메뉴 건너뛰기




Volumn 41, Issue 2, 2006, Pages 229-241

Mass spectrometric characterization of lipid-modified peptides for the analysis of acylated proteins

Author keywords

Farnesylation; Marker ion; Myristoylation; Neutral loss; Palmitoylation

Indexed keywords

IONIZATION; LASER BEAM EFFECTS; LIPIDS; MASS SPECTROMETERS; PH; PROTEINS;

EID: 32944474517     PISSN: 10765174     EISSN: None     Source Type: Journal    
DOI: 10.1002/jms.981     Document Type: Article
Times cited : (37)

References (45)
  • 1
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M, Jensen ON. Proteomic analysis of post-translational modifications. Nat. Biotechnol. 2003; 21: 255.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255
    • Mann, M.1    Jensen, O.N.2
  • 2
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh MD. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1999; 1451: 1.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1
    • Resh, M.D.1
  • 3
    • 0023198719 scopus 로고
    • Myristoylation of picornavirus capsid protein VP4 and its structural significance
    • Chow M, Newman JFE, Filman D, Hogle JM, Rowlands DJ, Brown F. Myristoylation of picornavirus capsid protein VP4 and its structural significance. Nature 1987; 327: 482.
    • (1987) Nature , vol.327 , pp. 482
    • Chow, M.1    Newman, J.F.E.2    Filman, D.3    Hogle, J.M.4    Rowlands, D.J.5    Brown, F.6
  • 4
    • 0027429591 scopus 로고
    • Crystal structures of the myristoylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformation
    • Zheng J, Knighton DR, Xuong NH, Taylor SS, Sowadski JM, Ten Eyck LF. Crystal structures of the myristoylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformation. Protein Sci. 1993; 2: 1559.
    • (1993) Protein Sci. , vol.2 , pp. 1559
    • Zheng, J.1    Knighton, D.R.2    Xuong, N.H.3    Taylor, S.S.4    Sowadski, J.M.5    Ten Eyck, L.F.6
  • 5
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Gottlinger HG, Sodroski JG, Haseltine WA. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. U.S.A. 1989; 86: 5781.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5781
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 6
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant M, Ratner L. Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc. Natl. Acad. Sci. U.S.A. 1990; 87: 523.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 523
    • Bryant, M.1    Ratner, L.2
  • 7
    • 0024515364 scopus 로고
    • GAG is excluded from virus assembly and mutation events
    • GAG is excluded from virus assembly and mutation events. J. Virol. 1989; 63: 2370.
    • (1989) J. Virol. , vol.63 , pp. 2370
    • Schultz, A.M.1    Rein, A.2
  • 8
    • 0025307422 scopus 로고
    • N-myristoylation of the spleen necrosis virus matrix protein is required for correct association of the gag polyprotein with intracellular membranes and for particle formation
    • Weaver TA, Panganiban AT. N-myristoylation of the spleen necrosis virus matrix protein is required for correct association of the gag polyprotein with intracellular membranes and for particle formation. J. Virol. 1990; 64: 3995.
    • (1990) J. Virol. , vol.64 , pp. 3995
    • Weaver, T.A.1    Panganiban, A.T.2
  • 10
    • 0029861657 scopus 로고    scopus 로고
    • Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
    • Zhou W, Resh MD. Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 1996; 70: 8540.
    • (1996) J. Virol. , vol.70 , pp. 8540
    • Zhou, W.1    Resh, M.D.2
  • 11
    • 0029786317 scopus 로고    scopus 로고
    • Regulation of membrane and subunit interactions by N-myristoylation of a G protein α subunit in yeast
    • Song J, Hirschman J, Gunn K, Dohlman HG. Regulation of membrane and subunit interactions by N-myristoylation of a G protein α subunit in yeast. J. Biol. Chem. 1996; 271: 20273.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20273
    • Song, J.1    Hirschman, J.2    Gunn, K.3    Dohlman, H.G.4
  • 13
    • 0034630098 scopus 로고    scopus 로고
    • Recent advances in the study of prenylated proteins
    • Sinesky M. Recent advances in the study of prenylated proteins. Biochim. Biophys. Acta. 2000; 1484: 93.
    • (2000) Biochim. Biophys. Acta. , vol.1484 , pp. 93
    • Sinesky, M.1
  • 14
    • 0027026591 scopus 로고
    • Protein prenylation: More than just glue?
    • Cox AD, Der CJ. Protein prenylation: more than just glue? Curr. Opin. Cell Biol. 1992; 4: 1008.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 1008
    • Cox, A.D.1    Der, C.J.2
  • 15
    • 0027284950 scopus 로고
    • Protein prenylation: A mediator of protein-protein interactions
    • Marshall CJ. Protein prenylation: a mediator of protein-protein interactions. Science 1993; 259: 1865.
    • (1993) Science , vol.259 , pp. 1865
    • Marshall, C.J.1
  • 16
    • 0034777538 scopus 로고    scopus 로고
    • Protein farnesylation in mammalian cells: Effects of farnesyltransferase inhibitors on cancer cells
    • Tamanoi F, Gau CL, Jiang C, Edamatsu H, Kato-Stankiewicz J. Protein farnesylation in mammalian cells: effects of farnesyltransferase inhibitors on cancer cells. Cell. Mol. Life Sci. 2001; 58: 1636.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1636
    • Tamanoi, F.1    Gau, C.L.2    Jiang, C.3    Edamatsu, H.4    Kato-Stankiewicz, J.5
  • 17
    • 0026747866 scopus 로고
    • Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity
    • Kato K, Cox AD, Hisaka MM, Graham SM, Buss JE, Der CJ. Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 6403.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6403
    • Kato, K.1    Cox, A.D.2    Hisaka, M.M.3    Graham, S.M.4    Buss, J.E.5    Der, C.J.6
  • 19
    • 0034698068 scopus 로고    scopus 로고
    • Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions
    • Williams JG, Drugan JK, Yi GS, Clark GJ, Der CJ, Campbell SL. Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions. J. Biol. Chem. 2000; 275: 22172.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22172
    • Williams, J.G.1    Drugan, J.K.2    Yi, G.S.3    Clark, G.J.4    Der, C.J.5    Campbell, S.L.6
  • 20
    • 0038321812 scopus 로고    scopus 로고
    • New insights into the mechanisms of protein palmitoylation
    • Linder ME, Deschenes RJ. New insights into the mechanisms of protein palmitoylation. Biochemistry 2003; 42: 4311.
    • (2003) Biochemistry , vol.42 , pp. 4311
    • Linder, M.E.1    Deschenes, R.J.2
  • 21
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan G, Parenti M, Magee AI. The dynamic role of palmitoylation in signal transduction. Trends Biochem. Sci. 1995; 20: 181.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 181
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 22
    • 0032497835 scopus 로고    scopus 로고
    • Signalling functions of protein palmitoylation
    • Dunphy JT, Linder ME. Signalling functions of protein palmitoylation. Biochim. Biophys. Acta 1998; 1436: 245.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 245
    • Dunphy, J.T.1    Linder, M.E.2
  • 23
    • 0037213362 scopus 로고    scopus 로고
    • The on - Off story of protein palmitoylation
    • Bijlmakers MJ, Marsh M. The on - off story of protein palmitoylation. Trends Cell Biol. 2003; 13: 32.
    • (2003) Trends Cell Biol. , vol.13 , pp. 32
    • Bijlmakers, M.J.1    Marsh, M.2
  • 24
    • 0029558210 scopus 로고
    • Determination of N-myristoyl peptide sequence both by MALDITOF mass and with an N-myristoyl cleaving enzyme (polymysin acylase)
    • Misumi S, Tsuruta M, Furuishi K, Shoji S. Determination of N-myristoyl peptide sequence both by MALDITOF mass and with an N-myristoyl cleaving enzyme (polymysin acylase). Biochem. Biophys. Res. Commun. 1995; 217: 632.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 632
    • Misumi, S.1    Tsuruta, M.2    Furuishi, K.3    Shoji, S.4
  • 26
    • 0024477082 scopus 로고
    • Myristic acid is the NK2-terminal blocking group of the 43-kDa protein of Torpedo nicotinic post-synaptic membranes
    • Carr SA, Tyler AN, Cohen LB. Myristic acid is the NK2-terminal blocking group of the 43-kDa protein of Torpedo nicotinic post-synaptic membranes. FEBS Lett. 1989; 243: 65.
    • (1989) FEBS Lett. , vol.243 , pp. 65
    • Carr, S.A.1    Tyler, A.N.2    Cohen, L.B.3
  • 27
    • 4644234453 scopus 로고    scopus 로고
    • Mass spectrometry analysis of synthetically myristoylated peptides
    • DOI 10.1255/ejms.652
    • Chen TS, Yoder JD, Hruby DE. Mass spectrometry analysis of synthetically myristoylated peptides. Eur. J. Mass Spectrom. 2004; 10: 501, DOI 10.1255/ejms.652.
    • (2004) Eur. J. Mass Spectrom. , vol.10 , pp. 501
    • Chen, T.S.1    Yoder, J.D.2    Hruby, D.E.3
  • 28
    • 0031081363 scopus 로고    scopus 로고
    • Detection of modified peprides in enzymatic digests by capillary liquid chromatography/electrospray mass spectrometry and a programmable skimmer CID acquisition routine
    • Jedrzejewski PT, Lehmann WD. Detection of modified peprides in enzymatic digests by capillary liquid chromatography/electrospray mass spectrometry and a programmable skimmer CID acquisition routine. Anal. Chem. 1997; 69: 294.
    • (1997) Anal. Chem. , vol.69 , pp. 294
    • Jedrzejewski, P.T.1    Lehmann, W.D.2
  • 29
    • 0024279583 scopus 로고
    • Structure of saaccharomyces cerevisiae mating hormone a-factor - Identification of S-farnesyl cysteine as a structural component
    • Anderegg RJ, Betz R, Carr SA, Crabb JW, Duntze W. Structure of saaccharomyces cerevisiae mating hormone a-factor - identification of S-farnesyl cysteine as a structural component. J. Biol. Chem. 1988; 263: 18236.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18236
    • Anderegg, R.J.1    Betz, R.2    Carr, S.A.3    Crabb, J.W.4    Duntze, W.5
  • 30
    • 12944260584 scopus 로고    scopus 로고
    • Top-down analysis of protein isoprenylation by electrospray ionization hybrid quadrupole time-of-flight tandem mass spectrometry; the mouse Tγ protein
    • DOI: 10.1002/rcm.1782
    • Kassai H, Satomi Y, Fukada Y, Takao T. Top-down analysis of protein isoprenylation by electrospray ionization hybrid quadrupole time-of-flight tandem mass spectrometry; the mouse Tγ protein. Rapid Commun. Mass Spectrom. 2005; 19: 269, DOI: 10.1002/rcm.1782.
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 269
    • Kassai, H.1    Satomi, Y.2    Fukada, Y.3    Takao, T.4
  • 31
    • 0033605680 scopus 로고    scopus 로고
    • Correlations in palmitoylation and multiple phosphorylation of rat bradykinin B2 receptor in Chinese hamster ovary cells
    • Soskic V, Nyakatura E, Roos M, Muller-Esterl W, Godovac-Zimmermann J. Correlations in palmitoylation and multiple phosphorylation of rat bradykinin B2 receptor in Chinese hamster ovary cells. J. Biol. Chem. 1999; 26: 8539.
    • (1999) J. Biol. Chem. , vol.26 , pp. 8539
    • Soskic, V.1    Nyakatura, E.2    Roos, M.3    Muller-Esterl, W.4    Godovac-Zimmermann, J.5
  • 32
    • 0037450538 scopus 로고    scopus 로고
    • Galpha(s) is palmitoylated at the N-terminal glycine
    • Kleuss C, Krause E. Galpha(s) is palmitoylated at the N-terminal glycine. EMBO J. 2003; 22: 826.
    • (2003) EMBO J. , vol.22 , pp. 826
    • Kleuss, C.1    Krause, E.2
  • 33
    • 0035046806 scopus 로고    scopus 로고
    • Mass spectrometric analysis of recombinant adenylate cyclase toxin from Bordetella pertussis strain 18323/pHSP9
    • Havlicek V, Higgins L, Chen W, Halada P, Sebo P, Sakamoto H, Hackett M. Mass spectrometric analysis of recombinant adenylate cyclase toxin from Bordetella pertussis strain 18323/pHSP9. J. Mass Spectrom. 2001; 36: 384.
    • (2001) J. Mass Spectrom. , vol.36 , pp. 384
    • Havlicek, V.1    Higgins, L.2    Chen, W.3    Halada, P.4    Sebo, P.5    Sakamoto, H.6    Hackett, M.7
  • 35
    • 0022476767 scopus 로고
    • Protein fatty acid acylation: Enzymatic synthesis of an N-myristoylglycyl peptide
    • Towler D, Glaser L. Protein fatty acid acylation: enzymatic synthesis of an N-myristoylglycyl peptide. Proc. Natl. Acad. Sci. U.S.A. 1986; 83: 2812.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 2812
    • Towler, D.1    Glaser, L.2
  • 36
    • 0033230492 scopus 로고    scopus 로고
    • Method for S- and O-palmitoylation of peptides: Synthesis of pulmonary surfactant protein-C models
    • Yousefi-Salakdeh E, Johansson J, Stromberg R. A method for S- and O-palmitoylation of peptides: synthesis of pulmonary surfactant protein-C models. Biochem. J. 1999; 343: 557.
    • (1999) Biochem. J. , vol.343 , pp. 557
    • Yousefi-Salakdeh, E.1    Johansson, J.2    Stromberg, R.A.3
  • 38
    • 0030612440 scopus 로고    scopus 로고
    • Synthesis of prenylated peptides and peptide esters
    • Naider FR, Becker JM. Synthesis of prenylated peptides and peptide esters. Biopolymers 1997; 43: 3.
    • (1997) Biopolymers , vol.43 , pp. 3
    • Naider, F.R.1    Becker, J.M.2
  • 39
    • 0034506737 scopus 로고    scopus 로고
    • Five-membered ring formation in unimolecular reactions of peptides: A key structural element controlling low-energy collision-induced dissociation of peptides
    • Schlosser A, Lehmann WD. Five-membered ring formation in unimolecular reactions of peptides: a key structural element controlling low-energy collision-induced dissociation of peptides. J. Mess Spectrom. 2000; 35: 1382.
    • (2000) J. Mess Spectrom. , vol.35 , pp. 1382
    • Schlosser, A.1    Lehmann, W.D.2
  • 40
    • 0027461675 scopus 로고
    • Tandem mass spectrometry of very large molecules. 2. Dissociation of multiply charged proline-containing proteins from electrospray ionization
    • Loo JA, Edmonds CG, Smith RD. Tandem mass spectrometry of very large molecules. 2. Dissociation of multiply charged proline-containing proteins from electrospray ionization. Anal. Chem. 1993; 65: 425.
    • (1993) Anal. Chem. , vol.65 , pp. 425
    • Loo, J.A.1    Edmonds, C.G.2    Smith, R.D.3
  • 42
    • 0031837553 scopus 로고    scopus 로고
    • Gas-phase fragmentation of protonated Mono-N-methylated peptides. Analogy with solution-phase acid-catalyzed hydrolysis
    • Vaisar T, Urban J. Gas-phase fragmentation of protonated Mono-N-methylated peptides. Analogy with solution-phase acid-catalyzed hydrolysis. J. Mass Spectrom. 1998; 33: 505.
    • (1998) J. Mass Spectrom. , vol.33 , pp. 505
    • Vaisar, T.1    Urban, J.2
  • 43
    • 84913106998 scopus 로고
    • McLafferty FW (ed). Academic Press: New York
    • Reed RI. In Mass Spectrometry of Organic Ions, McLafferty FW (ed). Academic Press: New York, 1983; 637.
    • (1983) Mass Spectrometry of Organic Ions , pp. 637
    • Reed, R.I.1
  • 45
    • 0032792042 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometric method for the determination of cannabinoid precursors: N-acetylethanolamine phospholipids (NAPEs)
    • Hansen HH, Hansen SH, Bjørnsdottir I, Hansen HS. Electrospray ionization mass spectrometric method for the determination of cannabinoid precursors: N-acetylethanolamine phospholipids (NAPEs). J. Mass Spectrom. 1999; 34: 761.
    • (1999) J. Mass Spectrom. , vol.34 , pp. 761
    • Hansen, H.H.1    Hansen, S.H.2    Bjørnsdottir, I.3    Hansen, H.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.