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Volumn 35, Issue 5, 2015, Pages 584-599

Role for Lipid Droplet Biogenesis and Microlipophagy in Adaptation to Lipid Imbalance in Yeast

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; ESCRT PROTEIN; FAT DROPLET; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 104P; LIPID; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; TRIACYLGLYCEROL; UNCLASSIFIED DRUG; ATG7 PROTEIN, S CEREVISIAE; AUTOPHAGY RELATED PROTEIN 7; CHO2 PROTEIN, S CEREVISIAE; GREEN FLUORESCENT PROTEIN; PHOSPHATIDYLETHANOLAMINE METHYLTRANSFERASE; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN;

EID: 84961662044     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2015.11.010     Document Type: Article
Times cited : (150)

References (63)
  • 1
    • 67650915066 scopus 로고    scopus 로고
    • Selective processing and metabolism of disease-causing mutant prion proteins
    • Ashok A., Hegde R.S. Selective processing and metabolism of disease-causing mutant prion proteins. PLoS Pathog. 2009, 5:e1000479.
    • (2009) PLoS Pathog. , vol.5 , pp. e1000479
    • Ashok, A.1    Hegde, R.S.2
  • 2
    • 77955051681 scopus 로고    scopus 로고
    • A surveillance pathway monitors the fitness of the endoplasmic reticulum to control its inheritance
    • Babour A., Bicknell A.A., Tourtellotte J., Niwa M. A surveillance pathway monitors the fitness of the endoplasmic reticulum to control its inheritance. Cell 2010, 142:256-269.
    • (2010) Cell , vol.142 , pp. 256-269
    • Babour, A.1    Bicknell, A.A.2    Tourtellotte, J.3    Niwa, M.4
  • 3
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • Bernales S., McDonald K.L., Walter P. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 2006, 4:e423.
    • (2006) PLoS Biol. , vol.4 , pp. e423
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 4
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • Brodsky J.L. Cleaning up: ER-associated degradation to the rescue. Cell 2012, 151:1163-1167.
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 5
    • 0032730257 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes
    • Carman G.M., Henry S.A. Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes. Prog. Lipid Res. 1999, 38:361-399.
    • (1999) Prog. Lipid Res. , vol.38 , pp. 361-399
    • Carman, G.M.1    Henry, S.A.2
  • 7
    • 0034612345 scopus 로고    scopus 로고
    • Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants
    • Dahlqvist A., Stahl U., Lenman M., Banas A., Lee M., Sandager L., Ronne H., Stymne S. Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants. Proc. Natl. Acad. Sci. USA 2000, 97:6487-6492.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6487-6492
    • Dahlqvist, A.1    Stahl, U.2    Lenman, M.3    Banas, A.4    Lee, M.5    Sandager, L.6    Ronne, H.7    Stymne, S.8
  • 8
    • 34147192803 scopus 로고    scopus 로고
    • Visualization and quantification of mitochondrial dynamics in living animal cells
    • De Vos K.J., Sheetz M.P. Visualization and quantification of mitochondrial dynamics in living animal cells. Methods Cell Biol. 2007, 80:627-682.
    • (2007) Methods Cell Biol. , vol.80 , pp. 627-682
    • De Vos, K.J.1    Sheetz, M.P.2
  • 9
    • 84885095437 scopus 로고    scopus 로고
    • Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
    • Escusa-Toret S., Vonk W.I., Frydman J. Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat. Cell Biol. 2013, 15:1231-1243.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1231-1243
    • Escusa-Toret, S.1    Vonk, W.I.2    Frydman, J.3
  • 11
    • 70350700684 scopus 로고    scopus 로고
    • Conditions of endoplasmic reticulum stress stimulate lipid droplet formation in Saccharomyces cerevisiae
    • Fei W., Wang H., Fu X., Bielby C., Yang H. Conditions of endoplasmic reticulum stress stimulate lipid droplet formation in Saccharomyces cerevisiae. Biochem. J. 2009, 424:61-67.
    • (2009) Biochem. J. , vol.424 , pp. 61-67
    • Fei, W.1    Wang, H.2    Fu, X.3    Bielby, C.4    Yang, H.5
  • 12
    • 84929502727 scopus 로고    scopus 로고
    • How to control self-digestion: transcriptional, post-transcriptional, and post-translational regulation of autophagy
    • Feng Y., Yao Z., Klionsky D.J. How to control self-digestion: transcriptional, post-transcriptional, and post-translational regulation of autophagy. Trends Cell Biol. 2015, 25:354-363.
    • (2015) Trends Cell Biol. , vol.25 , pp. 354-363
    • Feng, Y.1    Yao, Z.2    Klionsky, D.J.3
  • 13
    • 0028916511 scopus 로고
    • Characterization of a microsomal subfraction associated with mitochondria of the yeast, Saccharomyces cerevisiae. Involvement in synthesis and import of phospholipids into mitochondria
    • Gaigg B., Simbeni R., Hrastnik C., Paltauf F., Daum G. Characterization of a microsomal subfraction associated with mitochondria of the yeast, Saccharomyces cerevisiae. Involvement in synthesis and import of phospholipids into mitochondria. Biochim. Biophys. Acta 1995, 1234:214-220.
    • (1995) Biochim. Biophys. Acta , vol.1234 , pp. 214-220
    • Gaigg, B.1    Simbeni, R.2    Hrastnik, C.3    Paltauf, F.4    Daum, G.5
  • 15
    • 77953591461 scopus 로고    scopus 로고
    • The Kennedy pathway--De novo synthesis of phosphatidylethanolamine and phosphatidylcholine
    • Gibellini F., Smith T.K. The Kennedy pathway--De novo synthesis of phosphatidylethanolamine and phosphatidylcholine. IUBMB Life 2010, 62:414-428.
    • (2010) IUBMB Life , vol.62 , pp. 414-428
    • Gibellini, F.1    Smith, T.K.2
  • 16
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    • Glover J.R., Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 1998, 94:73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 17
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids
    • Gruner S.M. Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. Proc. Natl. Acad. Sci. USA 1985, 82:3665-3669.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 19
    • 84901832063 scopus 로고    scopus 로고
    • Activation of the endoplasmic reticulum unfolded protein response by lipid disequilibrium without disturbed proteostasis in vivo
    • Hou N.S., Gutschmidt A., Choi D.Y., Pather K., Shi X., Watts J.L., Hoppe T., Taubert S. Activation of the endoplasmic reticulum unfolded protein response by lipid disequilibrium without disturbed proteostasis in vivo. Proc Natl Acad Sci U S A. 2014, 111:E2271-2280.
    • (2014) Proc Natl Acad Sci U S A. , vol.111 , pp. E2271-2280
    • Hou, N.S.1    Gutschmidt, A.2    Choi, D.Y.3    Pather, K.4    Shi, X.5    Watts, J.L.6    Hoppe, T.7    Taubert, S.8
  • 20
    • 79960398841 scopus 로고    scopus 로고
    • Lipid droplets are functionally connected to the endoplasmic reticulum in Saccharomyces cerevisiae
    • Jacquier N., Choudhary V., Mari M., Toulmay A., Reggiori F., Schneiter R. Lipid droplets are functionally connected to the endoplasmic reticulum in Saccharomyces cerevisiae. J. Cell Sci. 2011, 124:2424-2437.
    • (2011) J. Cell Sci. , vol.124 , pp. 2424-2437
    • Jacquier, N.1    Choudhary, V.2    Mari, M.3    Toulmay, A.4    Reggiori, F.5    Schneiter, R.6
  • 21
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D., Kopito R., Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008, 454:1088-1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 22
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Käll L., Krogh A., Sonnhammer E.L. A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol. 2004, 338:1027-1036.
    • (2004) J. Mol. Biol. , vol.338 , pp. 1027-1036
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 23
    • 0031552996 scopus 로고    scopus 로고
    • The phospholipid methyltransferases in yeast
    • Kanipes M.I., Henry S.A. The phospholipid methyltransferases in yeast. Biochim. Biophys. Acta 1997, 1348:134-141.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 134-141
    • Kanipes, M.I.1    Henry, S.A.2
  • 24
    • 67449088036 scopus 로고    scopus 로고
    • The unfolded protein response is necessary but not sufficient to compensate for defects in disulfide isomerization
    • Kim J.H., Zhao Y., Pan X., He X., Gilbert H.F. The unfolded protein response is necessary but not sufficient to compensate for defects in disulfide isomerization. J. Biol. Chem. 2009, 284:10400-10408.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10400-10408
    • Kim, J.H.1    Zhao, Y.2    Pan, X.3    He, X.4    Gilbert, H.F.5
  • 28
    • 33947375637 scopus 로고    scopus 로고
    • Nucleus-vacuole junctions and piecemeal microautophagy of the nucleus in S. cerevisiae
    • Kvam E., Goldfarb D.S. Nucleus-vacuole junctions and piecemeal microautophagy of the nucleus in S. cerevisiae. Autophagy 2007, 3:85-92.
    • (2007) Autophagy , vol.3 , pp. 85-92
    • Kvam, E.1    Goldfarb, D.S.2
  • 29
    • 84877730782 scopus 로고    scopus 로고
    • Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases
    • Lamari F., Mochel F., Sedel F., Saudubray J.M. Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases. J. Inherit. Metab. Dis. 2013, 36:411-425.
    • (2013) J. Inherit. Metab. Dis. , vol.36 , pp. 411-425
    • Lamari, F.1    Mochel, F.2    Sedel, F.3    Saudubray, J.M.4
  • 30
    • 84859161154 scopus 로고    scopus 로고
    • Microautophagy: lesser-known self-eating
    • Li W.W., Li J., Bao J.K. Microautophagy: lesser-known self-eating. Cell. Mol. Life Sci. 2012, 69:1125-1136.
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 1125-1136
    • Li, W.W.1    Li, J.2    Bao, J.K.3
  • 31
    • 84924915240 scopus 로고    scopus 로고
    • Ubiquitin-dependent lysosomal membrane protein sorting and degradation
    • Li M., Rong Y., Chuang Y.S., Peng D., Emr S.D. Ubiquitin-dependent lysosomal membrane protein sorting and degradation. Mol. Cell 2015, 57:467-478.
    • (2015) Mol. Cell , vol.57 , pp. 467-478
    • Li, M.1    Rong, Y.2    Chuang, Y.S.3    Peng, D.4    Emr, S.D.5
  • 32
    • 41949129594 scopus 로고    scopus 로고
    • Heat shock response relieves ER stress
    • Liu Y., Chang A. Heat shock response relieves ER stress. EMBO J. 2008, 27:1049-1059.
    • (2008) EMBO J. , vol.27 , pp. 1049-1059
    • Liu, Y.1    Chang, A.2
  • 33
    • 84870793680 scopus 로고    scopus 로고
    • ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology
    • Manford A.G., Stefan C.J., Yuan H.L., Macgurn J.A., Emr S.D. ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology. Dev. Cell 2012, 23:1129-1140.
    • (2012) Dev. Cell , vol.23 , pp. 1129-1140
    • Manford, A.G.1    Stefan, C.J.2    Yuan, H.L.3    Macgurn, J.A.4    Emr, S.D.5
  • 35
    • 84934449988 scopus 로고    scopus 로고
    • Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus
    • Mochida K., Oikawa Y., Kimura Y., Kirisako H., Hirano H., Ohsumi Y., Nakatogawa H. Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus. Nature 2015, 522:359-362.
    • (2015) Nature , vol.522 , pp. 359-362
    • Mochida, K.1    Oikawa, Y.2    Kimura, Y.3    Kirisako, H.4    Hirano, H.5    Ohsumi, Y.6    Nakatogawa, H.7
  • 36
    • 58149290227 scopus 로고    scopus 로고
    • Trans-Golgi network and endosome dynamics connect ceramide homeostasis with regulation of the unfolded protein response and TOR signaling in yeast
    • Mousley C.J., Tyeryar K., Ile K.E., Schaaf G., Brost R.L., Boone C., Guan X., Wenk M.R., Bankaitis V.A. Trans-Golgi network and endosome dynamics connect ceramide homeostasis with regulation of the unfolded protein response and TOR signaling in yeast. Mol. Biol. Cell 2008, 19:4785-4803.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4785-4803
    • Mousley, C.J.1    Tyeryar, K.2    Ile, K.E.3    Schaaf, G.4    Brost, R.L.5    Boone, C.6    Guan, X.7    Wenk, M.R.8    Bankaitis, V.A.9
  • 37
    • 0024395160 scopus 로고
    • S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
    • Normington K., Kohno K., Kozutsumi Y., Gething M.J., Sambrook J. S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 1989, 57:1223-1236.
    • (1989) Cell , vol.57 , pp. 1223-1236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.J.4    Sambrook, J.5
  • 39
    • 34547216748 scopus 로고    scopus 로고
    • A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum
    • Ploegh H.L. A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum. Nature 2007, 448:435-438.
    • (2007) Nature , vol.448 , pp. 435-438
    • Ploegh, H.L.1
  • 41
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants
    • Raymond C.K., Howald-Stevenson I., Vater C.A., Stevens T.H. Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol. Biol. Cell 1992, 3:1389-1402.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 42
    • 0027973135 scopus 로고
    • A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins
    • Rusiñol A.E., Cui Z., Chen M.H., Vance J.E. A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins. J. Biol. Chem. 1994, 269:27494-27502.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27494-27502
    • Rusiñol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 45
    • 18544408439 scopus 로고    scopus 로고
    • IRE1- and HAC1-independent transcriptional regulation in the unfolded protein response of yeast
    • Schröder M., Clark R., Kaufman R.J. IRE1- and HAC1-independent transcriptional regulation in the unfolded protein response of yeast. Mol. Microbiol. 2003, 49:591-606.
    • (2003) Mol. Microbiol. , vol.49 , pp. 591-606
    • Schröder, M.1    Clark, R.2    Kaufman, R.J.3
  • 46
    • 84907042769 scopus 로고    scopus 로고
    • ER-phagy mediates selective degradation of endoplasmic reticulum independently of the core autophagy machinery
    • Schuck S., Gallagher C.M., Walter P. ER-phagy mediates selective degradation of endoplasmic reticulum independently of the core autophagy machinery. J. Cell Sci. 2014, 127:4078-4088.
    • (2014) J. Cell Sci. , vol.127 , pp. 4078-4088
    • Schuck, S.1    Gallagher, C.M.2    Walter, P.3
  • 47
    • 84901851577 scopus 로고    scopus 로고
    • The ESCRT machinery: from the plasma membrane to endosomes and back again
    • Schuh A.L., Audhya A. The ESCRT machinery: from the plasma membrane to endosomes and back again. Crit. Rev. Biochem. Mol. Biol. 2014, 49:242-261.
    • (2014) Crit. Rev. Biochem. Mol. Biol. , vol.49 , pp. 242-261
    • Schuh, A.L.1    Audhya, A.2
  • 48
    • 79960610118 scopus 로고    scopus 로고
    • REVIGO summarizes and visualizes long lists of gene ontology terms
    • Supek F., Bošnjak M., Škunca N., Šmuc T. REVIGO summarizes and visualizes long lists of gene ontology terms. PLoS ONE 2011, 6:e21800.
    • (2011) PLoS ONE , vol.6 , pp. e21800
    • Supek, F.1    Bošnjak, M.2    Škunca, N.3    Šmuc, T.4
  • 50
    • 0035503594 scopus 로고    scopus 로고
    • The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
    • Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y. The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation. EMBO J. 2001, 20:5971-5981.
    • (2001) EMBO J. , vol.20 , pp. 5971-5981
    • Suzuki, K.1    Kirisako, T.2    Kamada, Y.3    Mizushima, N.4    Noda, T.5    Ohsumi, Y.6
  • 52
    • 70350418594 scopus 로고    scopus 로고
    • Depletion of phosphatidylcholine affects endoplasmic reticulum morphology and protein traffic at the Golgi complex
    • Testerink N., van der Sanden M.H.M., Houweling M., Helms J.B., Vaandrager A.B. Depletion of phosphatidylcholine affects endoplasmic reticulum morphology and protein traffic at the Golgi complex. J. Lipid Res. 2009, 50:2182-2192.
    • (2009) J. Lipid Res. , vol.50 , pp. 2182-2192
    • Testerink, N.1    van der Sanden, M.H.M.2    Houweling, M.3    Helms, J.B.4    Vaandrager, A.B.5
  • 53
    • 84867400127 scopus 로고    scopus 로고
    • The membrane stress response buffers lethal effects of lipid disequilibrium by reprogramming the protein homeostasis network
    • Thibault G., Shui G., Kim W., McAlister G.C., Ismail N., Gygi S.P., Wenk M.R., Ng D.T.W. The membrane stress response buffers lethal effects of lipid disequilibrium by reprogramming the protein homeostasis network. Mol. Cell 2012, 48:16-27.
    • (2012) Mol. Cell , vol.48 , pp. 16-27
    • Thibault, G.1    Shui, G.2    Kim, W.3    McAlister, G.C.4    Ismail, N.5    Gygi, S.P.6    Wenk, M.R.7    Ng, D.T.W.8
  • 56
    • 22144463880 scopus 로고    scopus 로고
    • Metabolism and functions of phosphatidylserine
    • Vance J.E., Steenbergen R. Metabolism and functions of phosphatidylserine. Prog. Lipid Res. 2005, 44:207-234.
    • (2005) Prog. Lipid Res. , vol.44 , pp. 207-234
    • Vance, J.E.1    Steenbergen, R.2
  • 57
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar S.S., Brodsky J.L. One step at a time: endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 2008, 9:944-957.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 58
    • 85060748714 scopus 로고    scopus 로고
    • Ratiometric biosensors that measure mitochondrial redox state and ATP in living yeast cells
    • Vevea J.D., Wolken D.M., Swayne T.C., White A.B., Pon L.A. Ratiometric biosensors that measure mitochondrial redox state and ATP in living yeast cells. J. Vis. Exp. 2013, (77).
    • (2013) J. Vis. Exp. , Issue.77
    • Vevea, J.D.1    Wolken, D.M.2    Swayne, T.C.3    White, A.B.4    Pon, L.A.5
  • 59
    • 0031553041 scopus 로고    scopus 로고
    • Phosphatidylserine decarboxylase
    • Voelker D.R. Phosphatidylserine decarboxylase. Biochim. Biophys. Acta 1997, 1348:236-244.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 236-244
    • Voelker, D.R.1
  • 60
    • 84875242776 scopus 로고    scopus 로고
    • Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains
    • Volmer R., van der Ploeg K., Ron D. Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains. Proc. Natl. Acad. Sci. USA 2013, 110:4628-4633.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 4628-4633
    • Volmer, R.1    van der Ploeg, K.2    Ron, D.3
  • 62
    • 79955488489 scopus 로고    scopus 로고
    • A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature
    • West M., Zurek N., Hoenger A., Voeltz G.K. A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature. J. Cell Biol. 2011, 193:333-346.
    • (2011) J. Cell Biol. , vol.193 , pp. 333-346
    • West, M.1    Zurek, N.2    Hoenger, A.3    Voeltz, G.K.4
  • 63
    • 84863238103 scopus 로고    scopus 로고
    • Monodansylpentane as a blue-fluorescent lipid-droplet marker for multi-color live-cell imaging
    • Yang H.-J., Hsu C.-L., Yang J.-Y., Yang W.Y. Monodansylpentane as a blue-fluorescent lipid-droplet marker for multi-color live-cell imaging. PLoS ONE 2012, 7:e32693.
    • (2012) PLoS ONE , vol.7 , pp. e32693
    • Yang, H.-J.1    Hsu, C.-L.2    Yang, J.-Y.3    Yang, W.Y.4


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