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Volumn 1298, Issue , 2015, Pages 29-45

Rab-nanops: Fret biosensors for rab membrane nanoclustering and prenylation detection in mammalian cells

Author keywords

Drug discovery; Flow cytometry; FRET; Geranylgeranylation; GTPase; Membrane; Nanocluster; Rab; Trafficking

Indexed keywords

RAB PROTEIN; ENZYME INHIBITOR; RAB GERANYLGERANYLTRANSFERASE; TRANSFERASE;

EID: 84926050372     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-2569-8_3     Document Type: Article
Times cited : (4)

References (51)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer SJ, Nicolson GL (1972) The fluid mosaic model of the structure of cell membranes. Science 175:720–731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K, van Meer G (1988) Lipid sorting in epithelial cells. Biochemistry 27:6197–6202
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 3
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E (1997) Functional rafts in cell membranes. Nature 387:569–572. doi: 10.1038/42408
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 4
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: Contentious only from simplistic standpoints
    • Hancock JF (2006) Lipid rafts: Contentious only from simplistic standpoints. Nat Rev Mol Cell Biol 7:456–462. doi: 10.1038/nrm1925
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 456-462
    • Hancock, J.F.1
  • 5
    • 61349094652 scopus 로고    scopus 로고
    • Direct observation of the nanoscale dynamics of membrane lipids in a living cell
    • Eggeling C, Ringemann C, Medda R et al (2009) Direct observation of the nanoscale dynamics of membrane lipids in a living cell. Nature 457:1159–1162. doi: 10.1038/nature07596
    • (2009) Nature , vol.457 , pp. 1159-1162
    • Eggeling, C.1    Ringemann, C.2    Medda, R.3
  • 6
    • 80053354873 scopus 로고    scopus 로고
    • STED Nanoscopy Reveals Molecular Details of Cholesterol- and Cytoskeleton- Modulated Lipid Interactions in Living Cells
    • Mueller V, Ringemann C, Honigmann A et al (2011) STED Nanoscopy Reveals Molecular Details of Cholesterol- and Cytoskeleton- Modulated Lipid Interactions in Living Cells. Biophys J 101:1651–1660. doi: 10.1016/j.bpj.2011.09.006
    • (2011) Biophys J , vol.101 , pp. 1651-1660
    • Mueller, V.1    Ringemann, C.2    Honigmann, A.3
  • 7
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R, Mayor S (1998) GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394:798–801. doi: 10.1038/29563
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 8
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPIanchored proteins in living cell membranes
    • Sharma P, Varma R, Sarasij RC et al (2004) Nanoscale organization of multiple GPIanchored proteins in living cell membranes. Cell 116:577–589
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3
  • 9
    • 57149125825 scopus 로고    scopus 로고
    • Nanoclusters of GPI-anchored proteins are formed by cortical actin-driven activity
    • Goswami D, Gowrishankar K, Bilgrami S 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
  • 10
    • 0035067187 scopus 로고    scopus 로고
    • GTPdependent segregation of H-ras from lipid rafts is required for biological activity
    • Prior IA, Harding A, Yan J et al (2001) GTPdependent 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
  • 11
    • 1442274700 scopus 로고    scopus 로고
    • Lipid rafts and plasma membrane microorganization: Insights from Ras
    • Parton RG, Hancock JF (2004) Lipid rafts and plasma membrane microorganization: insights from Ras. Trends Cell Biol 14:141–147. doi: 10.1016/j.tcb.2004.02.001
    • (2004) Trends Cell Biol , vol.14 , pp. 141-147
    • Parton, R.G.1    Hancock, J.F.2
  • 12
    • 35648980477 scopus 로고    scopus 로고
    • Ras nanoclusters: Molecular structure and assembly
    • 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
  • 13
    • 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
    • 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
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 14
    • 84893839471 scopus 로고    scopus 로고
    • Signal Integration by Lipid-Mediated Spatial Cross Talk between Ras Nanoclusters
    • Zhou Y, Liang H, Rodkey T et al (2014) Signal Integration by Lipid-Mediated Spatial Cross Talk between Ras Nanoclusters. Mol Cell Biol 34:862–876. doi: 10.1128/MCB.01227-13
    • (2014) Mol Cell Biol , vol.34 , pp. 862-876
    • Zhou, Y.1    Liang, H.2    Rodkey, T.3
  • 15
    • 34547561587 scopus 로고    scopus 로고
    • Plasma membrane nano switches generate high-fidelity Ras signal transduction
    • Tian T, Harding A, Inder K et al (2007) Plasma membrane nano switches 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
  • 16
    • 2442538177 scopus 로고    scopus 로고
    • Single-molecule imaging analysis of Ras activation in living cells
    • Murakoshi H, Iino R, Kobayashi T et al (2004) Single-molecule imaging analysis of Ras activation in living cells. Proc Natl Acad Sci U S A 101:7317–7322. doi: 10.1073/pnas.0401354101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7317-7322
    • Murakoshi, H.1    Iino, R.2    Kobayashi, T.3
  • 17
    • 0041309461 scopus 로고    scopus 로고
    • Single- and Multiple-Molecule Dynamics of the Signaling from H-Ras to cRaf-1 Visualized on the Plasma Membrane of Living Cells
    • Hibino K, Watanabe TM, Kozuka J et al (2003) Single- and Multiple-Molecule Dynamics of the Signaling from H-Ras to cRaf-1 Visualized on the Plasma Membrane of Living Cells. ChemPhysChem 4:748–753. doi: 10.1002/cphc.200300731
    • (2003) Chemphyschem , vol.4 , pp. 748-753
    • Hibino, K.1    Watanabe, T.M.2    Kozuka, J.3
  • 18
    • 84898063580 scopus 로고    scopus 로고
    • The efficacy of Raf kinase recruitment to the GTPase H-ras depends on H-ras membrane conformer specifi c nanoclustering
    • Guzmán C, Šolman M, Ligabue A et al (2014) The efficacy of Raf kinase recruitment to the GTPase H-ras depends on H-ras membrane conformer specifi c nanoclustering. J Biol Chem. doi: 10.1074/jbc.M113.537001
    • (2014) J Biol Chem
    • Guzmán, C.1    Šolman, M.2    Ligabue, A.3
  • 19
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior IA, Muncke C, Parton RG, Hancock JF (2003) Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J Cell Biol 160:165–170. doi: 10.1083/jcb.200209091
    • (2003) J Cell Biol , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 20
    • 77957785819 scopus 로고    scopus 로고
    • H-Ras nanocluster stability regulates the magnitude of MAPK signal output
    • Rotblat B, Belanis L, Liang H et al (2010) H-Ras nanocluster stability regulates the magnitude of MAPK signal output. PLoS One 5:e11991. doi: 10.1371/journal.pone.0011991
    • (2010) Plos One , vol.5
    • Rotblat, B.1    Belanis, L.2    Liang, H.3
  • 21
    • 44949124597 scopus 로고    scopus 로고
    • Galectin-1 is a novel structural component and a major regulator of H-Ras nanoclusters
    • Belanis L, Plowman SJ, Rotblat B et al (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
  • 22
    • 53049098385 scopus 로고    scopus 로고
    • K-ras nanoclustering is subverted by overexpression of the scaffold protein galectin- 3
    • Shalom-Feuerstein R, Plowman SJ, Rotblat B et al (2008) K-ras nanoclustering is subverted by overexpression of the scaffold protein galectin- 3. Cancer Res 68:6608–6616. doi: 10.1158/0008-5472.CAN-08-1117
    • (2008) Cancer Res , vol.68 , pp. 6608-6616
    • Shalom-Feuerstein, R.1    Plowman, S.J.2    Rotblat, B.3
  • 23
    • 84861874745 scopus 로고    scopus 로고
    • Raf inhibitors target ras spatiotemporal dynamics
    • Cho K-J, Kasai RS, Park J-H et al (2012) Raf inhibitors target ras spatiotemporal dynamics. Curr Biol 22:945–955. doi: 10.1016/j.cub.2012.03.067
    • (2012) Curr Biol , vol.22 , pp. 945-955
    • Cho, K.-J.1    Kasai, R.S.2    Park, J.-H.3
  • 24
    • 40949130399 scopus 로고    scopus 로고
    • A novel switch region regulates H-ras membrane orientation and signal output
    • Abankwa D, Hanzal-Bayer M, Ariotti N 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.2    Ariotti, N.3
  • 25
    • 84864408572 scopus 로고    scopus 로고
    • Design and Application of In Vivo FRET Biosensors to Identify Protein Prenylation and Nanoclustering Inhibitors
    • Köhnke M, Schmitt S, Ariotti N et al (2012) Design and Application of In Vivo FRET Biosensors to Identify Protein Prenylation and Nanoclustering Inhibitors. Chem Biol 19: 866–874. doi: 10.1016/j.chembiol.2012.05.019
    • (2012) Chem Biol , vol.19 , pp. 866-874
    • Köhnke, M.1    Schmitt, S.2    Ariotti, N.3
  • 26
    • 84871538883 scopus 로고    scopus 로고
    • Staurosporines disrupt phosphatidylserine trafficking and mislocalize Ras proteins
    • Cho K-J, Park J-H, Piggott AM et al (2012) Staurosporines disrupt phosphatidylserine trafficking and mislocalize Ras proteins. J Biol Chem 287:43573–43584. doi: 10.1074/jbc.M112.424457
    • (2012) J Biol Chem , vol.287 , pp. 43573-43584
    • Cho, K.-J.1    Park, J.-H.2    Piggott, A.M.3
  • 27
    • 78049410557 scopus 로고    scopus 로고
    • The Anti-infl amatory Drug Indomethacin Alters Nanoclustering in Synthetic and Cell Plasma Membranes
    • Zhou Y, Plowman SJ, Lichtenberger LM, Hancock JF (2010) The Anti-infl amatory Drug Indomethacin Alters Nanoclustering in Synthetic and Cell Plasma Membranes. J Biol Chem 285:35188–35195. doi: 10.1074/jbc.M110.141200
    • (2010) J Biol Chem , vol.285
    • Zhou, Y.1    Plowman, S.J.2    Lichtenberger, L.M.3    Hancock, J.F.4
  • 28
    • 84860857782 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs alter the spatiotemporal organization of Ras proteins on the plasma membrane
    • Zhou Y, Cho K-J, Plowman SJ, Hancock JF (2012) Nonsteroidal anti-inflammatory drugs alter the spatiotemporal organization of Ras proteins on the plasma membrane. J Biol Chem 287:16586–16595. doi: 10.1074/jbc.M112.348490
    • (2012) J Biol Chem , vol.287
    • Zhou, Y.1    Cho, K.-J.2    Plowman, S.J.3    Hancock, J.F.4
  • 29
    • 34548561606 scopus 로고    scopus 로고
    • A FRET map of membrane anchors suggests distinct microdomains of heterotrimeric G proteins
    • 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
  • 30
    • 77957231106 scopus 로고    scopus 로고
    • An N-terminal polybasic motif of Gαq is required for signaling and infl uences membrane nanodomain distribution
    • Crouthamel M, Abankwa D, Zhang L et al (2010) An N-terminal polybasic motif of Gαq is required for signaling and infl uences membrane nanodomain distribution. Mol Pharmacol 78:767–777. doi: 10.1124/mol.110.066340
    • (2010) Mol Pharmacol , vol.78 , pp. 767-777
    • Crouthamel, M.1    Abankwa, D.2    Zhang, L.3
  • 31
    • 84879152912 scopus 로고    scopus 로고
    • Cellular FRET-Biosensors to Detect Membrane Targeting Inhibitors of N-Myristoylated Proteins
    • Najumudeen AK, Köhnke M, Šolman M et al (2013) Cellular FRET-Biosensors to Detect Membrane Targeting Inhibitors of N-Myristoylated Proteins. PLoS One 8:e66425. doi: 10.1371/journal.pone.0066425.s007
    • (2013) Plos One , vol.8
    • Najumudeen, A.K.1    Köhnke, M.2    Šolman, M.3
  • 32
    • 23844445866 scopus 로고    scopus 로고
    • The structural and mechanistic basis for recycling of Rab proteins between membrane compartments
    • Goody RS, Rak A, Alexandrov K (2005) The structural and mechanistic basis for recycling of Rab proteins between membrane compartments. Cell Mol Life Sci 62:1657–1670. doi: 10.1007/s00018-005-4486-8
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1657-1670
    • Goody, R.S.1    Rak, A.2    Alexandrov, K.3
  • 34
    • 0028067898 scopus 로고
    • Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes
    • Alexandrov K, Horiuchi H, Steele-Mortimer O et al (1994) Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes. EMBO J 13:5262–5273
    • (1994) EMBO J , vol.13 , pp. 5262-5273
    • Alexandrov, K.1    Horiuchi, H.2    Steele-Mortimer, O.3
  • 35
    • 84894332323 scopus 로고    scopus 로고
    • The role of the hypervariable C-terminal domain in Rab GTPases membrane targeting
    • Li F, Yi L, Zhao L et al (2014) The role of the hypervariable C-terminal domain in Rab GTPases membrane targeting. Proc Natl Acad Sci U S A 111:2572–2577. doi: 10.1073/pnas.1313655111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 2572-2577
    • Li, F.1    Yi, L.2    Zhao, L.3
  • 36
    • 0036137684 scopus 로고    scopus 로고
    • Rab GTPases, intracellular traffic and disease
    • Seabra MC, Mules EH, Hume AN (2002) Rab GTPases, intracellular traffic and disease. Trends Mol Med 8:23–30
    • (2002) Trends Mol Med , vol.8 , pp. 23-30
    • Seabra, M.C.1    Mules, E.H.2    Hume, A.N.3
  • 37
    • 84870196513 scopus 로고    scopus 로고
    • Novel functions for Rab GTPases in multiple aspects of tumour progression
    • Recchi C, Seabra MC (2012) Novel functions for Rab GTPases in multiple aspects of tumour progression. Biochem Soc Trans 40:1398–1403. doi: 10.1016/S1471-4914(01)02227-4
    • (2012) Biochem Soc Trans , vol.40 , pp. 1398-1403
    • Recchi, C.1    Seabra, M.C.2
  • 38
    • 65449173985 scopus 로고    scopus 로고
    • Phosphonocarboxylates inhibit the second geranylgeranyl addition by Rab geranylgeranyl transferase
    • Baron RA, Tavaré R, Figueiredo AC et al (2009) Phosphonocarboxylates inhibit the second geranylgeranyl addition by Rab geranylgeranyl transferase. J Biol Chem 284:6861–6868. doi: 10.1074/jbc.M806952200
    • (2009) J Biol Chem , vol.284 , pp. 6861-6868
    • Baron, R.A.1    Tavaré, R.2    Figueiredo, A.C.3
  • 39
    • 20244378061 scopus 로고    scopus 로고
    • Chemical genetics identifies Rab geranylgeranyl transferase as an apoptotic target of farnesyl transferase inhibitors
    • Lackner MR, Kindt RM, Carroll PM et al (2005) Chemical genetics identifies Rab geranylgeranyl transferase as an apoptotic target of farnesyl transferase inhibitors. Cancer Cell 7:325–336. doi: 10.1016/j.ccr.2005.03.024
    • (2005) Cancer Cell , vol.7 , pp. 325-336
    • Lackner, M.R.1    Kindt, R.M.2    Carroll, P.M.3
  • 40
    • 23844443254 scopus 로고    scopus 로고
    • Phosphonocarboxylate inhibitors of Rab geranylgeranyl transferase disrupt the prenylation and membrane localization of Rab proteins in osteoclasts in vitro and in vivo
    • Coxon FP, Ebetino FH, Mules EH et al (2005) Phosphonocarboxylate inhibitors of Rab geranylgeranyl transferase disrupt the prenylation and membrane localization of Rab proteins in osteoclasts in vitro and in vivo. Bone 37:349–358. doi: 10.1016/j.bone.2005.04.021
    • (2005) Bone , vol.37 , pp. 349-358
    • Coxon, F.P.1    Ebetino, F.H.2    Mules, E.H.3
  • 41
    • 79955779844 scopus 로고    scopus 로고
    • Structure-Guided Development of Selective RabGGTase Inhibitors
    • Bon RS, Guo Z, Stigter EA et al (2011) Structure-Guided Development of Selective RabGGTase Inhibitors. Angew Chem Int Ed 50:4957–4961. doi: 10.1002/anie.201101210
    • (2011) Angew Chem Int Ed , vol.50 , pp. 4957-4961
    • Bon, R.S.1    Guo, Z.2    Stigter, E.A.3
  • 42
    • 44349178715 scopus 로고    scopus 로고
    • Inhibitors of protein geranylgeranyltransferase I and Rab geranylgeranyltransferase identifi ed from a library of allenoate-derived compounds
    • Watanabe M, Fiji HDG, Guo L et al (2008) Inhibitors of protein geranylgeranyltransferase I and Rab geranylgeranyltransferase identifi ed from a library of allenoate-derived compounds. J Biol Chem 283:9571–9579. doi: 10.1074/jbc.M706229200
    • (2008) J Biol Chem , vol.283 , pp. 9571-9579
    • Watanabe, M.1    Fiji, H.2    Guo, L.3
  • 43
  • 44
    • 0028903255 scopus 로고
    • Calculation of resonance energy transfer in crowded biological membranes
    • Zimet DB, Thevenin BJ, Verkman AS et al (1995) Calculation of resonance energy transfer in crowded biological membranes. Biophys J 68:1592–1603. doi: 10.1016/S0006-3495(95)80332-2
    • (1995) Biophys J , vol.68 , pp. 1592-1603
    • Zimet, D.B.1    Thevenin, B.J.2    Verkman, A.S.3
  • 45
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • Berney C, Danuser G (2003) FRET or no FRET: A quantitative comparison. Biophys J 84:3992–4010
    • (2003) Biophys J , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 46
    • 0018650688 scopus 로고
    • An analytic solution to the Förster energy transfer problem in two dimensions
    • Wolber PK, Hudson BS (1979) An analytic solution to the Förster energy transfer problem in two dimensions. Biophys J 28:197–210
    • (1979) Biophys J , vol.28 , pp. 197-210
    • Wolber, P.K.1    Hudson, B.S.2
  • 47
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon GW, Berry G, Liang XH et al (1998) Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys J 74:2702
    • (1998) Biophys J , vol.74 , pp. 2702
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3
  • 48
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modifi ed monomeric GFPs into membrane microdomains of live cells
    • Zacharias DA, Violin JD, Newton AC, Tsien RY (2002) Partitioning of lipid-modifi ed monomeric GFPs into membrane microdomains of live cells. Science 296:913–916
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 50
    • 0035800773 scopus 로고    scopus 로고
    • Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications
    • Griesbeck O, Baird GS, Campbell RE et al (2001) Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications. J Biol Chem 276:29188–29194. doi: 10.1074/jbc.M102815200
    • (2001) J Biol Chem , vol.276
    • Griesbeck, O.1    Baird, G.S.2    Campbell, R.E.3
  • 51
    • 0035930612 scopus 로고    scopus 로고
    • Identification of a novel phosphonocarboxylate inhibitor of Rab geranylgeranyl transferase that specifi cally prevents Rab prenylation in osteoclasts and macrophages
    • Coxon FP, Helfrich MH, Larijani B et al (2001) Identification of a novel phosphonocarboxylate inhibitor of Rab geranylgeranyl transferase that specifi cally prevents Rab prenylation in osteoclasts and macrophages. J Biol Chem 276:48213–48222. doi: 10.1074/jbc.M106473200
    • (2001) J Biol Chem , vol.276
    • Coxon, F.P.1    Helfrich, M.H.2    Larijani, B.3


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