메뉴 건너뛰기




Volumn 1822, Issue 9, 2012, Pages 1343-1357

Fission and proliferation of peroxisomes

Author keywords

DLP1 DRP1; FIS1; Mff; Organelle dynamics; Peroxisome proliferation; Pex11

Indexed keywords

ADAPTOR PROTEIN; ETHYL CHLOROPHENOXY ISOBUTYRATE; FATTY ACID; ISOBUTYRIC ACID; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; PEROXIN 11; PEROXIN 19; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84864067919     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2011.12.014     Document Type: Review
Times cited : (155)

References (208)
  • 1
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders R.J.A., Waterham H.R. Biochemistry of mammalian peroxisomes revisited. Annu. Rev. Biochem. 2006, 75:295-332.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 295-332
    • Wanders, R.J.A.1    Waterham, H.R.2
  • 4
    • 77955259144 scopus 로고    scopus 로고
    • Peroxisomes as dynamic organelles: autophagic degradation
    • Oku M., Sakai Y. Peroxisomes as dynamic organelles: autophagic degradation. FEBS J. 2010, 277:3289-3294.
    • (2010) FEBS J. , vol.277 , pp. 3289-3294
    • Oku, M.1    Sakai, Y.2
  • 6
    • 33845503273 scopus 로고    scopus 로고
    • Growth and division of peroxisomes
    • Schrader M., Fahimi H.D. Growth and division of peroxisomes. Int. Rev. Cytol. 2006, 255:237-290.
    • (2006) Int. Rev. Cytol. , vol.255 , pp. 237-290
    • Schrader, M.1    Fahimi, H.D.2
  • 7
    • 69649097710 scopus 로고    scopus 로고
    • How peroxisomes multiply
    • Hettema E.H., Motley A.M. How peroxisomes multiply. J. Cell Sci. 2009, 122:2331-2336.
    • (2009) J. Cell Sci. , vol.122 , pp. 2331-2336
    • Hettema, E.H.1    Motley, A.M.2
  • 9
    • 73549108735 scopus 로고    scopus 로고
    • Divide et impera: the dictum of peroxisomes
    • Nagotu S., Veenhuis M., van der Klei I.J. Divide et impera: the dictum of peroxisomes. Traffic 2010, 11:175-184.
    • (2010) Traffic , vol.11 , pp. 175-184
    • Nagotu, S.1    Veenhuis, M.2    van der Klei, I.J.3
  • 10
    • 33646791462 scopus 로고    scopus 로고
    • The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER
    • Kim P.K., Mullen R.T., Schumann U., Lippincott-Schwartz J. The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER. J. Cell Biol. 2006, 173:521-532.
    • (2006) J. Cell Biol. , vol.173 , pp. 521-532
    • Kim, P.K.1    Mullen, R.T.2    Schumann, U.3    Lippincott-Schwartz, J.4
  • 11
    • 77953507085 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins insert into the endoplasmic reticulum
    • van der Zand A., Braakman I., Tabak H.F. Peroxisomal membrane proteins insert into the endoplasmic reticulum. Mol. Biol. Cell 2010, 21:2057-2065.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2057-2065
    • van der Zand, A.1    Braakman, I.2    Tabak, H.F.3
  • 12
    • 79959370908 scopus 로고    scopus 로고
    • Cell-free sorting of peroxisomal membrane proteins from the endoplasmic reticulum
    • Agrawal G., Joshi S., Subramani S. Cell-free sorting of peroxisomal membrane proteins from the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:9113-9118.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 9113-9118
    • Agrawal, G.1    Joshi, S.2    Subramani, S.3
  • 13
    • 79959777921 scopus 로고    scopus 로고
    • A vesicle carrier that mediates peroxisome protein traffic from the endoplasmic reticulum
    • Lam S.K., Yoda N., Schekman R. A vesicle carrier that mediates peroxisome protein traffic from the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:E51-E52.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108
    • Lam, S.K.1    Yoda, N.2    Schekman, R.3
  • 14
    • 0013854955 scopus 로고
    • Nature of the hepatomegalic effect produced by ethyl-chlorophenoxy-isobutyrate in the rat
    • Hess R., Staubli W., Riess W. Nature of the hepatomegalic effect produced by ethyl-chlorophenoxy-isobutyrate in the rat. Nature 1965, 208:856-858.
    • (1965) Nature , vol.208 , pp. 856-858
    • Hess, R.1    Staubli, W.2    Riess, W.3
  • 15
    • 0342528190 scopus 로고
    • A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug
    • Lazarow P.B., De Duve C. A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug. Proc. Natl. Acad. Sci. U. S. A. 1976, 73:2043-2046.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2043-2046
    • Lazarow, P.B.1    De Duve, C.2
  • 16
    • 0017284938 scopus 로고
    • Hepatocellular carcinomas in acatalasemic mice treated with nafenopin, a hypolipidemic peroxisome proliferator
    • Reddy J.K., Rao S., Moody D.E. Hepatocellular carcinomas in acatalasemic mice treated with nafenopin, a hypolipidemic peroxisome proliferator. Cancer Res. 1976, 36:1211-1217.
    • (1976) Cancer Res. , vol.36 , pp. 1211-1217
    • Reddy, J.K.1    Rao, S.2    Moody, D.E.3
  • 17
    • 77953715734 scopus 로고    scopus 로고
    • Be different-the diversity of peroxisomes in the animal kingdom
    • Islinger M., Cardoso M.J., Schrader M. Be different-the diversity of peroxisomes in the animal kingdom. Biochim. Biophys. Acta 2010, 1803:881-897.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 881-897
    • Islinger, M.1    Cardoso, M.J.2    Schrader, M.3
  • 18
    • 0026100678 scopus 로고
    • Peroxisome proliferation and nongenotoxic carcinogenesis: commentary on a symposium
    • Moody D.E., Reddy J.K., Lake B.G., Popp J.A., Reese D.H. Peroxisome proliferation and nongenotoxic carcinogenesis: commentary on a symposium. Fundam. Appl. Toxicol. 1991, 16:233-248.
    • (1991) Fundam. Appl. Toxicol. , vol.16 , pp. 233-248
    • Moody, D.E.1    Reddy, J.K.2    Lake, B.G.3    Popp, J.A.4    Reese, D.H.5
  • 19
    • 0018888058 scopus 로고
    • Hypolipidaemic hepatic peroxisome proliferators form a novel class of chemical carcinogens
    • Reddy J.K., Azarnoff D.L., Hignite C.E. Hypolipidaemic hepatic peroxisome proliferators form a novel class of chemical carcinogens. Nature 1980, 283:397-398.
    • (1980) Nature , vol.283 , pp. 397-398
    • Reddy, J.K.1    Azarnoff, D.L.2    Hignite, C.E.3
  • 20
    • 0020002341 scopus 로고
    • Hepatic and renal effects of peroxisome proliferators: biological implications
    • Reddy J.K., Warren J.R., Reddy M.K., Lalwani N.D. Hepatic and renal effects of peroxisome proliferators: biological implications. Ann. N. Y. Acad. Sci. 1982, 386:81-110.
    • (1982) Ann. N. Y. Acad. Sci. , vol.386 , pp. 81-110
    • Reddy, J.K.1    Warren, J.R.2    Reddy, M.K.3    Lalwani, N.D.4
  • 22
    • 0025132245 scopus 로고
    • Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
    • Issemann I., Green S. Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators. Nature 1990, 347:645-650.
    • (1990) Nature , vol.347 , pp. 645-650
    • Issemann, I.1    Green, S.2
  • 24
    • 78349283454 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha target genes
    • Rakhshandehroo M., Knoch B., Muller M., Kersten S. Peroxisome proliferator-activated receptor alpha target genes. PPAR Res. 2010, 2010.
    • (2010) PPAR Res. , vol.2010
    • Rakhshandehroo, M.1    Knoch, B.2    Muller, M.3    Kersten, S.4
  • 25
    • 0027278522 scopus 로고
    • Positive regulation of the peroxisomal beta-oxidation pathway by fatty acids through activation of peroxisome proliferator-activated receptors (PPAR)
    • Dreyer C., Keller H., Mahfoudi A., Laudet V., Krey G., Wahli W. Positive regulation of the peroxisomal beta-oxidation pathway by fatty acids through activation of peroxisome proliferator-activated receptors (PPAR). Biol. Cell 1993, 77:67-76.
    • (1993) Biol. Cell , vol.77 , pp. 67-76
    • Dreyer, C.1    Keller, H.2    Mahfoudi, A.3    Laudet, V.4    Krey, G.5    Wahli, W.6
  • 26
    • 0030841938 scopus 로고    scopus 로고
    • Recent update on the PPAR alpha-null mouse
    • Gonzalez F.J. Recent update on the PPAR alpha-null mouse. Biochimie 1997, 79:139-144.
    • (1997) Biochimie , vol.79 , pp. 139-144
    • Gonzalez, F.J.1
  • 27
    • 0028997684 scopus 로고
    • Targeted disruption of the alpha isoform of the peroxisome proliferator-activated receptor gene in mice results in abolishment of the pleiotropic effects of peroxisome proliferators
    • Lee S.S., Pineau T., Drago J., Lee E.J., Owens J.W., Kroetz D.L., Fernandez-Salguero P.M., Westphal H., Gonzalez F.J. Targeted disruption of the alpha isoform of the peroxisome proliferator-activated receptor gene in mice results in abolishment of the pleiotropic effects of peroxisome proliferators. Mol. Cell. Biol. 1995, 15:3012-3022.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3012-3022
    • Lee, S.S.1    Pineau, T.2    Drago, J.3    Lee, E.J.4    Owens, J.W.5    Kroetz, D.L.6    Fernandez-Salguero, P.M.7    Westphal, H.8    Gonzalez, F.J.9
  • 28
    • 0036882106 scopus 로고    scopus 로고
    • PEX11alpha is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation
    • Li X., Baumgart E., Dong G.X., Morrell J.C., Jimenez-Sanchez G., Valle D., Smith K.D., Gould S.J. PEX11alpha is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation. Mol. Cell. Biol. 2002, 22:8226-8240.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8226-8240
    • Li, X.1    Baumgart, E.2    Dong, G.X.3    Morrell, J.C.4    Jimenez-Sanchez, G.5    Valle, D.6    Smith, K.D.7    Gould, S.J.8
  • 29
    • 0029994543 scopus 로고    scopus 로고
    • Role of the peroxisome proliferator-activated receptor (PPAR) in mediating the effects of fibrates and fatty acids on gene expression
    • Schoonjans K., Staels B., Auwerx J. Role of the peroxisome proliferator-activated receptor (PPAR) in mediating the effects of fibrates and fatty acids on gene expression. J. Lipid Res. 1996, 37:907-925.
    • (1996) J. Lipid Res. , vol.37 , pp. 907-925
    • Schoonjans, K.1    Staels, B.2    Auwerx, J.3
  • 30
    • 0026705751 scopus 로고
    • Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors
    • Kliewer S.A., Umesono K., Noonan D.J., Heyman R.A., Evans R.M. Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors. Nature 1992, 358:771-774.
    • (1992) Nature , vol.358 , pp. 771-774
    • Kliewer, S.A.1    Umesono, K.2    Noonan, D.J.3    Heyman, R.A.4    Evans, R.M.5
  • 31
    • 0035956863 scopus 로고    scopus 로고
    • Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors alpha- and gamma-mediated gene expression via liver fatty acid binding protein: a signaling path to the nucleus
    • Wolfrum C., Borrmann C.M., Borchers T., Spener F. Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors alpha- and gamma-mediated gene expression via liver fatty acid binding protein: a signaling path to the nucleus. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:2323-2328.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2323-2328
    • Wolfrum, C.1    Borrmann, C.M.2    Borchers, T.3    Spener, F.4
  • 36
    • 0031915653 scopus 로고    scopus 로고
    • A peroxisome proliferator-activated receptor-alpha (PPARalpha) cDNA cloned from guinea-pig liver encodes a protein with similar properties to the mouse PPARalpha: implications for species differences in responses to peroxisome proliferators
    • Tugwood J.D., Holden P.R., James N.H., Prince R.A., Roberts R.A. A peroxisome proliferator-activated receptor-alpha (PPARalpha) cDNA cloned from guinea-pig liver encodes a protein with similar properties to the mouse PPARalpha: implications for species differences in responses to peroxisome proliferators. Arch. Toxicol. 1998, 72:169-177.
    • (1998) Arch. Toxicol. , vol.72 , pp. 169-177
    • Tugwood, J.D.1    Holden, P.R.2    James, N.H.3    Prince, R.A.4    Roberts, R.A.5
  • 37
    • 33748422385 scopus 로고    scopus 로고
    • Differential regulation of the cynomolgus, human, and rat acyl-CoA oxidase promoters by PPARalpha
    • Kane C.D., Francone O.L., Stevens K.A. Differential regulation of the cynomolgus, human, and rat acyl-CoA oxidase promoters by PPARalpha. Gene 2006, 380:84-94.
    • (2006) Gene , vol.380 , pp. 84-94
    • Kane, C.D.1    Francone, O.L.2    Stevens, K.A.3
  • 38
    • 36949024511 scopus 로고    scopus 로고
    • The PPAR alpha-humanized mouse: a model to investigate species differences in liver toxicity mediated by PPAR alpha
    • Yang Q., Nagano T., Shah Y., Cheung C., Ito S., Gonzalez F.J. The PPAR alpha-humanized mouse: a model to investigate species differences in liver toxicity mediated by PPAR alpha. Toxicol. Sci. 2008, 101:132-139.
    • (2008) Toxicol. Sci. , vol.101 , pp. 132-139
    • Yang, Q.1    Nagano, T.2    Shah, Y.3    Cheung, C.4    Ito, S.5    Gonzalez, F.J.6
  • 39
    • 67649668902 scopus 로고    scopus 로고
    • Differential regulation of peroxisome proliferator-activated receptor (PPAR)-alpha1 and truncated PPARalpha2 as an adaptive response to fasting in the control of hepatic peroxisomal fatty acid beta-oxidation in the hibernating mammal
    • El Kebbaj Z., Andreoletti P., Mountassif D., Kabine M., Schohn H., Dauca M., Latruffe N., El Kebbaj M.S., Cherkaoui-Malki M. Differential regulation of peroxisome proliferator-activated receptor (PPAR)-alpha1 and truncated PPARalpha2 as an adaptive response to fasting in the control of hepatic peroxisomal fatty acid beta-oxidation in the hibernating mammal. Endocrinology 2009, 150:1192-1201.
    • (2009) Endocrinology , vol.150 , pp. 1192-1201
    • El Kebbaj, Z.1    Andreoletti, P.2    Mountassif, D.3    Kabine, M.4    Schohn, H.5    Dauca, M.6    Latruffe, N.7    El Kebbaj, M.S.8    Cherkaoui-Malki, M.9
  • 41
    • 0141956038 scopus 로고    scopus 로고
    • Changes of peroxisomal fatty acid metabolism during cold acclimatization in hibernating jerboa (Jaculus orientalis)
    • Kabine M., Clemencet M.C., Bride J., El Kebbaj M.S., Latruffe N., Cherkaoui-Malki M. Changes of peroxisomal fatty acid metabolism during cold acclimatization in hibernating jerboa (Jaculus orientalis). Biochimie 2003, 85:707-714.
    • (2003) Biochimie , vol.85 , pp. 707-714
    • Kabine, M.1    Clemencet, M.C.2    Bride, J.3    El Kebbaj, M.S.4    Latruffe, N.5    Cherkaoui-Malki, M.6
  • 42
    • 78650575544 scopus 로고    scopus 로고
    • Transcriptional coactivator PGC-1alpha promotes peroxisomal remodeling and biogenesis
    • Bagattin A., Hugendubler L., Mueller E. Transcriptional coactivator PGC-1alpha promotes peroxisomal remodeling and biogenesis. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:20376-20381.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 20376-20381
    • Bagattin, A.1    Hugendubler, L.2    Mueller, E.3
  • 43
    • 68649109608 scopus 로고    scopus 로고
    • The biology of PGC-1alpha and its therapeutic potential
    • Handschin C. The biology of PGC-1alpha and its therapeutic potential. Trends Pharmacol. Sci. 2009, 30:322-329.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 322-329
    • Handschin, C.1
  • 44
    • 6444240653 scopus 로고    scopus 로고
    • The effect of thalidomide on non-small cell lung cancer (NSCLC) cell lines: possible involvement in the PPARgamma pathway
    • DeCicco K.L., Tanaka T., Andreola F., De Luca L.M. The effect of thalidomide on non-small cell lung cancer (NSCLC) cell lines: possible involvement in the PPARgamma pathway. Carcinogenesis 2004, 25:1805-1812.
    • (2004) Carcinogenesis , vol.25 , pp. 1805-1812
    • DeCicco, K.L.1    Tanaka, T.2    Andreola, F.3    De Luca, L.M.4
  • 46
    • 0025265816 scopus 로고
    • Proliferation of peroxisomes without simultaneous induction of the peroxisomal fatty acid beta-oxidation
    • Baumgart E., Volkl A., Pill J., Fahimi H.D. Proliferation of peroxisomes without simultaneous induction of the peroxisomal fatty acid beta-oxidation. FEBS Lett. 1990, 264:5-9.
    • (1990) FEBS Lett. , vol.264 , pp. 5-9
    • Baumgart, E.1    Volkl, A.2    Pill, J.3    Fahimi, H.D.4
  • 48
    • 0031933152 scopus 로고    scopus 로고
    • Tubular peroxisomes in HepG2 cells: selective induction by growth factors and arachidonic acid
    • Schrader M., Krieglstein K., Fahimi H.D. Tubular peroxisomes in HepG2 cells: selective induction by growth factors and arachidonic acid. Eur. J. Cell Biol. 1998, 75:87-96.
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 87-96
    • Schrader, M.1    Krieglstein, K.2    Fahimi, H.D.3
  • 50
    • 0033620686 scopus 로고    scopus 로고
    • Ultrastructural alterations in the liver and intestine of carp Cyprinus carpio induced orally by ultra-low doses of endosulfan
    • Braunbeck T., Appelbaum S. Ultrastructural alterations in the liver and intestine of carp Cyprinus carpio induced orally by ultra-low doses of endosulfan. Dis. Aquat. Organ. 1999, 36:183-200.
    • (1999) Dis. Aquat. Organ. , vol.36 , pp. 183-200
    • Braunbeck, T.1    Appelbaum, S.2
  • 51
    • 84855829944 scopus 로고    scopus 로고
    • Ultrastructural changes in the rat kidney after single dose of cyclophosphamide-possible roles for peroxisome proliferation and lysosomal dysfunction in cyclophosphamide induced renal damage
    • Abraham P., Isaac B. Ultrastructural changes in the rat kidney after single dose of cyclophosphamide-possible roles for peroxisome proliferation and lysosomal dysfunction in cyclophosphamide induced renal damage. Hum. Exp. Toxicol. 2011, 30(12):1924-1930.
    • (2011) Hum. Exp. Toxicol. , vol.30 , Issue.12 , pp. 1924-1930
    • Abraham, P.1    Isaac, B.2
  • 52
    • 25144466898 scopus 로고    scopus 로고
    • Effects of selected xenoestrogens on liver peroxisomes, vitellogenin levels and spermatogenic cell proliferation in male zebrafish
    • Ortiz-Zarragoitia M., Cajaraville M.P. Effects of selected xenoestrogens on liver peroxisomes, vitellogenin levels and spermatogenic cell proliferation in male zebrafish. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2005, 141:133-144.
    • (2005) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.141 , pp. 133-144
    • Ortiz-Zarragoitia, M.1    Cajaraville, M.P.2
  • 53
    • 0028339813 scopus 로고
    • Effects of acetylsalicylic acid on parameters related to peroxisome proliferation in mouse liver
    • Cai Y., Sohlenius A.K., Andersson K., Sundberg C., DePierre J.W. Effects of acetylsalicylic acid on parameters related to peroxisome proliferation in mouse liver. Biochem. Pharmacol. 1994, 47:2213-2219.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 2213-2219
    • Cai, Y.1    Sohlenius, A.K.2    Andersson, K.3    Sundberg, C.4    DePierre, J.W.5
  • 54
    • 0025896706 scopus 로고
    • Induction of biotransformation in the liver of Eel (Anguilla anguilla L.) by sublethal exposure to dinitro-o-cresol: an ultrastructural and biochemical study
    • Braunbeck T., Volkl A. Induction of biotransformation in the liver of Eel (Anguilla anguilla L.) by sublethal exposure to dinitro-o-cresol: an ultrastructural and biochemical study. Ecotoxicol. Environ. Saf. 1991, 21:109-127.
    • (1991) Ecotoxicol. Environ. Saf. , vol.21 , pp. 109-127
    • Braunbeck, T.1    Volkl, A.2
  • 55
    • 0029067225 scopus 로고
    • Signaling cross-talk between peroxisome proliferator-activated receptor/retinoid X receptor and estrogen receptor through estrogen response elements
    • Keller H., Givel F., Perroud M., Wahli W. Signaling cross-talk between peroxisome proliferator-activated receptor/retinoid X receptor and estrogen receptor through estrogen response elements. Mol. Endocrinol. 1995, 9:794-804.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 794-804
    • Keller, H.1    Givel, F.2    Perroud, M.3    Wahli, W.4
  • 56
    • 0343742625 scopus 로고    scopus 로고
    • Retinoid X receptor and peroxisome proliferator-activated receptor activate an estrogen responsive gene independent of the estrogen receptor
    • Nunez S.B., Medin J.A., Braissant O., Kemp L., Wahli W., Ozato K., Segars J.H. Retinoid X receptor and peroxisome proliferator-activated receptor activate an estrogen responsive gene independent of the estrogen receptor. Mol. Cell. Endocrinol. 1997, 127:27-40.
    • (1997) Mol. Cell. Endocrinol. , vol.127 , pp. 27-40
    • Nunez, S.B.1    Medin, J.A.2    Braissant, O.3    Kemp, L.4    Wahli, W.5    Ozato, K.6    Segars, J.H.7
  • 57
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • Circu M.L., Aw T.Y. Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic. Biol. Med. 2010, 48:749-762.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 58
    • 33846117134 scopus 로고    scopus 로고
    • The signaling mechanism of ROS in tumor progression
    • Wu W.S. The signaling mechanism of ROS in tumor progression. Cancer Metastasis Rev. 2006, 25:695-705.
    • (2006) Cancer Metastasis Rev. , vol.25 , pp. 695-705
    • Wu, W.S.1
  • 59
    • 70449715463 scopus 로고    scopus 로고
    • Reactive oxygen species and peroxisomes: struggling for balance
    • Bonekamp N.A., Volkl A., Fahimi H.D., Schrader M. Reactive oxygen species and peroxisomes: struggling for balance. Biofactors 2009, 35:346-355.
    • (2009) Biofactors , vol.35 , pp. 346-355
    • Bonekamp, N.A.1    Volkl, A.2    Fahimi, H.D.3    Schrader, M.4
  • 61
    • 0029128915 scopus 로고
    • Alterations of peroxisomes in steatosis of the human liver: a quantitative study
    • De Craemer D., Pauwels M., Van den Branden C. Alterations of peroxisomes in steatosis of the human liver: a quantitative study. Hepatology 1995, 22:744-752.
    • (1995) Hepatology , vol.22 , pp. 744-752
    • De Craemer, D.1    Pauwels, M.2    Van den Branden, C.3
  • 62
    • 0032754922 scopus 로고    scopus 로고
    • Immunocytochemical investigation of catalase and peroxisomal lipid beta-oxidation enzymes in human hepatocellular tumors and liver cirrhosis
    • Litwin J.A., Beier K., Volkl A., Hofmann W.J., Fahimi H.D. Immunocytochemical investigation of catalase and peroxisomal lipid beta-oxidation enzymes in human hepatocellular tumors and liver cirrhosis. Virchows Arch. 1999, 435:486-495.
    • (1999) Virchows Arch. , vol.435 , pp. 486-495
    • Litwin, J.A.1    Beier, K.2    Volkl, A.3    Hofmann, W.J.4    Fahimi, H.D.5
  • 63
    • 0034666132 scopus 로고    scopus 로고
    • Defect in peroxisome proliferator-activated receptor alpha-inducible fatty acid oxidation determines the severity of hepatic steatosis in response to fasting
    • Hashimoto T., Cook W.S., Qi C., Yeldandi A.V., Reddy J.K., Rao M.S. Defect in peroxisome proliferator-activated receptor alpha-inducible fatty acid oxidation determines the severity of hepatic steatosis in response to fasting. J. Biol. Chem. 2000, 275:28918-28928.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28918-28928
    • Hashimoto, T.1    Cook, W.S.2    Qi, C.3    Yeldandi, A.V.4    Reddy, J.K.5    Rao, M.S.6
  • 64
    • 0042847330 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha (PPARalpha) agonist treatment reverses PPARalpha dysfunction and abnormalities in hepatic lipid metabolism in ethanol-fed mice
    • Fischer M., You M., Matsumoto M., Crabb D.W. Peroxisome proliferator-activated receptor alpha (PPARalpha) agonist treatment reverses PPARalpha dysfunction and abnormalities in hepatic lipid metabolism in ethanol-fed mice. J. Biol. Chem. 2003, 278:27997-28004.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27997-28004
    • Fischer, M.1    You, M.2    Matsumoto, M.3    Crabb, D.W.4
  • 65
    • 2342644813 scopus 로고    scopus 로고
    • Administration of the potent PPARalpha agonist, Wy-14,643, reverses nutritional fibrosis and steatohepatitis in mice
    • Ip E., Farrell G., Hall P., Robertson G., Leclercq I. Administration of the potent PPARalpha agonist, Wy-14,643, reverses nutritional fibrosis and steatohepatitis in mice. Hepatology 2004, 39:1286-1296.
    • (2004) Hepatology , vol.39 , pp. 1286-1296
    • Ip, E.1    Farrell, G.2    Hall, P.3    Robertson, G.4    Leclercq, I.5
  • 66
    • 3042635055 scopus 로고    scopus 로고
    • Alcoholic liver injury in the rat is associated with reduced expression of peroxisome proliferator-alpha (PPARalpha)-regulated genes and is ameliorated by PPARalpha activation
    • Nanji A.A., Dannenberg A.J., Jokelainen K., Bass N.M. Alcoholic liver injury in the rat is associated with reduced expression of peroxisome proliferator-alpha (PPARalpha)-regulated genes and is ameliorated by PPARalpha activation. J. Pharmacol. Exp. Ther. 2004, 310:417-424.
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 417-424
    • Nanji, A.A.1    Dannenberg, A.J.2    Jokelainen, K.3    Bass, N.M.4
  • 67
    • 0028869502 scopus 로고
    • Expression of the peroxisome proliferator-activated receptor gene is decreased in experimental alcoholic liver disease
    • Wan Y.J., Morimoto M., Thurman R.G., Bojes H.K., French S.W. Expression of the peroxisome proliferator-activated receptor gene is decreased in experimental alcoholic liver disease. Life Sci. 1995, 56:307-317.
    • (1995) Life Sci. , vol.56 , pp. 307-317
    • Wan, Y.J.1    Morimoto, M.2    Thurman, R.G.3    Bojes, H.K.4    French, S.W.5
  • 68
    • 39749090649 scopus 로고    scopus 로고
    • Oxidative mechanisms in the pathogenesis of alcoholic liver disease
    • Albano E. Oxidative mechanisms in the pathogenesis of alcoholic liver disease. Mol. Aspects Med. 2008, 29:9-16.
    • (2008) Mol. Aspects Med. , vol.29 , pp. 9-16
    • Albano, E.1
  • 69
    • 79956301571 scopus 로고    scopus 로고
    • The role of oxidative stress in non-alcoholic steatohepatitis
    • Koek G.H., Liedorp P.R., Bast A. The role of oxidative stress in non-alcoholic steatohepatitis. Clin. Chim. Acta 2011, 412:1297-1305.
    • (2011) Clin. Chim. Acta , vol.412 , pp. 1297-1305
    • Koek, G.H.1    Liedorp, P.R.2    Bast, A.3
  • 70
    • 40149088797 scopus 로고    scopus 로고
    • The blind men 'see' the elephant-the many faces of fatty liver disease
    • Sanal M.G. The blind men 'see' the elephant-the many faces of fatty liver disease. World J. Gastroenterol. 2008, 14:831-844.
    • (2008) World J. Gastroenterol. , vol.14 , pp. 831-844
    • Sanal, M.G.1
  • 71
    • 0025227870 scopus 로고
    • Alterations of hepatocellular peroxisomes in viral hepatitis in the mouse
    • De Craemer D., Bingen A., Langendries M., Martin J.P., Roels F. Alterations of hepatocellular peroxisomes in viral hepatitis in the mouse. J. Hepatol. 1990, 11:145-152.
    • (1990) J. Hepatol. , vol.11 , pp. 145-152
    • De Craemer, D.1    Bingen, A.2    Langendries, M.3    Martin, J.P.4    Roels, F.5
  • 72
    • 0027198872 scopus 로고
    • Alterations of hepatocellular peroxisomes in patients with cancer. Catalase cytochemistry and morphometry
    • De Craemer D., Pauwels M., Hautekeete M., Roels F. Alterations of hepatocellular peroxisomes in patients with cancer. Catalase cytochemistry and morphometry. Cancer 1993, 71:3851-3858.
    • (1993) Cancer , vol.71 , pp. 3851-3858
    • De Craemer, D.1    Pauwels, M.2    Hautekeete, M.3    Roels, F.4
  • 73
    • 0037218573 scopus 로고    scopus 로고
    • Oxidative stress in viral and alcoholic hepatitis
    • Loguercio C., Federico A. Oxidative stress in viral and alcoholic hepatitis. Free Radic. Biol. Med. 2003, 34:1-10.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1-10
    • Loguercio, C.1    Federico, A.2
  • 74
    • 77950166065 scopus 로고    scopus 로고
    • Steatosis as a co-factor in chronic liver diseases
    • Persico M., Iolascon A. Steatosis as a co-factor in chronic liver diseases. World J. Gastroenterol. 2010, 16:1171-1176.
    • (2010) World J. Gastroenterol. , vol.16 , pp. 1171-1176
    • Persico, M.1    Iolascon, A.2
  • 76
    • 0028859252 scopus 로고
    • Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p
    • Erdmann R., Blobel G. Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p. J. Cell Biol. 1995, 128:509-523.
    • (1995) J. Cell Biol. , vol.128 , pp. 509-523
    • Erdmann, R.1    Blobel, G.2
  • 78
    • 33845295814 scopus 로고    scopus 로고
    • The biochemistry of oleate induction: transcriptional upregulation and peroxisome proliferation
    • Gurvitz A., Rottensteiner H. The biochemistry of oleate induction: transcriptional upregulation and peroxisome proliferation. Biochim. Biophys. Acta 2006, 1763:1392-1402.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1392-1402
    • Gurvitz, A.1    Rottensteiner, H.2
  • 80
    • 0035943674 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Adr1p governs fatty acid beta-oxidation and peroxisome proliferation by regulating POX1 and PEX11
    • Gurvitz A., Hiltunen J.K., Erdmann R., Hamilton B., Hartig A., Ruis H., Rottensteiner H. Saccharomyces cerevisiae Adr1p governs fatty acid beta-oxidation and peroxisome proliferation by regulating POX1 and PEX11. J. Biol. Chem. 2001, 276:31825-31830.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31825-31830
    • Gurvitz, A.1    Hiltunen, J.K.2    Erdmann, R.3    Hamilton, B.4    Hartig, A.5    Ruis, H.6    Rottensteiner, H.7
  • 81
    • 44849142482 scopus 로고    scopus 로고
    • Binding characteristics and regulatory mechanisms of the transcription factors controlling oleate-responsive genes in Saccharomyces cerevisiae
    • Karpichev I.V., Durand-Heredia J.M., Luo Y., Small G.M. Binding characteristics and regulatory mechanisms of the transcription factors controlling oleate-responsive genes in Saccharomyces cerevisiae. J. Biol. Chem. 2008, 283:10264-10275.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10264-10275
    • Karpichev, I.V.1    Durand-Heredia, J.M.2    Luo, Y.3    Small, G.M.4
  • 83
    • 0026508262 scopus 로고
    • Control of peroxisome proliferation in Saccharomyces cerevisiae by ADR1, SNF1 (CAT1, CCR1) and SNF4 (CAT3)
    • Simon M., Binder M., Adam G., Hartig A., Ruis H. Control of peroxisome proliferation in Saccharomyces cerevisiae by ADR1, SNF1 (CAT1, CCR1) and SNF4 (CAT3). Yeast 1992, 8:303-309.
    • (1992) Yeast , vol.8 , pp. 303-309
    • Simon, M.1    Binder, M.2    Adam, G.3    Hartig, A.4    Ruis, H.5
  • 84
    • 70349310032 scopus 로고    scopus 로고
    • Snf1 controls the activity of adr1 through dephosphorylation of Ser230
    • Ratnakumar S., Kacherovsky N., Arms E., Young E.T. Snf1 controls the activity of adr1 through dephosphorylation of Ser230. Genetics 2009, 182:735-745.
    • (2009) Genetics , vol.182 , pp. 735-745
    • Ratnakumar, S.1    Kacherovsky, N.2    Arms, E.3    Young, E.T.4
  • 85
    • 77951245389 scopus 로고    scopus 로고
    • Snf1 dependence of peroxisomal gene expression is mediated by Adr1
    • Ratnakumar S., Young E.T. Snf1 dependence of peroxisomal gene expression is mediated by Adr1. J. Biol. Chem. 2010, 285:10703-10714.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10703-10714
    • Ratnakumar, S.1    Young, E.T.2
  • 86
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell?
    • Hardie D.G., Carling D., Carlson M. The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell?. Annu. Rev. Biochem. 1998, 67:821-855.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 87
    • 33744933445 scopus 로고    scopus 로고
    • Regulatory genes controlling fatty acid catabolism and peroxisomal functions in the filamentous fungus Aspergillus nidulans
    • Hynes M.J., Murray S.L., Duncan A., Khew G.S., Davis M.A. Regulatory genes controlling fatty acid catabolism and peroxisomal functions in the filamentous fungus Aspergillus nidulans. Eukaryot. Cell 2006, 5:794-805.
    • (2006) Eukaryot. Cell , vol.5 , pp. 794-805
    • Hynes, M.J.1    Murray, S.L.2    Duncan, A.3    Khew, G.S.4    Davis, M.A.5
  • 88
    • 45149118668 scopus 로고    scopus 로고
    • Genetic analysis of the role of peroxisomes in the utilization of acetate and fatty acids in Aspergillus nidulans
    • Hynes M.J., Murray S.L., Khew G.S., Davis M.A. Genetic analysis of the role of peroxisomes in the utilization of acetate and fatty acids in Aspergillus nidulans. Genetics 2008, 178:1355-1369.
    • (2008) Genetics , vol.178 , pp. 1355-1369
    • Hynes, M.J.1    Murray, S.L.2    Khew, G.S.3    Davis, M.A.4
  • 89
    • 77950860948 scopus 로고    scopus 로고
    • AoxA is a major peroxisomal long chain fatty acyl-CoA oxidase required for beta-oxidation in A. nidulans
    • Reiser K., Davis M.A., Hynes M.J. AoxA is a major peroxisomal long chain fatty acyl-CoA oxidase required for beta-oxidation in A. nidulans. Curr. Genet. 2010, 56:139-150.
    • (2010) Curr. Genet. , vol.56 , pp. 139-150
    • Reiser, K.1    Davis, M.A.2    Hynes, M.J.3
  • 90
    • 77952097870 scopus 로고    scopus 로고
    • Aspergillus nidulans contains six possible fatty acyl-CoA synthetases with FaaB being the major synthetase for fatty acid degradation
    • Reiser K., Davis M.A., Hynes M.J. Aspergillus nidulans contains six possible fatty acyl-CoA synthetases with FaaB being the major synthetase for fatty acid degradation. Arch. Microbiol. 2010, 192:373-382.
    • (2010) Arch. Microbiol. , vol.192 , pp. 373-382
    • Reiser, K.1    Davis, M.A.2    Hynes, M.J.3
  • 91
    • 78649444905 scopus 로고    scopus 로고
    • An ortholog of farA of Aspergillus nidulans is implicated in the transcriptional activation of genes involved in fatty acid utilization in the yeast Yarrowia lipolytica
    • Poopanitpan N., Kobayashi S., Fukuda R., Horiuchi H., Ohta A. An ortholog of farA of Aspergillus nidulans is implicated in the transcriptional activation of genes involved in fatty acid utilization in the yeast Yarrowia lipolytica. Biochem. Biophys. Res. Commun. 2010, 402:731-735.
    • (2010) Biochem. Biophys. Res. Commun. , vol.402 , pp. 731-735
    • Poopanitpan, N.1    Kobayashi, S.2    Fukuda, R.3    Horiuchi, H.4    Ohta, A.5
  • 93
    • 77949673517 scopus 로고    scopus 로고
    • Salt stress causes peroxisome proliferation, but inducing peroxisome proliferation does not improve NaCl tolerance in Arabidopsis thaliana
    • Mitsuya S., El-Shami M., Sparkes I.A., Charlton W.L., Lousa Cde M., Johnson B., Baker A. Salt stress causes peroxisome proliferation, but inducing peroxisome proliferation does not improve NaCl tolerance in Arabidopsis thaliana. PLoS One 2010, 5:e9408.
    • (2010) PLoS One , vol.5
    • Mitsuya, S.1    El-Shami, M.2    Sparkes, I.A.3    Charlton, W.L.4    Lousa Cde, M.5    Johnson, B.6    Baker, A.7
  • 94
    • 0025801196 scopus 로고
    • Peroxisome proliferation and oxidative stress mediated by activated oxygen species in plant peroxisomes
    • Palma J.M., Garrido M., Rodriguez-Garcia M.I., del Rio L.A. Peroxisome proliferation and oxidative stress mediated by activated oxygen species in plant peroxisomes. Arch. Biochem. Biophys. 1991, 287:68-74.
    • (1991) Arch. Biochem. Biophys. , vol.287 , pp. 68-74
    • Palma, J.M.1    Garrido, M.2    Rodriguez-Garcia, M.I.3    del Rio, L.A.4
  • 95
    • 67649752350 scopus 로고    scopus 로고
    • Peroxule extension over ER defined paths constitutes a rapid subcellular response to hydroxyl stress
    • Sinclair A.M., Trobacher C.P., Mathur N., Greenwood J.S., Mathur J. Peroxule extension over ER defined paths constitutes a rapid subcellular response to hydroxyl stress. Plant J. 2009, 59(2):231-242.
    • (2009) Plant J. , vol.59 , Issue.2 , pp. 231-242
    • Sinclair, A.M.1    Trobacher, C.P.2    Mathur, N.3    Greenwood, J.S.4    Mathur, J.5
  • 96
    • 40749153546 scopus 로고    scopus 로고
    • Peroxisome proliferation, wound-activated responses and expression of peroxisome-associated genes are cross-regulated but uncoupled in Arabidopsis thaliana
    • Castillo M.C., Sandalio L.M., Del Rio L.A., Leon J. Peroxisome proliferation, wound-activated responses and expression of peroxisome-associated genes are cross-regulated but uncoupled in Arabidopsis thaliana. Plant Cell Environ. 2008, 31:492-505.
    • (2008) Plant Cell Environ. , vol.31 , pp. 492-505
    • Castillo, M.C.1    Sandalio, L.M.2    Del Rio, L.A.3    Leon, J.4
  • 97
    • 0027650968 scopus 로고
    • Targeting of glyoxysomal proteins to peroxisomes in leaves and roots of a higher plant
    • Olsen L.J., Ettinger W.F., Damsz B., Matsudaira K., Webb M.A., Harada J.J. Targeting of glyoxysomal proteins to peroxisomes in leaves and roots of a higher plant. Plant Cell 1993, 5:941-952.
    • (1993) Plant Cell , vol.5 , pp. 941-952
    • Olsen, L.J.1    Ettinger, W.F.2    Damsz, B.3    Matsudaira, K.4    Webb, M.A.5    Harada, J.J.6
  • 98
    • 48949120153 scopus 로고    scopus 로고
    • Light induces peroxisome proliferation in Arabidopsis seedlings through the photoreceptor phytochrome A, the transcription factor HY5 HOMOLOG, and the peroxisomal protein PEROXIN11b
    • Desai M., Hu J. Light induces peroxisome proliferation in Arabidopsis seedlings through the photoreceptor phytochrome A, the transcription factor HY5 HOMOLOG, and the peroxisomal protein PEROXIN11b. Plant Physiol. 2008, 146:1117-1127.
    • (2008) Plant Physiol. , vol.146 , pp. 1117-1127
    • Desai, M.1    Hu, J.2
  • 99
    • 77957894981 scopus 로고    scopus 로고
    • Molecular basis of peroxisome division and proliferation in plants
    • Hu J. Molecular basis of peroxisome division and proliferation in plants. Int. Rev. Cell Mol. Biol. 2010, 279:79-99.
    • (2010) Int. Rev. Cell Mol. Biol. , vol.279 , pp. 79-99
    • Hu, J.1
  • 100
    • 0038000470 scopus 로고    scopus 로고
    • Dissecting the phytochrome A-dependent signaling network in higher plants
    • Wang H., Deng X.W. Dissecting the phytochrome A-dependent signaling network in higher plants. Trends Plant Sci. 2003, 8:172-178.
    • (2003) Trends Plant Sci. , vol.8 , pp. 172-178
    • Wang, H.1    Deng, X.W.2
  • 101
    • 0032545023 scopus 로고    scopus 로고
    • CDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p
    • Abe I., Fujiki Y. cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p. Biochem. Biophys. Res. Commun. 1998, 252:529-533.
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 529-533
    • Abe, I.1    Fujiki, Y.2
  • 102
    • 0032563281 scopus 로고    scopus 로고
    • Clofibrate-inducible, 28-kDa peroxisomal integral membrane protein is encoded by PEX11
    • Abe I., Okumoto K., Tamura S., Fujiki Y. Clofibrate-inducible, 28-kDa peroxisomal integral membrane protein is encoded by PEX11. FEBS Lett. 1998, 431:468-472.
    • (1998) FEBS Lett. , vol.431 , pp. 468-472
    • Abe, I.1    Okumoto, K.2    Tamura, S.3    Fujiki, Y.4
  • 103
    • 77955986557 scopus 로고    scopus 로고
    • PEX11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance
    • Koch J., Pranjic K., Huber A., Ellinger A., Hartig A., Kragler F., Brocard C. PEX11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance. J. Cell Sci. 2010, 123:3389-3400.
    • (2010) J. Cell Sci. , vol.123 , pp. 3389-3400
    • Koch, J.1    Pranjic, K.2    Huber, A.3    Ellinger, A.4    Hartig, A.5    Kragler, F.6    Brocard, C.7
  • 104
    • 0022998575 scopus 로고
    • The membrane proteins of the methanol-induced peroxisome of Candida boidinii. Initial characterization and generation of monoclonal antibodies
    • Goodman J.M., Maher J., Silver P.A., Pacifico A., Sanders D. The membrane proteins of the methanol-induced peroxisome of Candida boidinii. Initial characterization and generation of monoclonal antibodies. J. Biol. Chem. 1986, 261:3464-3468.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3464-3468
    • Goodman, J.M.1    Maher, J.2    Silver, P.A.3    Pacifico, A.4    Sanders, D.5
  • 105
    • 0027944155 scopus 로고
    • The peroxisomal membrane proteins of Candida boidinii: gene isolation and expression
    • Moreno M., Lark R., Campbell K.L., Goodman J.M. The peroxisomal membrane proteins of Candida boidinii: gene isolation and expression. Yeast 1994, 10:1447-1457.
    • (1994) Yeast , vol.10 , pp. 1447-1457
    • Moreno, M.1    Lark, R.2    Campbell, K.L.3    Goodman, J.M.4
  • 106
    • 0141541655 scopus 로고    scopus 로고
    • Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis
    • Rottensteiner H., Stein K., Sonnenhol E., Erdmann R. Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis. Mol. Biol. Cell 2003, 14:4316-4328.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4316-4328
    • Rottensteiner, H.1    Stein, K.2    Sonnenhol, E.3    Erdmann, R.4
  • 107
    • 0141764783 scopus 로고    scopus 로고
    • Pex11-related proteins in peroxisome dynamics: a role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae
    • Tam Y.Y., Torres-Guzman J.C., Vizeacoumar F.J., Smith J.J., Marelli M., Aitchison J.D., Rachubinski R.A. Pex11-related proteins in peroxisome dynamics: a role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae. Mol. Biol. Cell 2003, 14:4089-4102.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4089-4102
    • Tam, Y.Y.1    Torres-Guzman, J.C.2    Vizeacoumar, F.J.3    Smith, J.J.4    Marelli, M.5    Aitchison, J.D.6    Rachubinski, R.A.7
  • 108
    • 0032125799 scopus 로고    scopus 로고
    • Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p
    • Lorenz P., Maier A.G., Baumgart E., Erdmann R., Clayton C. Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p. EMBO J. 1998, 17:3542-3555.
    • (1998) EMBO J. , vol.17 , pp. 3542-3555
    • Lorenz, P.1    Maier, A.G.2    Baumgart, E.3    Erdmann, R.4    Clayton, C.5
  • 109
    • 0035062359 scopus 로고    scopus 로고
    • An essential dimeric membrane protein of trypanosome glycosomes
    • Maier A., Lorenz P., Voncken F., Clayton C. An essential dimeric membrane protein of trypanosome glycosomes. Mol. Microbiol. 2001, 39:1443-1451.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1443-1451
    • Maier, A.1    Lorenz, P.2    Voncken, F.3    Clayton, C.4
  • 110
    • 0041816190 scopus 로고    scopus 로고
    • Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes
    • (Epub 32003 Jun 35226)
    • Voncken F., van Hellemond J.J., Pfisterer I., Maier A., Hillmer S., Clayton C. Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes. J. Biol. Chem. 2003, 278:35299-35310. (Epub 32003 Jun 35226).
    • (2003) J. Biol. Chem. , vol.278 , pp. 35299-35310
    • Voncken, F.1    van Hellemond, J.J.2    Pfisterer, I.3    Maier, A.4    Hillmer, S.5    Clayton, C.6
  • 111
    • 79959462996 scopus 로고    scopus 로고
    • Peroxisome reintroduction in Hansenula polymorpha requires Pex25 and Rho1
    • Saraya R., Krikken A.M., Veenhuis M., van der Klei I.J. Peroxisome reintroduction in Hansenula polymorpha requires Pex25 and Rho1. J. Cell Biol. 2011, 193:885-900.
    • (2011) J. Cell Biol. , vol.193 , pp. 885-900
    • Saraya, R.1    Krikken, A.M.2    Veenhuis, M.3    van der Klei, I.J.4
  • 112
    • 83255187158 scopus 로고    scopus 로고
    • A subtle interplay between three Pex11 proteins shapes de novo formation and fission of peroxisomes
    • Huber A., Koch J., Kragler F., Brocard C., Hartig A. A subtle interplay between three Pex11 proteins shapes de novo formation and fission of peroxisomes. Traffic 2011, 13(1):157-167.
    • (2011) Traffic , vol.13 , Issue.1 , pp. 157-167
    • Huber, A.1    Koch, J.2    Kragler, F.3    Brocard, C.4    Hartig, A.5
  • 113
    • 33748565936 scopus 로고    scopus 로고
    • PEX genes in fungal genomes: common, rare or redundant
    • Kiel J.A., Veenhuis M., van der Klei I.J. PEX genes in fungal genomes: common, rare or redundant. Traffic 2006, 7:1291-1303.
    • (2006) Traffic , vol.7 , pp. 1291-1303
    • Kiel, J.A.1    Veenhuis, M.2    van der Klei, I.J.3
  • 114
    • 0036261777 scopus 로고    scopus 로고
    • PEX11 beta deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function
    • Li X., Baumgart E., Morrell J.C., Jimenez-Sanchez G., Valle D., Gould S.J. PEX11 beta deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function. Mol. Cell. Biol. 2002, 22:4358-4365.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4358-4365
    • Li, X.1    Baumgart, E.2    Morrell, J.C.3    Jimenez-Sanchez, G.4    Valle, D.5    Gould, S.J.6
  • 116
    • 1642458359 scopus 로고    scopus 로고
    • Tissue-selective, bidirectional regulation of PEX11 alpha and perilipin genes through a common peroxisome proliferator response element
    • Shimizu M., Takeshita A., Tsukamoto T., Gonzalez F.J., Osumi T. Tissue-selective, bidirectional regulation of PEX11 alpha and perilipin genes through a common peroxisome proliferator response element. Mol. Cell. Biol. 2004, 24:1313-1323.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1313-1323
    • Shimizu, M.1    Takeshita, A.2    Tsukamoto, T.3    Gonzalez, F.J.4    Osumi, T.5
  • 117
    • 0037462961 scopus 로고    scopus 로고
    • CDNA cloning and characterization of the third isoform of human peroxin Pex11p
    • Tanaka A., Okumoto K., Fujiki Y. cDNA cloning and characterization of the third isoform of human peroxin Pex11p. Biochem. Biophys. Res. Commun. 2003, 300:819-823.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 819-823
    • Tanaka, A.1    Okumoto, K.2    Fujiki, Y.3
  • 118
    • 61949336473 scopus 로고    scopus 로고
    • Disruption of the Aopex11-1 gene involved in peroxisome proliferation leads to impaired Woronin body formation in Aspergillus oryzae
    • Escano C.S., Juvvadi P.R., Jin F.J., Takahashi T., Koyama Y., Yamashita S., Maruyama J., Kitamoto K. Disruption of the Aopex11-1 gene involved in peroxisome proliferation leads to impaired Woronin body formation in Aspergillus oryzae. Eukaryot. Cell 2009, 8:296-305.
    • (2009) Eukaryot. Cell , vol.8 , pp. 296-305
    • Escano, C.S.1    Juvvadi, P.R.2    Jin, F.J.3    Takahashi, T.4    Koyama, Y.5    Yamashita, S.6    Maruyama, J.7    Kitamoto, K.8
  • 119
    • 33744519174 scopus 로고    scopus 로고
    • Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, division without elongation, or aggregation
    • Lingard M.J., Trelease R.N. Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, division without elongation, or aggregation. J. Cell Sci. 2006, 119:1961-1972.
    • (2006) J. Cell Sci. , vol.119 , pp. 1961-1972
    • Lingard, M.J.1    Trelease, R.N.2
  • 120
    • 70450188176 scopus 로고    scopus 로고
    • Dynamics of peroxisome abundance: a tale of division and proliferation
    • Kaur N., Hu J. Dynamics of peroxisome abundance: a tale of division and proliferation. Curr. Opin. Plant Biol. 2009, 12:781-788.
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 781-788
    • Kaur, N.1    Hu, J.2
  • 121
    • 34249804174 scopus 로고    scopus 로고
    • The PEROXIN11 protein family controls peroxisome proliferation in Arabidopsis
    • Orth T., Reumann S., Zhang X., Fan J., Wenzel D., Quan S., Hu J. The PEROXIN11 protein family controls peroxisome proliferation in Arabidopsis. Plant Cell 2007, 19:333-350.
    • (2007) Plant Cell , vol.19 , pp. 333-350
    • Orth, T.1    Reumann, S.2    Zhang, X.3    Fan, J.4    Wenzel, D.5    Quan, S.6    Hu, J.7
  • 122
    • 0029792856 scopus 로고    scopus 로고
    • Redox-sensitive homodimerization of Pex11p: a proposed mechanism to regulate peroxisomal division
    • Marshall P.A., Dyer J.M., Quick M.E., Goodman J.M. Redox-sensitive homodimerization of Pex11p: a proposed mechanism to regulate peroxisomal division. J. Cell Biol. 1996, 135:123-137.
    • (1996) J. Cell Biol. , vol.135 , pp. 123-137
    • Marshall, P.A.1    Dyer, J.M.2    Quick, M.E.3    Goodman, J.M.4
  • 123
    • 57749113632 scopus 로고    scopus 로고
    • Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A cooperate in cell cycle-associated replication of peroxisomes
    • Lingard M.J., Gidda S.K., Bingham S., Rothstein S.J., Mullen R.T., Trelease R.N. Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A cooperate in cell cycle-associated replication of peroxisomes. Plant Cell 2008, 20:1567-1585.
    • (2008) Plant Cell , vol.20 , pp. 1567-1585
    • Lingard, M.J.1    Gidda, S.K.2    Bingham, S.3    Rothstein, S.J.4    Mullen, R.T.5    Trelease, R.N.6
  • 125
    • 27144513797 scopus 로고    scopus 로고
    • Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation
    • Thoms S., Erdmann R. Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation. FEBS J. 2005, 272:5169-5181.
    • (2005) FEBS J. , vol.272 , pp. 5169-5181
    • Thoms, S.1    Erdmann, R.2
  • 126
    • 22044444453 scopus 로고    scopus 로고
    • The control of peroxisome number and size during division and proliferation
    • Yan M., Rayapuram N., Subramani S. The control of peroxisome number and size during division and proliferation. Curr. Opin. Cell Biol. 2005, 17:376-383.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 376-383
    • Yan, M.1    Rayapuram, N.2    Subramani, S.3
  • 130
    • 34547595860 scopus 로고    scopus 로고
    • Yeast peroxisomes multiply by growth and division
    • Motley A.M., Hettema E.H. Yeast peroxisomes multiply by growth and division. J. Cell Biol. 2007, 178:399-410.
    • (2007) J. Cell Biol. , vol.178 , pp. 399-410
    • Motley, A.M.1    Hettema, E.H.2
  • 133
    • 84859823763 scopus 로고    scopus 로고
    • Membrane elongation factors in organelle maintenance: the case of peroxisome proliferation
    • Koch J., Brocard C. Membrane elongation factors in organelle maintenance: the case of peroxisome proliferation. Biomol Concepts 2011, 2:353-364.
    • (2011) Biomol Concepts , vol.2 , pp. 353-364
    • Koch, J.1    Brocard, C.2
  • 134
    • 24944520856 scopus 로고    scopus 로고
    • Peroxisome biogenesis: end of the debate
    • Kunau W.H. Peroxisome biogenesis: end of the debate. Curr. Biol. 2005, 15:R774-R776.
    • (2005) Curr. Biol. , vol.15
    • Kunau, W.H.1
  • 135
    • 79958767409 scopus 로고    scopus 로고
    • Peroxisome fission is associated with reorganization of specific membrane proteins
    • Cepinska M.N., Veenhuis M., van der Klei I.J., Nagotu S. Peroxisome fission is associated with reorganization of specific membrane proteins. Traffic 2011, 12:925-937.
    • (2011) Traffic , vol.12 , pp. 925-937
    • Cepinska, M.N.1    Veenhuis, M.2    van der Klei, I.J.3    Nagotu, S.4
  • 136
    • 60349105123 scopus 로고    scopus 로고
    • Hansenula polymorpha pex11 cells are affected in peroxisome retention
    • Krikken A.M., Veenhuis M., van der Klei I.J. Hansenula polymorpha pex11 cells are affected in peroxisome retention. FEBS J. 2009, 276:1429-1439.
    • (2009) FEBS J. , vol.276 , pp. 1429-1439
    • Krikken, A.M.1    Veenhuis, M.2    van der Klei, I.J.3
  • 138
    • 77951896130 scopus 로고    scopus 로고
    • Amphipathic helices and membrane curvature
    • Drin G., Antonny B. Amphipathic helices and membrane curvature. FEBS Lett. 2010, 584:1840-1847.
    • (2010) FEBS Lett. , vol.584 , pp. 1840-1847
    • Drin, G.1    Antonny, B.2
  • 139
    • 77949876577 scopus 로고    scopus 로고
    • Phosphorylation-dependent activation of peroxisome proliferator protein PEX11 controls peroxisome abundance
    • Knoblach B., Rachubinski R.A. Phosphorylation-dependent activation of peroxisome proliferator protein PEX11 controls peroxisome abundance. J. Biol. Chem. 2010, 285:6670-6680.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6670-6680
    • Knoblach, B.1    Rachubinski, R.A.2
  • 140
    • 0038746700 scopus 로고    scopus 로고
    • YHR150w and YDR479c encode peroxisomal integral membrane proteins involved in the regulation of peroxisome number, size, and distribution in Saccharomyces cerevisiae
    • Vizeacoumar F.J., Torres-Guzman J.C., Tam Y.Y., Aitchison J.D., Rachubinski R.A. YHR150w and YDR479c encode peroxisomal integral membrane proteins involved in the regulation of peroxisome number, size, and distribution in Saccharomyces cerevisiae. J. Cell Biol. 2003, 161:321-332.
    • (2003) J. Cell Biol. , vol.161 , pp. 321-332
    • Vizeacoumar, F.J.1    Torres-Guzman, J.C.2    Tam, Y.Y.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 141
    • 1842853027 scopus 로고    scopus 로고
    • Peroxisome biogenesis and the role of protein import
    • Brown L.A., Baker A. Peroxisome biogenesis and the role of protein import. J. Cell Mol. Med. 2003, 7:388-400.
    • (2003) J. Cell Mol. Med. , vol.7 , pp. 388-400
    • Brown, L.A.1    Baker, A.2
  • 142
    • 0742288046 scopus 로고    scopus 로고
    • Pex30p, Pex31p, and Pex32p form a family of peroxisomal integral membrane proteins regulating peroxisome size and number in Saccharomyces cerevisiae
    • Vizeacoumar F.J., Torres-Guzman J.C., Bouard D., Aitchison J.D., Rachubinski R.A. Pex30p, Pex31p, and Pex32p form a family of peroxisomal integral membrane proteins regulating peroxisome size and number in Saccharomyces cerevisiae. Mol. Biol. Cell 2004, 15:665-677.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 665-677
    • Vizeacoumar, F.J.1    Torres-Guzman, J.C.2    Bouard, D.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 143
    • 79955959815 scopus 로고    scopus 로고
    • The peroxin Pex34p functions with the Pex11 family of peroxisomal divisional proteins to regulate the peroxisome population in yeast
    • Tower R.J., Fagarasanu A., Aitchison J.D., Rachubinski R.A. The peroxin Pex34p functions with the Pex11 family of peroxisomal divisional proteins to regulate the peroxisome population in yeast. Mol. Biol. Cell 2011, 22:1727-1738.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1727-1738
    • Tower, R.J.1    Fagarasanu, A.2    Aitchison, J.D.3    Rachubinski, R.A.4
  • 144
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • Praefcke G.J., McMahon H.T. The dynamin superfamily: universal membrane tubulation and fission molecules?. Nat. Rev. Mol. Cell Biol. 2004, 5:133-147.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 146
    • 0035166812 scopus 로고    scopus 로고
    • Mammalian dynamin-like protein DLP1 tubulates membranes
    • Yoon Y., Pitts K.R., McNiven M.A. Mammalian dynamin-like protein DLP1 tubulates membranes. Mol. Biol. Cell 2001, 12:2894-2905.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2894-2905
    • Yoon, Y.1    Pitts, K.R.2    McNiven, M.A.3
  • 148
    • 4444236087 scopus 로고    scopus 로고
    • Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1
    • Koch A., Schneider G., Luers G.H., Schrader M. Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1. J. Cell Sci. 2004, 117:3995-4006.
    • (2004) J. Cell Sci. , vol.117 , pp. 3995-4006
    • Koch, A.1    Schneider, G.2    Luers, G.H.3    Schrader, M.4
  • 149
    • 44649129342 scopus 로고    scopus 로고
    • The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells
    • Gandre-Babbe S., van der Bliek A.M. The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell 2008, 19:2402-2412.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2402-2412
    • Gandre-Babbe, S.1    van der Bliek, A.M.2
  • 150
    • 27144557499 scopus 로고    scopus 로고
    • A role for fis1 in both mitochondrial and peroxisomal fission in mammalian cells
    • Koch A., Yoon Y., Bonekamp N.A., McNiven M.A., Schrader M. A role for fis1 in both mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell 2005, 16:5077-5086.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5077-5086
    • Koch, A.1    Yoon, Y.2    Bonekamp, N.A.3    McNiven, M.A.4    Schrader, M.5
  • 151
    • 78650167618 scopus 로고    scopus 로고
    • Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
    • Otera H., Wang C., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K. Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J. Cell Biol. 2010, 191:1141-1158.
    • (2010) J. Cell Biol. , vol.191 , pp. 1141-1158
    • Otera, H.1    Wang, C.2    Cleland, M.M.3    Setoguchi, K.4    Yokota, S.5    Youle, R.J.6    Mihara, K.7
  • 153
    • 46249130452 scopus 로고    scopus 로고
    • Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p
    • Motley A.M., Ward G.P., Hettema E.H. Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. J. Cell Sci. 2008, 121:1633-1640.
    • (2008) J. Cell Sci. , vol.121 , pp. 1633-1640
    • Motley, A.M.1    Ward, G.P.2    Hettema, E.H.3
  • 154
    • 0035842904 scopus 로고    scopus 로고
    • A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae
    • Hoepfner D., van den Berg M., Philippsen P., Tabak H.F., Hettema E.H. A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J. Cell Biol. 2001, 155:979-990.
    • (2001) J. Cell Biol. , vol.155 , pp. 979-990
    • Hoepfner, D.1    van den Berg, M.2    Philippsen, P.3    Tabak, H.F.4    Hettema, E.H.5
  • 155
    • 33744960494 scopus 로고    scopus 로고
    • The dynamin-like protein Vps1p of the yeast Saccharomyces cerevisiae associates with peroxisomes in a Pex19p-dependent manner
    • Vizeacoumar F.J., Vreden W.N., Eitzen G.A., Aitchison J.D., Rachubinski R.A. The dynamin-like protein Vps1p of the yeast Saccharomyces cerevisiae associates with peroxisomes in a Pex19p-dependent manner. J. Biol. Chem. 2006, 281:12817-12823.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12817-12823
    • Vizeacoumar, F.J.1    Vreden, W.N.2    Eitzen, G.A.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 156
    • 79958284774 scopus 로고    scopus 로고
    • The conserved fission complex on peroxisomes and mitochondria
    • Pan R., Hu J. The conserved fission complex on peroxisomes and mitochondria. Plant Signal. Behav. 2011, 6:870-872.
    • (2011) Plant Signal. Behav. , vol.6 , pp. 870-872
    • Pan, R.1    Hu, J.2
  • 157
    • 84863011557 scopus 로고    scopus 로고
    • The Arabidopsis Tail-anchored protein PEROXISOMAL AND MITOCHONDRIAL DIVISION FACTOR1 is involved in the morphogenesis and proliferation of peroxisomes and mitochondria
    • Dec. 9 Epub ahead of print doi:org/10.1105/tpc.111.090142
    • Aung K., Hu J. The Arabidopsis Tail-anchored protein PEROXISOMAL AND MITOCHONDRIAL DIVISION FACTOR1 is involved in the morphogenesis and proliferation of peroxisomes and mitochondria. Plant Cell 2011, Dec. 9 Epub ahead of print doi:org/10.1105/tpc.111.090142.
    • (2011) Plant Cell
    • Aung, K.1    Hu, J.2
  • 158
    • 64649093836 scopus 로고    scopus 로고
    • Biogenesis of peroxisomes and mitochondria: linked by division
    • Delille H.K., Alves R., Schrader M. Biogenesis of peroxisomes and mitochondria: linked by division. Histochem. Cell Biol. 2009, 131:441-446.
    • (2009) Histochem. Cell Biol. , vol.131 , pp. 441-446
    • Delille, H.K.1    Alves, R.2    Schrader, M.3
  • 159
    • 64449084971 scopus 로고    scopus 로고
    • Organelle dynamics and dysfunction: a closer link between peroxisomes and mitochondria
    • Camoes F., Bonekamp N.A., Delille H.K., Schrader M. Organelle dynamics and dysfunction: a closer link between peroxisomes and mitochondria. J. Inherit. Metab. Dis. 2009, 32:163-180.
    • (2009) J. Inherit. Metab. Dis. , vol.32 , pp. 163-180
    • Camoes, F.1    Bonekamp, N.A.2    Delille, H.K.3    Schrader, M.4
  • 160
    • 35848932285 scopus 로고    scopus 로고
    • Mitochondria and peroxisomes: are the 'Big Brother' and the 'Little Sister' closer than assumed?
    • Schrader M., Yoon Y. Mitochondria and peroxisomes: are the 'Big Brother' and the 'Little Sister' closer than assumed?. Bioessays 2007, 29:1105-1114.
    • (2007) Bioessays , vol.29 , pp. 1105-1114
    • Schrader, M.1    Yoon, Y.2
  • 161
    • 79955506970 scopus 로고    scopus 로고
    • Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk
    • Ivashchenko O., Van Veldhoven P.P., Brees C., Ho Y.S., Terlecky S.R., Fransen M. Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk. Mol. Biol. Cell 2011, 22:1440-1451.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1440-1451
    • Ivashchenko, O.1    Van Veldhoven, P.P.2    Brees, C.3    Ho, Y.S.4    Terlecky, S.R.5    Fransen, M.6
  • 163
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins S., Lackner L., Nunnari J. The machines that divide and fuse mitochondria. Annu. Rev. Biochem. 2007, 76:751-780.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 164
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K., Shaw J.M. Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 2005, 39:503-536.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 165
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and death
    • Westermann B. Mitochondrial fusion and fission in cell life and death. Nat. Rev. Mol. Cell Biol. 2010, 11:872-884.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 872-884
    • Westermann, B.1
  • 167
  • 168
    • 0033739889 scopus 로고    scopus 로고
    • Real time imaging reveals a peroxisomal reticulum in living cells
    • Schrader M., King S.J., Stroh T.A., Schroer T.A. Real time imaging reveals a peroxisomal reticulum in living cells. J. Cell Sci. 2000, 113:3663-3671.
    • (2000) J. Cell Sci. , vol.113 , pp. 3663-3671
    • Schrader, M.1    King, S.J.2    Stroh, T.A.3    Schroer, T.A.4
  • 169
    • 34247107180 scopus 로고    scopus 로고
    • Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis
    • Kobayashi S., Tanaka A., Fujiki Y. Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis. Exp. Cell Res. 2007, 313:1675-1686.
    • (2007) Exp. Cell Res. , vol.313 , pp. 1675-1686
    • Kobayashi, S.1    Tanaka, A.2    Fujiki, Y.3
  • 171
    • 0037930873 scopus 로고    scopus 로고
    • The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11
    • Li X., Gould S.J. The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11. J. Biol. Chem. 2003, 278:17012-17020.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17012-17020
    • Li, X.1    Gould, S.J.2
  • 172
    • 0030071925 scopus 로고    scopus 로고
    • Interaction of microtubules with peroxisomes. Tubular and spherical peroxisomes in HepG2 cells and their alterations induced by microtubule-active drugs
    • Schrader M., Burkhardt J.K., Baumgart E., Luers G., Spring H., Volkl A., Fahimi H.D. Interaction of microtubules with peroxisomes. Tubular and spherical peroxisomes in HepG2 cells and their alterations induced by microtubule-active drugs. Eur. J. Cell Biol. 1996, 69:24-35.
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 24-35
    • Schrader, M.1    Burkhardt, J.K.2    Baumgart, E.3    Luers, G.4    Spring, H.5    Volkl, A.6    Fahimi, H.D.7
  • 174
    • 77957798188 scopus 로고    scopus 로고
    • A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division
    • Chang C.R., Manlandro C.M., Arnoult D., Stadler J., Posey A.E., Hill R.B., Blackstone C. A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division. J. Biol. Chem. 2010, 285:32494-32503.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32494-32503
    • Chang, C.R.1    Manlandro, C.M.2    Arnoult, D.3    Stadler, J.4    Posey, A.E.5    Hill, R.B.6    Blackstone, C.7
  • 176
    • 33646136227 scopus 로고    scopus 로고
    • Peroxisome division is impaired in a CHO cell mutant with an inactivating point-mutation in dynamin-like protein 1 gene
    • Tanaka A., Kobayashi S., Fujiki Y. Peroxisome division is impaired in a CHO cell mutant with an inactivating point-mutation in dynamin-like protein 1 gene. Exp. Cell Res. 2006, 312:1671-1684.
    • (2006) Exp. Cell Res. , vol.312 , pp. 1671-1684
    • Tanaka, A.1    Kobayashi, S.2    Fujiki, Y.3
  • 179
    • 68949151976 scopus 로고    scopus 로고
    • Peroxisomes, myelination, and axonal integrity in the CNS
    • Baes M., Aubourg P. Peroxisomes, myelination, and axonal integrity in the CNS. Neuroscientist 2009, 15:367-379.
    • (2009) Neuroscientist , vol.15 , pp. 367-379
    • Baes, M.1    Aubourg, P.2
  • 182
    • 78149410577 scopus 로고    scopus 로고
    • Dynamin-like protein 1 at the Golgi complex: a novel component of the sorting/targeting machinery en route to the plasma membrane
    • Bonekamp N.A., Vormund K., Jacob R., Schrader M. Dynamin-like protein 1 at the Golgi complex: a novel component of the sorting/targeting machinery en route to the plasma membrane. Exp. Cell Res. 2010, 316:3454-3467.
    • (2010) Exp. Cell Res. , vol.316 , pp. 3454-3467
    • Bonekamp, N.A.1    Vormund, K.2    Jacob, R.3    Schrader, M.4
  • 184
    • 78751470559 scopus 로고    scopus 로고
    • Aberrant mitochondrial fission in neurons induced by protein kinase C{delta} under oxidative stress conditions in vivo
    • Qi X., Disatnik M.H., Shen N., Sobel R.A., Mochly-Rosen D. Aberrant mitochondrial fission in neurons induced by protein kinase C{delta} under oxidative stress conditions in vivo. Mol. Biol. Cell 2011, 22:256-265.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 256-265
    • Qi, X.1    Disatnik, M.H.2    Shen, N.3    Sobel, R.A.4    Mochly-Rosen, D.5
  • 185
    • 0141592470 scopus 로고    scopus 로고
    • HFis1, a novel component of the mammalian mitochondrial fission machinery
    • James D.I., Parone P.A., Mattenberger Y., Martinou J.C. hFis1, a novel component of the mammalian mitochondrial fission machinery. J. Biol. Chem. 2003, 278:36373-36379.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36373-36379
    • James, D.I.1    Parone, P.A.2    Mattenberger, Y.3    Martinou, J.C.4
  • 186
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • Lee Y.J., Jeong S.Y., Karbowski M., Smith C.L., Youle R.J. Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol. Biol. Cell 2004, 15:5001-5011.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 187
    • 1842479419 scopus 로고    scopus 로고
    • Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology
    • Stojanovski D., Koutsopoulos O.S., Okamoto K., Ryan M.T. Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology. J. Cell Sci. 2004, 117:1201-1210.
    • (2004) J. Cell Sci. , vol.117 , pp. 1201-1210
    • Stojanovski, D.1    Koutsopoulos, O.S.2    Okamoto, K.3    Ryan, M.T.4
  • 188
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Yoon Y., Krueger E.W., Oswald B.J., McNiven M.A. The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol. Cell. Biol. 2003, 23:5409-5420.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5409-5420
    • Yoon, Y.1    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 189
    • 84954358239 scopus 로고    scopus 로고
    • The mitochondrial outer membrane protein hFis1 regulates mitochondrial morphology and fission through self-interaction
    • Serasinghe M.N., Yoon Y. The mitochondrial outer membrane protein hFis1 regulates mitochondrial morphology and fission through self-interaction. Exp. Cell Res. 2008, 314:3494-3507.
    • (2008) Exp. Cell Res. , vol.314 , pp. 3494-3507
    • Serasinghe, M.N.1    Yoon, Y.2
  • 190
    • 27544450920 scopus 로고    scopus 로고
    • The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly
    • Karren M.A., Coonrod E.M., Anderson T.K., Shaw J.M. The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly. J. Cell Biol. 2005, 171:291-301.
    • (2005) J. Cell Biol. , vol.171 , pp. 291-301
    • Karren, M.A.1    Coonrod, E.M.2    Anderson, T.K.3    Shaw, J.M.4
  • 191
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy A.D., McCaffery J.M., Shaw J.M. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 2000, 151:367-380.
    • (2000) J. Cell Biol. , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 192
    • 57649219450 scopus 로고    scopus 로고
    • Targeting of hFis1 to peroxisomes is mediated by Pex19p
    • Delille H.K., Schrader M. Targeting of hFis1 to peroxisomes is mediated by Pex19p. J. Biol. Chem. 2008, 283:31107-31115.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31107-31115
    • Delille, H.K.1    Schrader, M.2
  • 193
    • 34248182897 scopus 로고    scopus 로고
    • Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death
    • Wasiak S., Zunino R., McBride H.M. Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. J. Cell Biol. 2007, 177:439-450.
    • (2007) J. Cell Biol. , vol.177 , pp. 439-450
    • Wasiak, S.1    Zunino, R.2    McBride, H.M.3
  • 194
    • 79958819666 scopus 로고    scopus 로고
    • Discovery of the membrane receptor for mitochondrial fission GTPase Drp1
    • Otera H., Mihara K. Discovery of the membrane receptor for mitochondrial fission GTPase Drp1. Small GTPases 2011, 2:167-172.
    • (2011) Small GTPases , vol.2 , pp. 167-172
    • Otera, H.1    Mihara, K.2
  • 195
    • 79959585289 scopus 로고    scopus 로고
    • The cytosolic domain of Fis1 binds and reversibly clusters lipid vesicles
    • Wells R.C., Hill R.B. The cytosolic domain of Fis1 binds and reversibly clusters lipid vesicles. PLoS One 2011, 6:e21384.
    • (2011) PLoS One , vol.6
    • Wells, R.C.1    Hill, R.B.2
  • 196
    • 50949115617 scopus 로고    scopus 로고
    • High levels of Fis1, a pro-fission mitochondrial protein, trigger autophagy
    • Gomes L.C., Scorrano L. High levels of Fis1, a pro-fission mitochondrial protein, trigger autophagy. Biochim. Biophys. Acta 2008, 1777:860-866.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 860-866
    • Gomes, L.C.1    Scorrano, L.2
  • 197
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • Suen D.F., Norris K.L., Youle R.J. Mitochondrial dynamics and apoptosis. Genes Dev. 2008, 22:1577-1590.
    • (2008) Genes Dev. , vol.22 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 199
    • 79960621726 scopus 로고    scopus 로고
    • Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission
    • Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M. Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission. EMBO J. 2011, 30:2762-2778.
    • (2011) EMBO J. , vol.30 , pp. 2762-2778
    • Zhao, J.1    Liu, T.2    Jin, S.3    Wang, X.4    Qu, M.5    Uhlen, P.6    Tomilin, N.7    Shupliakov, O.8    Lendahl, U.9    Nister, M.10
  • 200
    • 79960629183 scopus 로고    scopus 로고
    • How to split up: lessons from mitochondria
    • Dikov D., Reichert A.S. How to split up: lessons from mitochondria. EMBO J. 2011, 30:2751-2753.
    • (2011) EMBO J. , vol.30 , pp. 2751-2753
    • Dikov, D.1    Reichert, A.S.2
  • 201
    • 0034515057 scopus 로고    scopus 로고
    • The genetics of peroxisome biogenesis
    • Sacksteder K.A., Gould S.J. The genetics of peroxisome biogenesis. Annu. Rev. Genet. 2000, 34:623-652.
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 623-652
    • Sacksteder, K.A.1    Gould, S.J.2
  • 203
    • 79751472085 scopus 로고    scopus 로고
    • Peroxisome metabolism and cellular aging
    • Titorenko V.I., Terlecky S.R. Peroxisome metabolism and cellular aging. Traffic 2011, 12:252-259.
    • (2011) Traffic , vol.12 , pp. 252-259
    • Titorenko, V.I.1    Terlecky, S.R.2
  • 204
    • 49749135155 scopus 로고    scopus 로고
    • Peroxisome fission in Hansenula polymorpha requires Mdv1 and Fis1, two proteins also involved in mitochondrial fission
    • Nagotu S., Krikken A.M., Otzen M., Kiel J.A., Veenhuis M., van der Klei I.J. Peroxisome fission in Hansenula polymorpha requires Mdv1 and Fis1, two proteins also involved in mitochondrial fission. Traffic 2008, 9:1471-1484.
    • (2008) Traffic , vol.9 , pp. 1471-1484
    • Nagotu, S.1    Krikken, A.M.2    Otzen, M.3    Kiel, J.A.4    Veenhuis, M.5    van der Klei, I.J.6
  • 205
    • 41949118972 scopus 로고    scopus 로고
    • Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation
    • Nagotu S., Saraya R., Otzen M., Veenhuis M., van der Klei I.J. Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation. Biochim. Biophys. Acta 2008, 1783:760-769.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 760-769
    • Nagotu, S.1    Saraya, R.2    Otzen, M.3    Veenhuis, M.4    van der Klei, I.J.5
  • 207
    • 63849331278 scopus 로고    scopus 로고
    • Proteins involved in microbody biogenesis and degradation in Aspergillus nidulans
    • Kiel J.A., van der Klei I.J. Proteins involved in microbody biogenesis and degradation in Aspergillus nidulans. Fungal Genet. Biol. 2009, 46(Suppl. 1):S62-S71.
    • (2009) Fungal Genet. Biol. , vol.46 , Issue.SUPPL. 1
    • Kiel, J.A.1    van der Klei, I.J.2
  • 208
    • 77950352526 scopus 로고    scopus 로고
    • The Arabidopsis chloroplast division protein DYNAMIN-RELATED PROTEIN5B also mediates peroxisome division
    • Zhang X., Hu J. The Arabidopsis chloroplast division protein DYNAMIN-RELATED PROTEIN5B also mediates peroxisome division. Plant Cell 2010, 22:431-442.
    • (2010) Plant Cell , vol.22 , pp. 431-442
    • Zhang, X.1    Hu, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.