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Volumn 192, Issue 3, 2011, Pages 447-462

Barth syndrome mutations that cause tafazzin complex lability

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; NUCLEAR PROTEIN; PROTEINASE; TAFAZZIN; UNCLASSIFIED DRUG;

EID: 79551700415     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201008177     Document Type: Article
Times cited : (57)

References (59)
  • 3
    • 66449086494 scopus 로고    scopus 로고
    • Identification of a cardiolipin-specific phospholipase encoded by the gene CLD1 (YGR110W) in yeast
    • doi:10.1074/jbc.M805511200
    • Beranek, A., G. Rechberger, H. Knauer, H. Wolinski, S.D. Kohlwein, and R. Leber. 2009. Identification of a cardiolipin-specific phospholipase encoded by the gene CLD1 (YGR110W) in yeast. J. Biol. Chem. 284:11572-11578. doi:10.1074/jbc.M805511200
    • (2009) J. Biol. Chem. , vol.284 , pp. 11572-11578
    • Beranek, A.1    Rechberger, G.2    Knauer, H.3    Wolinski, H.4    Kohlwein, S.D.5    Leber, R.6
  • 4
    • 73549112874 scopus 로고    scopus 로고
    • The role of Coa2 in hemylation of yeast Cox1 revealed by its genetic interaction with Cox10
    • doi:10.1128/MCB.00869-09
    • Bestwick, M., O. Khalimonchuk, F. Pierrel, and D.R. Winge. 2010. The role of Coa2 in hemylation of yeast Cox1 revealed by its genetic interaction with Cox10. Mol. Cell. Biol. 30:172-185. doi:10.1128/MCB.00869-09
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 172-185
    • Bestwick, M.1    Khalimonchuk, O.2    Pierrel, F.3    Winge, D.R.4
  • 5
    • 0029963145 scopus 로고    scopus 로고
    • A novel X-linked gene, G4.5. is responsible for Barth syndrome
    • DOI 10.1038/ng0496-385
    • Bione, S., P. D'Adamo, E. Maestrini, A.K. Gedeon, P.A. Bolhuis, and D. Toniolo. 1996. A novel X-linked gene, G4.5. is responsible for Barth syndrome. Nat. Genet. 12:385-389. doi:10.1038/ng0496385 (Pubitemid 26106250)
    • (1996) Nature Genetics , vol.12 , Issue.4 , pp. 385-389
    • Bione, S.1    D'Adamo, P.2    Maestrini, E.3    Gedeon, A.K.4    Bolhuis, P.A.5    Toniolo, D.6
  • 6
    • 27644437287 scopus 로고    scopus 로고
    • Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: Implications for Barth syndrome
    • DOI 10.1091/mbc.E05-03-0256
    • Brandner, K., D.U. Mick, A.E. Frazier, R.D. Taylor, C. Meisinger, and P. Rehling. 2005. Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth Syndrome. Mol. Biol. Cell. 16:5202-5214. doi:10.1091/mbc.E05-03-0256 (Pubitemid 41566832)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.11 , pp. 5202-5214
    • Brandner, K.1    Mick, D.U.2    Frazier, A.E.3    Taylor, R.D.4    Meisinger, C.5    Rehling, P.6
  • 7
    • 77957957247 scopus 로고    scopus 로고
    • The mitochondrial proteome and human disease
    • doi:10.1146/annurev-genom-082509-141720
    • Calvo, S.E., and V.K. Mootha. 2010. The mitochondrial proteome and human disease. Annu. Rev. Genomics Hum. Genet. 11:25-44. doi:10.1146/annurev-genom- 082509-141720
    • (2010) Annu. Rev. Genomics Hum. Genet. , vol.11 , pp. 25-44
    • Calvo, S.E.1    Mootha, V.K.2
  • 9
    • 33746606474 scopus 로고    scopus 로고
    • Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins
    • DOI 10.1083/jcb.200605043
    • Claypool, S.M., J.M. McCaffery, and C.M. Koehler. 2006. Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins. J. Cell Biol. 174:379-390. doi:10.1083/jcb.200605043 (Pubitemid 44156768)
    • (2006) Journal of Cell Biology , vol.174 , Issue.3 , pp. 379-390
    • Claypool, S.M.1    McCaffery, J.M.2    Koehler, C.M.3
  • 10
    • 59449108212 scopus 로고    scopus 로고
    • The cardiolipin transacylase, tafazzin, associates with two distinct respiratory components providing insight into Barth syndrome
    • doi:10.1091/mbc.E08-09-0896
    • Claypool, S.M., P. Boontheung, J.M. McCaffery, J.A. Loo, and C.M. Koehler. 2008a. The cardiolipin transacylase, tafazzin, associates with two distinct respiratory components providing insight into Barth syndrome. Mol. Biol. Cell. 19:5143-5155. doi:10.1091/mbc.E08-09-0896
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 5143-5155
    • Claypool, S.M.1    Boontheung, P.2    McCaffery, J.M.3    Loo, J.A.4    Koehler, C.M.5
  • 11
    • 51649096941 scopus 로고    scopus 로고
    • Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane
    • doi:10.1083/jcb.200801152
    • Claypool, S.M., Y. Oktay, P. Boontheung, J.A. Loo, and C.M. Koehler. 2008b. Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane. J. Cell Biol. 182:937-950. doi:10.1083/jcb.200801152
    • (2008) J. Cell Biol. , vol.182 , pp. 937-950
    • Claypool, S.M.1    Oktay, Y.2    Boontheung, P.3    Loo, J.A.4    Koehler, C.M.5
  • 12
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum, G., P.C. Böhni, and G. Schatz. 1982. Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257:13028-13033.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Böhni, P.C.2    Schatz, G.3
  • 13
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DOI 10.1056/NEJMra022567
    • DiMauro, S., and E.A. Schon. 2003. Mitochondrial respiratory-chain diseases. N. Engl. J. Med. 348:2656-2668. doi:10.1056/NEJMra022567 (Pubitemid 36741594)
    • (2003) New England Journal of Medicine , vol.348 , Issue.26 , pp. 2656-2668
    • DiMauro, S.1    Schon, E.A.2
  • 14
    • 0017806140 scopus 로고
    • Identification of enzymically inactive apocytochrome c peroxidase in anaerobically grown Saccharomyces cerevisiae
    • Djavadi-Ohaniance, L., Y. Rudin, and G. Schatz. 1978. Identification of enzymically inactive apocytochrome c peroxidase in anaerobically grown Saccharomyces cerevisiae. J. Biol. Chem. 253:4402-4407. (Pubitemid 8384134)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.12 , pp. 4402-4407
    • Djavadi-Ohaniance, L.1    Rudin, Y.2    Schatz, G.3
  • 15
    • 30044444717 scopus 로고    scopus 로고
    • A genomewide screen for petite-negative yeast strains yields a new subunit of the i-AAA protease complex
    • DOI 10.1091/mbc.E05-06-0585
    • Dunn, C.D., M.S. Lee, F.A. Spencer, and R.E. Jensen. 2006. A genomewide screen for petite-negative yeast strains yields a new subunit of the i-AAA protease complex. Mol. Biol. Cell. 17:213-226. doi:10.1091/mbc.E05-06-0585 (Pubitemid 43049475)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.1 , pp. 213-226
    • Dunn, C.D.1    Lee, M.S.2    Spencer, F.A.3    Jensen, R.E.4
  • 16
    • 59449100177 scopus 로고    scopus 로고
    • Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex
    • doi:10.1091/mbc.E08-01-0103
    • Dunn, C.D., Y. Tamura, H. Sesaki, and R.E. Jensen. 2008. Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex. Mol. Biol. Cell. 19:5387-5397. doi:10.1091/mbc.E08-01-0103
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 5387-5397
    • Dunn, C.D.1    Tamura, Y.2    Sesaki, H.3    Jensen, R.E.4
  • 17
    • 0000041138 scopus 로고
    • Enzymic activities of human skeletal muscle mitochondria: A tool in clinical metabolic research
    • doi:10.1038/1841851a0
    • Ernster, L., D. Ikkos, and R. Luft. 1959. Enzymic activities of human skeletal muscle mitochondria: a tool in clinical metabolic research. Nature. 184:1851-1854. doi:10.1038/1841851a0
    • (1959) Nature , vol.184 , pp. 1851-1854
    • Ernster, L.1    Ikkos, D.2    Luft, R.3
  • 18
    • 72449137691 scopus 로고    scopus 로고
    • Mitochondrial cardiolipin involved in outer-membrane protein biogenesis: Implications for Barth syndrome
    • doi:10.1016/j.cub.2009.10.074
    • Gebert, N., A.S. Joshi, S. Kutik, T. Becker, M. McKenzie, X.L. Guan, V.P. Mooga, D.A. Stroud, G. Kulkarni, M.R. Wenk, et al. 2009. Mitochondrial cardiolipin involved in outer-membrane protein biogenesis: implications for Barth syndrome. Curr. Biol. 19:2133-2139. doi:10.1016/j.cub.2009.10.074
    • (2009) Curr. Biol. , vol.19 , pp. 2133-2139
    • Gebert, N.1    Joshi, A.S.2    Kutik, S.3    Becker, T.4    McKenzie, M.5    Guan, X.L.6    Mooga, V.P.7    Stroud, D.A.8    Kulkarni, G.9    Wenk, M.R.10
  • 19
    • 0026611680 scopus 로고
    • Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism
    • doi:10.1016/0092-8674(92)90292-K
    • Glick, B.S., A. Brandt, K. Cunningham, S. Müller, R.L. Hallberg, and G. Schatz. 1992. Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Cell. 69:809-822. doi:10.1016/0092-8674(92)90292-K
    • (1992) Cell. , vol.69 , pp. 809-822
    • Glick, B.S.1    Brandt, A.2    Cunningham, K.3    Müller, S.4    Hallberg, R.L.5    Schatz, G.6
  • 21
    • 41949098832 scopus 로고    scopus 로고
    • The in-depth evaluation of suspected mitochondrial disease
    • Mitochondrial Medicine Society's Committee on Diagnosis. doi:10.1016/j.ymgme.2007.11.018
    • Haas, R.H., S. Parikh, M.J. Falk, R.P. Saneto, N.I. Wolf, N. Darin, L.J. Wong, B.H. Cohen, and R.K. Naviaux; Mitochondrial Medicine Society's Committee on Diagnosis. 2008. The in-depth evaluation of suspected mitochondrial disease. Mol. Genet. Metab. 94:16-37. doi:10.1016/j.ymgme.2007.11.018
    • (2008) Mol. Genet. Metab. , vol.94 , pp. 16-37
    • Haas, R.H.1    Parikh, S.2    Falk, M.J.3    Saneto, R.P.4    Wolf, N.I.5    Darin, N.6    Wong, L.J.7    Cohen, B.H.8    Naviaux, R.K.9
  • 22
    • 18344393519 scopus 로고    scopus 로고
    • Shotgun lipidomics: Electrospray ionization mass spectrometric analysis and quantitation of cellular lipidomes directly from crude extracts of biological samples
    • DOI 10.1002/mas.20023
    • Han, X., and R.W. Gross. 2005. Shotgun lipidomics: electrospray ionization mass spectrometric analysis and quantitation of cellular lipidomes directly from crude extracts of biological samples. Mass Spectrom. Rev. 24:367-412. doi:10.1002/mas.20023 (Pubitemid 40665798)
    • (2005) Mass Spectrometry Reviews , vol.24 , Issue.3 , pp. 367-412
    • Han, X.1    Gross, R.W.2
  • 23
    • 33645522850 scopus 로고    scopus 로고
    • Shotgun lipidomics of cardiolipin molecular species in lipid extracts of biological samples
    • doi:10.1194/jlr.D500044-JLR200
    • Han, X., K. Yang, J. Yang, H. Cheng, and R.W. Gross. 2006. Shotgun lipidomics of cardiolipin molecular species in lipid extracts of biological samples. J. Lipid Res. 47:864-879. doi:10.1194/jlr.D500044-JLR200
    • (2006) J. Lipid Res. , vol.47 , pp. 864-879
    • Han, X.1    Yang, K.2    Yang, J.3    Cheng, H.4    Gross, R.W.5
  • 24
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • DOI 10.1016/0378-1119(89)90358-2
    • Ho, S.N., H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77:51-59. doi:10.1016/0378-1119(89)90358-2 (Pubitemid 19125653)
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 25
    • 0030933229 scopus 로고    scopus 로고
    • Sequential action of two hsp70 complexes during protein import into mitochondria
    • DOI 10.1093/emboj/16.8.1842
    • Horst, M., W. Oppliger, S. Rospert, H.J. Schönfeld, G. Schatz, and A. Azem. 1997. Sequential action of two hsp70 complexes during protein import into mitochondria. EMBO J. 16:1842-1849. doi:10.1093/emboj/16.8.1842 (Pubitemid 27170945)
    • (1997) EMBO Journal , vol.16 , Issue.8 , pp. 1842-1849
    • Horst, M.1    Oppliger, W.2    Rospert, S.3    Schonfeld, H.-J.4    Schatz, G.5    Azem, A.6
  • 26
    • 61849141218 scopus 로고    scopus 로고
    • Cardiolipin and monolysocardiolipin analysis in fibroblasts, lymphocytes, and tissues using high-performance liquid chromatography-mass spectrometry as a diagnostic test for Barth syndrome
    • doi:10.1016/j.ab.2009.01.032
    • Houtkooper, R.H., R.J. Rodenburg, C. Thiels, H. van Lenthe, F. Stet, B.T. Poll-The, J.E. Stone, C.G. Steward, R.J. Wanders, J. Smeitink, et al. 2009a. Cardiolipin and monolysocardiolipin analysis in fibroblasts, lymphocytes, and tissues using high-performance liquid chromatography-mass spectrometry as a diagnostic test for Barth syndrome. Anal. Biochem. 387:230-237. doi:10.1016/j.ab.2009.01.032
    • (2009) Anal. Biochem. , vol.387 , pp. 230-237
    • Houtkooper, R.H.1    Rodenburg, R.J.2    Thiels, C.3    Van Lenthe, H.4    Stet, F.5    Poll-The, B.T.6    Stone, J.E.7    Steward, C.G.8    Wanders, R.J.9    Smeitink, J.10
  • 28
    • 34748833589 scopus 로고    scopus 로고
    • Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion
    • DOI 10.1083/jcb.200706195
    • Hwang, D.K., S.M. Claypool, D. Leuenberger, H.L. Tienson, and C.M. Koehler. 2007. Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion. J. Cell Biol. 178:1161-1175. doi:10.1083/jcb.200706195 (Pubitemid 47480224)
    • (2007) Journal of Cell Biology , vol.178 , Issue.7 , pp. 1161-1175
    • Hwang, D.K.1    Claypool, S.M.2    Leuenberger, D.3    Tienson, H.L.4    Koehler, C.M.5
  • 29
    • 0032536045 scopus 로고    scopus 로고
    • Import of mitochondrial carriers mediated by essential proteins of the intermembrane space
    • DOI 10.1126/science.279.5349.369
    • Koehler, C.M., E. Jarosch, K. Tokatlidis, K. Schmid, R.J. Schweyen, and G. Schatz. 1998. Import of mitochondrial carriers mediated by essential proteins of the intermembrane space. Science. 279:369-373. doi:10.1126/science.279.5349. 369 (Pubitemid 28063370)
    • (1998) Science , vol.279 , Issue.5349 , pp. 369-373
    • Koehler, C.M.1    Jarosch, E.2    Tokatlidis, K.3    Schmid, K.4    Schweyen, R.J.5    Schatz, G.6
  • 31
    • 0029775087 scopus 로고    scopus 로고
    • AAA proteases with catalytic sites on apposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria
    • Leonhard, K., J.M. Herrmann, R.A. Stuart, G. Mannhaupt, W. Neupert, and T. Langer. 1996. AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria. EMBO J. 15:4218-4229. (Pubitemid 26278704)
    • (1996) EMBO Journal , vol.15 , Issue.16 , pp. 4218-4229
    • Leonhard, K.1    Herrmann, J.M.2    Stuart, R.A.3    Mannhaupt, G.4    Neupert, W.5    Langer, T.6
  • 32
    • 0033602381 scopus 로고    scopus 로고
    • Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
    • doi:10.1038/18704
    • Leonhard, K., A. Stiegler, W. Neupert, and T. Langer. 1999. Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease. Nature. 398:348-351. doi:10.1038/18704
    • (1999) Nature , vol.398 , pp. 348-351
    • Leonhard, K.1    Stiegler, A.2    Neupert, W.3    Langer, T.4
  • 33
    • 0028558576 scopus 로고
    • The development of mitochondrial medicine
    • doi:10.1073/pnas.91.19.8731
    • Luft, R. 1994. The development of mitochondrial medicine. Proc. Natl. Acad. Sci. USA. 91:8731-8738. doi:10.1073/pnas.91.19.8731
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8731-8738
    • Luft, R.1
  • 34
    • 78651126508 scopus 로고
    • A case of severe hypermetabolism of nonthyroid origin with a defect in the maintenance of mitochondrial respiratory control: A correlated clinical, biochemical, and morphological study
    • doi:10.1172/JCI104637
    • Luft, R., D. Ikkos, G. Palmieri, L. Ernster, and B. Afzelius. 1962. A case of severe hypermetabolism of nonthyroid origin with a defect in the maintenance of mitochondrial respiratory control: a correlated clinical, biochemical, and morphological study. J. Clin. Invest. 41:1776-1804. doi:10.1172/JCI104637
    • (1962) J. Clin. Invest. , vol.41 , pp. 1776-1804
    • Luft, R.1    Ikkos, D.2    Palmieri, G.3    Ernster, L.4    Afzelius, B.5
  • 35
    • 7244224978 scopus 로고    scopus 로고
    • The human TAZ gene complements mitochondrial dysfunction in the yeast taz1Delta mutant: Implications for Barth syndrome
    • DOI 10.1074/jbc.M405479200
    • Ma, L., F.M. Vaz, Z. Gu, R.J. Wanders, and M.L. Greenberg. 2004. The human TAZ gene complements mitochondrial dysfunction in the yeast taz1Delta mutant. Implications for Barth syndrome. J. Biol. Chem. 279:44394-44399. doi:10.1074/jbc.M405479200 (Pubitemid 39430844)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 44394-44399
    • Ma, L.1    Vaz, F.M.2    Gu, Z.3    Wanders, R.J.A.4    Greenberg, M.L.5
  • 37
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial Respiratory Chain Supercomplexes Are Destabilized in Barth Syndrome Patients
    • DOI 10.1016/j.jmb.2006.06.057, PII S0022283606007959
    • McKenzie, M., M. Lazarou, D.R. Thorburn, and M.T. Ryan. 2006. Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients. J. Mol. Biol. 361:462-469. doi:10.1016/j.jmb.2006.06.057 (Pubitemid 44118343)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.3 , pp. 462-469
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 38
    • 57749116223 scopus 로고    scopus 로고
    • Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery
    • doi:10.1074/jbc.M806424200
    • Metzger, M.B., M.J. Maurer, B.M. Dancy, and S. Michaelis. 2008. Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery. J. Biol. Chem. 283:32302-32316. doi:10.1074/jbc. M806424200
    • (2008) J. Biol. Chem. , vol.283 , pp. 32302-32316
    • Metzger, M.B.1    Maurer, M.J.2    Dancy, B.M.3    Michaelis, S.4
  • 39
    • 0020479711 scopus 로고
    • Import of proteins into mitochondria. The precursor of cytochrome c1 is processed in two steps, one of them heme-dependent
    • Ohashi, A., J. Gibson, I. Gregor, and G. Schatz. 1982. Import of proteins into mitochondria. The precursor of cytochrome c1 is processed in two steps, one of them heme-dependent. J. Biol. Chem. 257:13042-13047.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13042-13047
    • Ohashi, A.1    Gibson, J.2    Gregor, I.3    Schatz, G.4
  • 41
    • 0037225928 scopus 로고    scopus 로고
    • Choline head groups stabilize the matrix loop regions of the ATP/ADP carrier ScAAC2
    • DOI 10.1016/S0006-291X(02)02795-X, PII S0006291X0202795X
    • Panneels, V., U. Schüssler, S. Costagliola, and I. Sinning. 2003. Choline head groups stabilize the matrix loop regions of the ATP/ADP carrier ScAAC2. Biochem. Biophys. Res. Commun. 300:65-74. doi:10.1016/S0006-291X(02) 02795-X (Pubitemid 36042931)
    • (2003) Biochemical and Biophysical Research Communications , vol.300 , Issue.1 , pp. 65-74
    • Panneels, V.1    Schussler, U.2    Costagliola, S.3    Sinning, I.4
  • 42
    • 0016661083 scopus 로고
    • Cytochrome c oxidase from bakers' yeast. IV. Immunological evidence for the participation of a mitochondrially synthesized subunit in enzymatic activity
    • Poyton, R.O., and G. Schatz. 1975. Cytochrome c oxidase from bakers' yeast. IV. Immunological evidence for the participation of a mitochondrially synthesized subunit in enzymatic activity. J. Biol. Chem. 250:762-766.
    • (1975) J. Biol. Chem. , vol.250 , pp. 762-766
    • Poyton, R.O.1    Schatz, G.2
  • 44
    • 0345063375 scopus 로고
    • The outer membrane of yeast mitochondria: Isolation of outside-out sealed vesicles
    • Riezman, H., R. Hay, S. Gasser, G. Daum, G. Schneider, C. Witte, and G. Schatz. 1983. The outer membrane of yeast mitochondria: isolation of outside-out sealed vesicles. EMBO J. 2:1105-1111.
    • (1983) EMBO J. , vol.2 , pp. 1105-1111
    • Riezman, H.1    Hay, R.2    Gasser, S.3    Daum, G.4    Schneider, G.5    Witte, C.6    Schatz, G.7
  • 45
    • 0025673942 scopus 로고
    • A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein
    • Scherer, P.E., U.C. Krieg, S.T. Hwang, D. Vestweber, and G. Schatz. 1990. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein. EMBO J. 9:4315-4322. (Pubitemid 120025987)
    • (1990) EMBO Journal , vol.9 , Issue.13 , pp. 4315-4322
    • Scherer, P.E.1    Krieg, U.C.2    Hwang, S.T.3    Vestweber, D.4    Schatz, G.5
  • 46
    • 33749061065 scopus 로고    scopus 로고
    • Barth syndrome, a human disorder of cardiolipin metabolism
    • DOI 10.1016/j.febslet.2006.07.022, PII S001457930600857X
    • Schlame, M., and M. Ren. 2006. Barth syndrome, a human disorder of cardiolipin metabolism. FEBS Lett. 580:5450-5455. doi:10.1016/j.febslet.2006.07. 022 (Pubitemid 44465900)
    • (2006) FEBS Letters , vol.580 , Issue.23 , pp. 5450-5455
    • Schlame, M.1    Ren, M.2
  • 47
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • DOI 10.1016/S0163-7827(00)00005-9, PII S0163782700000059
    • Schlame, M., D. Rua, and M.L. Greenberg. 2000. The biosynthesis and functional role of cardiolipin. Prog. Lipid Res. 39:257-288. doi:10.1016/S0163-7827(00)00005-9 (Pubitemid 30224706)
    • (2000) Progress in Lipid Research , vol.39 , Issue.3 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 48
    • 27644533754 scopus 로고    scopus 로고
    • Molecular symmetry in mitochondrial cardiolipins
    • DOI 10.1016/j.chemphyslip.2005.08.002, PII S0009308405001222
    • Schlame, M., M. Ren, Y. Xu, M.L. Greenberg, and I. Haller. 2005. Molecular symmetry in mitochondrial cardiolipins. Chem. Phys. Lipids. 138:38-49. doi:10.1016/j.chemphyslip.2005.08.002 (Pubitemid 41579001)
    • (2005) Chemistry and Physics of Lipids , vol.138 , Issue.1-2 , pp. 38-49
    • Schlame, M.1    Ren, M.2    Xu, Y.3    Greenberg, M.L.4    Haller, I.5
  • 50
    • 67449138848 scopus 로고    scopus 로고
    • Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria
    • doi:10.1083/jcb.200812018
    • Tamura, Y., T. Endo, M. Iijima, and H. Sesaki. 2009. Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria. J. Cell Biol. 185:1029-1045. doi:10.1083/jcb.200812018
    • (2009) J. Cell Biol. , vol.185 , pp. 1029-1045
    • Tamura, Y.1    Endo, T.2    Iijima, M.3    Sesaki, H.4
  • 51
    • 70350064588 scopus 로고    scopus 로고
    • Protein quality control in mitochondria
    • doi:10.1093/jb/mvp122
    • Tatsuta, T. 2009. Protein quality control in mitochondria. J. Biochem. 146:455-461. doi:10.1093/jb/mvp122
    • (2009) J. Biochem. , vol.146 , pp. 455-461
    • Tatsuta, T.1
  • 52
    • 71749117953 scopus 로고    scopus 로고
    • AAA proteases in mitochondria: Diverse functions of membrane-bound proteolytic machines
    • doi:10.1016/j.resmic.2009.09.005
    • Tatsuta, T., and T. Langer. 2009. AAA proteases in mitochondria: diverse functions of membrane-bound proteolytic machines. Res. Microbiol. 160:711-717. doi:10.1016/j.resmic.2009.09.005
    • (2009) Res. Microbiol. , vol.160 , pp. 711-717
    • Tatsuta, T.1    Langer, T.2
  • 53
    • 2942562564 scopus 로고    scopus 로고
    • Mitochondrial disorders: Prevalence, myths and advances
    • DOI 10.1023/B:BOLI.0000031098.41409.55
    • Thorburn, D.R. 2004. Mitochondrial disorders: prevalence, myths and advances. J. Inherit. Metab. Dis. 27:349-362. doi:10.1023/B:BOLI.0000031098. 41409.55 (Pubitemid 38756321)
    • (2004) Journal of Inherited Metabolic Disease , vol.27 , Issue.3 , pp. 349-362
    • Thorburn, D.R.1
  • 56
    • 0242322008 scopus 로고    scopus 로고
    • Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism
    • doi:10.1074/jbc.M305956200
    • Vaz, F.M., R.H. Houtkooper, F. Valianpour, P.G. Barth, and R.J. Wanders. 2003. Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism. J. Biol. Chem. 278:43089-43094. doi:10.1074/jbc.M305956200
    • (2003) J. Biol. Chem. , vol.278 , pp. 43089-43094
    • Vaz, F.M.1    Houtkooper, R.H.2    Valianpour, F.3    Barth, P.G.4    Wanders, R.J.5
  • 57
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • doi:10.1002/yea.320101310
    • Wach, A., A. Brachat, R. Pöhlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast. 10:1793-1808. doi:10.1002/yea.320101310
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pöhlmann, R.3    Philippsen, P.4
  • 58
    • 33845983684 scopus 로고    scopus 로고
    • The enzymatic function of tafazzin
    • DOI 10.1074/jbc.M606100200
    • Xu, Y., A. Malhotra, M. Ren, and M. Schlame. 2006. The enzymatic function of tafazzin. J. Biol. Chem. 281:39217-39224. doi:10.1074/jbc.M606100200 (Pubitemid 46041881)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39217-39224
    • Xu, Y.1    Malhotra, A.2    Ren, M.3    Schlame, M.4
  • 59
    • 66349116161 scopus 로고    scopus 로고
    • Automated lipid identification and quantification by multidimensional mass spectrometrybased shotgun lipidomics
    • doi:10.1021/ac900241u
    • Yang, K., H. Cheng, R.W. Gross, and X. Han. 2009. Automated lipid identification and quantification by multidimensional mass spectrometrybased shotgun lipidomics. Anal. Chem. 81:4356-4368. doi:10.1021/ac900241u
    • (2009) Anal. Chem. , vol.81 , pp. 4356-4368
    • Yang, K.1    Cheng, H.2    Gross, R.W.3    Han, X.4


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