메뉴 건너뛰기




Volumn 52, Issue , 2002, Pages 371-395

Lipidated peptides as tools for understanding the membrane interactions of lipid-modified proteins

Author keywords

[No Author keywords available]

Indexed keywords


EID: 35448990534     PISSN: 10635823     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s1063-5823(02)52015-9     Document Type: Review
Times cited : (25)

References (106)
  • 1
    • 0030891289 scopus 로고    scopus 로고
    • N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange
    • B. Antonny S. Beraud-Dufour P. Chardin M. Chabre N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange Biochemistry 36 1997 4675 4684
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 2
    • 0031795796 scopus 로고    scopus 로고
    • MARCKS, membranes, and calmodulin: Kinetics of their interaction
    • A. Arbuzova D. Murray S. McLaughlin MARCKS, membranes, and calmodulin: Kinetics of their interaction Biochim. Biophys. Acta 1376 1998 369 379
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 369-379
    • Arbuzova, A.1    Murray, D.2    McLaughlin, S.3
  • 3
    • 0034642495 scopus 로고    scopus 로고
    • Bio-organic synthesis of lipid-modified proteins for the study of signal transduction
    • B. Bader K. Kuhn D.J. Owen H. Waldmann A. Wittinghofer J. Kuhlmann Bio-organic synthesis of lipid-modified proteins for the study of signal transduction Nature 403 2000 223 226
    • (2000) Nature , vol.403 , pp. 223-226
    • Bader, B.1    Kuhn, K.2    Owen, D.J.3    Waldmann, H.4    Wittinghofer, A.5    Kuhlmann, J.6
  • 4
    • 0032031584 scopus 로고    scopus 로고
    • Pseudo-enzymatic S-acylation of a myristoylated yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo
    • M.C. Bano C.S. Jackson A.I. Magee Pseudo-enzymatic S-acylation of a myristoylated yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo Biochem. J. 330 1998 723 731
    • (1998) Biochem. J. , vol.330 , pp. 723-731
    • Bano, M.C.1    Jackson, C.S.2    Magee, A.I.3
  • 5
    • 0029145798 scopus 로고
    • Biochemical characterization of a palmitoyl acyltransferase activity that palmitoylates myristoylated proteins
    • L. Berthiaume M.D. Resh Biochemical characterization of a palmitoyl acyltransferase activity that palmitoylates myristoylated proteins J. Biol. Chem. 270 1995 22399 22405
    • (1995) J. Biol. Chem. , vol.270 , pp. 22399-22405
    • Berthiaume, L.1    Resh, M.D.2
  • 6
    • 0033519347 scopus 로고    scopus 로고
    • Trafficking of an acylated cytosolic protein: Newly synthesized p56lck travels to the plasma membrane via the exocytic pathway
    • lck travels to the plasma membrane via the exocytic pathway J. Cell Biol. 145 1999 457 468
    • (1999) J. Cell Biol. , vol.145 , pp. 457-468
    • Bijlmakers, M.J.1    Marsh, M.2
  • 8
    • 0030788654 scopus 로고    scopus 로고
    • The mechanism and functional roles of protein palmitoylation in the nervous system
    • O.A. Bizzozero The mechanism and functional roles of protein palmitoylation in the nervous system Neuropediatrics 28 1997 23 26
    • (1997) Neuropediatrics , vol.28 , pp. 23-26
    • Bizzozero, O.A.1
  • 9
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • D.A. Brown E. London Functions of lipid rafts in biological membranes Annu. Rev. Cell Dev. Biol. 14 1998 111 136
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 11
    • 0033180113 scopus 로고    scopus 로고
    • The role of ARF and Rab GTPases in membrane transport
    • P. Chavrier B. Goud The role of ARF and Rab GTPases in membrane transport Curr. Opin. Cell Biol. 11 1999 466 475
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 466-475
    • Chavrier, P.1    Goud, B.2
  • 13
    • 0032986772 scopus 로고    scopus 로고
    • Synthesis of the N-terminal lipohexapeptide of human Gαo-protein and fluorescent-labeled analogues for biological studies
    • αo-protein and fluorescent-labeled analogues for biological studies Chem. Ear. J. 5 1999 922 936
    • (1999) Chem. Ear. J. , vol.5 , pp. 922-936
    • Cotte, A.1    Bader, B.2    Kuhlmann, J.3    Waldmann, H.4
  • 14
    • 0030765042 scopus 로고    scopus 로고
    • G-protein-coupled receptors for peptide hormones in yeast
    • K. Davis J. Davey G-protein-coupled receptors for peptide hormones in yeast Biochim. Soc. Trans. 25 1997 1015 1021
    • (1997) Biochim. Soc. Trans. , vol.25 , pp. 1015-1021
    • Davis, K.1    Davey, J.2
  • 15
    • 0030846849 scopus 로고    scopus 로고
    • Novel modifications to the farnesyl moiety of the a-factor lipopeptide pheromone from Saccharomyces cerevisiae: A role for isoprene modifications in ligand presentation
    • A.L. Dawe J.M. Becker Y. Jiang F. Naider J.T. Eummer Y.Q. Mu R.A. Gibbs Novel modifications to the farnesyl moiety of the a -factor lipopeptide pheromone from Saccharomyces cerevisiae : A role for isoprene modifications in ligand presentation Biochemistry 36 1997 12036 12044
    • (1997) Biochemistry , vol.36 , pp. 12036-12044
    • Dawe, A.L.1    Becker, J.M.2    Jiang, Y.3    Naider, F.4    Eummer, J.T.5    Mu, Y.Q.6    Gibbs, R.A.7
  • 16
    • 0030749022 scopus 로고    scopus 로고
    • Replacement of the H-Ras farnesyl group by lipid analogues: Implications for downstream processing and effector activation in Xenopus oocytes
    • T. Dudler M.H. Gelb Replacement of the H-Ras farnesyl group by lipid analogues: Implications for downstream processing and effector activation in Xenopus oocytes Biochemistry 36 1997 12434 12441
    • (1997) Biochemistry , vol.36 , pp. 12434-12441
    • Dudler, T.1    Gelb, M.H.2
  • 17
    • 0029814190 scopus 로고    scopus 로고
    • Autoacylation of G protein alpha subunits
    • J.A. Duncan A.G. Gilman Autoacylation of G protein alpha subunits J. Biol. Chem. 271 1996 23594 23600
    • (1996) J. Biol. Chem. , vol.271 , pp. 23594-23600
    • Duncan, J.A.1    Gilman, A.G.2
  • 18
    • 0032546946 scopus 로고    scopus 로고
    • A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21ras
    • ras J. Biol. Chem. 273 1998 15830 15837
    • (1998) J. Biol. Chem. , vol.273 , pp. 15830-15837
    • Duncan, J.A.1    Gilman, A.G.2
  • 19
    • 0032497835 scopus 로고    scopus 로고
    • Signalling functions of protein palmitoylation
    • J.T. Dunphy M.E. Linder Signalling functions of protein palmitoylation Biochim. Biophys. Acta 1436 1998 245 261
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 245-261
    • Dunphy, J.T.1    Linder, M.E.2
  • 20
    • 0029927840 scopus 로고    scopus 로고
    • G-protein palmitoyltransferase activity is enriched in plasma membranes
    • J.T. Dunphy W.K. Greentree C.L. Manahan M.E. Linder G-protein palmitoyltransferase activity is enriched in plasma membranes J. Biol. Chem. 271 1996 7154 7159
    • (1996) J. Biol. Chem. , vol.271 , pp. 7154-7159
    • Dunphy, J.T.1    Greentree, W.K.2    Manahan, C.L.3    Linder, M.E.4
  • 22
    • 0030612441 scopus 로고    scopus 로고
    • Biophysical studies of lipopeptide-membrane interactions
    • R.M. Epand Biophysical studies of lipopeptide-membrane interactions Biopolymers 43 1997 15 24
    • (1997) Biopolymers , vol.43 , pp. 15-24
    • Epand, R.M.1
  • 23
    • 0027321058 scopus 로고
    • Role of prenylation in the interaction of the a-factor mating pheromone with phospholipid bilayers
    • R.F. Epand C.B. Xue S.H. Wang F. Naider J.M. Becker R.M. Epand Role of prenylation in the interaction of the a -factor mating pheromone with phospholipid bilayers Biochemistry 32 1993 8368 8373
    • (1993) Biochemistry , vol.32 , pp. 8368-8373
    • Epand, R.F.1    Xue, C.B.2    Wang, S.H.3    Naider, F.4    Becker, J.M.5    Epand, R.M.6
  • 26
    • 0033392946 scopus 로고    scopus 로고
    • Enzymology and biology of CaaX protein prenylation
    • H.W. Fu P.J. Casey Enzymology and biology of CaaX protein prenylation Rec. Prog. Hormone Res. 54 1999 315 342
    • (1999) Rec. Prog. Hormone Res. , vol.54 , pp. 315-342
    • Fu, H.W.1    Casey, P.J.2
  • 27
    • 0029127725 scopus 로고
    • Binding of prenylated and polybasic peptides to membranes: Affinities and intervesicle exchange
    • F. Ghomashchi X. Zhang L. Liu M.H. Gelb Binding of prenylated and polybasic peptides to membranes: Affinities and intervesicle exchange Biochemistry 34 1995 11910 11918
    • (1995) Biochemistry , vol.34 , pp. 11910-11918
    • Ghomashchi, F.1    Zhang, X.2    Liu, L.3    Gelb, M.H.4
  • 28
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • J. Goldberg Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching Cell 95 1998 237 248
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 29
    • 0030992879 scopus 로고    scopus 로고
    • C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases
    • Y.Q. Gosser T.K. Nomanbhoy B. Aghazadeh D. Manor C. Combs R.A. Cerione M.K. Rosen C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases Nature 387 1997 814 819
    • (1997) Nature , vol.387 , pp. 814-819
    • Gosser, Y.Q.1    Nomanbhoy, T.K.2    Aghazadeh, B.3    Manor, D.4    Combs, C.5    Cerione, R.A.6    Rosen, M.K.7
  • 30
    • 0029760018 scopus 로고    scopus 로고
    • Binding of hisactophilin I and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch
    • F. Hanakam G. Gerisch S. Lotz T. Alt A. Seelig Binding of hisactophilin I and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch Biochemistry 35 1996 11036 11044
    • (1996) Biochemistry , vol.35 , pp. 11036-11044
    • Hanakam, F.1    Gerisch, G.2    Lotz, S.3    Alt, T.4    Seelig, A.5
  • 32
    • 0033588290 scopus 로고    scopus 로고
    • The prostacyclin receptor is isoprenylated. Isoprenylation is required for efficient receptor-effector coupling
    • J.S. Hayes O.A. Lawler M.T. Walsh B.T. Kinsella The prostacyclin receptor is isoprenylated. Isoprenylation is required for efficient receptor-effector coupling J. Biol. Chem. 274 1999 23707 23718
    • (1999) J. Biol. Chem. , vol.274 , pp. 23707-23718
    • Hayes, J.S.1    Lawler, O.A.2    Walsh, M.T.3    Kinsella, B.T.4
  • 33
    • 0034603198 scopus 로고    scopus 로고
    • Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI
    • G.R. Hoffman N. Nassar R.A. Cerione Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI Cell 100 2000 345 356
    • (2000) Cell , vol.100 , pp. 345-356
    • Hoffman, G.R.1    Nassar, N.2    Cerione, R.A.3
  • 34
    • 0022409872 scopus 로고
    • Three-dimensional structure of poliovirus at 2.9 resolution
    • J.M. Hogle M. Chow D.J. Filman Three-dimensional structure of poliovirus at 2.9 resolution Science 229 1985 1358 1365
    • (1985) Science , vol.229 , pp. 1358-1365
    • Hogle, J.M.1    Chow, M.2    Filman, D.J.3
  • 35
    • 0029089024 scopus 로고
    • Calcium-dependent solvation of the myristoyl group of recoverin
    • R.E. Hughes P.S. Brzovic R.E. Klevit J.B. Hurley Calcium-dependent solvation of the myristoyl group of recoverin Biochemistry 34 1995 11410 11416
    • (1995) Biochemistry , vol.34 , pp. 11410-11416
    • Hughes, R.E.1    Brzovic, P.S.2    Klevit, R.E.3    Hurley, J.B.4
  • 37
    • 0026726050 scopus 로고
    • Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases
    • J. Inglese W.J. Koch M.G. Caron R.J. lefkowitz Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases Nature 359 1992 147 150
    • (1992) Nature , vol.359 , pp. 147-150
    • Inglese, J.1    Koch, W.J.2    Caron, M.G.3    lefkowitz, R.J.4
  • 40
    • 0029147830 scopus 로고
    • Conformations of peptides corresponding to fatty acylation sites in proteins. A circular dichroism study
    • M. Joseph R. Nagaraj Conformations of peptides corresponding to fatty acylation sites in proteins. A circular dichroism study J. Biol. Chem. 270 1995 19439 19445
    • (1995) J. Biol. Chem. , vol.270 , pp. 19439-19445
    • Joseph, M.1    Nagaraj, R.2
  • 41
    • 0026026295 scopus 로고
    • Stoichiometric interaction of smg p21 with its GDP/GTP exchange protein and its novel action to regulate the translocation of smg p21 between membrane and cytoplasm
    • S. Kawamura K. Kaibuchi M. Hiroyoshi Y. Hata Y. Takai Stoichiometric interaction of smg p21 with its GDP/GTP exchange protein and its novel action to regulate the translocation of smg p21 between membrane and cytoplasm Biochem. Biophys. Res. Commun. 174 1991 1095 1102
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 1095-1102
    • Kawamura, S.1    Kaibuchi, K.2    Hiroyoshi, M.3    Hata, Y.4    Takai, Y.5
  • 43
    • 0028361026 scopus 로고
    • Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin
    • J. Kim P.J. Blackshear J.D. Johnson S. McLaughlin Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin Biophys. 67 1994 227 237
    • (1994) Biophys. , vol.67 , pp. 227-237
    • Kim, J.1    Blackshear, P.J.2    Johnson, J.D.3    McLaughlin, S.4
  • 44
    • 0028845341 scopus 로고
    • Efficient interaction with a receptor requires a specific type of prenyl group on the G protein gamma subunit
    • O. Kisselev M. Ermolaeva N. Gautam Efficient interaction with a receptor requires a specific type of prenyl group on the G protein gamma subunit J. Biol. Chem. 270 1995 25356 25358
    • (1995) J. Biol. Chem. , vol.270 , pp. 25356-25358
    • Kisselev, O.1    Ermolaeva, M.2    Gautam, N.3
  • 45
    • 0030610232 scopus 로고    scopus 로고
    • Gαs contains an unidentified covalent modification that increases its affinity for adenylyl cyclase
    • αs contains an unidentified covalent modification that increases its affinity for adenylyl cyclase Proc. Natl. Acad. Sci. USA 94 1997 6116 6120
    • (1997) , pp. 6116-6120
    • Kleuss, C.1    Gilman, A.G.2
  • 47
    • 0033540056 scopus 로고    scopus 로고
    • Ghrelin is a growth-hormone-releasing acylated peptide from stomach
    • M. Kojima H. Hosoda Y. Date M. Nakazato H. Matsuo K. Kangawa Ghrelin is a growth-hormone-releasing acylated peptide from stomach Nature 402 1999 656 659
    • (1999) Nature , vol.402 , pp. 656-659
    • Kojima, M.1    Hosoda, H.2    Date, Y.3    Nakazato, M.4    Matsuo, H.5    Kangawa, K.6
  • 48
    • 0032546549 scopus 로고    scopus 로고
    • Lipid-binding characteristics of the polybasic carboxy-terminal sequence of K-Ras4B
    • R. Leventis J.R. Silvius Lipid-binding characteristics of the polybasic carboxy-terminal sequence of K-Ras4B Biochemistry 37 1998 7640 7648
    • (1998) Biochemistry , vol.37 , pp. 7640-7648
    • Leventis, R.1    Silvius, J.R.2
  • 49
    • 0030955679 scopus 로고    scopus 로고
    • Acyl-CoA binding proteins inhibit the nonenzymic S-actvaion of cysteinyl-containing peptide sequences by long-chain acyl-CoAs
    • R. Leventis G. Juel J.K. Knudsen J.R. Silvius Acyl-CoA binding proteins inhibit the nonenzymic S-actvaion of cysteinyl-containing peptide sequences by long-chain acyl-CoAs Biochemistry 36 1997 5546 5553
    • (1997) Biochemistry , vol.36 , pp. 5546-5553
    • Leventis, R.1    Juel, G.2    Knudsen, J.K.3    Silvius, J.R.4
  • 50
    • 0029041182 scopus 로고
    • Synthetic prenylated peptides: Studying prenyl protein-specific endoprotease and other aspects of protein prenylation
    • L. Liu G.-F. Jang C. Farnsworth K. Yokoyama J.A. Glomset M.H. Gelb Synthetic prenylated peptides: Studying prenyl protein-specific endoprotease and other aspects of protein prenylation Meth. Enzymol. 250 1995 189 206
    • (1995) Meth. Enzymol. , vol.250 , pp. 189-206
    • Liu, L.1    Jang, G.-F.2    Farnsworth, C.3    Yokoyama, K.4    Glomset, J.A.5    Gelb, M.H.6
  • 51
    • 0032528863 scopus 로고    scopus 로고
    • Phosducin induces a structural change in transducin βγ
    • A. Loew Y.-K. Ho T. Blundell B. Bax Phosducin induces a structural change in transducin βγ Structure 6 1998 1007 1019
    • (1998) Structure , vol.6 , pp. 1007-1019
    • Loew, A.1    Ho, Y.-K.2    Blundell, T.3    Bax, B.4
  • 52
    • 0034603705 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of the N-terminal fragment of adenosine diphosphate ribosylation factor 1 in micelles and bicelles: Influence of N-myristoylation
    • J.A. Losonczi E. Tian J.H. Prestegard Nuclear magnetic resonance studies of the N-terminal fragment of adenosine diphosphate ribosylation factor 1 in micelles and bicelles: Influence of N-myristoylation Biochemistry 39 2000 3804 3816
    • (2000) Biochemistry , vol.39 , pp. 3804-3816
    • Losonczi, J.A.1    Tian, E.2    Prestegard, J.H.3
  • 53
    • 0032744491 scopus 로고    scopus 로고
    • Functional roles for fatty acylated amino-terminal domains in subcellular localization
    • J.B. McCabe L.G. Berthiaume Functional roles for fatty acylated amino-terminal domains in subcellular localization Mol. Biol. Cell 10 1999 3771 3786
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3771-3786
    • McCabe, J.B.1    Berthiaume, L.G.2
  • 54
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • M.J. McConville M.A. Ferguson The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes Biochem. J. 294 1993 305 324
    • (1993) Biochem. J. , vol.294 , pp. 305-324
    • McConville, M.J.1    Ferguson, M.A.2
  • 55
    • 0028848171 scopus 로고
    • The farnesyl group of H-Ras facilitates the activation of a soluble upstream activator of mitogen-activated protein kinase
    • E. McGeady S. Kuroda K. Shimizu Y. Takai M.H. Gelb The farnesyl group of H-Ras facilitates the activation of a soluble upstream activator of mitogen-activated protein kinase J. Biol. Chem. 270 1995 26347 26351
    • (1995) J. Biol. Chem. , vol.270 , pp. 26347-26351
    • McGeady, E.1    Kuroda, S.2    Shimizu, K.3    Takai, Y.4    Gelb, M.H.5
  • 56
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • K.A. Melkonian A.G. Ostermeyer J.Z. Chen M.G. Roth D.A. Brown Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated J. Biol. Chem. 274 1999 3910 3917
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 57
    • 0025962646 scopus 로고
    • Synthesis of novel immunologically active tripalmitoyl-S-glycerylcysteinyl lipopeptides as useful intermediates for immunogen preparations
    • J. Metzger K.H. Wiesmuller R. Schaude W.G. Bessler G. Jung Synthesis of novel immunologically active tripalmitoyl- S -glycerylcysteinyl lipopeptides as useful intermediates for immunogen preparations Int. J. Pept. Prot. Res. 37 1991 46 57
    • (1991) Int. J. Pept. Prot. Res. , vol.37 , pp. 46-57
    • Metzger, J.1    Wiesmuller, K.H.2    Schaude, R.3    Bessler, W.G.4    Jung, G.5
  • 58
    • 0021307433 scopus 로고
    • Post-translational modification and processing of outer membrane prolipoproteins in Escherichia coli
    • S. Mizushima Post-translational modification and processing of outer membrane prolipoproteins in Escherichia coli Mol. Cell. Biochem. 60 1984 5 15
    • (1984) Mol. Cell. Biochem. , vol.60 , pp. 5-15
    • Mizushima, S.1
  • 59
    • 0034695484 scopus 로고    scopus 로고
    • Lipid-dependent targeting of G proteins into rafts
    • S. Moffett D.A. Brown M.E. Linder Lipid-dependent targeting of G proteins into rafts J. Biol. Chem. 275 2000 2191 2198
    • (2000) J. Biol. Chem. , vol.275 , pp. 2191-2198
    • Moffett, S.1    Brown, D.A.2    Linder, M.E.3
  • 60
    • 0034681170 scopus 로고    scopus 로고
    • The specific binding of small molecule isoprenoids to RhoGDP dissociation inhibitor (RhoGDI)
    • M.S. Mondal Z. Wang A.M. Seeds R.R. Rando The specific binding of small molecule isoprenoids to RhoGDP dissociation inhibitor (RhoGDI) Biochemistry 39 2000 406 412
    • (2000) Biochemistry , vol.39 , pp. 406-412
    • Mondal, M.S.1    Wang, Z.2    Seeds, A.M.3    Rando, R.R.4
  • 61
    • 0030346309 scopus 로고    scopus 로고
    • Palmitoylation: A post-translational modification that regulates signalling from G-protein coupled receptors
    • J.P. Morello M. Bouvier Palmitoylation: A post-translational modification that regulates signalling from G-protein coupled receptors Biochem. Cell Biol. 74 1996 449 457
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 449-457
    • Morello, J.P.1    Bouvier, M.2
  • 62
    • 0028355411 scopus 로고
    • Receptor regulation of G-protein palmitoylation
    • S.M. Mumby C. Kleuss A.G. Gilman Receptor regulation of G-protein palmitoylation Proc. Natl. Acad. Sci. USA 91 1994 2800 2804
    • (1994) , pp. 2800-2804
    • Mumby, S.M.1    Kleuss, C.2    Gilman, A.G.3
  • 64
    • 0030612440 scopus 로고    scopus 로고
    • Synthesis of prenylated peptides and peptide esters
    • F. Naider J.M. Becker Synthesis of prenylated peptides and peptide esters Biopolymers 43 1997 3 14
    • (1997) Biopolymers , vol.43 , pp. 3-14
    • Naider, F.1    Becker, J.M.2
  • 65
    • 0020353685 scopus 로고
    • Glyceride-cysteine lipoproteins and secretion by Grampositive bacteria
    • J.B. Nielsen J.O. Lampen Glyceride-cysteine lipoproteins and secretion by Grampositive bacteria J. Bacteriol. 152 1982 315 322
    • (1982) J. Bacteriol. , vol.152 , pp. 315-322
    • Nielsen, J.B.1    Lampen, J.O.2
  • 66
    • 0030564274 scopus 로고    scopus 로고
    • Isoprenylation/methylation of proteins enhances membrane association by a hydrophobic mechanism
    • C.A. Parish R.R. Rando Isoprenylation/methylation of proteins enhances membrane association by a hydrophobic mechanism Biochemistry 35 1996 8473 8477
    • (1996) Biochemistry , vol.35 , pp. 8473-8477
    • Parish, C.A.1    Rando, R.R.2
  • 67
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins
    • R.M. Peitzsch S. McLaughlin Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins Biochemistry 32 1993 10436 10443
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 69
    • 0029844192 scopus 로고    scopus 로고
    • Cholesterol modification of Hedgehog signaling proteins in animal development
    • J.A. Porter K.E. Young P.A. Beachy Cholesterol modification of Hedgehog signaling proteins in animal development Science 274 1996 255 259
    • (1996) Science , vol.274 , pp. 255-259
    • Porter, J.A.1    Young, K.E.2    Beachy, P.A.3
  • 70
    • 0028033931 scopus 로고
    • Cysteine-containing peptide sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface
    • S. Quesnel J.R. Silvius Cysteine-containing peptide sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface Biochemistry 33 1994 13340 13348
    • (1994) Biochemistry , vol.33 , pp. 13340-13348
    • Quesnel, S.1    Silvius, J.R.2
  • 71
    • 0026713293 scopus 로고
    • The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins
    • R. Regazzi A. Kikuchi Y. Takai C.B. Wollheim The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins J. Biol. Chem. 267 1992 17512 17519
    • (1992) J. Biol. Chem. , vol.267 , pp. 17512-17519
    • Regazzi, R.1    Kikuchi, A.2    Takai, Y.3    Wollheim, C.B.4
  • 72
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • M.D. Resh Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins Biochim. Biophys. Acta 1451 1999 1 16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 74
    • 0033135758 scopus 로고    scopus 로고
    • Synthesis of the palmitoylated and prenylated C-terminal lipopeptides of the human R- and N-Ras proteins
    • T. Schmittberger H. Waldmann Synthesis of the palmitoylated and prenylated C-terminal lipopeptides of the human R- and N-Ras proteins Bioorg. Med. Chem. 7 1999 749 762
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 749-762
    • Schmittberger, T.1    Waldmann, H.2
  • 75
    • 0029767683 scopus 로고    scopus 로고
    • Lipid-modified, cysteinyl-containing peptides of diverse structures are efficiently S-acylated at the plasma membrane of mammalian cells
    • H. Schroeder R. Leventis S. Shahinian P.A. Walton J.R. Silvius Lipid-modified, cysteinyl-containing peptides of diverse structures are efficiently S-acylated at the plasma membrane of mammalian cells J. Cell Biol. 134 1996 647 660
    • (1996) J. Cell Biol. , vol.134 , pp. 647-660
    • Schroeder, H.1    Leventis, R.2    Shahinian, S.3    Walton, P.A.4    Silvius, J.R.5
  • 76
    • 0030696229 scopus 로고    scopus 로고
    • S-Acylation and plasma membrane targeting of the famesylated carboxyl-terminal peptide of N-Ras in mammalian fibroblasts
    • H. Schroeder R. Leventis S. Rex M. Schelhaas E. Nägele H. Waldmann J.R. Silvius S-Acylation and plasma membrane targeting of the famesylated carboxyl-terminal peptide of N-Ras in mammalian fibroblasts Biochemistry 36 1997 13102 13109
    • (1997) Biochemistry , vol.36 , pp. 13102-13109
    • Schroeder, H.1    Leventis, R.2    Rex, S.3    Schelhaas, M.4    Nägele, E.5    Waldmann, H.6    Silvius, J.R.7
  • 77
    • 0033594815 scopus 로고    scopus 로고
    • Molecular determinants of the reversible membrane anchorage of the G-protein transducin
    • H.R. Seitz M. Heck K.P. Hofmann T. Alt J. Pellaud A. Seelig Molecular determinants of the reversible membrane anchorage of the G-protein transducin Biochemistry 38 1999 7950 7960
    • (1999) Biochemistry , vol.38 , pp. 7950-7960
    • Seitz, H.R.1    Heck, M.2    Hofmann, K.P.3    Alt, T.4    Pellaud, J.5    Seelig, A.6
  • 78
    • 0028968896 scopus 로고
    • Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes
    • S. Shahinian J.R. Silvius Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes Biochemistry 34 1995 3813 3822
    • (1995) Biochemistry , vol.34 , pp. 3813-3822
    • Shahinian, S.1    Silvius, J.R.2
  • 80
    • 0028196986 scopus 로고
    • Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers
    • J.R. Silvius F. l'Heureux Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers Biochemistry 33 1994 3014 3022
    • (1994) Biochemistry , vol.33 , pp. 3014-3022
    • Silvius, J.R.1    l'Heureux, F.2
  • 81
    • 0027415097 scopus 로고
    • Interbilayer transfer of phospholipid-anchored macromolecules via monomer diffusion
    • J.R. Silvius M.J. Zuckermann Interbilayer transfer of phospholipid-anchored macromolecules via monomer diffusion Biochemistry 32 1993 3153 3161
    • (1993) Biochemistry , vol.32 , pp. 3153-3161
    • Silvius, J.R.1    Zuckermann, M.J.2
  • 82
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 83
    • 0034630098 scopus 로고    scopus 로고
    • Recent advances in the study of prenylated proteins
    • M. Sinensky Recent advances in the study of prenylated proteins Biochim. Biophys. Acta 1484 2000 93 106
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 93-106
    • Sinensky, M.1
  • 84
    • 0030871064 scopus 로고    scopus 로고
    • Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity
    • A.A. Soyombo S.L. Hofmann Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity J. Biol. Chem. 272 1997 27456 27463
    • (1997) J. Biol. Chem. , vol.272 , pp. 27456-27463
    • Soyombo, A.A.1    Hofmann, S.L.2
  • 85
    • 0028567924 scopus 로고
    • Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin
    • P. Stanley L.C. Packman V. Koronakis C. Hughes Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin Science 266 1994 1992 1996
    • (1994) Science , vol.266 , pp. 1992-1996
    • Stanley, P.1    Packman, L.C.2    Koronakis, V.3    Hughes, C.4
  • 86
    • 0032480641 scopus 로고    scopus 로고
    • 2H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles
    • 2 H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles Biochemistry 37 1998 15523 15527
    • (1998) Biochemistry , vol.37 , pp. 15523-15527
    • Struppe, J.1    Komives, E.A.2    Taylor, S.S.3    Vold, R.R.4
  • 87
    • 0031990199 scopus 로고    scopus 로고
    • Differential isotope labeling strategy for determining the structure of myristoylated recoverin by NMR spectroscopy
    • T. Tanaka J.B. Ames M. Kainosho L. Stryer M. Ikura Differential isotope labeling strategy for determining the structure of myristoylated recoverin by NMR spectroscopy J. Biomol. NMR 11 1998 135 152
    • (1998) J. Biomol. NMR , vol.11 , pp. 135-152
    • Tanaka, T.1    Ames, J.B.2    Kainosho, M.3    Stryer, L.4    Ikura, M.5
  • 88
    • 0033552652 scopus 로고    scopus 로고
    • Protein myristoylation in protein-lipid and protein-protein interactions
    • H. Taniguchi Protein myristoylation in protein-lipid and protein-protein interactions Biophys. Chem. 82 1999 129 137
    • (1999) Biophys. Chem. , vol.82 , pp. 129-137
    • Taniguchi, H.1
  • 89
    • 0027286171 scopus 로고
    • Microsomal membranes contain a high affinity binding site for prenylated peptides
    • J.A. Thissen P.J. Casey Microsomal membranes contain a high affinity binding site for prenylated peptides J. Biol. Chem. 268 1993 13780 13783
    • (1993) J. Biol. Chem. , vol.268 , pp. 13780-13783
    • Thissen, J.A.1    Casey, P.J.2
  • 90
    • 0030727170 scopus 로고    scopus 로고
    • Prenylation-dependent association of Ki-Ras with microtubules. Evidence for a role in subcellular trafficking
    • J.A. Thissen J.M. Gross K. Subramanian T. Meyer P.J. Casey Prenylation-dependent association of Ki-Ras with microtubules. Evidence for a role in subcellular trafficking J. Biol. Chem. 272 1997 30362 30370
    • (1997) J. Biol. Chem. , vol.272 , pp. 30362-30370
    • Thissen, J.A.1    Gross, J.M.2    Subramanian, K.3    Meyer, T.4    Casey, P.J.5
  • 91
    • 84866476582 scopus 로고    scopus 로고
    • Rapid plasma membrane anchoring of newly synthesized p59fyn. Selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3
    • 2-terminal myristoylation and palmitoylation at cysteine-3 J. Cell Biol. 136 1997 1023 1035
    • (1997) J. Cell Biol. , vol.136 , pp. 1023-1035
    • van't Hof, W.1    Resh, M.D.2
  • 92
    • 0031680028 scopus 로고    scopus 로고
    • Palmitoylation of rhodopsin with S-protein acyltransferase: Enzyme catalyzed reaction versus autocatalytic acylation
    • M. Veit K. Sachs M. Heckelmann D. Maretzki K.P. Hofmann M.F. Schmidt Palmitoylation of rhodopsin with S-protein acyltransferase: Enzyme catalyzed reaction versus autocatalytic acylation Biochim. Biophys. Acta 1394 1999 90 98
    • (1999) Biochim. Biophys. Acta , vol.1394 , pp. 90-98
    • Veit, M.1    Sachs, K.2    Heckelmann, M.3    Maretzki, D.4    Hofmann, K.P.5    Schmidt, M.F.6
  • 93
    • 0029147499 scopus 로고
    • The myristoyl moiety of myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane
    • G. Vergères S. Manenti T. Weber C. Sturzinger The myristoyl moiety of myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane J. Biol. Chem. 270 1995 19879 19887
    • (1995) J. Biol. Chem. , vol.270 , pp. 19879-19887
    • Vergères, G.1    Manenti, S.2    Weber, T.3    Sturzinger, C.4
  • 94
    • 0032502263 scopus 로고    scopus 로고
    • Structure and position of the N-terminal membrane-binding domain of pp60src at the membrane interface
    • src at the membrane interface Biochemistry 37 1998 3402 3410
    • (1998) Biochemistry , vol.37 , pp. 3402-3410
    • Victor, K.1    Cafiso, D.S.2
  • 95
    • 0039182142 scopus 로고    scopus 로고
    • Interactions controlling the membrane binding of basic protein domains: Phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces
    • K. Victor J. Jacob D.S. Cafiso Interactions controlling the membrane binding of basic protein domains: Phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces Biochemistry 38 1999 12527 12536
    • (1999) Biochemistry , vol.38 , pp. 12527-12536
    • Victor, K.1    Jacob, J.2    Cafiso, D.S.3
  • 97
    • 0033869609 scopus 로고    scopus 로고
    • Fluorescence-based evaluation of the partitioning of lipids and lipidated peptides into liquid-ordered lipid microdomains: A model for molecular partitioning into “lipid rafts”
    • T. Wang R. Leventis J.R. Silvius Fluorescence-based evaluation of the partitioning of lipids and lipidated peptides into liquid-ordered lipid microdomains: A model for molecular partitioning into “lipid rafts” Biophys. J. 79 2000 919 933
    • (2000) Biophys. J. , vol.79 , pp. 919-933
    • Wang, T.1    Leventis, R.2    Silvius, J.R.3
  • 98
    • 0035980238 scopus 로고    scopus 로고
    • Partitioning of lipidated peptide sequences into liquid-ordered lipid domains in model and biological membranes
    • T.-Y. Wang R. Leventis J.R. Silvius Partitioning of lipidated peptide sequences into liquid-ordered lipid domains in model and biological membranes Biochemistry 40 2001 13031 13040
    • (2001) Biochemistry , vol.40 , pp. 13031-13040
    • Wang, T.-Y.1    Leventis, R.2    Silvius, J.R.3
  • 99
    • 0034614557 scopus 로고    scopus 로고
    • Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids
    • Y. Webb L. Hermida-Matsumoto M.D. Resh Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids J. Biol. Chem. 275 2000 261 270
    • (2000) J. Biol. Chem. , vol.275 , pp. 261-270
    • Webb, Y.1    Hermida-Matsumoto, L.2    Resh, M.D.3
  • 101
    • 0025132866 scopus 로고
    • Solution phase synthesis of Saccharomyces cerevisiaea-mating factor and its analogs
    • C.B. Xue A. Ewenson J.M. Becker F. Naider Solution phase synthesis of Saccharomyces cerevisiae a -mating factor and its analogs Int. J. Pept. Prot. Res. 36 1990 362 373
    • (1990) Int. J. Pept. Prot. Res. , vol.36 , pp. 362-373
    • Xue, C.B.1    Ewenson, A.2    Becker, J.M.3    Naider, F.4
  • 102
    • 0025893761 scopus 로고
    • Synthesis of S-alkyl and C-terminal analogs of the Saccharomyces cerevisiaea-factor. Influence of temperature on the stability of Fmoc and OFm groups toward HF
    • C.B. Xue J.M. Becker F. Naider Synthesis of S-alkyl and C-terminal analogs of the Saccharomyces cerevisiae a -factor. Influence of temperature on the stability of Fmoc and OFm groups toward HF Int. J. Pept. Prot. Res. 37 1991 476 486
    • (1991) Int. J. Pept. Prot. Res. , vol.37 , pp. 476-486
    • Xue, C.B.1    Becker, J.M.2    Naider, F.3
  • 103
    • 0026554482 scopus 로고
    • Efficient regioselective isoprenylation of peptides in acidic aqueous solution using zinc acetate as catalyst
    • C.B. Xue J. Becker F. Naider Efficient regioselective isoprenylation of peptides in acidic aqueous solution using zinc acetate as catalyst Tetrahedron Lett. 33 1992 1435 1438
    • (1992) Tetrahedron Lett. , vol.33 , pp. 1435-1438
    • Xue, C.B.1    Becker, J.2    Naider, F.3
  • 104
    • 0033230492 scopus 로고    scopus 로고
    • A method for S- and O-palmitoylation of peptides: Synthesis of pulmonary surfactant protein-C models
    • E. Yousefi-Salakdeh J. Johansson R. Stromberg A method for S- and O-palmitoylation of peptides: Synthesis of pulmonary surfactant protein-C models Biochem. J. 343 1999 3557 3562
    • (1999) Biochem. J. , vol.343 , pp. 3557-3562
    • Yousefi-Salakdeh, E.1    Johansson, J.2    Stromberg, R.3
  • 105
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • F.L. Zhang P.J. Casey Protein prenylation: Molecular mechanisms and functional consequences Anna. Rev. Biochem. 65 1996 241 269
    • (1996) Anna. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 106
    • 0030948362 scopus 로고    scopus 로고
    • Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif
    • P. Zlatkine B. Mehul A.I. Magee Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif J. Cell Sci. 110 1997 673 679
    • (1997) J. Cell Sci. , vol.110 , pp. 673-679
    • Zlatkine, P.1    Mehul, B.2    Magee, A.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.