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Volumn 209, Issue 4, 2015, Pages 539-548

Ltc1 is an ER-localized sterol transporter and a component of ER-mitochondria and ER-vacuole contacts

Author keywords

[No Author keywords available]

Indexed keywords

FKS 1 PROTEIN; GEM 1 PROTEIN; LSP 1 PROTEIN; LTC 1 PROTEIN; MDM 10 PROTEIN; MDM 12 PROTEIN; MDM 34 PROTEIN; MITOCHONDRIAL PROTEIN; MMM 1 PROTEIN; MSC 7 PROTEIN; MYO 2 PROTEIN; PBN1 PROTEIN; PHO 84 PROTEIN; POR 1 PROTEIN; PROTEIN; SPT 10 PROTEIN; STEROL; TOM 71 PROTEIN; UNCLASSIFIED DRUG; VAC 8 PROTEIN; VTC 1 PROTEIN; YLR072W PROTEIN; ANTIPORTER; ERGOSTEROL; LTC1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; STEROL REGULATORY ELEMENT BINDING PROTEIN 2;

EID: 84951019875     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201502033     Document Type: Article
Times cited : (216)

References (53)
  • 1
    • 27644467457 scopus 로고    scopus 로고
    • Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae
    • Altmann, K., and B. Westermann. 2005. Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol. Biol. Cell. 16:5410-5417. http://dx.doi.org/10.1091/mbc.E05-07-0678
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 5410-5417
    • Altmann, K.1    Westermann, B.2
  • 2
    • 70449232257 scopus 로고
    • Colorimetric assay methods for free and phosphorylated glyceric acids
    • Bartlett, G.R. 1959. Colorimetric assay methods for free and phosphorylated glyceric acids. J. Biol. Chem. 234:469-471.
    • (1959) J. Biol. Chem. , vol.234 , pp. 469-471
    • Bartlett, G.R.1
  • 3
    • 0346156077 scopus 로고    scopus 로고
    • Crystal structure of a phosphoinositide phosphatase, MTMR2: insights into myotubular myopathy and Charcot-Marie-Tooth syndrome
    • Begley, M.J., G.S. Taylor, S.A. Kim, D.M. Veine, J.E. Dixon, and J.A. Stuckey. 2003. Crystal structure of a phosphoinositide phosphatase, MTMR2: insights into myotubular myopathy and Charcot-Marie-Tooth syndrome. Mol. Cell. 12:1391-1402. http://dx.doi.org/10.1016/S1097-2765(03)00486-6
    • (2003) Mol. Cell. , vol.12 , pp. 1391-1402
    • Begley, M.J.1    Taylor, G.S.2    Kim, S.A.3    Veine, D.M.4    Dixon, J.E.5    Stuckey, J.A.6
  • 4
    • 84860501617 scopus 로고    scopus 로고
    • Plasma membrane stress induces relocalization of Slm proteins and activation of TORC2 to promote sphingolipid synthesis
    • Berchtold, D., M. Piccolis, N. Chiaruttini, I. Riezman, H. Riezman, A. Roux, T.C. Walther, and R. Loewith. 2012. Plasma membrane stress induces relocalization of Slm proteins and activation of TORC2 to promote sphingolipid synthesis. Nat. Cell Biol. 14:542-547. http://dx.doi.org/10.1038/ncb2480
    • (2012) Nat. Cell Biol. , vol.14 , pp. 542-547
    • Berchtold, D.1    Piccolis, M.2    Chiaruttini, N.3    Riezman, I.4    Riezman, H.5    Roux, A.6    Walther, T.C.7    Loewith, R.8
  • 5
    • 84894326290 scopus 로고    scopus 로고
    • Mitochondrial ER contacts are crucial for mitophagy in yeast
    • Böckler, S., and B. Westermann. 2014. Mitochondrial ER contacts are crucial for mitophagy in yeast. Dev. Cell. 28:450-458. http://dx.doi.org/10.1016/j.devcel.2014.01.012
    • (2014) Dev. Cell. , vol.28 , pp. 450-458
    • Böckler, S.1    Westermann, B.2
  • 7
    • 0034306454 scopus 로고    scopus 로고
    • GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins
    • Doerks, T., M. Strauss, M. Brendel, and P. Bork. 2000. GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Trends Biochem. Sci. 25:483-485. http://dx.doi.org/10.1016/S0968-0004(00)01664-9
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 483-485
    • Doerks, T.1    Strauss, M.2    Brendel, M.3    Bork, P.4
  • 8
    • 21244448694 scopus 로고    scopus 로고
    • The TOR and EGO protein complexes orchestrate microautophagy in yeast
    • Dubouloz, F., O. Deloche, V. Wanke, E. Cameroni, and C. De Virgilio. 2005. The TOR and EGO protein complexes orchestrate microautophagy in yeast. Mol. Cell. 19:15-26. http://dx.doi.org/10.1016/j.molcel.2005.05.020
    • (2005) Mol. Cell. , vol.19 , pp. 15-26
    • Dubouloz, F.1    Deloche, O.2    Wanke, V.3    Cameroni, E.4    De Virgilio, C.5
  • 10
    • 84884487128 scopus 로고    scopus 로고
    • ER exit sites are physical and functional core autophagosome biogenesis components
    • Graef, M., J.R. Friedman, C. Graham, M. Babu, and J. Nunnari. 2013. ER exit sites are physical and functional core autophagosome biogenesis components. Mol. Biol. Cell. 24:2918-2931. http://dx.doi.org/10.1091/mbc.E13-07-0381
    • (2013) Mol. Biol. Cell. , vol.24 , pp. 2918-2931
    • Graef, M.1    Friedman, J.R.2    Graham, C.3    Babu, M.4    Nunnari, J.5
  • 11
    • 49549084586 scopus 로고    scopus 로고
    • Ligand binding by repeat proteins: natural and designed
    • Grove, T.Z., A.L. Cortajarena, and L. Regan. 2008. Ligand binding by repeat proteins: natural and designed. Curr. Opin. Struct. Biol. 18:507-515. http://dx.doi.org/10.1016/j.sbi.2008.05.008
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 507-515
    • Grove, T.Z.1    Cortajarena, A.L.2    Regan, L.3
  • 12
    • 0025035851 scopus 로고
    • Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70
    • Hines, V., A. Brandt, G. Griffiths, H. Horstmann, H. Brütsch, and G. Schatz. 1990. Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70. EMBO J. 9:3191-3200.
    • (1990) EMBO J. , vol.9 , pp. 3191-3200
    • Hines, V.1    Brandt, A.2    Griffiths, G.3    Horstmann, H.4    Brütsch, H.5    Schatz, G.6
  • 14
    • 84871011474 scopus 로고    scopus 로고
    • An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast
    • Hughes, A.L., and D.E. Gottschling. 2012. An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast. Nature. 492:261-265. http://dx.doi.org/10.1038/nature11654
    • (2012) Nature. , vol.492 , pp. 261-265
    • Hughes, A.L.1    Gottschling, D.E.2
  • 15
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley, L.A., and M.J. Sternberg. 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4:363-371. http://dx.doi.org/10.1038/nprot.2009.2
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 16
    • 84902916356 scopus 로고    scopus 로고
    • Identification and phylogenetic analyses of VASt, an uncharacterized protein domain associated with lipid-binding domains in Eukaryotes
    • Khafif, M., L. Cottret, C. Balagué, and S. Raffaele. 2014. Identification and phylogenetic analyses of VASt, an uncharacterized protein domain associated with lipid-binding domains in Eukaryotes. BMC Bioinformatics. 15:222. http://dx.doi.org/10.1186/1471-2105-15-222
    • (2014) BMC Bioinformatics. , vol.15 , pp. 222
    • Khafif, M.1    Cottret, L.2    Balagué, C.3    Raffaele, S.4
  • 17
    • 37849015898 scopus 로고    scopus 로고
    • Tetratricopeptide repeat proteins Tom70 and Tom71 mediate yeast mitochondrial morphogenesis
    • Kondo-Okamoto, N., J.M. Shaw, and K. Okamoto. 2008. Tetratricopeptide repeat proteins Tom70 and Tom71 mediate yeast mitochondrial morphogenesis. EMBO Rep. 9:63-69. http://dx.doi.org/10.1038/sj.embor.7401113
    • (2008) EMBO Rep. , vol.9 , pp. 63-69
    • Kondo-Okamoto, N.1    Shaw, J.M.2    Okamoto, K.3
  • 18
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondria tethering complex revealed by a synthetic biology screen
    • Kornmann, B., E. Currie, S.R. Collins, M. Schuldiner, J. Nunnari, J.S. Weissman, and P. Walter. 2009. An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science. 325:477-481. http://dx.doi.org/10.1126/science.1175088
    • (2009) Science. , vol.325 , pp. 477-481
    • Kornmann, B.1    Currie, E.2    Collins, S.R.3    Schuldiner, M.4    Nunnari, J.5    Weissman, J.S.6    Walter, P.7
  • 19
    • 80052172908 scopus 로고    scopus 로고
    • The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections
    • Kornmann, B., C. Osman, and P. Walter. 2011. The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections. Proc. Natl. Acad. Sci. USA. 108:14151-14156. http://dx.doi.org/10.1073/pnas.1111314108
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 14151-14156
    • Kornmann, B.1    Osman, C.2    Walter, P.3
  • 20
    • 84873460115 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated mitochondria-cortex tether functions in the distribution and inheritance of mitochondria
    • Lackner, L.L., H. Ping, M. Graef, A. Murley, and J. Nunnari. 2013. Endoplasmic reticulum-associated mitochondria-cortex tether functions in the distribution and inheritance of mitochondria. Proc. Natl. Acad. Sci. USA. 110:E458-E467. http://dx.doi.org/10.1073/pnas.1215232110
    • (2013) Proc. Natl. Acad. Sci. USA. , vol.110 , pp. E458-E467
    • Lackner, L.L.1    Ping, H.2    Graef, M.3    Murley, A.4    Nunnari, J.5
  • 21
    • 84920413092 scopus 로고    scopus 로고
    • A conserved endoplasmic reticulum membrane protein complex (EMC) facilitates phospholipid transfer from the ER to mitochondria
    • Lahiri, S., J.T. Chao, S. Tavassoli, A.K. Wong, V. Choudhary, B.P. Young, C.J. Loewen, and W.A. Prinz. 2014. A conserved endoplasmic reticulum membrane protein complex (EMC) facilitates phospholipid transfer from the ER to mitochondria. PLoS Biol. 12:e1001969. http://dx.doi.org/10.1371/journal.pbio.1001969
    • (2014) PLoS Biol. , vol.12
    • Lahiri, S.1    Chao, J.T.2    Tavassoli, S.3    Wong, A.K.4    Choudhary, V.5    Young, B.P.6    Loewen, C.J.7    Prinz, W.A.8
  • 22
    • 69949142739 scopus 로고    scopus 로고
    • Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading
    • Li, J., X. Qian, J. Hu, and B. Sha. 2009. Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading. J. Biol. Chem. 284:23852-23859. http://dx.doi.org/10.1074/jbc.M109.023986
    • (2009) J. Biol. Chem. , vol.284 , pp. 23852-23859
    • Li, J.1    Qian, X.2    Hu, J.3    Sha, B.4
  • 23
    • 33646424635 scopus 로고    scopus 로고
    • The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function
    • Madrid, A.S., J. Mancuso, W.Z. Cande, and K. Weis. 2006. The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function. J. Cell Biol. 173:361-371. http://dx.doi.org/10.1083/jcb.200506199
    • (2006) J. Cell Biol. , vol.173 , pp. 361-371
    • Madrid, A.S.1    Mancuso, J.2    Cande, W.Z.3    Weis, K.4
  • 24
    • 84868146597 scopus 로고    scopus 로고
    • A transcriptome-wide screen for mRNAs enriched in fetal Leydig cells: CRHR1 agonism stimulates rat and mouse fetal testis steroidogenesis
    • McDowell, E.N., A.E. Kisielewski, J.W. Pike, H.L. Franco, H.H. Yao, and K.J. Johnson. 2012. A transcriptome-wide screen for mRNAs enriched in fetal Leydig cells: CRHR1 agonism stimulates rat and mouse fetal testis steroidogenesis. PLoS ONE. 7:e47359. http://dx.doi.org/10.1371/journal.pone.0047359
    • (2012) PLoS ONE. , vol.7
    • McDowell, E.N.1    Kisielewski, A.E.2    Pike, J.W.3    Franco, H.L.4    Yao, H.H.5    Johnson, K.J.6
  • 25
    • 51849144648 scopus 로고    scopus 로고
    • The luminal N-terminus of yeast Nvj1 is an inner nuclear membrane anchor
    • Millen, J.I., J. Pierson, E. Kvam, L.J. Olsen, and D.S. Goldfarb. 2008. The luminal N-terminus of yeast Nvj1 is an inner nuclear membrane anchor. Traffic. 9:1653-1664. http://dx.doi.org/10.1111/j.1600-0854.2008.00789.x
    • (2008) Traffic. , vol.9 , pp. 1653-1664
    • Millen, J.I.1    Pierson, J.2    Kvam, E.3    Olsen, L.J.4    Goldfarb, D.S.5
  • 26
    • 84879059164 scopus 로고    scopus 로고
    • ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast
    • Murley, A., L.L. Lackner, C. Osman, M. West, G.K. Voeltz, P. Walter, and J. Nunnari. 2013. ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast. eLife. 2:e00422. http://dx.doi.org/10.7554/eLife.00422
    • (2013) eLife , vol.2
    • Murley, A.1    Lackner, L.L.2    Osman, C.3    West, M.4    Voeltz, G.K.5    Walter, P.6    Nunnari, J.7
  • 27
    • 84857131380 scopus 로고    scopus 로고
    • Plasma membrane recruitment and activation of the AGC kinase Ypk1 is mediated by target of rapamycin complex 2 (TORC2) and its effector proteins Slm1 and Slm2
    • Niles, B.J., H. Mogri, A. Hill, A. Vlahakis, and T. Powers. 2012. Plasma membrane recruitment and activation of the AGC kinase Ypk1 is mediated by target of rapamycin complex 2 (TORC2) and its effector proteins Slm1 and Slm2. Proc. Natl. Acad. Sci. USA. 109:1536-1541. http://dx.doi.org/10.1073/pnas.1117563109
    • (2012) Proc. Natl. Acad. Sci. USA. , vol.109 , pp. 1536-1541
    • Niles, B.J.1    Mogri, H.2    Hill, A.3    Vlahakis, A.4    Powers, T.5
  • 28
    • 79959907600 scopus 로고    scopus 로고
    • The eisosome core is composed of BAR domain proteins
    • Olivera-Couto, A., M. Graña, L. Harispe, and P.S. Aguilar. 2011. The eisosome core is composed of BAR domain proteins. Mol. Biol. Cell. 22:2360-2372. http://dx.doi.org/10.1091/mbc.E10-12-1021
    • (2011) Mol. Biol. Cell. , vol.22 , pp. 2360-2372
    • Olivera-Couto, A.1    Graña, M.2    Harispe, L.3    Aguilar, P.S.4
  • 29
    • 0033944449 scopus 로고    scopus 로고
    • Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p
    • Pan, X., P. Roberts, Y. Chen, E. Kvam, N. Shulga, K. Huang, S. Lemmon, and D.S. Goldfarb. 2000. Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p. Mol. Biol. Cell. 11:2445-2457. http://dx.doi.org/10.1091/mbc.11.7.2445
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 2445-2457
    • Pan, X.1    Roberts, P.2    Chen, Y.3    Kvam, E.4    Shulga, N.5    Huang, K.6    Lemmon, S.7    Goldfarb, D.S.8
  • 32
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein, R.J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202-211. http://dx.doi.org/10.1016/0076-6879(83)01015-0
    • (1983) Methods Enzymol. , vol.101 , pp. 202-211
    • Rothstein, R.J.1
  • 34
    • 0029994354 scopus 로고    scopus 로고
    • Tom71, a novel homologue of the mitochondrial preprotein receptor Tom70
    • Schlossmann, J., R. Lill, W. Neupert, and D.A. Court. 1996. Tom71, a novel homologue of the mitochondrial preprotein receptor Tom70. J. Biol. Chem. 271:17890-17895. http://dx.doi.org/10.1074/jbc.271.30.17890
    • (1996) J. Biol. Chem. , vol.271 , pp. 17890-17895
    • Schlossmann, J.1    Lill, R.2    Neupert, W.3    Court, D.A.4
  • 35
    • 77956090193 scopus 로고    scopus 로고
    • Mitochondrial protein import: from proteomics to functional mechanisms
    • Schmidt, O., N. Pfanner, and C. Meisinger. 2010. Mitochondrial protein import: from proteomics to functional mechanisms. Nat. Rev. Mol. Cell Biol. 11:655-667. http://dx.doi.org/10.1038/nrm2959
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 37
    • 74049122402 scopus 로고    scopus 로고
    • Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues
    • Schulz, T.A., M.G. Choi, S. Raychaudhuri, J.A. Mears, R. Ghirlando, J.E. Hinshaw, and W.A. Prinz. 2009. Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues. J. Cell Biol. 187:889-903. http://dx.doi.org/10.1083/jcb.200905007
    • (2009) J. Cell Biol. , vol.187 , pp. 889-903
    • Schulz, T.A.1    Choi, M.G.2    Raychaudhuri, S.3    Mears, J.A.4    Ghirlando, R.5    Hinshaw, J.E.6    Prinz, W.A.7
  • 38
    • 3042722112 scopus 로고    scopus 로고
    • Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae
    • Sheff, M.A., and K.S. Thorn. 2004. Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae. Yeast. 21:661-670. http://dx.doi.org/10.1002/yea.1130
    • (2004) Yeast. , vol.21 , pp. 661-670
    • Sheff, M.A.1    Thorn, K.S.2
  • 39
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics. , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 40
    • 0025327946 scopus 로고
    • A mitochondrial import receptor for the ADP/ATP carrier
    • Söllner, T., R. Pfaller, G. Griffiths, N. Pfanner, and W. Neupert. 1990. A mitochondrial import receptor for the ADP/ATP carrier. Cell. 62:107-115. http://dx.doi.org/10.1016/0092-8674(90)90244-9
    • (1990) Cell. , vol.62 , pp. 107-115
    • Söllner, T.1    Pfaller, R.2    Griffiths, G.3    Pfanner, N.4    Neupert, W.5
  • 44
    • 84883411824 scopus 로고    scopus 로고
    • Mcp1 and Mcp2, two novel proteins involved in mitochondrial lipid homeostasis
    • Tan, T., C. Ozbalci, B. Brügger, D. Rapaport, and K.S. Dimmer. 2013. Mcp1 and Mcp2, two novel proteins involved in mitochondrial lipid homeostasis. J. Cell Sci. 126:3563-3574. http://dx.doi.org/10.1242/jcs.121244
    • (2013) J. Cell Sci. , vol.126 , pp. 3563-3574
    • Tan, T.1    Ozbalci, C.2    Brügger, B.3    Rapaport, D.4    Dimmer, K.S.5
  • 45
    • 33748527156 scopus 로고    scopus 로고
    • Vac8p, an armadillo repeat protein, coordinates vacuole inheritance with multiple vacuolar processes
    • Tang, F., Y. Peng, J.J. Nau, E.J. Kauffman, and L.S. Weisman. 2006. Vac8p, an armadillo repeat protein, coordinates vacuole inheritance with multiple vacuolar processes. Traffic. 7:1368-1377. http://dx.doi.org/10.1111/j.1600-0854.2006.00458.x
    • (2006) Traffic. , vol.7 , pp. 1368-1377
    • Tang, F.1    Peng, Y.2    Nau, J.J.3    Kauffman, E.J.4    Weisman, L.S.5
  • 46
    • 84858123139 scopus 로고    scopus 로고
    • A conserved membrane-binding domain targets proteins to organelle contact sites
    • Toulmay, A., and W.A. Prinz. 2012. A conserved membrane-binding domain targets proteins to organelle contact sites. J. Cell Sci. 125:49-58. http://dx.doi.org/10.1242/jcs.085118
    • (2012) J. Cell Sci. , vol.125 , pp. 49-58
    • Toulmay, A.1    Prinz, W.A.2
  • 47
    • 84880596969 scopus 로고    scopus 로고
    • Direct imaging reveals stable, micrometerscale lipid domains that segregate proteins in live cells
    • Toulmay, A., and W.A. Prinz. 2013. Direct imaging reveals stable, micrometerscale lipid domains that segregate proteins in live cells. J. Cell Biol. 202:35-44. http://dx.doi.org/10.1083/jcb.201301039
    • (2013) J. Cell Biol. , vol.202 , pp. 35-44
    • Toulmay, A.1    Prinz, W.A.2
  • 48
    • 0035876373 scopus 로고    scopus 로고
    • Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion
    • Veit, M., R. Laage, L. Dietrich, L. Wang, and C. Ungermann. 2001. Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion. EMBO J. 20:3145-3155. http://dx.doi.org/10.1093/emboj/20.12.3145
    • (2001) EMBO J. , vol.20 , pp. 3145-3155
    • Veit, M.1    Laage, R.2    Dietrich, L.3    Wang, L.4    Ungermann, C.5
  • 49
    • 84905981861 scopus 로고    scopus 로고
    • A sterol-enriched vacuolar microdomain mediates stationary phase lipophagy in budding yeast
    • Wang, C.W., Y.H. Miao, and Y.S. Chang. 2014. A sterol-enriched vacuolar microdomain mediates stationary phase lipophagy in budding yeast. J. Cell Biol. 206:357-366. http://dx.doi.org/10.1083/jcb.201404115
    • (2014) J. Cell Biol. , vol.206 , pp. 357-366
    • Wang, C.W.1    Miao, Y.H.2    Chang, Y.S.3
  • 50
    • 0032498794 scopus 로고    scopus 로고
    • Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole
    • Wang, Y.X., N.L. Catlett, and L.S. Weisman. 1998. Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. J. Cell Biol. 140:1063-1074. http://dx.doi.org/10.1083/jcb.140.5.1063
    • (1998) J. Cell Biol. , vol.140 , pp. 1063-1074
    • Wang, Y.X.1    Catlett, N.L.2    Weisman, L.S.3
  • 51
    • 0033672549 scopus 로고    scopus 로고
    • Mitochondria-targeted green fluorescent proteins: convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae
    • Westermann, B., and W. Neupert. 2000. Mitochondria-targeted green fluorescent proteins: convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae. Yeast. 16:1421-1427. http://dx.doi.org/10.1002/1097-0061(200011)16:15<1421::AID-YEA624>3.0.CO;2-U
    • (2000) Yeast. , vol.16 , pp. 1421-1427
    • Westermann, B.1    Neupert, W.2
  • 52
    • 33745841363 scopus 로고    scopus 로고
    • Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p
    • Wu, Y., and B. Sha. 2006. Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p. Nat. Struct. Mol. Biol. 13:589-593. http://dx.doi.org/10.1038/nsmb1106
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 589-593
    • Wu, Y.1    Sha, B.2
  • 53
    • 84925156346 scopus 로고    scopus 로고
    • The I-TASSER Suite: protein structure and function prediction
    • Yang, J., R. Yan, A. Roy, D. Xu, J. Poisson, and Y. Zhang. 2015. The I-TASSER Suite: protein structure and function prediction. Nat. Methods. 12:7-8. http://dx.doi.org/10.1038/nmeth.3213
    • (2015) Nat. Methods. , vol.12 , pp. 7-8
    • Yang, J.1    Yan, R.2    Roy, A.3    Xu, D.4    Poisson, J.5    Zhang, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.