메뉴 건너뛰기




Volumn 194, Issue 1, 2011, Pages 89-103

α-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN;

EID: 79960279832     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201011118     Document Type: Article
Times cited : (165)

References (66)
  • 1
    • 79959397904 scopus 로고    scopus 로고
    • Mechanisms of membrane curvature sensing
    • Antonny, B. 2011. Mechanisms of membrane curvature sensing. Annu. Rev. Biochem. 80:101-123.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 101-123
    • Antonny, B.1
  • 2
    • 77958449984 scopus 로고    scopus 로고
    • α-Synuclein: membrane interactions and toxicity in Parkinson's disease
    • Auluck, P.K., G. Caraveo, and S. Lindquist. 2010. α-Synuclein: membrane interactions and toxicity in Parkinson's disease. Annu. Rev. Cell Dev. Biol. 26:211-233.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3
  • 3
    • 77649159735 scopus 로고    scopus 로고
    • The Sec14 superfamily and mechanisms for crosstalk between lipid metabolism and lipid signaling
    • Bankaitis, V.A., C.J. Mousley, and G. Schaaf. 2010. The Sec14 superfamily and mechanisms for crosstalk between lipid metabolism and lipid signaling. Trends Biochem. Sci. 35:150-160.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 150-160
    • Bankaitis, V.A.1    Mousley, C.J.2    Schaaf, G.3
  • 4
    • 0032519306 scopus 로고    scopus 로고
    • An activator/repressor dual system allows tight tetracycline-regulated gene expression in budding yeast
    • Bellí, G., E. Garí, L. Piedrafita, M. Aldea, and E. Herrero. 1998. An activator/repressor dual system allows tight tetracycline-regulated gene expression in budding yeast. Nucleic Acids Res. 26:942-947.
    • (1998) Nucleic Acids Res , vol.26 , pp. 942-947
    • Bellí, G.1    Garí, E.2    Piedrafita, L.3    Aldea, M.4    Herrero, E.5
  • 5
    • 58549089901 scopus 로고    scopus 로고
    • Alpha-synuclein and polyunsaturated fatty acids promote clathrinmediated endocytosis and synaptic vesicle recycling
    • Ben Gedalya, T., V. Loeb, E. Israeli, Y. Altschuler, D.J. Selkoe, and R. Sharon. 2009. Alpha-synuclein and polyunsaturated fatty acids promote clathrinmediated endocytosis and synaptic vesicle recycling. Traffic. 10:218-234.
    • (2009) Traffic , vol.10 , pp. 218-234
    • Ben Gedalya, T.1    Loeb, V.2    Israeli, E.3    Altschuler, Y.4    Selkoe, D.J.5    Sharon, R.6
  • 6
    • 22744442219 scopus 로고    scopus 로고
    • ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif
    • Bigay, J., J.F. Casella, G. Drin, B. Mesmin, and B. Antonny. 2005. ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif. EMBO J. 24:2244-2253.
    • (2005) EMBO J , vol.24 , pp. 2244-2253
    • Bigay, J.1    Casella, J.F.2    Drin, G.3    Mesmin, B.4    Antonny, B.5
  • 7
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino J.S., and B.S. Glick. 2004. The mechanisms of vesicle budding and fusion. Cell. 116:153-166.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 10
    • 70350029562 scopus 로고    scopus 로고
    • Golgi localisation of GMAP210 requires two distinct cis-membrane binding mechanisms
    • Cardenas, J., S. Rivero, B. Goud, M. Bornens, and R.M. Rios. 2009. Golgi localisation of GMAP210 requires two distinct cis-membrane binding mechanisms. BMC Biol. 7:56.
    • (2009) BMC Biol , vol.7 , pp. 56
    • Cardenas, J.1    Rivero, S.2    Goud, B.3    Bornens, M.4    Rios, R.M.5
  • 12
    • 0031050445 scopus 로고    scopus 로고
    • Yeast-enhanced green fluorescent protein (yEGFP) a reporter of gene expression in Candida albicans
    • Cormack, B.P., G. Bertram, M. Egerton, N.A. Gow, S. Falkow, and A.J. Brown. 1997. Yeast-enhanced green fluorescent protein (yEGFP) a reporter of gene expression in Candida albicans. Microbiology. 143:303-311.
    • (1997) Microbiology , vol.143 , pp. 303-311
    • Cormack, B.P.1    Bertram, G.2    Egerton, M.3    Gow, N.A.4    Falkow, S.5    Brown, A.J.6
  • 13
    • 33845350971 scopus 로고    scopus 로고
    • Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties
    • Cornell, R.B., and S.G. Taneva. 2006. Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties. Curr. Protein Pept. Sci. 7:539-552.
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 539-552
    • Cornell, R.B.1    Taneva, S.G.2
  • 14
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W.S., A. Jonas, D.F. Clayton, and J.M. George. 1998. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273:9443-9449.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 15
    • 58049099709 scopus 로고    scopus 로고
    • A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor
    • Deng, Y., M.P. Golinelli-Cohen, E. Smirnova, and C.L. Jackson. 2009. A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor. EMBO Rep. 10:58-64.
    • (2009) EMBO Rep , vol.10 , pp. 58-64
    • Deng, Y.1    Golinelli-Cohen, M.P.2    Smirnova, E.3    Jackson, C.L.4
  • 16
    • 77953724768 scopus 로고    scopus 로고
    • Cell cycle-dependent differences in nuclear pore complex assembly in metazoa
    • Doucet, C.M., J.A. Talamas, and M.W. Hetzer. 2010. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell. 141:1030-1041.
    • (2010) Cell , vol.141 , pp. 1030-1041
    • Doucet, C.M.1    Talamas, J.A.2    Hetzer, M.W.3
  • 17
    • 77951896130 scopus 로고    scopus 로고
    • Amphipathic helices and membrane curvature
    • Drin, G., and B. Antonny. 2010. Amphipathic helices and membrane curvature. FEBS Lett. 584:1840-1847.
    • (2010) FEBS Lett , vol.584 , pp. 1840-1847
    • Drin, G.1    Antonny, B.2
  • 19
    • 43249126878 scopus 로고    scopus 로고
    • Asymmetric tethering of flat and curved lipid membranes by a golgin
    • Drin, G., V. Morello, J.F. Casella, P. Gounon, and B. Antonny. 2008. Asymmetric tethering of flat and curved lipid membranes by a golgin. Science. 320:670-673.
    • (2008) Science , vol.320 , pp. 670-673
    • Drin, G.1    Morello, V.2    Casella, J.F.3    Gounon, P.4    Antonny, B.5
  • 22
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain superfamily: membrane-molding macromolecules
    • Frost, A., V.M. Unger, and P. De Camilli. 2009. The BAR domain superfamily: membrane-molding macromolecules. Cell. 137:191-196.
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 24
    • 0036242551 scopus 로고    scopus 로고
    • Molecular architecture of SMC proteins and the yeast cohesin complex
    • Haering, C.H., J. Löwe, A. Hochwagen, and K. Nasmyth. 2002. Molecular architecture of SMC proteins and the yeast cohesin complex. Mol. Cell. 9:773-788.
    • (2002) Mol. Cell. , vol.9 , pp. 773-788
    • Haering, C.H.1    Löwe, J.2    Hochwagen, A.3    Nasmyth, K.4
  • 27
    • 58149380718 scopus 로고    scopus 로고
    • Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement
    • Jao, C.C., B.G. Hegde, J. Chen, I.S. Haworth, and R. Langen. 2008. Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement. Proc. Natl. Acad. Sci. USA. 105:19666-19671.
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 19666-19671
    • Jao, C.C.1    Hegde, B.G.2    Chen, J.3    Haworth, I.S.4    Langen, R.5
  • 28
    • 27744545622 scopus 로고    scopus 로고
    • Fluorescence approaches for determining protein conformations, interactions and mechanisms at membranes
    • Johnson, A.E. 2005. Fluorescence approaches for determining protein conformations, interactions and mechanisms at membranes. Traffic. 6:1078-1092.
    • (2005) Traffic , vol.6 , pp. 1078-1092
    • Johnson, A.E.1
  • 30
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • Kaksonen, M., Y. Sun, and D.G. Drubin. 2003. A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell. 115:475-487.
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 31
    • 1242329989 scopus 로고    scopus 로고
    • Capping protein binding to actin in yeast: biochemical mechanism and physiological relevance
    • Kim, K., A. Yamashita, M.A. Wear, Y. Maéda, and J.A. Cooper. 2004. Capping protein binding to actin in yeast: biochemical mechanism and physiological relevance. J. Cell Biol. 164:567-580.
    • (2004) J. Cell Biol. , vol.164 , pp. 567-580
    • Kim, K.1    Yamashita, A.2    Wear, M.A.3    Maéda, Y.4    Cooper, J.A.5
  • 33
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer, J.R., D.N. Mastronarde, and J.R. McIntosh. 1996. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116:71-76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 36
    • 75749114150 scopus 로고    scopus 로고
    • Mechanochemical crosstalk during endocytic vesicle formation
    • Liu, J., Y. Sun, G.F. Oster, and D.G. Drubin. 2010. Mechanochemical crosstalk during endocytic vesicle formation. Curr. Opin. Cell Biol. 22:36-43.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 36-43
    • Liu, J.1    Sun, Y.2    Oster, G.F.3    Drubin, D.G.4
  • 37
    • 35348819374 scopus 로고    scopus 로고
    • In vitro fusion catalyzed by the sporulation-specific t-SNARE light-chain Spo20p is stimulated by phosphatidic acid
    • Liu, S., K.A. Wilson, T. Rice-Stitt, A.M. Neiman, and J.A. McNew. 2007. In vitro fusion catalyzed by the sporulation-specific t-SNARE light-chain Spo20p is stimulated by phosphatidic acid. Traffic. 8:1630-1643.
    • (2007) Traffic , vol.8 , pp. 1630-1643
    • Liu, S.1    Wilson, K.A.2    Rice-Stitt, T.3    Neiman, A.M.4    McNew, J.A.5
  • 38
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S., A. McKenzie III, D.J. Demarini, N.G. Shah, A. Wach, A. Brachat, P. Philippsen, and J.R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast. 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 39
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon, H.T., and J.L. Gallop. 2005. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature. 438:590-596.
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 40
    • 33847075871 scopus 로고    scopus 로고
    • Two lipid-packing sensor motifs contribute to the sensitivity of ArfGAP1 to membrane curvature
    • Mesmin, B., G. Drin, S. Levi, M. Rawet, D. Cassel, J. Bigay, and B. Antonny. 2007. Two lipid-packing sensor motifs contribute to the sensitivity of ArfGAP1 to membrane curvature. Biochemistry. 46:1779-1790.
    • (2007) Biochemistry , vol.46 , pp. 1779-1790
    • Mesmin, B.1    Drin, G.2    Levi, S.3    Rawet, M.4    Cassel, D.5    Bigay, J.6    Antonny, B.7
  • 41
    • 77958455514 scopus 로고    scopus 로고
    • Effects of curvature and composition on (-synuclein binding to lipid vesicles
    • Middleton, E.R., and E. Rhoades. 2010. Effects of curvature and composition on (-synuclein binding to lipid vesicles. Biophys. J. 99:2279-2288.
    • (2010) Biophys. J. , vol.99 , pp. 2279-2288
    • Middleton, E.R.1    Rhoades, E.2
  • 42
    • 1642546271 scopus 로고    scopus 로고
    • Positive and negative regulation of a SNARE protein by control of intracellular localization
    • Nakanishi, H., P. de los Santos, and A.M. Neiman. 2004. Positive and negative regulation of a SNARE protein by control of intracellular localization. Mol. Biol. Cell. 15:1802-1815.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 1802-1815
    • Nakanishi, H.1    de los Santos, P.2    Neiman, A.M.3
  • 43
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani, V.M., W. Lu, V. Berge, K. Nakamura, B. Onoa, M.K. Lee, F.A. Chaudhry, R.A. Nicoll, and R.H. Edwards. 2010. Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron. 65:66-79.
    • (2010) Neuron , vol.65 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3    Nakamura, K.4    Onoa, B.5    Lee, M.K.6    Chaudhry, F.A.7    Nicoll, R.A.8    Edwards, R.H.9
  • 44
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into alpha-synuclein biology and pathobiology
    • Outeiro, T.F., and S. Lindquist. 2003. Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science. 302:1772-1775.
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 45
    • 34249094787 scopus 로고    scopus 로고
    • Organelle association visualized by three-dimensional ultrastructural imaging of the yeast cell
    • Perktold, A., B. Zechmann, G. Daum, and G. Zellnig. 2007. Organelle association visualized by three-dimensional ultrastructural imaging of the yeast cell. FEM. Yeast Res. 7:629-638.
    • (2007) FEM. Yeast Res. , vol.7 , pp. 629-638
    • Perktold, A.1    Zechmann, B.2    Daum, G.3    Zellnig, G.4
  • 46
    • 0037193471 scopus 로고    scopus 로고
    • ARF- GAP- mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
    • Rein, U., U. Andag, R. Duden, H.D. Schmitt, and A. Spang. 2002. ARF-GAP- mediated interaction between the ER-Golgi v-SNAREs and the COPI coat. J. Cell Biol. 157:395-404.
    • (2002) J. Cell Biol. , vol.157 , pp. 395-404
    • Rein, U.1    Andag, U.2    Duden, R.3    Schmitt, H.D.4    Spang, A.5
  • 47
    • 79952853575 scopus 로고    scopus 로고
    • Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis
    • Rossi, G., and P. Brennwald. 2011. Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis. Mol. Biol. Cell. 22:842-857.
    • (2011) Mol. Biol. Cell. , vol.22 , pp. 842-857
    • Rossi, G.1    Brennwald, P.2
  • 48
    • 0034682560 scopus 로고    scopus 로고
    • Mutational and biochemical analysis of plasma membrane targeting mediated by the farnesylated, polybasic carboxy terminus of K-ras4B
    • Roy, M.O., R. Leventis, and J.R. Silvius. 2000. Mutational and biochemical analysis of plasma membrane targeting mediated by the farnesylated, polybasic carboxy terminus of K-ras4B. Biochemistry. 39:8298-8307.
    • (2000) Biochemistry , vol.39 , pp. 8298-8307
    • Roy, M.O.1    Leventis, R.2    Silvius, J.R.3
  • 49
    • 0038783732 scopus 로고    scopus 로고
    • Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesicles
    • Sato, K., and A. Nakano. 2003. Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesicles. Mol. Biol. Cell. 14:3055-3063.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 3055-3063
    • Sato, K.1    Nakano, A.2
  • 50
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • Schneiter, R., B. Brügger, R. Sandhoff, G. Zellnig, A. Leber, M. Lampl, K. Athenstaedt, C. Hrastnik, S. Eder, G. Daum, et al. 1999. Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane. J. Cell Biol. 146:741-754.
    • (1999) J. Cell Biol. , vol.146 , pp. 741-754
    • Schneiter, R.1    Brügger, B.2    Sandhoff, R.3    Zellnig, G.4    Leber, A.5    Lampl, M.6    Athenstaedt, K.7    Hrastnik, C.8    Eder, S.9    Daum, G.10
  • 52
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe, H.J., T.J. Stevens, and S. Munro. 2010. A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell. 142:158-169.
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.J.1    Stevens, T.J.2    Munro, S.3
  • 53
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman, F. 2002. Getting started with yeast. Methods Enzymol. 350:3-41.
    • (2002) Methods Enzymol , vol.350 , pp. 3-41
    • Sherman, F.1
  • 55
    • 79953846844 scopus 로고    scopus 로고
    • Aggregation of β-synuclein in S. cerevisiae is associated with defects in endosomal trafficking and phospholipid biosynthesis
    • Soper, J.H., V. Kehm, C.G. Burd, V.A. Bankaitis, and V.M. Lee. 2011. Aggregation of β-synuclein in S. cerevisiae is associated with defects in endosomal trafficking and phospholipid biosynthesis. J. Mol. Neurosci. 43:391-405.
    • (2011) J. Mol. Neurosci. , vol.43 , pp. 391-405
    • Soper, J.H.1    Kehm, V.2    Burd, C.G.3    Bankaitis, V.A.4    Lee, V.M.5
  • 56
    • 33748300590 scopus 로고    scopus 로고
    • Phosphatidic acid- and phosphatidylserinebinding proteins
    • Stace, C.L., and N.T. Ktistakis. 2006. Phosphatidic acid- and phosphatidylserinebinding proteins. Biochim. Biophys. Acta. 1761:913-926.
    • (2006) Biochim. Biophys. Acta. , vol.1761 , pp. 913-926
    • Stace, C.L.1    Ktistakis, N.T.2
  • 57
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: grappling with SNARE and SM proteins
    • Südhof, T.C., and J.E. Rothman. 2009. Membrane fusion: grappling with SNARE and SM proteins. Science. 323:474-477.
    • (2009) Science , vol.323 , pp. 474-477
    • Südhof, T.C.1    Rothman, J.E.2
  • 59
    • 77952900626 scopus 로고    scopus 로고
    • Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs
    • Thayanidhi, N., J.R. Helm, D.C. Nycz, M. Bentley, Y. Liang, and J.C. Hay. 2010. Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs. Mol. Biol. Cell. 21:1850-1863.
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 1850-1863
    • Thayanidhi, N.1    Helm, J.R.2    Nycz, D.C.3    Bentley, M.4    Liang, Y.5    Hay, J.C.6
  • 61
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida, T.A., and S.D. Emr. 1995. A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J. Cell Biol. 128:779-792.
    • (1995) J. Cell Biol. , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 62
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • Voeltz, G.K., W.A. Prinz, Y. Shibata, J.M. Rist, and T.A. Rapoport. 2006. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell. 124:573-586.
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 64
    • 0031665836 scopus 로고    scopus 로고
    • The dynamics of golgi protein traffic visualized in living yeast cells
    • Wooding, S., and H.R. Pelham. 1998. The dynamics of golgi protein traffic visualized in living yeast cells. Mol. Biol. Cell. 9:2667-2680.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 2667-2680
    • Wooding, S.1    Pelham, H.R.2
  • 65
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung, T., G.E. Gilbert, J. Shi, J. Silvius, A. Kapus, and S. Grinstein. 2008. Membrane phosphatidylserine regulates surface charge and protein localization. Science. 319:210-213.
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 66
    • 0026082909 scopus 로고
    • Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae
    • Zinser, E., C.D. Sperka-Gottlieb, E.V. Fasch, S.D. Kohlwein, F. Paltauf, and G. Daum. 1991. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae. J. Bacteriol. 173:2026-2034.
    • (1991) J. Bacteriol. , vol.173 , pp. 2026-2034
    • Zinser, E.1    Sperka-Gottlieb, C.D.2    Fasch, E.V.3    Kohlwein, S.D.4    Paltauf, F.5    Daum, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.