:DyaK2MXntFWrsrg%3D
    • (1995) Trends Biochem Sci , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 34
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • D Murray N Ben-Tal B Honig S McLaughlin 1997 Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology Structure 5 985 989 9309215 10.1016/S0969-2126(97)00251-7 1:CAS:528: DyaK2sXmt1Wgsr8%3D (Pubitemid 27393084)
    • (1997) Structure , vol.5 , Issue.8 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 35
    • 1842639175 scopus 로고    scopus 로고
    • 2+/Myristoyl Switch in Neuronal Calcium Sensor-1
    • DOI 10.1074/jbc.M310152200
    • 2+/myristoyl switch in neuronal calcium sensor-1 J Biol Chem 279 14347 14354 14726528 10.1074/jbc.M310152200 (Pubitemid 38468976)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 14347-14354
    • O'Callaghan, D.W.1    Burgoyne, R.D.2
  • 36
    • 0031009909 scopus 로고    scopus 로고
    • Calcium binding, but not a calcium-myristoyl switch, controls the ability of guanylyl cyclase-activating protein GCAP-2 to regulate photoreceptor guanylyl cyclase
    • DOI 10.1074/jbc.272.22.14327
    • EV Olshevskaya RE Hughes JB Hurley AM Dizhoor 1997 Calcium binding, but not a calcium-myristoyl switch, controls the ability of guanylyl cyclase-activating protein GCAP-2 to regulate photoreceptor guanylyl cyclase J Biol Chem 272 14327 14333 9162068 10.1074/jbc.272.22.14327 1:CAS:528: DyaK2sXjsFOru78%3D (Pubitemid 27232847)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.22 , pp. 14327-14333
    • Olshevskaya, E.V.1    Hughes, R.E.2    Hurley, J.B.3    Dizhoor, A.M.4
  • 37
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected 2-dimensional heteronuclear correlation NMR spectroscopy
    • 1:CAS:528:DyaK3MXkt1Sksbs%3D
    • AG Palmer J Cavanagh PE Wright M Rance 1991 Sensitivity improvement in proton-detected 2-dimensional heteronuclear correlation NMR spectroscopy J Magn Reson 93 151 170 1:CAS:528:DyaK3MXkt1Sksbs%3D
    • (1991) J Magn Reson , vol.93 , pp. 151-170
    • Palmer, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 38
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins
    • DOI 10.1021/bi00090a020
    • RM Peitzsch S McLaughlin 1993 Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins Biochemistry 32 10436 10443 8399188 10.1021/bi00090a020 1:CAS:528: DyaK3sXmt1SjsLg%3D (Pubitemid 23320168)
    • (1993) Biochemistry , vol.32 , Issue.39 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 39
    • 78651252937 scopus 로고    scopus 로고
    • Structure and dynamics of the lipid modifications of a transmembrane alpha-helical peptide determined by (2)H solid-state NMR spectroscopy
    • Penk A, Muller M, Scheidt HA, Langosch D, Huster D (2011) Structure and dynamics of the lipid modifications of a transmembrane alpha-helical peptide determined by (2)H solid-state NMR spectroscopy. Biochim Biophys Acta 1808:784-791
    • (2011) Biochim Biophys Acta 1808:784-791
    • Penk, A.1    Muller, M.2    Scheidt, H.A.3    Langosch, D.4    Huster, D.5
  • 40
    • 0033637460 scopus 로고    scopus 로고
    • 2H NMR spectroscopy
    • 11106622 10.1016/S0006-3495(00)76551-9 1:CAS:528:DC%2BD3MXitFCn
    • 2H NMR spectroscopy Biophys J 79 3172 3192 11106622 10.1016/S0006-3495(00)76551-9 1:CAS:528:DC%2BD3MXitFCn
    • (2000) Biophys J , vol.79 , pp. 3172-3192
    • Petrache, H.I.1    Dodd, S.W.2    Brown, M.F.3
  • 41
    • 33750343071 scopus 로고    scopus 로고
    • The lipidated membrane anchor of full length N-Ras protein shows an extensive dynamics as revealed by solid-state NMR spectroscopy
    • DOI 10.1021/ja063635s
    • G Reuther K-T Tan A Vogel C Nowak J Kuhlmann H Waldmann D Huster 2006 The lipidated membrane anchor of the N-ras protein shows an extensive dynamics as revealed by solid-state NMR J Am Chem Soc 128 13840 13846 17044712 10.1021/ja063635s 1:CAS:528:DC%2BD28XhtVajtrbM (Pubitemid 44632863)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.42 , pp. 13840-13846
    • Reuther, G.1    Tan, K.-T.2    Vogel, A.3    Nowak, C.4    Arnold, K.5    Kuhlmann, J.6    Waldmann, H.7    Muster, D.8
  • 43
    • 67650381847 scopus 로고    scopus 로고
    • 2H solid-state NMR spectroscopy
    • 19413971 10.1016/j.bpj.2009.02.028 1:CAS:528:DC%2BD1MXnvVertL0%3D
    • 2H solid-state NMR spectroscopy Biophys J 96 3663 3672 19413971 10.1016/j.bpj.2009.02.028 1:CAS:528:DC%2BD1MXnvVertL0%3D
    • (2009) Biophys J , vol.96 , pp. 3663-3672
    • Scheidt, H.A.1    Huster, D.2
  • 44
    • 0028389502 scopus 로고
    • A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed-field gradients
    • 8019138 10.1007/BF00175254 1:CAS:528:DyaK2cXjtFymtLk%3D
    • J Schleucher M Schwendinger M Sattler P Schmidt O Schedletzky SJ Glaser OW Sorensen C Griesinger 1994 A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed-field gradients J Biomol NMR 4 301 306 8019138 10.1007/BF00175254 1:CAS:528:DyaK2cXjtFymtLk%3D
    • (1994) J Biomol NMR , vol.4 , pp. 301-306
    • Schleucher, J.1    Schwendinger, M.2    Sattler, M.3    Schmidt, P.4    Schedletzky, O.5    Glaser, S.J.6    Sorensen, O.W.7    Griesinger, C.8
  • 45
    • 0018982584 scopus 로고
    • Lipid conformation in model membranes and biological membranes
    • 7220788 10.1017/S0033583500000305 1:CAS:528:DyaL3MXhtFKrtA%3D%3D
    • J Seelig A Seelig 1980 Lipid conformation in model membranes and biological membranes Q Rev Biophys 13 19 61 7220788 10.1017/S0033583500000305 1:CAS:528:DyaL3MXhtFKrtA%3D%3D
    • (1980) Q Rev Biophys , vol.13 , pp. 19-61
    • Seelig, J.1    Seelig, A.2
  • 47
    • 34547179849 scopus 로고    scopus 로고
    • Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology
    • DOI 10.1007/s10858-007-9166-6
    • Y Shen A Bax 2007 Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology J Biomol NMR 38 289 302 17610132 10.1007/s10858-007-9166-6 1:CAS:528:DC%2BD2sXotVantbg%3D (Pubitemid 47108511)
    • (2007) Journal of Biomolecular NMR , vol.38 , Issue.4 , pp. 289-302
    • Shen, Y.1    Bax, A.2
  • 48
    • 35448990534 scopus 로고    scopus 로고
    • Lipidated peptides as tools for understanding the membrane interactions of lipid-modified proteins
    • S.A. Simon T.J. McIntosh (eds). Elsevier Amsterdam. 10.1016/S1063- 5823(02)52015-9
    • Silvius JR (2002) Lipidated peptides as tools for understanding the membrane interactions of lipid-modified proteins. In: Simon SA, McIntosh TJ (eds) Peptide-lipid interactions. Elsevier, Amsterdam, pp 371-395
    • (2002) Peptide-lipid Interactions , pp. 371-395
    • Silvius, J.R.1
  • 49
    • 33646192721 scopus 로고    scopus 로고
    • The crystal structure of GCAP3 suggests molecular mechanism of GCAP-linked cone dystrophies
    • 16626734 10.1016/j.jmb.2006.03.042 1:CAS:528:DC%2BD28XksVahtrc%3D
    • R Stephen K Palczewski MC Sousa 2006 The crystal structure of GCAP3 suggests molecular mechanism of GCAP-linked cone dystrophies J Mol Biol 359 266 275 16626734 10.1016/j.jmb.2006.03.042 1:CAS:528:DC%2BD28XksVahtrc%3D
    • (2006) J Mol Biol , vol.359 , pp. 266-275
    • Stephen, R.1    Palczewski, K.2    Sousa, M.C.3
  • 50
    • 35748956109 scopus 로고    scopus 로고
    • Stabilizing Function for Myristoyl Group Revealed by the Crystal Structure of a Neuronal Calcium Sensor, Guanylate Cyclase-Activating Protein 1
    • DOI 10.1016/j.str.2007.09.013, PII S0969212607003395
    • R Stephen G Bereta M Golczak K Palczewski MC Sousa 2007 Stabilizing function for myristoyl group revealed by the crystal structure of a neuronal calcium sensor, guanylate cyclase-activating protein 1 Structure 15 1392 1402 17997965 10.1016/j.str.2007.09.013 1:CAS:528:DC%2BD2sXht12iu73M (Pubitemid 350051925)
    • (2007) Structure , vol.15 , Issue.11 , pp. 1392-1402
    • Stephen, R.1    Bereta, G.2    Golczak, M.3    Palczewski, K.4    Sousa, M.C.5
  • 51
    • 0029135419 scopus 로고
    • Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state
    • 7630423 10.1038/376444a0 1:CAS:528:DyaK2MXntlCqs7k%3D
    • T Tanaka JB Ames TS Harvey L Stryer M Ikura 1995 Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state Nature 376 444 447 7630423 10.1038/376444a0 1:CAS:528:DyaK2MXntlCqs7k%3D
    • (1995) Nature , vol.376 , pp. 444-447
    • Tanaka, T.1    Ames, J.B.2    Harvey, T.S.3    Stryer, L.4    Ikura, M.5
  • 53
    • 74249107842 scopus 로고    scopus 로고
    • A solid-state NMR study of the structure and dynamics of the myristoylated N-terminus of the guanylate cyclase-activating protein-2
    • 19616509 10.1016/j.bbamem.2009.06.028 1:CAS:528:DC%2BC3cXhtVGks7s%3D
    • S Theisgen HA Scheidt A Magalhaes TJ Bonagamba D Huster 2010 A solid-state NMR study of the structure and dynamics of the myristoylated N-terminus of the guanylate cyclase-activating protein-2 Biochim Biophys Acta 1798 266 274 19616509 10.1016/j.bbamem.2009.06.028 1:CAS:528: DC%2BC3cXhtVGks7s%3D
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 266-274
    • Theisgen, S.1    Scheidt, H.A.2    Magalhaes, A.3    Bonagamba, T.J.4    Huster, D.5
  • 54
    • 0027515072 scopus 로고
    • Molecular dynamics simulations of a lipid bilayer and of hexadecane: An investigation of membrane fluidity
    • RM Venable Y Zhang BJ Hardy RW Pastor 1993 Molecular dynamics simulations of a lipid bilayer and of hexadecane: an investigation of membrane fluidity Science 262 223 226 8211140 10.1126/science.8211140 1:CAS:528:DyaK3sXms1Cqu7k%3D (Pubitemid 23344464)
    • (1993) Science , vol.262 , Issue.5131 , pp. 223-226
    • Venable, R.M.1    Zhang, Y.2    Hardy, B.J.3    Pastor, R.W.4
  • 60
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • DOI 10.1146/annurev.biophys.28.1.319
    • SH White WC Wimley 1999 Membrane protein folding and stability: physical principles Annu Rev Biophys Biomol Struct 28 319 365 10410805 10.1146/annurev.biophys.28.1.319 1:CAS:528:DyaK1MXkt1erurs%3D (Pubitemid 29319262)
    • (1999) Annual Review of Biophysics and Biomolecular Structure , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 61
    • 0026468238 scopus 로고
    • Calcium-myristoyl protein switch
    • 1454850 10.1073/pnas.89.23.11569 1:CAS:528:DyaK3sXps1Ghtw%3D%3D
    • S Zozulya L Stryer 1992 Calcium-myristoyl protein switch Proc Natl Acad Sci USA 89 11569 11573 1454850 10.1073/pnas.89.23.11569 1:CAS:528: DyaK3sXps1Ghtw%3D%3D
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11569-11573
    • Zozulya, S.1    Stryer, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.