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Volumn 8, Issue 6, 2013, Pages

Cellular FRET-Biosensors to Detect Membrane Targeting Inhibitors of N-Myristoylated Proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANISOMYCIN; CURVULARIN; CYTOSPORONE B; DDD 85646; FLAGRANONE A; FUMAGILLIN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; INTEGRACIN A; LACTONE DERIVATIVE; PROTEIN KINASE YES; PROTEIN N MYRISTOYLTRANSFERASE INHIBITOR; PROTEIN TYROSINE KINASE; PSEUDOMONIC ACID; REVEROMYCIN A; REVEROMYCIN B; TETRADECANOYL LEVO HOMOSERINE LACTONE; UNCLASSIFIED DRUG; MEMBRANE PROTEIN; MYRISTIC ACID;

EID: 84879152912     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0066425     Document Type: Article
Times cited : (24)

References (58)
  • 1
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • 10.1038/nchembio834
    • Resh MD, (2006) Trafficking and signaling by fatty-acylated and prenylated proteins. Nat Chem Biol 2: 584-590 doi:10.1038/nchembio834.
    • (2006) Nat Chem Biol , vol.2 , pp. 584-590
    • Resh, M.D.1
  • 2
    • 0034722890 scopus 로고    scopus 로고
    • Farnesyltransferase and geranylgeranyltransferase I inhibitors and cancer therapy: lessons from mechanism and bench-to-bedside translational studies
    • 10.1038/sj.onc.1204146
    • Sebti SM, Hamilton AD, (2000) Farnesyltransferase and geranylgeranyltransferase I inhibitors and cancer therapy: lessons from mechanism and bench-to-bedside translational studies. Oncogene 19: 6584-6593 doi:10.1038/sj.onc.1204146.
    • (2000) Oncogene , vol.19 , pp. 6584-6593
    • Sebti, S.M.1    Hamilton, A.D.2
  • 3
    • 0345073644 scopus 로고    scopus 로고
    • Protein farnesyl and N-myristoyl transferases: piggy-back medicinal chemistry targets for the development of antitrypanosomatid and antimalarial therapeutics
    • 10.1016/S0166-6851(02)00282-7
    • Gelb MH, Van Voorhis WC, Buckner FS, Yokoyama K, Eastman R, et al. (2003) Protein farnesyl and N-myristoyl transferases: piggy-back medicinal chemistry targets for the development of antitrypanosomatid and antimalarial therapeutics. Mol Biochem Parasitol 126: 155-163 doi:10.1016/S0166-6851(02)00282-7.
    • (2003) Mol Biochem Parasitol , vol.126 , pp. 155-163
    • Gelb, M.H.1    Van Voorhis, W.C.2    Buckner, F.S.3    Yokoyama, K.4    Eastman, R.5
  • 5
    • 38949093546 scopus 로고    scopus 로고
    • Inhibitors of chronically active ras: potential for treatment of human malignancies
    • 10.2174/157489208783478702
    • Blum R, Cox AD, Kloog Y, (2008) Inhibitors of chronically active ras: potential for treatment of human malignancies. Recent patents on anti-cancer drug discovery 3: 31-47 doi:10.2174/157489208783478702.
    • (2008) Recent Patents on Anti-Cancer Drug Discovery , vol.3 , pp. 31-47
    • Blum, R.1    Cox, A.D.2    Kloog, Y.3
  • 6
    • 0021285532 scopus 로고
    • A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation
    • 10.1128/MCB.4.9.1834
    • Cross FR, Garber EA, Pellman D, Hanafusa H, (1984) A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Mol Cell Biol 4: 1834-1842 doi:10.1128/MCB.4.9.1834.
    • (1984) Mol Cell Biol , vol.4 , pp. 1834-1842
    • Cross, F.R.1    Garber, E.A.2    Pellman, D.3    Hanafusa, H.4
  • 7
    • 0022398521 scopus 로고
    • Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation
    • Kamps MP, Buss JE, Sefton BM, (1985) Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation. Proc Natl Acad Sci USA 82: 4625-4628.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4625-4628
    • Kamps, M.P.1    Buss, J.E.2    Sefton, B.M.3
  • 8
    • 0021170342 scopus 로고
    • The p21 ras C-terminus is required for transformation and membrane association
    • 10.1038/310583a0
    • Willumsen BM, Christensen A, Hubbert NL, Papageorge AG, Lowy DR, (1984) The p21 ras C-terminus is required for transformation and membrane association. Nature 310: 583-586 doi:10.1038/310583a0.
    • (1984) Nature , vol.310 , pp. 583-586
    • Willumsen, B.M.1    Christensen, A.2    Hubbert, N.L.3    Papageorge, A.G.4    Lowy, D.R.5
  • 9
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • 10.1016/0092-8674(89)90054-8
    • Hancock JF, Magee AI, Childs JE, Marshall CJ, (1989) All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57: 1167-1177 doi:10.1016/0092-8674(89)90054-8.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 10
    • 35648980477 scopus 로고    scopus 로고
    • Ras nanoclusters: molecular structure and assembly
    • 10.1016/j.semcdb.2007.08.003
    • Abankwa D, Gorfe AA, Hancock JF, (2007) Ras nanoclusters: molecular structure and assembly. Semin Cell Dev Biol 18: 599-607 doi:10.1016/j.semcdb.2007.08.003.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 599-607
    • Abankwa, D.1    Gorfe, A.A.2    Hancock, J.F.3
  • 11
    • 0035067187 scopus 로고    scopus 로고
    • GTP-dependent segregation of H-ras from lipid rafts is required for biological activity
    • 10.1038/35070050
    • Prior IA, Harding A, Yan J, Sluimer J, Parton RG, et al. (2001) GTP-dependent segregation of H-ras from lipid rafts is required for biological activity. Nat Cell Biol 3: 368-375 doi:10.1038/35070050.
    • (2001) Nat Cell Biol , vol.3 , pp. 368-375
    • Prior, I.A.1    Harding, A.2    Yan, J.3    Sluimer, J.4    Parton, R.G.5
  • 12
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • 10.1073/pnas.0504114102
    • Plowman SJ, Muncke C, Parton RG, Hancock JF, (2005) H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc Natl Acad Sci U S A 102: 15500-15505 doi:10.1073/pnas.0504114102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 13
    • 34547561587 scopus 로고    scopus 로고
    • Plasma membrane nanoswitches generate high-fidelity Ras signal transduction
    • 10.1038/ncb1615
    • Tian T, Harding A, Inder K, Plowman S, Parton RG, et al. (2007) Plasma membrane nanoswitches generate high-fidelity Ras signal transduction. Nat Cell Biol 9: 905-914 doi:10.1038/ncb1615.
    • (2007) Nat Cell Biol , vol.9 , pp. 905-914
    • Tian, T.1    Harding, A.2    Inder, K.3    Plowman, S.4    Parton, R.G.5
  • 14
    • 84867555260 scopus 로고    scopus 로고
    • Formation and Domain Partitioning of H-ras Peptide Nanoclusters: Effects of Peptide Concentration and Lipid Composition
    • 10.1021/ja307716z
    • Li Z, Janosi L, Gorfe AA, (2012) Formation and Domain Partitioning of H-ras Peptide Nanoclusters: Effects of Peptide Concentration and Lipid Composition. J Am Chem Soc: 17 134(41): 17278-85 doi:10.1021/ja307716z.
    • (2012) J Am Chem Soc: 17 , vol.134 , Issue.41 , pp. 17278-17285
    • Li, Z.1    Janosi, L.2    Gorfe, A.A.3
  • 15
    • 84861438588 scopus 로고    scopus 로고
    • Organization, dynamics, and segregation of Ras nanoclusters in membrane domains
    • 10.1073/pnas.1200773109
    • Janosi L, Li Z, Hancock JF, Gorfe AA, (2012) Organization, dynamics, and segregation of Ras nanoclusters in membrane domains. Proc Natl Acad Sci U S A 109: 8097-8102 doi:10.1073/pnas.1200773109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 8097-8102
    • Janosi, L.1    Li, Z.2    Hancock, J.F.3    Gorfe, A.A.4
  • 16
    • 34548561606 scopus 로고    scopus 로고
    • A FRET map of membrane anchors suggests distinct microdomains of heterotrimeric G proteins
    • 10.1242/jcs.001404
    • Abankwa D, Vogel H, (2007) A FRET map of membrane anchors suggests distinct microdomains of heterotrimeric G proteins. J Cell Sci 120: 2953-2962 doi:10.1242/jcs.001404.
    • (2007) J Cell Sci , vol.120 , pp. 2953-2962
    • Abankwa, D.1    Vogel, H.2
  • 17
    • 84864408572 scopus 로고    scopus 로고
    • Design and Application of In Vivo FRET Biosensors to Identify Protein Prenylation and Nanoclustering Inhibitors
    • 10.1016/j.chembiol.2012.05.019
    • Köhnke M, Schmitt S, Ariotti N, Piggott AM, Parton RG, et al. (2012) Design and Application of In Vivo FRET Biosensors to Identify Protein Prenylation and Nanoclustering Inhibitors. Chemistry & Biology 19: 866-874 doi:10.1016/j.chembiol.2012.05.019.
    • (2012) Chemistry & Biology , vol.19 , pp. 866-874
    • Köhnke, M.1    Schmitt, S.2    Ariotti, N.3    Piggott, A.M.4    Parton, R.G.5
  • 18
    • 57149125825 scopus 로고    scopus 로고
    • Nanoclusters of GPI-anchored proteins are formed by cortical actin-driven activity
    • 10.1016/j.cell.2008.11.032
    • Goswami D, Gowrishankar K, Bilgrami S, Ghosh S, Raghupathy R, et al. (2008) Nanoclusters of GPI-anchored proteins are formed by cortical actin-driven activity. Cell 135: 1085-1097 doi:10.1016/j.cell.2008.11.032.
    • (2008) Cell , vol.135 , pp. 1085-1097
    • Goswami, D.1    Gowrishankar, K.2    Bilgrami, S.3    Ghosh, S.4    Raghupathy, R.5
  • 19
    • 40949130399 scopus 로고    scopus 로고
    • A novel switch region regulates H-ras membrane orientation and signal output
    • 10.1038/emboj.2008.10
    • Abankwa D, Hanzal-Bayer MF, Ariotti N, Plowman SJ, Gorfe AA, et al. (2008) A novel switch region regulates H-ras membrane orientation and signal output. EMBO J 27: 727-735 doi:10.1038/emboj.2008.10.
    • (2008) EMBO J , vol.27 , pp. 727-735
    • Abankwa, D.1    Hanzal-Bayer, M.F.2    Ariotti, N.3    Plowman, S.J.4    Gorfe, A.A.5
  • 20
    • 80054866000 scopus 로고    scopus 로고
    • Targeting protein prenylation for cancer therapy
    • 10.1038/nrc3151
    • Berndt N, Hamilton AD, Sebti SM, (2011) Targeting protein prenylation for cancer therapy. Nat Rev Cancer 11: 775-791 doi:10.1038/nrc3151.
    • (2011) Nat Rev Cancer , vol.11 , pp. 775-791
    • Berndt, N.1    Hamilton, A.D.2    Sebti, S.M.3
  • 21
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • 10.1016/S0167-4889(99)00075-0
    • Resh M, (1999) Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochimica et Biophysica Acta (BBA)- Molecular Cell Research 1451: 1-16 doi:10.1016/S0167-4889(99)00075-0.
    • (1999) Biochimica Et Biophysica Acta (BBA) - Molecular Cell Research , vol.1451 , pp. 1-16
    • Resh, M.1
  • 22
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristoylation
    • 10.1074/jbc.R100042200
    • Farazi TA, Waksman G, Gordon JI, (2001) The biology and enzymology of protein N-myristoylation. J Biol Chem 276: 39501-39504 doi:10.1074/jbc.R100042200.
    • (2001) J Biol Chem , vol.276 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 23
    • 0036295384 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: refinement of the sequence motif and its taxon-specific differences
    • 10.1006/jmbi.2002.5425
    • Maurer-Stroh S, Eisenhaber B, Eisenhaber F, (2002) N-terminal N-myristoylation of proteins: refinement of the sequence motif and its taxon-specific differences. J Mol Biol 317: 523-540 doi:10.1006/jmbi.2002.5425.
    • (2002) J Mol Biol , vol.317 , pp. 523-540
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 24
    • 0037470198 scopus 로고    scopus 로고
    • Myristoyl-CoA: protein N-myristoyltransferase, an essential enzyme and potential drug target in kinetoplastid parasites
    • 10.1074/jbc.M211391200
    • Price HP, Menon MR, Panethymitaki C, Goulding D, McKean PG, et al. (2003) Myristoyl-CoA: protein N-myristoyltransferase, an essential enzyme and potential drug target in kinetoplastid parasites. J Biol Chem 278: 7206-7214 doi:10.1074/jbc.M211391200.
    • (2003) J Biol Chem , vol.278 , pp. 7206-7214
    • Price, H.P.1    Menon, M.R.2    Panethymitaki, C.3    Goulding, D.4    McKean, P.G.5
  • 25
    • 0036290648 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: prediction of substrate proteins from amino acid sequence
    • 10.1006/jmbi.2002.5426
    • Maurer-Stroh S, Eisenhaber B, Eisenhaber F, (2002) N-terminal N-myristoylation of proteins: prediction of substrate proteins from amino acid sequence. J Mol Biol 317: 541-557 doi:10.1006/jmbi.2002.5426.
    • (2002) J Mol Biol , vol.317 , pp. 541-557
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 26
    • 21444459919 scopus 로고    scopus 로고
    • N-myristoyltransferase 1 is essential in early mouse development
    • 10.1074/jbc.M412917200
    • Yang SH, Shrivastav A, Kosinski C, Sharma RK, Chen M-H, et al. (2005) N-myristoyltransferase 1 is essential in early mouse development. J Biol Chem 280: 18990-18995 doi:10.1074/jbc.M412917200.
    • (2005) J Biol Chem , vol.280 , pp. 18990-18995
    • Yang, S.H.1    Shrivastav, A.2    Kosinski, C.3    Sharma, R.K.4    Chen, M.-H.5
  • 27
    • 0032549571 scopus 로고    scopus 로고
    • A Second Mammalian N-Myristoyltransferase
    • 10.1074/jbc.273.12.6595
    • Giang DK, Cravatt BF, (1998) A Second Mammalian N-Myristoyltransferase. J Biol Chem 273: 6595-6598 doi:10.1074/jbc.273.12.6595.
    • (1998) J Biol Chem , vol.273 , pp. 6595-6598
    • Giang, D.K.1    Cravatt, B.F.2
  • 28
    • 0027276545 scopus 로고
    • A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase
    • Rocque WJ, McWherter CA, Wood DC, Gordon JI, (1993) A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase. J Biol Chem 268: 9964-9971.
    • (1993) J Biol Chem , vol.268 , pp. 9964-9971
    • Rocque, W.J.1    McWherter, C.A.2    Wood, D.C.3    Gordon, J.I.4
  • 29
    • 0031752275 scopus 로고    scopus 로고
    • Lipid modifications and membrane targeting of G alpha
    • 10.1159/000014538
    • Wedegaertner PB, (1998) Lipid modifications and membrane targeting of G alpha. Biol Signals Recept 7: 125-135 doi: 10.1159/000014538.
    • (1998) Biol Signals Recept , vol.7 , pp. 125-135
    • Wedegaertner, P.B.1
  • 30
    • 20144375061 scopus 로고    scopus 로고
    • An acylation cycle regulates localization and activity of palmitoylated Ras isoforms
    • 10.1126/science.1105654
    • Rocks O, Peyker A, Kahms M, Verveer PJ, Koerner C, et al. (2005) An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science 307: 1746-1752 doi:10.1126/science.1105654.
    • (2005) Science , vol.307 , pp. 1746-1752
    • Rocks, O.1    Peyker, A.2    Kahms, M.3    Verveer, P.J.4    Koerner, C.5
  • 31
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: the fats of the matter
    • 10.1016/0092-8674(94)90104-X
    • Resh MD, (1994) Myristylation and palmitylation of Src family members: the fats of the matter. Cell 76: 411-413 doi: -10.1016/0092-8674(94)90104-X.
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 32
    • 24144464240 scopus 로고    scopus 로고
    • Two N-myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis
    • 10.1158/1541-7786.MCR-05-0037
    • Ducker CE, Upson JJ, French KJ, Smith CD, (2005) Two N-myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis. Mol Cancer Res 3: 463-476 doi:10.1158/1541-7786.MCR-05-0037.
    • (2005) Mol Cancer Res , vol.3 , pp. 463-476
    • Ducker, C.E.1    Upson, J.J.2    French, K.J.3    Smith, C.D.4
  • 33
    • 14944374011 scopus 로고    scopus 로고
    • Functional analysis of TbARL1, an N-myristoylated Golgi protein essential for viability in bloodstream trypanosomes
    • 10.1242/jcs.01624
    • Price HP, (2005) Functional analysis of TbARL1, an N-myristoylated Golgi protein essential for viability in bloodstream trypanosomes. J Cell Sci 118: 831-841 doi:10.1242/jcs.01624.
    • (2005) J Cell Sci , vol.118 , pp. 831-841
    • Price, H.P.1
  • 34
    • 1642340046 scopus 로고    scopus 로고
    • Myristoylation of viral and bacterial proteins
    • 10.1016/j.tim.2004.02.006
    • Maurer-Stroh S, Eisenhaber F, (2004) Myristoylation of viral and bacterial proteins. Trends Microbiol 12: 178-185 doi:10.1016/j.tim.2004.02.006.
    • (2004) Trends Microbiol , vol.12 , pp. 178-185
    • Maurer-Stroh, S.1    Eisenhaber, F.2
  • 35
    • 33845310513 scopus 로고    scopus 로고
    • Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression
    • 10.1073/pnas.0608389103
    • Hu X, Addlagatta A, Lu J, Matthews BW, Liu JO, (2006) Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proceedings of the National Academy of Sciences 103: 18148-18153 doi:10.1073/pnas.0608389103.
    • (2006) Proceedings of the National Academy of Sciences , vol.103 , pp. 18148-18153
    • Hu, X.1    Addlagatta, A.2    Lu, J.3    Matthews, B.W.4    Liu, J.O.5
  • 36
    • 34447547502 scopus 로고    scopus 로고
    • Regulation of c-Src Nonreceptor Tyrosine Kinase Activity by Bengamide A through Inhibition of Methionine Aminopeptidases
    • 10.1016/j.chembiol.2007.05.010
    • Hu X, Dang Y, Tenney K, Crews P, Tsai CW, et al. (2007) Regulation of c-Src Nonreceptor Tyrosine Kinase Activity by Bengamide A through Inhibition of Methionine Aminopeptidases. Chemistry & Biology 14: 764-774 doi:10.1016/j.chembiol.2007.05.010.
    • (2007) Chemistry & Biology , vol.14 , pp. 764-774
    • Hu, X.1    Dang, Y.2    Tenney, K.3    Crews, P.4    Tsai, C.W.5
  • 37
    • 0031171961 scopus 로고    scopus 로고
    • Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin
    • 10.1016/S1074-5521(97)90198-8
    • Griffith EC, Su Z, Turk BE, Chen S, Chang YH, et al. (1997) Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin. Chemistry & Biology 4: 461-471 doi:10.1016/S1074-5521(97)90198-8.
    • (1997) Chemistry & Biology , vol.4 , pp. 461-471
    • Griffith, E.C.1    Su, Z.2    Turk, B.E.3    Chen, S.4    Chang, Y.H.5
  • 38
    • 53249101817 scopus 로고    scopus 로고
    • Tris (dibenzylideneacetone) dipalladium, a N-myristoyltransferase-1 inhibitor, is effective against melanoma growth in vitro and in vivo
    • 10.1158/1078-0432.CCR-08-0405
    • Bhandarkar SS, Bromberg J, Carrillo C, Selvakumar P, Sharma RK, et al. (2008) Tris (dibenzylideneacetone) dipalladium, a N-myristoyltransferase-1 inhibitor, is effective against melanoma growth in vitro and in vivo. Clin Cancer Res 14: 5743-5748 doi:10.1158/1078-0432.CCR-08-0405.
    • (2008) Clin Cancer Res , vol.14 , pp. 5743-5748
    • Bhandarkar, S.S.1    Bromberg, J.2    Carrillo, C.3    Selvakumar, P.4    Sharma, R.K.5
  • 39
    • 77950406212 scopus 로고    scopus 로고
    • N-myristoyltransferase inhibitors as new leads to treat sleeping sickness
    • 10.1038/nature08893
    • Frearson JA, Brand S, Mcelroy SP, Cleghorn LAT, Smid O, et al. (2010) N-myristoyltransferase inhibitors as new leads to treat sleeping sickness. Nature 464: 728-732 doi:10.1038/nature08893.
    • (2010) Nature , vol.464 , pp. 728-732
    • Frearson, J.A.1    Brand, S.2    Mcelroy, S.P.3    Cleghorn, L.A.T.4    Smid, O.5
  • 40
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: policing protein stability and traffic
    • 10.1038/nrm2084
    • Linder ME, Deschenes RJ, (2007) Palmitoylation: policing protein stability and traffic. Nat Rev Mol Cell Biol 8: 74-84 doi: 10.1038/nrm2084.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 41
    • 77249134163 scopus 로고    scopus 로고
    • Protein palmitoylation in neuronal development and synaptic plasticity
    • 10.1038/nrn2788
    • Fukata Y, Fukata M, (2010) Protein palmitoylation in neuronal development and synaptic plasticity. Nat Rev Neurosci 11: 161-175 doi:10.1038/nrn2788.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 161-175
    • Fukata, Y.1    Fukata, M.2
  • 42
    • 0034614557 scopus 로고    scopus 로고
    • Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids
    • 10.1074/jbc.275.1.261
    • Webb Y, Hermida-Matsumoto L, Resh MD, (2000) Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids. J Biol Chem 275: 261-270 doi: 10.1074/jbc.275.1.261.
    • (2000) J Biol Chem , vol.275 , pp. 261-270
    • Webb, Y.1    Hermida-Matsumoto, L.2    Resh, M.D.3
  • 43
    • 61449170090 scopus 로고    scopus 로고
    • Palmitoyl acyltransferase assays and inhibitors (Review)
    • 10.1080/09687680802683839
    • Draper JM, Smith CD, (2009) Palmitoyl acyltransferase assays and inhibitors (Review). Mol Membr Biol 26: 5-13 doi:10.1080/09687680802683839.
    • (2009) Mol Membr Biol , vol.26 , pp. 5-13
    • Draper, J.M.1    Smith, C.D.2
  • 44
    • 77952541156 scopus 로고    scopus 로고
    • Small-molecule inhibition of APT1 affects Ras localization and signaling
    • 10.1038/nchembio.362
    • Dekker FJ, Rocks O, Vartak N, Menninger S, Hedberg C, et al. (2010) Small-molecule inhibition of APT1 affects Ras localization and signaling. Nat Chem Biol 6: 449-456 doi:10.1038/nchembio.362.
    • (2010) Nat Chem Biol , vol.6 , pp. 449-456
    • Dekker, F.J.1    Rocks, O.2    Vartak, N.3    Menninger, S.4    Hedberg, C.5
  • 45
    • 80053929889 scopus 로고    scopus 로고
    • Development of Highly Potent Inhibitors of the Ras-Targeting Human Acyl Protein Thioesterases Based on Substrate Similarity Design. Angew Chem Int Ed Engl
    • 10.1002/anie.201102965
    • Hedberg C, Dekker FJ, Rusch M, Renner S, Wetzel S, et al. (2011) Development of Highly Potent Inhibitors of the Ras-Targeting Human Acyl Protein Thioesterases Based on Substrate Similarity Design. Angew Chem Int Ed Engl. 50: 9832-9837 doi:10.1002/anie.201102965.
    • (2011) , vol.50 , pp. 9832-9837
    • Hedberg, C.1    Dekker, F.J.2    Rusch, M.3    Renner, S.4    Wetzel, S.5
  • 46
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: a quantitative comparison
    • 10.1016/S0006-3495(03)75126-1
    • Berney C, Danuser G, (2003) FRET or no FRET: a quantitative comparison. Biophys J 84: 3992-4010 doi:-10.1016/S0006-3495(03)75126-1.
    • (2003) Biophys J , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 47
    • 0035831239 scopus 로고    scopus 로고
    • Bengamides revisited: new structures and antitumor studies
    • 10.1021/jo001380
    • Thale Z, Kinder FR, Bair KW, Bontempo J, Czuchta AM, et al. (2001) Bengamides revisited: new structures and antitumor studies. J Org Chem 66: 1733-1741 doi: 10.1021/jo001380.
    • (2001) J Org Chem , vol.66 , pp. 1733-1741
    • Thale, Z.1    Kinder, F.R.2    Bair, K.W.3    Bontempo, J.4    Czuchta, A.M.5
  • 48
    • 0035950061 scopus 로고    scopus 로고
    • Synthesis and Antitumor Activity of Ester-Modified Analogues of Bengamide B. J Med Chem
    • 10.1021/jm010188c
    • Kinder FR, Versace RW, Bair KW, Bontempo JM, Cesarz D, et al. (2001) Synthesis and Antitumor Activity of Ester-Modified Analogues of Bengamide B. J Med Chem. 44: 3692-3699 doi:10.1021/jm010188c.
    • (2001) , vol.44 , pp. 3692-3699
    • Kinder, F.R.1    Versace, R.W.2    Bair, K.W.3    Bontempo, J.M.4    Cesarz, D.5
  • 49
    • 0035829731 scopus 로고    scopus 로고
    • Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation
    • 10.1038/sj.onc.1204950
    • Paz A, Haklai R, Elad-Sfadia G, Ballan E, Kloog Y, (2001) Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation. Oncogene 20: 7486-7493 doi:10.1038/sj.onc.1204950.
    • (2001) Oncogene , vol.20 , pp. 7486-7493
    • Paz, A.1    Haklai, R.2    Elad-Sfadia, G.3    Ballan, E.4    Kloog, Y.5
  • 50
    • 44949124597 scopus 로고    scopus 로고
    • Galectin-1 is a novel structural component and a major regulator of h-ras nanoclusters
    • 10.1091/mbc.E07-10-1053
    • Belanis L, Plowman SJ, Rotblat B, Hancock JF, Kloog Y, (2008) Galectin-1 is a novel structural component and a major regulator of h-ras nanoclusters. Mol Biol Cell 19: 1404-1414 doi:10.1091/mbc.E07-10-1053.
    • (2008) Mol Biol Cell , vol.19 , pp. 1404-1414
    • Belanis, L.1    Plowman, S.J.2    Rotblat, B.3    Hancock, J.F.4    Kloog, Y.5
  • 51
    • 84876019965 scopus 로고    scopus 로고
    • Spatial partitioning improves the reliability of biochemical signaling
    • 10.1073/pnas.1218301110
    • Mugler A, Tostevin F, Wolde PRT, (2013) Spatial partitioning improves the reliability of biochemical signaling. Proceedings of the National Academy of Sciences 15: 5927-5932 doi:10.1073/pnas.1218301110.
    • (2013) Proceedings of the National Academy of Sciences , vol.15 , pp. 5927-5932
    • Mugler, A.1    Tostevin, F.2    Wolde, P.R.T.3
  • 52
    • 77956514977 scopus 로고    scopus 로고
    • The plasma membrane of bloodstream-form African trypanosomes confers susceptibility and specificity to killing by hydrophobic peptides
    • 10.1074/jbc.M110.151886
    • Harrington JM, Widener J, Stephens N, Johnson T, Francia M, et al. (2010) The plasma membrane of bloodstream-form African trypanosomes confers susceptibility and specificity to killing by hydrophobic peptides. Journal of Biological Chemistry 285: 28659-28666 doi:10.1074/jbc.M110.151886.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 28659-28666
    • Harrington, J.M.1    Widener, J.2    Stephens, N.3    Johnson, T.4    Francia, M.5
  • 53
    • 84855879725 scopus 로고    scopus 로고
    • A fluorescence-based assay for N-myristoyltransferase activity. Anal Biochem
    • 10.1016/j.ab.2011.10.013
    • Goncalves V, Brannigan JA, Thinon E, Olaleye TO, Serwa R, et al. (2011) A fluorescence-based assay for N-myristoyltransferase activity. Anal Biochem. 421: 342-344 doi:10.1016/j.ab.2011.10.013.
    • (2011) , vol.421 , pp. 342-344
    • Goncalves, V.1    Brannigan, J.A.2    Thinon, E.3    Olaleye, T.O.4    Serwa, R.5
  • 54
    • 84867365063 scopus 로고    scopus 로고
    • A new, robust, and nonradioactive approach for exploring N-myristoylation
    • 10.1194/jlr.D026997
    • Rampoldi F, Sandhoff R, Owen RW, Grone H-J, Porubsky S, (2012) A new, robust, and nonradioactive approach for exploring N-myristoylation. J Lipid Res 53: 2459-2468 doi:10.1194/jlr.D026997.
    • (2012) J Lipid Res , vol.53 , pp. 2459-2468
    • Rampoldi, F.1    Sandhoff, R.2    Owen, R.W.3    Grone, H.-J.4    Porubsky, S.5
  • 55
    • 84862520770 scopus 로고    scopus 로고
    • Fiji: an open-source platform for biological-image analysis
    • 10.1038/nmeth.2019
    • Schindelin J, Arganda-Carreras I, Frise E, Kaynig V, Longair M, et al. (2012) Fiji: an open-source platform for biological-image analysis. Nat Meth 9: 676-682 doi:10.1038/nmeth.2019.
    • (2012) Nat Meth , vol.9 , pp. 676-682
    • Schindelin, J.1    Arganda-Carreras, I.2    Frise, E.3    Kaynig, V.4    Longair, M.5
  • 56
    • 0035959942 scopus 로고    scopus 로고
    • Preassociation of calmodulin with voltage-gated Ca2+ channels revealed by FRET in single living cells
    • 10.1016/S0896-6273(01)00438-X
    • Erickson M, Alseikhan B, Peterson B, Yue D, (2001) Preassociation of calmodulin with voltage-gated Ca2+ channels revealed by FRET in single living cells. Neuron 31: 973-985 doi:10.1016/S0896-6273(01)00438-X.
    • (2001) Neuron , vol.31 , pp. 973-985
    • Erickson, M.1    Alseikhan, B.2    Peterson, B.3    Yue, D.4
  • 57
    • 84871604254 scopus 로고    scopus 로고
    • The effects of transmembrane sequence and dimerization on cleavage of the p75 neurotrophin receptor by γ-secretase. Journal of Biological Chemistry
    • 10.1074/jbc.M112.382903
    • Sykes AM, Palstra N, Abankwa D, Hill JM, Skeldal S, et al. (2012) The effects of transmembrane sequence and dimerization on cleavage of the p75 neurotrophin receptor by γ-secretase. Journal of Biological Chemistry. 287: 43810-43824 doi:10.1074/jbc.M112.382903.
    • (2012) , vol.287 , pp. 43810-43824
    • Sykes, A.M.1    Palstra, N.2    Abankwa, D.3    Hill, J.M.4    Skeldal, S.5
  • 58
    • 0033003760 scopus 로고    scopus 로고
    • A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays
    • 10.1177/108705719900400206
    • Zhang J, Chung T, Oldenburg K, (1999) A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays. J Biomol Screen 4: 67-73 doi:10.1177/108705719900400206.
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.1    Chung, T.2    Oldenburg, K.3


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