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Volumn 14, Issue 12, 2013, Pages 803-817

Peroxisomes take shape

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX PROTEIN; PEROXIN;

EID: 84888338804     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3700     Document Type: Review
Times cited : (354)

References (170)
  • 2
    • 84872255359 scopus 로고    scopus 로고
    • Peroxisome assembly and functional diversity in eukaryotic microorganisms
    • Pieuchot, L. & Jedd, G. Peroxisome assembly and functional diversity in eukaryotic microorganisms. Annu. Rev. Microbiol. 66, 237-263 (2012
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 237-263
    • Pieuchot, L.1    Jedd, G.2
  • 3
    • 24944520856 scopus 로고    scopus 로고
    • Peroxisome biogenesis: End of the debate
    • Kunau, W. H. Peroxisome biogenesis: End of the debate. Curr. Biol. 15, R774-R776 (2005
    • (2005) Curr. Biol. , vol.15
    • Kunau, W.H.1
  • 4
    • 80052742250 scopus 로고    scopus 로고
    • Import oligomers induce positive feedback to promote peroxisome differentiation and control organelle abundance
    • Liu, F., Lu, Y., Pieuchot, L., Dhavale, T. & Jedd, G. Import oligomers induce positive feedback to promote peroxisome differentiation and control organelle abundance. Dev. Cell 21, 457-468 (2011
    • (2011) Dev. Cell , vol.21 , pp. 457-468
    • Liu, F.1    Lu, Y.2    Pieuchot, L.3    Dhavale, T.4    Jedd, G.5
  • 7
    • 0013897667 scopus 로고
    • Peroxisomes (microbodies and related particles)
    • De Duve, C. & Baudhuin, P. Peroxisomes (microbodies and related particles). Physiol. Rev. 46, 323-357 (1966
    • (1966) Physiol. Rev. , vol.46 , pp. 323-357
    • De Duve, C.1    Baudhuin, P.2
  • 8
    • 4744371532 scopus 로고    scopus 로고
    • Peroxisomes lipid metabolism, and peroxisomal disorders
    • Wanders, R. J. Peroxisomes, lipid metabolism, and peroxisomal disorders. Mol. Genet. Metab. 83, 16-27 (2004
    • (2004) Mol. Genet. Metab. , vol.83 , pp. 16-27
    • Wanders, R.J.1
  • 9
    • 0034576965 scopus 로고    scopus 로고
    • Three-dimensional ultrastructural analysis of peroxisomes in HepG2 cells Absence of peroxisomal reticulum but evidence of close spatial association with the endoplasmic reticulum
    • Grabenbauer, M., Satzler, K., Baumgart, E. & Fahimi, H. D. Three-dimensional ultrastructural analysis of peroxisomes in HepG2 cells. Absence of peroxisomal reticulum but evidence of close spatial association with the endoplasmic reticulum. Cell Biochem. Biophys. 32, 37-49 (2000
    • (2000) Cell Biochem. Biophys. , vol.32 , pp. 37-49
    • Grabenbauer, M.1    Satzler, K.2    Baumgart, E.3    Fahimi, H.D.4
  • 10
    • 33845292901 scopus 로고    scopus 로고
    • Peroxisomes and oxidative stress
    • Schrader, M. & Fahimi, H. D. Peroxisomes and oxidative stress. Biochim. Biophys. Acta 1763, 1755-1766 (2006
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1755-1766
    • Schrader, M.1    Fahimi, H.D.2
  • 11
    • 3242785163 scopus 로고    scopus 로고
    • Fibrates induce hepatic peroxisome and mitochondrial proliferation without overt evidence of cellular proliferation and oxidative stress in cynomolgus monkeys
    • Hoivik, D. J. et al. Fibrates induce hepatic peroxisome and mitochondrial proliferation without overt evidence of cellular proliferation and oxidative stress in cynomolgus monkeys. Carcinogenesis 25, 1757-1769 (2004
    • (2004) Carcinogenesis , vol.25 , pp. 1757-1769
    • Hoivik, D.J.1
  • 12
    • 2942579780 scopus 로고    scopus 로고
    • Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis
    • Ishizuka, M. et al. Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. Exp. Cell Res. 297, 127-141 (2004
    • (2004) Exp. Cell Res. , vol.297 , pp. 127-141
    • Ishizuka, M.1
  • 13
    • 84877596630 scopus 로고    scopus 로고
    • Global analysis of condition-specific subcellular protein distribution and abundance
    • Jung, S. et al. Global analysis of condition-specific subcellular protein distribution and abundance. Mol. Cell Proteom. 12, 1421-1435 (2013
    • (2013) Mol. Cell Proteom. , vol.12 , pp. 1421-1435
    • Jung, S.1
  • 14
    • 12844252572 scopus 로고    scopus 로고
    • Overproduction of a single protein, Pc-Pex11p, results in 2-fold enhanced penicillin production by Penicillium chrysogenum
    • Kiel, J. A., van der Klei, I. J., van den Berg, M. A., Bovenberg, R. A. & Veenhuis, M. Overproduction of a single protein, Pc-Pex11p, results in 2-fold enhanced penicillin production by Penicillium chrysogenum. Fungal Genet. Biol. 42, 154-164 (2005
    • (2005) Fungal Genet. Biol. , vol.42 , pp. 154-164
    • Kiel, J.A.1    Van Der Klei, I.J.2    Van Den Berg, M.A.3    Bovenberg, R.A.4    Veenhuis, M.5
  • 15
    • 41949138471 scopus 로고    scopus 로고
    • Controlling the rates of biochemical reactions and signaling networks by shape and volume changes
    • Lizana, L., Bauer, B. & Orwar, O. Controlling the rates of biochemical reactions and signaling networks by shape and volume changes. Proc. Natl Acad. Sci. USA 105, 4099-4104 (2008
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 4099-4104
    • Lizana, L.1    Bauer, B.2    Orwar, O.3
  • 16
    • 33746813983 scopus 로고    scopus 로고
    • How can biochemical reactions within cells differ from those in test tubes?
    • Minton, A. P. How can biochemical reactions within cells differ from those in test tubes? J. Cell Sci. 119, 2863-2869 (2006
    • (2006) J. Cell Sci. , vol.119 , pp. 2863-2869
    • Minton, A.P.1
  • 17
    • 0033607810 scopus 로고    scopus 로고
    • Localization of a portion of extranuclear ATM to peroxisomes
    • Watters, D. et al. Localization of a portion of extranuclear ATM to peroxisomes. J. Biol. Chem. 274, 34277-34282 (1999
    • (1999) J. Biol. Chem. , vol.274 , pp. 34277-34282
    • Watters, D.1
  • 18
    • 77949883591 scopus 로고    scopus 로고
    • Dynamic changes in the subcellular distribution of Gpd1p in response to cell stress
    • Jung, S., Marelli, M., Rachubinski, R. A., Goodlett, D. R. & Aitchison, J. D. Dynamic changes in the subcellular distribution of Gpd1p in response to cell stress. J. Biol. Chem. 285, 6739-6749 (2010
    • (2010) J. Biol. Chem. , vol.285 , pp. 6739-6749
    • Jung, S.1    Marelli, M.2    Rachubinski, R.A.3    Goodlett, D.R.4    Aitchison, J.D.5
  • 19
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O. & Sinclair, D. A. Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 423, 181-185 (2003
    • (2003) Nature , vol.423 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Sinclair, D.A.5
  • 20
    • 84866514677 scopus 로고    scopus 로고
    • Integration of peroxisomes into an endomembrane system that governs cellular aging
    • Beach, A. et al. Integration of peroxisomes into an endomembrane system that governs cellular aging. Front. Physiol. 3, 283 (2012
    • (2012) Front. Physiol. , vol.3 , Issue.283
    • Beach, A.1
  • 21
    • 84888355753 scopus 로고    scopus 로고
    • Zellweger spectrum disorder with mild phenotype caused by PEX2 gene mutations
    • Mignarri, A. et al. Zellweger spectrum disorder with mild phenotype caused by PEX2 gene mutations. JIMD Rep. 6, 43-46 (2012
    • (2012) JIMD Rep. , vol.6 , pp. 43-46
    • Mignarri, A.1
  • 22
    • 84883464683 scopus 로고    scopus 로고
    • Newly identified milder phenotype of peroxisome biogenesis disorder caused by mutated PEX3 gene
    • Matsui, S., Funahashi, M., Honda, A. & Shimozawa, N. Newly identified milder phenotype of peroxisome biogenesis disorder caused by mutated PEX3 gene. Brain Dev. 35, 842-848 (2012
    • (2012) Brain Dev. , vol.35 , pp. 842-848
    • Matsui, S.1    Funahashi, M.2    Honda, A.3    Shimozawa, N.4
  • 23
    • 84864105217 scopus 로고    scopus 로고
    • First PEX11β patient extends spectrum of peroxisomal biogenesis disorder phenotypes
    • Thoms, S. & Gartner, J. First PEX11β patient extends spectrum of peroxisomal biogenesis disorder phenotypes. J. Med. Genet. 49, 314-316 (2012
    • (2012) J. Med. Genet. , vol.49 , pp. 314-316
    • Thoms, S.1    Gartner, J.2
  • 24
    • 84864035725 scopus 로고    scopus 로고
    • A novel defect of peroxisome division due to a homozygous non-sense mutation in the PEX11β gene
    • Ebberink, M. S. et al. A novel defect of peroxisome division due to a homozygous non-sense mutation in the PEX11β gene. J. Med. Genet. 49, 307-313 (2012
    • (2012) J. Med. Genet. , vol.49 , pp. 307-313
    • Ebberink, M.S.1
  • 25
    • 76549112206 scopus 로고    scopus 로고
    • α-synuclein abnormalities in mouse models of peroxisome biogenesis disorders
    • Yakunin, E. et al. α-synuclein abnormalities in mouse models of peroxisome biogenesis disorders. J. Neurosci. Res. 88, 866-876 (2010
    • (2010) J. Neurosci. Res. , vol.88 , pp. 866-876
    • Yakunin, E.1
  • 26
    • 28844467909 scopus 로고    scopus 로고
    • Peroxisomal proliferation protects from β-Amyloid neurodegeneration
    • Santos, M. J. et al. Peroxisomal proliferation protects from β-Amyloid neurodegeneration. J. Biol. Chem. 280, 41057-41068 (2005
    • (2005) J. Biol. Chem. , vol.280 , pp. 41057-41068
    • Santos, M.J.1
  • 27
    • 80052301114 scopus 로고    scopus 로고
    • A Drosophila model for the Zellweger spectrum of peroxisome biogenesis disorders
    • Mast, F. D. et al. A Drosophila model for the Zellweger spectrum of peroxisome biogenesis disorders. Dis. Model. Mech. 4, 659-672 (2011
    • (2011) Dis. Model. Mech. , vol.4 , pp. 659-672
    • Mast, F.D.1
  • 28
    • 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 7, 1291-1303 (2006
    • (2006) Traffic , vol.7 , pp. 1291-1303
    • Kiel, J.A.1    Veenhuis, M.2    Van Der Klei, I.J.3
  • 29
    • 1642423544 scopus 로고    scopus 로고
    • Multiple targeting modules on peroxisomal proteins are not redundant: Discrete functions of targeting signals within Pmp47 and Pex8p
    • Wang, X. et al. Multiple targeting modules on peroxisomal proteins are not redundant: Discrete functions of targeting signals within Pmp47 and Pex8p. Mol. Biol. Cell 15, 1702-1710 (2004
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1702-1710
    • Wang, X.1
  • 30
    • 0029010680 scopus 로고
    • Import of stably folded proteins into peroxisomes
    • Walton, P. A., Hill, P. E. & Subramani, S. Import of stably folded proteins into peroxisomes. Mol. Biol. Cell 6, 675-683 (1995
    • (1995) Mol. Biol. Cell , vol.6 , pp. 675-683
    • Walton, P.A.1    Hill, P.E.2    Subramani, S.3
  • 31
    • 10944248003 scopus 로고    scopus 로고
    • The rat liver peroxisomal membrane forms a permeability barrier for cofactors but not for small metabolites in vitro
    • Antonenkov, V. D., Sormunen, R. T. & Hiltunen, J. K. The rat liver peroxisomal membrane forms a permeability barrier for cofactors but not for small metabolites in vitro. J. Cell Sci. 117, 5633-5642 (2004
    • (2004) J. Cell Sci. , vol.117 , pp. 5633-5642
    • Antonenkov, V.D.1    Sormunen, R.T.2    Hiltunen, J.K.3
  • 33
    • 27744523622 scopus 로고    scopus 로고
    • Peroxisomal matrix protein import: The transient pore model
    • Erdmann, R. & Schliebs, W. Peroxisomal matrix protein import: The transient pore model. Nature Rev. Mol. Cell Biol. 6, 738-742 (2005
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 738-742
    • Erdmann, R.1    Schliebs, W.2
  • 34
    • 84865279926 scopus 로고    scopus 로고
    • Recent advances in peroxisomal matrix protein import
    • Liu, X., Ma, C. & Subramani, S. Recent advances in peroxisomal matrix protein import. Curr. Opin. Cell Biol. 24, 484-489 (2012
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 484-489
    • Liu, X.1    Ma, C.2    Subramani, S.3
  • 35
    • 84876684927 scopus 로고    scopus 로고
    • The exportomer: The peroxisomal receptor export machinery
    • Platta, H. W., Hagen, S. & Erdmann, R. The exportomer: The peroxisomal receptor export machinery. Cell. Mol. Life Sci. 70, 1393-1411 (2013
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 1393-1411
    • Platta, H.W.1    Hagen, S.2    Erdmann, R.3
  • 36
    • 77649267086 scopus 로고    scopus 로고
    • The peroxisomal importomer constitutes a large and highly dynamic pore
    • Meinecke, M. et al. The peroxisomal importomer constitutes a large and highly dynamic pore. Nature Cell Biol. 12, 273-277 (2010
    • (2010) Nature Cell Biol. , vol.12 , pp. 273-277
    • Meinecke, M.1
  • 37
    • 69949102267 scopus 로고    scopus 로고
    • The peroxisomal matrix import of Pex8p requires only PTS receptors and Pex14p
    • Ma, C., Schumann, U., Rayapuram, N. & Subramani, S. The peroxisomal matrix import of Pex8p requires only PTS receptors and Pex14p. Mol. Biol. Cell 20, 3680-3689 (2009
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3680-3689
    • Ma, C.1    Schumann, U.2    Rayapuram, N.3    Subramani, S.4
  • 38
    • 0034693260 scopus 로고    scopus 로고
    • Characterization of peroxisomal Pex5p from rat liver Pex5p in the Pex5p-Pex14p membrane complex is a transmembrane protein
    • Gouveia, A. M., Reguenga, C., Oliveira, M. E., Sa-Miranda, C. & Azevedo, J. E. Characterization of peroxisomal Pex5p from rat liver. Pex5p in the Pex5p-Pex14p membrane complex is a transmembrane protein. J. Biol. Chem. 275, 32444-32451 (2000
    • (2000) J. Biol. Chem. , Issue.275 , pp. 32444-32451
    • Gouveia, A.M.1    Reguenga, C.2    Oliveira, M.E.3    Sa-Miranda, C.4    Azevedo, J.E.5
  • 39
    • 33748746818 scopus 로고    scopus 로고
    • Membrane association of the cycling peroxisome import receptor Pex5p
    • Kerssen, D. et al. Membrane association of the cycling peroxisome import receptor Pex5p. J. Biol. Chem. 281, 27003-27015 (2006
    • (2006) J. Biol. Chem. , vol.281 , pp. 27003-27015
    • Kerssen, D.1
  • 40
    • 33744519453 scopus 로고    scopus 로고
    • Functional domains and dynamic assembly of the peroxin Pex14p, the entry site of matrix proteins
    • Itoh, R. & Fujiki, Y. Functional domains and dynamic assembly of the peroxin Pex14p, the entry site of matrix proteins. J. Biol. Chem. 281, 10196-10205 (2006
    • (2006) J. Biol. Chem. , vol.281 , pp. 10196-10205
    • Itoh, R.1    Fujiki, Y.2
  • 41
    • 0033605116 scopus 로고    scopus 로고
    • Recombinant human peroxisomal targeting signal receptor PEX5 Structural basis for interaction of PEX5 with PEX14
    • Schliebs, W. et al. Recombinant human peroxisomal targeting signal receptor PEX5. Structural basis for interaction of PEX5 with PEX14. J. Biol. Chem. 274, 5666-5673 (1999
    • (1999) J. Biol. Chem. , vol.274 , pp. 5666-5673
    • Schliebs, W.1
  • 42
    • 27444445080 scopus 로고    scopus 로고
    • Yeast Pex14p possesses two functionally distinct Pex5p and one Pex7p binding sites
    • Niederhoff, K. et al. Yeast Pex14p possesses two functionally distinct Pex5p and one Pex7p binding sites. J. Biol. Chem. 280, 35571-35578 (2005
    • (2005) J. Biol. Chem. , vol.280 , pp. 35571-35578
    • Niederhoff, K.1
  • 43
    • 0037017392 scopus 로고    scopus 로고
    • Hitchhiking fads en route to peroxisomes
    • Subramani, S. Hitchhiking fads en route to peroxisomes. J. Cell Biol. 156, 415-417 (2002
    • (2002) J. Cell Biol. , vol.156 , pp. 415-417
    • Subramani, S.1
  • 44
    • 0036273592 scopus 로고    scopus 로고
    • Peroxisomal-protein import: Is it really that complex?
    • Gould, S. J. & Collins, C. S. Peroxisomal-protein import: Is it really that complex? Nature Rev. Mol. Cell Biol. 3, 382-389 (2002
    • (2002) Nature Rev Mol. Cell Biol. , vol.3 , pp. 382-389
    • Gould, S.J.1    Collins, C.S.2
  • 45
    • 0032479155 scopus 로고    scopus 로고
    • The effects of chaperones and the influence of protein assembly on peroxisomal protein import
    • Crookes, W. J. & Olsen, L. J. The effects of chaperones and the influence of protein assembly on peroxisomal protein import. J. Biol. Chem. 273, 17236-17242 (1998
    • (1998) J. Biol. Chem. , vol.273 , pp. 17236-17242
    • Crookes, W.J.1    Olsen, L.J.2
  • 46
    • 81755181731 scopus 로고    scopus 로고
    • PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-Terminal domain of PEX14
    • Freitas, M. O. et al. PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-Terminal domain of PEX14. J. Biol. Chem. 286, 40509-40519 (2011
    • (2011) J. Biol. Chem. , vol.286 , pp. 40509-40519
    • Freitas, M.O.1
  • 47
    • 29944438326 scopus 로고    scopus 로고
    • Dynamics of the peroxisomal import cycle of PpPex20p: Ubiquitin-dependent localization and regulation
    • Leon, S. et al. Dynamics of the peroxisomal import cycle of PpPex20p: Ubiquitin-dependent localization and regulation. J. Cell Biol. 172, 67-78 (2006
    • (2006) J. Cell Biol. , vol.172 , pp. 67-78
    • Leon, S.1
  • 48
    • 34247487864 scopus 로고    scopus 로고
    • Ubiquitination of the peroxisomal import receptor Pex5p is required for its recycling
    • Platta, H. W. et al. Ubiquitination of the peroxisomal import receptor Pex5p is required for its recycling. J. Cell Biol. 177, 197-204 (2007
    • (2007) J. Cell Biol. , vol.177 , pp. 197-204
    • Platta, H.W.1
  • 49
    • 70350447348 scopus 로고    scopus 로고
    • Pex2 and pex12 function as protein-ubiquitin ligases in peroxisomal protein import
    • Platta, H. W. et al. Pex2 and pex12 function as protein-ubiquitin ligases in peroxisomal protein import. Mol. Cell. Biol. 29, 5505-5516 (2009
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5505-5516
    • Platta, H.W.1
  • 50
    • 23144446970 scopus 로고    scopus 로고
    • Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol
    • Platta, H. W., Grunau, S., Rosenkranz, K., Girzalsky, W. & Erdmann, R. Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol. Nature Cell Biol. 7, 817-822 (2005
    • (2005) Nature Cell Biol. , vol.7 , pp. 817-822
    • Platta, H.W.1    Grunau, S.2    Rosenkranz, K.3    Girzalsky, W.4    Erdmann, R.5
  • 51
    • 28544451220 scopus 로고    scopus 로고
    • Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export
    • Miyata, N. & Fujiki, Y. Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export. Mol. Cell. Biol. 25, 10822-10832 (2005
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10822-10832
    • Miyata, N.1    Fujiki, Y.2
  • 52
    • 0037632981 scopus 로고    scopus 로고
    • Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes
    • Birschmann, I. et al. Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes. Mol. Biol. Cell 14, 2226-2236 (2003
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2226-2236
    • Birschmann, I.1
  • 53
    • 0038394714 scopus 로고    scopus 로고
    • The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes
    • Matsumoto, N., Tamura, S. & Fujiki, Y. The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes. Nature Cell Biol. 5, 454-460 (2003
    • (2003) Nature Cell Biol. , vol.5 , pp. 454-460
    • Matsumoto, N.1    Tamura, S.2    Fujiki, Y.3
  • 54
    • 78649403829 scopus 로고    scopus 로고
    • Peroxisomal protein import and ERAD: Variations on a common theme
    • Schliebs, W., Girzalsky, W. & Erdmann, R. Peroxisomal protein import and ERAD: Variations on a common theme. Nature Rev. Mol. Cell Biol. 11, 885-890 (2010
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 885-890
    • Schliebs, W.1    Girzalsky, W.2    Erdmann, R.3
  • 55
    • 33747893546 scopus 로고    scopus 로고
    • Origin and evolution of the peroxisomal proteome
    • Gabaldon, T. et al. Origin and evolution of the peroxisomal proteome. Biol. Direct 1, 8 (2006
    • (2006) Biol. Direct , vol.1 , pp. 8
    • Gabaldon, T.1
  • 56
    • 33644907201 scopus 로고    scopus 로고
    • The evolutionary origin of peroxisomes: An ER-peroxisome connection
    • Schluter, A. et al. The evolutionary origin of peroxisomes: An ER-peroxisome connection. Mol. Biol. Evol. 23, 838-845 (2006
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 838-845
    • Schluter, A.1
  • 57
    • 34147175418 scopus 로고    scopus 로고
    • A conserved cysteine residue of Pichia pastoris Pex20p is essential for its recycling from the peroxisome to the cytosol
    • Leon, S. & Subramani, S. A conserved cysteine residue of Pichia pastoris Pex20p is essential for its recycling from the peroxisome to the cytosol. J. Biol. Chem. 282, 7424-7430 (2007
    • (2007) J. Biol. Chem. , vol.282 , pp. 7424-7430
    • Leon, S.1    Subramani, S.2
  • 58
    • 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. USA 108, 9113-9118 (2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 9113-9118
    • Agrawal, G.1    Joshi, S.2    Subramani, S.3
  • 59
    • 83355169741 scopus 로고    scopus 로고
    • Cysteine-dependent ubiquitination of Pex18p is linked to cargo translocation across the peroxisomal membrane
    • Hensel, A. et al. Cysteine-dependent ubiquitination of Pex18p is linked to cargo translocation across the peroxisomal membrane. J. Biol. Chem. 286, 43495-43505 (2011
    • (2011) J. Biol. Chem. , vol.286 , pp. 43495-43505
    • Hensel, A.1
  • 60
    • 0028110118 scopus 로고
    • Saccharomyces cerevisiae peroxisomal thiolase is imported as a dimer
    • Glover, J. R., Andrews, D. W. & Rachubinski, R. A. Saccharomyces cerevisiae peroxisomal thiolase is imported as a dimer. Proc. Natl Acad. Sci. USA 91, 10541-10545 (1994
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10541-10545
    • Glover, J.R.1    Andrews, D.W.2    Rachubinski, R.A.3
  • 61
    • 0035115053 scopus 로고    scopus 로고
    • Eci1p uses a PTS1 to enter peroxisomes: Either its own or that of a partner
    • Yang, X., Purdue, P. E. & Lazarow, P. B. Eci1p uses a PTS1 to enter peroxisomes: Either its own or that of a partner, Dci1p. Eur. J. Cell Biol. 80, 126-138 (2001
    • (2001) Dci1p. Eur. J. Cell Biol. , vol.80 , pp. 126-138
    • Yang, X.1    Purdue, P.E.2    Lazarow, P.B.3
  • 62
    • 38149067623 scopus 로고    scopus 로고
    • Lpx1p is a peroxisomal lipase required for normal peroxisome morphology
    • Thoms, S., Debelyy, M. O., Nau, K., Meyer, H. E. & Erdmann, R. Lpx1p is a peroxisomal lipase required for normal peroxisome morphology. FEBS J. 275, 504-514 (2008
    • (2008) FEBS J. , vol.275 , pp. 504-514
    • Thoms, S.1    Debelyy, M.O.2    Nau, K.3    Meyer, H.E.4    Erdmann, R.5
  • 64
    • 19044367930 scopus 로고    scopus 로고
    • Transcriptome profiling to identify genes involved in peroxisome assembly and function
    • Smith, J. J. et al. Transcriptome profiling to identify genes involved in peroxisome assembly and function. J. Cell Biol. 158, 259-271 (2002
    • (2002) J. Cell Biol. , vol.158 , pp. 259-271
    • Smith, J.J.1
  • 65
    • 84884579723 scopus 로고    scopus 로고
    • Redox-regulated cargo binding and release by the peroxisomal targeting signal receptor
    • Ma, C., Hagstrom, D., Polley, S. G. & Subramani, S. Redox-regulated cargo binding and release by the peroxisomal targeting signal receptor, Pex5. J. Biol. Chem. 288, 27220-27231 (2013
    • (2013) Pex5. J. Biol. Chem. , vol.288 , pp. 27220-27231
    • Ma, C.1    Hagstrom, D.2    Polley, S.G.3    Subramani, S.4
  • 66
    • 84876230401 scopus 로고    scopus 로고
    • Peroxisome membrane proteins: Multiple trafficking routes and multiple functions?
    • Theodoulou, F. L., Bernhardt, K., Linka, N. & Baker, A. Peroxisome membrane proteins: Multiple trafficking routes and multiple functions? Biochem. J. 451, 345-352 (2013
    • (2013) Biochem. J. , vol.451 , pp. 345-352
    • Theodoulou, F.L.1    Bernhardt, K.2    Linka, N.3    Baker, A.4
  • 67
    • 0345861756 scopus 로고    scopus 로고
    • PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins
    • Jones, J. M., Morrell, J. C. & Gould, S. J. PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins. J. Cell Biol. 164, 57-67 (2004
    • (2004) J. Cell Biol. , vol.164 , pp. 57-67
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 68
    • 59449104113 scopus 로고    scopus 로고
    • The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- And Pex16p-dependent pathway
    • Matsuzaki, T. & Fujiki, Y. The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- And Pex16p-dependent pathway. J. Cell Biol. 183, 1275-1286 (2008
    • (2008) J. Cell Biol. , vol.183 , pp. 1275-1286
    • Matsuzaki, T.1    Fujiki, Y.2
  • 69
    • 1842529548 scopus 로고    scopus 로고
    • Potential role for Pex19p in assembly of PTS-receptor docking complexes
    • Fransen, M. et al. Potential role for Pex19p in assembly of PTS-receptor docking complexes. J. Biol. Chem. 279, 12615-12624 (2004
    • (2004) J. Biol. Chem. , vol.279 , pp. 12615-12624
    • Fransen, M.1
  • 70
    • 84858293115 scopus 로고    scopus 로고
    • Peroxisome formation requires the endoplasmic reticulum channel protein Sec61
    • Thoms, S., Harms, I., Kalies, K. U. & Gartner, J. Peroxisome formation requires the endoplasmic reticulum channel protein Sec61. Traffic 13, 599-609 (2012
    • (2012) Traffic , vol.13 , pp. 599-609
    • Thoms, S.1    Harms, I.2    Kalies, K.U.3    Gartner, J.4
  • 71
    • 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 21, 2057-2065 (2010
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2057-2065
    • Van Der Zand, A.1    Braakman, I.2    Tabak, H.F.3
  • 72
    • 49549086224 scopus 로고    scopus 로고
    • The GET complex mediates insertion of tail-Anchored proteins into the ER membrane
    • Schuldiner, M. et al. The GET complex mediates insertion of tail-Anchored proteins into the ER membrane. Cell 134, 634-645 (2008
    • (2008) Cell , vol.134 , pp. 634-645
    • Schuldiner, M.1
  • 73
    • 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. 173, 521-532 (2006
    • (2006) J. Cell Biol. , vol.173 , pp. 521-532
    • Kim, P.K.1    Mullen, R.T.2    Schumann, U.3    Lippincott-Schwartz, J.4
  • 74
    • 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. 178, 399-410 (2007
    • (2007) J. Cell Biol. , vol.178 , pp. 399-410
    • Motley, A.M.1    Hettema, E.H.2
  • 75
    • 22144465170 scopus 로고    scopus 로고
    • Contribution of the endoplasmic reticulum to peroxisome formation
    • Hoepfner, D., Schildknegt, D., Braakman, I., Philippsen, P. & Tabak, H. F. Contribution of the endoplasmic reticulum to peroxisome formation. Cell 122, 85-95 (2005
    • (2005) Cell , vol.122 , pp. 85-95
    • Hoepfner, D.1    Schildknegt, D.2    Braakman, I.3    Philippsen, P.4    Tabak, H.F.5
  • 76
    • 0034962022 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins are properly targeted to peroxisomes in the absence of COPI- And COPII-mediated vesicular transport
    • Voorn-Brouwer, T., Kragt, A., Tabak, H. F. & Distel, B. Peroxisomal membrane proteins are properly targeted to peroxisomes in the absence of COPI- And COPII-mediated vesicular transport. J. Cell Sci. 114, 2199-2204 (2001
    • (2001) J. Cell Sci. , vol.114 , pp. 2199-2204
    • Voorn-Brouwer, T.1    Kragt, A.2    Tabak, H.F.3    Distel, B.4
  • 77
    • 0034717704 scopus 로고    scopus 로고
    • Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis
    • South, S. T., Sacksteder, K. A., Li, X., Liu, Y. & Gould, S. J. Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis. J. Cell Biol. 149, 1345-1360 (2000
    • (2000) J. Cell Biol. , vol.149 , pp. 1345-1360
    • South, S.T.1    Sacksteder, K.A.2    Li, X.3    Liu, Y.4    Gould, S.J.5
  • 78
    • 78650729949 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. USA 107, 21523-21528 (2010
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 21523-21528
    • Lam, S.K.1    Yoda, N.2    Schekman, R.3
  • 79
    • 33745437465 scopus 로고    scopus 로고
    • Expression and functional profiling reveal distinct gene classes involved in fatty acid metabolism
    • 2006 0009
    • Smith, J. J. et al. Expression and functional profiling reveal distinct gene classes involved in fatty acid metabolism. Mol. Syst. Biol. 2, 2006.0009 (2006
    • (2006) Mol. Syst. Biol. , vol.2
    • Smith, J.J.1
  • 80
    • 33846525962 scopus 로고    scopus 로고
    • The sensitivity of yeast mutants to oleic acid implicates the peroxisome and other processes in membrane function
    • Lockshon, D., Surface, L. E., Kerr, E. O., Kaeberlein, M. & Kennedy, B. K. The sensitivity of yeast mutants to oleic acid implicates the peroxisome and other processes in membrane function. Genetics 175, 77-91 (2007
    • (2007) Genetics , vol.175 , pp. 77-91
    • Lockshon, D.1    Surface, L.E.2    Kerr, E.O.3    Kaeberlein, M.4    Kennedy, B.K.5
  • 81
    • 66749160940 scopus 로고    scopus 로고
    • Endoplasmic reticulum-Associated secretory proteins sec20p sec39p and dsl1p are involved in peroxisome biogenesis
    • Perry, R. J., Mast, F. D. & Rachubinski, R. A. Endoplasmic reticulum-Associated secretory proteins Sec20p, Sec39p, and Dsl1p are involved in peroxisome biogenesis. Eukaryot. Cell 8, 830-843 (2009
    • (2009) Eukaryot. Cell , vol.8 , pp. 830-843
    • Perry, R.J.1    Mast, F.D.2    Rachubinski, R.A.3
  • 82
    • 84859745968 scopus 로고    scopus 로고
    • Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes
    • van der Zand, A., Gent, J., Braakman, I. & Tabak, H. F. Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes. Cell 149, 397-409 (2012
    • (2012) Cell , vol.149 , pp. 397-409
    • Van Der Zand, A.1    Gent, J.2    Braakman, I.3    Tabak, H.F.4
  • 83
    • 27144457472 scopus 로고    scopus 로고
    • Pex3p initiates the formation of a preperoxisomal compartment from a subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae
    • Tam, Y. Y., Fagarasanu, A., Fagarasanu, M. & Rachubinski, R. A. Pex3p initiates the formation of a preperoxisomal compartment from a subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae. J. Biol. Chem. 280, 34933-34939 (2005
    • (2005) J. Biol. Chem. , vol.280 , pp. 34933-34939
    • Tam, Y.Y.1    Fagarasanu, A.2    Fagarasanu, M.3    Rachubinski, R.A.4
  • 84
    • 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. 6, 870-872 (2011
    • (2011) Plant Signal. Behav. , vol.6 , pp. 870-872
    • Pan, R.1    Hu, J.2
  • 85
    • 84874639591 scopus 로고    scopus 로고
    • Fis1 Mff MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
    • Loson, O. C., Song, Z., Chen, H. & Chan, D. C. Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission. Mol. Biol. Cell 24, 659-667 (2013
    • (2013) Mol. Biol. Cell , vol.24 , pp. 659-667
    • Loson, O.C.1    Song, Z.2    Chen, H.3    Chan, D.C.4
  • 86
    • 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 1783, 760-769 (2008
    • (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
  • 87
    • 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. 278, 17012-17020 (2003
    • (2003) J. Biol. Chem. , vol.278 , pp. 17012-17020
    • Li, X.1    Gould, S.J.2
  • 88
    • 84867336378 scopus 로고    scopus 로고
    • PEX11 proteins attract Mff and human Fis1 to coordinate peroxisomal fission
    • Koch, J. & Brocard, C. PEX11 proteins attract Mff and human Fis1 to coordinate peroxisomal fission. J. Cell Sci. 125, 3813-3826 (2012
    • (2012) J. Cell Sci. , vol.125 , pp. 3813-3826
    • Koch, J.1    Brocard, C.2
  • 91
    • 0032491315 scopus 로고    scopus 로고
    • Expression of PEX11β mediates peroxisome proliferation in the absence of extracellular stimuli
    • Schrader, M. et al. Expression of PEX11β mediates peroxisome proliferation in the absence of extracellular stimuli. J. Biol. Chem. 273, 29607-29614 (1998
    • (1998) J. Biol. Chem. , vol.273 , pp. 29607-29614
    • Schrader, M.1
  • 92
    • 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 16, 5077-5086 (2005
    • (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
  • 93
    • 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. 121, 1633-1640 (2008
    • (2008) J. Cell Sci. , vol.121 , pp. 1633-1640
    • Motley, A.M.1    Ward, G.P.2    Hettema, E.H.3
  • 94
    • 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. 285, 6670-6680 (2010
    • (2010) J. Biol. Chem. , vol.285 , pp. 6670-6680
    • Knoblach, B.1    Rachubinski, R.A.2
  • 95
    • 84859416429 scopus 로고    scopus 로고
    • Phosphorylation-dependent Pex11p and Fis1p interaction regulates peroxisome division
    • Joshi, S., Agrawal, G. & Subramani, S. Phosphorylation-dependent Pex11p and Fis1p interaction regulates peroxisome division. Mol. Biol. Cell 23, 1307-1315 (2012
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1307-1315
    • Joshi, S.1    Agrawal, G.2    Subramani, S.3
  • 96
    • 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. 135, 123-137 (1996
    • (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
  • 97
    • 0029142737 scopus 로고
    • Muscle-specific overexpression of lipoprotein lipase causes a severe myopathy characterized by proliferation of mitochondria and peroxisomes in transgenic mice
    • Levak-Frank, S. et al. Muscle-specific overexpression of lipoprotein lipase causes a severe myopathy characterized by proliferation of mitochondria and peroxisomes in transgenic mice. J. Clin. Invest. 96, 976-986 (1995
    • (1995) J. Clin. Invest. , vol.96 , pp. 976-986
    • Levak-Frank, S.1
  • 98
    • 0035157544 scopus 로고    scopus 로고
    • Genome-wide responses to mitochondrial dysfunction
    • Epstein, C. B. et al. Genome-wide responses to mitochondrial dysfunction. Mol. Biol. Cell 12, 297-308 (2001
    • (2001) Mol. Biol. Cell , vol.12 , pp. 297-308
    • Epstein, C.B.1
  • 99
    • 1842665662 scopus 로고    scopus 로고
    • Mitochondrial signaling: The retrograde response
    • Butow, R. A. & Avadhani, N. G. Mitochondrial signaling: The retrograde response. Mol. Cell 14, 1-15 (2004
    • (2004) Mol. Cell , vol.14 , pp. 1-15
    • Butow, R.A.1    Avadhani, N.G.2
  • 100
    • 0034627808 scopus 로고    scopus 로고
    • Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multistep peroxisome assembly pathway of Yarrowia lipolytica
    • Titorenko, V. I., Chan, H. & Rachubinski, R. A. Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multistep peroxisome assembly pathway of Yarrowia lipolytica. J. Cell Biol. 148, 29-44 (2000
    • (2000) J. Cell Biol. , vol.148 , pp. 29-44
    • Titorenko, V.I.1    Chan, H.2    Rachubinski, R.A.3
  • 101
    • 0034698778 scopus 로고    scopus 로고
    • Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p
    • Titorenko, V. I. & Rachubinski, R. A. Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p. J. Cell Biol. 150, 881-886 (2000
    • (2000) J. Cell Biol. , vol.150 , pp. 881-886
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 103
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel, W. & Rabouille, C. Mechanisms of regulated unconventional protein secretion. Nature Rev. Mol. Cell Biol. 10, 148-155 (2009
    • (2009) Nature Rev. Mol. Cell Biol. , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 104
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function
    • Saftig, P. & Klumperman, J. Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function. Nature Rev. Mol. Cell Biol. 10, 623-635 (2009
    • (2009) Nature Rev. Mol. Cell Biol. , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 105
    • 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. 17, 376-383 (2005
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 376-383
    • Yan, M.1    Rayapuram, N.2    Subramani, S.3
  • 106
    • 0041765775 scopus 로고    scopus 로고
    • Peroxisome biogenesis: Advances and conundrums
    • Lazarow, P. B. Peroxisome biogenesis: Advances and conundrums. Curr. Opin. Cell Biol. 15, 489-497 (2003
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 489-497
    • Lazarow, P.B.1
  • 107
    • 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. 193, 885-900 (2011
    • (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
  • 108
    • 84864029381 scopus 로고    scopus 로고
    • Genetics and molecular basis of human peroxisome biogenesis disorders
    • Waterham, H. R. & Ebberink, M. S. Genetics and molecular basis of human peroxisome biogenesis disorders. Biochim. Biophys. Acta 1822, 1430-1441 (2012)
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1430-1441
    • Waterham, H.R.1    Ebberink, M.S.2
  • 109
    • 33646093006 scopus 로고    scopus 로고
    • The peroxisomal membrane protein Inp2p is the peroxisome-specific receptor for the myosin V motor Myo2p of Saccharomyces cerevisiae
    • Fagarasanu, A., Fagarasanu, M., Eitzen, G. A., Aitchison, J. D. & Rachubinski, R. A. The peroxisomal membrane protein Inp2p is the peroxisome-specific receptor for the myosin V motor Myo2p of Saccharomyces cerevisiae. Dev. Cell 10, 587-600 (2006
    • (2006) Dev. Cell , vol.10 , pp. 587-600
    • Fagarasanu, A.1    Fagarasanu, M.2    Eitzen, G.A.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 110
    • 22344452004 scopus 로고    scopus 로고
    • Inp1p is a peroxisomal membrane protein required for peroxisome inheritance in Saccharomyces cerevisiae
    • Fagarasanu, M., Fagarasanu, A., Tam, Y. Y., Aitchison, J. D. & Rachubinski, R. A. Inp1p is a peroxisomal membrane protein required for peroxisome inheritance in Saccharomyces cerevisiae. J. Cell Biol. 169, 765-775 (2005
    • (2005) J. Cell Biol. , vol.169 , pp. 765-775
    • Fagarasanu, M.1    Fagarasanu, A.2    Tam, Y.Y.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 111
    • 28644447348 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae
    • Reggiori, F., Monastyrska, I., Shintani, T. & Klionsky, D. J. The actin cytoskeleton is required for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae. Mol. Biol. Cell 16, 5843-5856 (2005
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5843-5856
    • Reggiori, F.1    Monastyrska, I.2    Shintani, T.3    Klionsky, D.J.4
  • 112
    • 79956071527 scopus 로고    scopus 로고
    • PEX14 is required for microtubule-based peroxisome motility in human cells
    • Bharti, P. et al. PEX14 is required for microtubule-based peroxisome motility in human cells. J. Cell Sci. 124, 1759-1768 (2011
    • (2011) J. Cell Sci. , vol.124 , pp. 1759-1768
    • Bharti, P.1
  • 113
    • 34347383511 scopus 로고    scopus 로고
    • Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex
    • Stelter, P. et al. Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex. Nature Cell Biol. 9, 788-796 (2007
    • (2007) Nature Cell Biol. , vol.9 , pp. 788-796
    • Stelter, P.1
  • 114
    • 38049062944 scopus 로고    scopus 로고
    • Pex14 is the sole component of the peroxisomal translocon that is required for pexophagy
    • Zutphen, T., Veenhuis, M. & van der Klei, I. J. Pex14 is the sole component of the peroxisomal translocon that is required for pexophagy. Autophagy 4, 63-66 (2008
    • (2008) Autophagy , vol.4 , pp. 63-66
    • Zutphen, T.1    Veenhuis, M.2    Van Der Klei, I.J.3
  • 115
    • 84884909413 scopus 로고    scopus 로고
    • Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency
    • Cogliati, S. et al. Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency. Cell 155, 160-171 (2013
    • (2013) Cell , vol.155 , pp. 160-171
    • Cogliati, S.1
  • 116
    • 0036678847 scopus 로고    scopus 로고
    • Dissection of transient oxidative stress response in Saccharomyces cerevisiae by using DNA microarrays
    • Koerkamp, M. G. et al. Dissection of transient oxidative stress response in Saccharomyces cerevisiae by using DNA microarrays. Mol. Biol. Cell 13, 2783-2794 (2002
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2783-2794
    • Koerkamp, M.G.1
  • 117
    • 34249931654 scopus 로고    scopus 로고
    • Transcriptional responses to fatty acid are coordinated by combinatorial control
    • Smith, J. J. et al. Transcriptional responses to fatty acid are coordinated by combinatorial control. Mol. Syst. Biol. 3, 115 (2007
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 115
    • Smith, J.J.1
  • 118
    • 0034733570 scopus 로고    scopus 로고
    • Regulation of peroxisome size and number by fatty acid β-oxidation in the yeast Yarrowia lipolytica
    • Smith, J. J., Brown, T. W., Eitzen, G. A. & Rachubinski, R. A. Regulation of peroxisome size and number by fatty acid β-oxidation in the yeast Yarrowia lipolytica. J. Biol. Chem. 275, 20168-20178 (2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 20168-20178
    • Smith, J.J.1    Brown, T.W.2    Eitzen, G.A.3    Rachubinski, R.A.4
  • 119
    • 0023878166 scopus 로고
    • A new peroxisomal disorder with enlarged peroxisomes and a specific deficiency of acyl- CoA oxidase (pseudo-neonatal adrenoleukodystrophy)
    • Poll-The, B. T. et al. A new peroxisomal disorder with enlarged peroxisomes and a specific deficiency of acyl- CoA oxidase (pseudo-neonatal adrenoleukodystrophy). Am. J. Hum. Genet. 42, 422-434 (1988
    • (1988) Am. J. Hum. Genet. , vol.42 , pp. 422-434
    • Poll-The, B.T.1
  • 120
    • 0033047785 scopus 로고    scopus 로고
    • Metabolic control of peroxisome abundance
    • Chang, C. C. et al. Metabolic control of peroxisome abundance. J. Cell Sci. 112, 1579-1590 (1999
    • (1999) J. Cell Sci. , vol.112 , pp. 1579-1590
    • Chang, C.C.1
  • 121
    • 77956513446 scopus 로고    scopus 로고
    • Integrated phosphoproteomics analysis of a signaling network governing nutrient response and peroxisome induction
    • Saleem, R. A. et al. Integrated phosphoproteomics analysis of a signaling network governing nutrient response and peroxisome induction. Mol. Cell Proteom. 9, 2076-2088 (2010
    • (2010) Mol. Cell Proteom. , vol.9 , pp. 2076-2088
    • Saleem, R.A.1
  • 122
    • 34247475252 scopus 로고    scopus 로고
    • A signal from inside the peroxisome initiates its division by promoting the remodeling of the peroxisomal membrane
    • Guo, T. et al. A signal from inside the peroxisome initiates its division by promoting the remodeling of the peroxisomal membrane. J. Cell Biol. 177, 289-303 (2007
    • (2007) J. Cell Biol. , vol.177 , pp. 289-303
    • Guo, T.1
  • 123
    • 84884284362 scopus 로고    scopus 로고
    • An ER-peroxisome tether exerts peroxisome population control in yeast
    • Knoblach, B. et al. An ER-peroxisome tether exerts peroxisome population control in yeast. EMBO J. 32, 2439-2453 (2013
    • (2013) EMBO J. , vol.32 , pp. 2439-2453
    • Knoblach, B.1
  • 124
    • 84884369584 scopus 로고    scopus 로고
    • A combined approach of quantitative interaction proteomics and live-cell imaging reveals a regulatory role for endoplasmic reticulum (ER) reticulon homology proteins in peroxisome biogenesis
    • David, C. et al. A combined approach of quantitative interaction proteomics and live-cell imaging reveals a regulatory role for endoplasmic reticulum (ER) reticulon homology proteins in peroxisome biogenesis. Mol. Cell Proteom. 12, 2408-2425 (2013
    • (2013) Mol. Cell Proteom. , vol.12 , pp. 2408-2425
    • David, C.1
  • 125
    • 84863843241 scopus 로고    scopus 로고
    • Pex3-Anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
    • Motley, A. M., Nuttall, J. M. & Hettema, E. H. Pex3-Anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae. EMBO J. 31, 2852-2868 (2012
    • (2012) EMBO J. , vol.31 , pp. 2852-2868
    • Motley, A.M.1    Nuttall, J.M.2    Hettema, E.H.3
  • 126
    • 0037044768 scopus 로고    scopus 로고
    • Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha
    • Bellu, A. R., Salomons, F. A., Kiel, J. A., Veenhuis, M. & Van Der Klei, I. J. Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha. J. Biol. Chem. 277, 42875-42880 (2002
    • (2002) J. Biol. Chem. , vol.277 , pp. 42875-42880
    • Bellu, A.R.1    Salomons, F.A.2    Kiel, J.A.3    Veenhuis, M.4    Van Der Klei, I.J.5
  • 127
    • 42049094041 scopus 로고    scopus 로고
    • PpAtg30 tags peroxisomes for turnover by selective autophagy
    • Farre, J. C., Manjithaya, R., Mathewson, R. D. & Subramani, S. PpAtg30 tags peroxisomes for turnover by selective autophagy. Dev. Cell 14, 365-376 (2008
    • (2008) Dev. Cell , vol.14 , pp. 365-376
    • Farre, J.C.1    Manjithaya, R.2    Mathewson, R.D.3    Subramani, S.4
  • 128
    • 79961124209 scopus 로고    scopus 로고
    • Damaged peroxisomes are subject to rapid autophagic degradation in the yeast Hansenula polymorpha
    • van Zutphen, T., Veenhuis, M. & van der Klei, I. J. Damaged peroxisomes are subject to rapid autophagic degradation in the yeast Hansenula polymorpha. Autophagy 7, 863-872 (2011
    • (2011) Autophagy , vol.7 , pp. 863-872
    • Van Zutphen, T.1    Veenhuis, M.2    Van Der Klei, I.J.3
  • 129
    • 73349103176 scopus 로고    scopus 로고
    • A dual function for Pex3p in peroxisome formation and inheritance
    • Munck, J. M., Motley, A. M., Nuttall, J. M. & Hettema, E. H. A dual function for Pex3p in peroxisome formation and inheritance. J. Cell Biol. 187, 463-471 (2009
    • (2009) J. Cell Biol. , vol.187 , pp. 463-471
    • Munck, J.M.1    Motley, A.M.2    Nuttall, J.M.3    Hettema, E.H.4
  • 130
    • 70449733045 scopus 로고    scopus 로고
    • Pex3 peroxisome biogenesis proteins function in peroxisome inheritance as class V myosin receptors
    • Chang, J. et al. Pex3 peroxisome biogenesis proteins function in peroxisome inheritance as class V myosin receptors. J. Cell Biol. 187, 233-246 (2009
    • (2009) J. Cell Biol. , vol.187 , pp. 233-246
    • Chang, J.1
  • 131
    • 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 13, 157-167 (2012
    • (2012) Traffic , vol.13 , pp. 157-167
    • Huber, A.1    Koch, J.2    Kragler, F.3    Brocard, C.4    Hartig, A.5
  • 132
    • 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. 276, 1429-1439 (2009
    • (2009) FEBS J. , vol.276 , pp. 1429-1439
    • Krikken, A.M.1    Veenhuis, M.2    Van Der Klei, I.J.3
  • 133
    • 84862267187 scopus 로고    scopus 로고
    • Pex19p contributes to peroxisome inheritance in the association of peroxisomes to Myo2p
    • Otzen, M. et al. Pex19p contributes to peroxisome inheritance in the association of peroxisomes to Myo2p. Traffic 13, 947-959 (2012
    • (2012) Traffic , vol.13 , pp. 947-959
    • Otzen, M.1
  • 134
  • 136
    • 0023571885 scopus 로고
    • Three-dimensional reconstruction of a peroxisomal reticulum in regenerating rat liver: Evidence of interconnections between heterogeneous segments
    • Yamamoto, K. & Fahimi, H. D. Three-dimensional reconstruction of a peroxisomal reticulum in regenerating rat liver: Evidence of interconnections between heterogeneous segments. J. Cell Biol. 105, 713-722 (1987
    • (1987) J. Cell Biol. , vol.105 , pp. 713-722
    • Yamamoto, K.1    Fahimi, H.D.2
  • 137
    • 0032845367 scopus 로고    scopus 로고
    • Induction of tubular peroxisomes by UV irradiation and reactive oxygen species in HepG2 cells
    • Schrader, M., Wodopia, R. & Fahimi, H. D. Induction of tubular peroxisomes by UV irradiation and reactive oxygen species in HepG2 cells. J. Histochem. Cytochem. 47, 1141-1148 (1999
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 1141-1148
    • Schrader, M.1    Wodopia, R.2    Fahimi, H.D.3
  • 138
    • 84934442532 scopus 로고    scopus 로고
    • Assessing heterogeneity of peroxisomes: Isolation of two subpopulations from rat liver
    • Islinger, M., Abdolzade-Bavil, A., Liebler, S., Weber, G. & Volkl, A. Assessing heterogeneity of peroxisomes: Isolation of two subpopulations from rat liver. Methods Mol. Biol. 909, 83-96 (2012
    • (2012) Methods Mol. Biol. , vol.909 , pp. 83-96
    • Islinger, M.1    Abdolzade-Bavil, A.2    Liebler, S.3    Weber, G.4    Volkl, A.5
  • 139
    • 84880863470 scopus 로고    scopus 로고
    • Lumenal peroxisomal protein aggregates are removed by concerted fission and autophagy events
    • Manivannan, S., de Boer, R., Veenhuis, M. & van der Klei, I. J. Lumenal peroxisomal protein aggregates are removed by concerted fission and autophagy events. Autophagy 9, 1044-1056 (2013
    • (2013) Autophagy , vol.9 , pp. 1044-1056
    • Manivannan, S.1    De Boer, R.2    Veenhuis, M.3    Van Der Klei, I.J.4
  • 140
    • 38749103478 scopus 로고    scopus 로고
    • Making two organelles from one: Woronin body biogenesis by peroxisomal protein sorting
    • Liu, F. et al. Making two organelles from one: Woronin body biogenesis by peroxisomal protein sorting. J. Cell Biol. 180, 325-339 (2008
    • (2008) J. Cell Biol. , vol.180 , pp. 325-339
    • Liu, F.1
  • 142
    • 7944224890 scopus 로고    scopus 로고
    • Biogenesis of peroxisomes and glycosomes: Trypanosomatid glycosome assembly is a promising new drug target
    • Moyersoen, J., Choe, J., Fan, E., Hol, W. G. & Michels, P. A. Biogenesis of peroxisomes and glycosomes: Trypanosomatid glycosome assembly is a promising new drug target. FEMS Microbiol. Rev. 28, 603-643 (2004
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 603-643
    • Moyersoen, J.1    Choe, J.2    Fan, E.3    Hol, W.G.4    Michels, P.A.5
  • 143
    • 42449096382 scopus 로고    scopus 로고
    • Genome-wide analysis of signaling networks regulating fatty acid-induced gene expression and organelle biogenesis
    • Saleem, R. A. et al. Genome-wide analysis of signaling networks regulating fatty acid-induced gene expression and organelle biogenesis. J. Cell Biol. 181, 281-292 (2008
    • (2008) J. Cell Biol. , vol.181 , pp. 281-292
    • Saleem, R.A.1
  • 144
    • 0036791370 scopus 로고    scopus 로고
    • Cellular responses to mitochondrial dysfunction: It's not always downhill
    • Butow, R. A. Cellular responses to mitochondrial dysfunction: It's not always downhill. Cell Death Differ. 9, 1043-1045 (2002
    • (2002) Cell Death Differ. , vol.9 , pp. 1043-1045
    • Butow, R.A.1
  • 145
    • 84896718031 scopus 로고    scopus 로고
    • Molecular mechanisms of system responses to novel stimuli are predictable from public datasets
    • Danziger, S. A. et al. Molecular mechanisms of system responses to novel stimuli are predictable from public datasets. Nucleic Acids Res. http://dx.doi. org/10.1093/nar/gkt938 (2013
    • (2013) Nucleic Acids Res.
    • Danziger, S.A.1
  • 146
    • 84861423416 scopus 로고    scopus 로고
    • Rab5 is necessary for the biogenesis of the endolysosomal system in vivo
    • Zeigerer, A. et al. Rab5 is necessary for the biogenesis of the endolysosomal system in vivo. Nature 485, 465-470 (2012
    • (2012) Nature , vol.485 , pp. 465-470
    • Zeigerer, A.1
  • 147
    • 77949534948 scopus 로고    scopus 로고
    • A conceptual mathematical model of the dynamic self-organisation of distinct cellular organelles
    • Binder, B., Goede, A., Berndt, N. & Holzhutter, H. G. A conceptual mathematical model of the dynamic self-organisation of distinct cellular organelles. PLoS ONE 4, e8295 (2009
    • (2009) PLoS ONE , vol.4
    • Binder, B.1    Goede, A.2    Berndt, N.3    Holzhutter, H.G.4
  • 148
    • 0035102918 scopus 로고    scopus 로고
    • Plasmalogens: Biosynthesis and functions
    • Nagan, N. & Zoeller, R. A. Plasmalogens: Biosynthesis and functions. Prog. Lipid Res. 40, 199-229 (2001
    • (2001) Prog. Lipid Res. , vol.40 , pp. 199-229
    • Nagan, N.1    Zoeller, R.A.2
  • 149
    • 80052496920 scopus 로고    scopus 로고
    • Peroxisome proliferation-Associated control of reactive oxygen species sets melanocortin tone and feeding in diet-induced obesity
    • Diano, S. et al. Peroxisome proliferation-Associated control of reactive oxygen species sets melanocortin tone and feeding in diet-induced obesity. Nature Med. 17, 1121-1127 (2011
    • (2011) Nature Med. , vol.17 , pp. 1121-1127
    • Diano, S.1
  • 150
    • 77952503750 scopus 로고    scopus 로고
    • Peroxisomes are signaling platforms for antiviral innate immunity
    • Dixit, E. et al. Peroxisomes are signaling platforms for antiviral innate immunity. Cell 141, 668-681 (2010
    • (2010) Cell , vol.141 , pp. 668-681
    • Dixit, E.1
  • 151
    • 78650933521 scopus 로고    scopus 로고
    • Environment-responsive transcription factors bind subtelomeric elements and regulate gene silencing
    • Smith, J. J. et al. Environment-responsive transcription factors bind subtelomeric elements and regulate gene silencing. Mol. Syst. Biol. 7, 455 (2011
    • (2011) Mol. Syst. Biol. , vol.7 , Issue.455
    • Smith, J.J.1
  • 152
    • 80054738928 scopus 로고    scopus 로고
    • Statistical analysis of dynamic transcriptional regulatory network structure
    • Smith, J. J., Saleem, R. A. & Aitchison, J. D. Statistical analysis of dynamic transcriptional regulatory network structure. Methods Mol. Biol. 781, 337-352 (2011
    • (2011) Methods Mol. Biol. , vol.781 , pp. 337-352
    • Smith, J.J.1    Saleem, R.A.2    Aitchison, J.D.3
  • 153
    • 56049119860 scopus 로고    scopus 로고
    • Control of transcriptional variability by overlapping feed-forward regulatory motifs
    • Ratushny, A. V. et al. Control of transcriptional variability by overlapping feed-forward regulatory motifs. Biophys. J. 95, 3715-3723 (2008
    • (2008) Biophys. J. , vol.95 , pp. 3715-3723
    • Ratushny, A.V.1
  • 155
    • 80054732970 scopus 로고    scopus 로고
    • Mathematical modeling of biomolecular network dynamics
    • Ratushny, A. V., Ramsey, S. A. & Aitchison, J. D. Mathematical modeling of biomolecular network dynamics. Methods Mol. Biol. 781, 415-433 (2011
    • (2011) Methods Mol. Biol. , vol.781 , pp. 415-433
    • Ratushny, A.V.1    Ramsey, S.A.2    Aitchison, J.D.3
  • 156
    • 79959813945 scopus 로고    scopus 로고
    • Trade-off between responsiveness and noise suppression in biomolecular system responses to environmental cues
    • Ratushny, A. V., Shmulevich, I. & Aitchison, J. D. Trade-off between responsiveness and noise suppression in biomolecular system responses to environmental cues. PLoS Comput. Biol. 7, e1002091 (2011
    • (2011) PLoS Comput. Biol. , vol.7
    • Ratushny, A.V.1    Shmulevich, I.2    Aitchison, J.D.3
  • 157
    • 33748311990 scopus 로고    scopus 로고
    • Dual feedback loops in the GAL regulon suppress cellular heterogeneity in yeast
    • Ramsey, S. A. et al. Dual feedback loops in the GAL regulon suppress cellular heterogeneity in yeast. Nature Genet. 38, 1082-1087 (2006
    • (2006) Nature Genet. , vol.38 , pp. 1082-1087
    • Ramsey, S.A.1
  • 158
    • 79551545326 scopus 로고    scopus 로고
    • Quantitative analysis of organelle abundance, morphology and dynamics
    • van Zutphen, T. & van der Klei, I. J. Quantitative analysis of organelle abundance, morphology and dynamics. Curr. Opin. Biotechnol. 22, 127-132 (2011
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 127-132
    • Van Zutphen, T.1    Van Der Klei, I.J.2
  • 159
    • 12244250140 scopus 로고    scopus 로고
    • Detecting patterns of protein distribution and gene expression in silico
    • Bassett, D. et al. Detecting patterns of protein distribution and gene expression in silico. Proc. Natl Acad. Sci. USA 102, 516 (2005
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 516
    • Bassett, D.1
  • 160
    • 0034569762 scopus 로고    scopus 로고
    • In silicio search for genes encoding peroxisomal proteins in Saccharomyces cerevisiae
    • Kal, A. J. et al. In silicio search for genes encoding peroxisomal proteins in Saccharomyces cerevisiae. Cell Biochem. Biophys. 32, 1-8 (2000
    • (2000) Cell Biochem. Biophys. , vol.32 , pp. 1-8
    • Kal, A.J.1
  • 161
    • 19944426486 scopus 로고    scopus 로고
    • Quantitative mass spectrometry reveals a role for the GTPase Rho1p in actin organization on the peroxisome membrane
    • Marelli, M. et al. Quantitative mass spectrometry reveals a role for the GTPase Rho1p in actin organization on the peroxisome membrane. J. Cell Biol. 167, 1099-1112 (2004
    • (2004) J. Cell Biol. , vol.167 , pp. 1099-1112
    • Marelli, M.1
  • 162
    • 0036747350 scopus 로고    scopus 로고
    • Approaching complete peroxisome characterization by gas-phase fractionation
    • Yi, E. C. et al. Approaching complete peroxisome characterization by gas-phase fractionation. Electrophoresis 23, 3205-3216 (2002
    • (2002) Electrophoresis , vol.23 , pp. 3205-3216
    • Yi, E.C.1
  • 163
    • 0034843468 scopus 로고    scopus 로고
    • Identification of peroxisomal membrane proteins of Saccharomyces cerevisiae by mass spectrometry
    • Schafer, H., Nau, K., Sickmann, A., Erdmann, R. & Meyer, H. E. Identification of peroxisomal membrane proteins of Saccharomyces cerevisiae by mass spectrometry. Electrophoresis 22, 2955-2968 (2001
    • (2001) Electrophoresis , vol.22 , pp. 2955-2968
    • Schafer, H.1    Nau, K.2    Sickmann, A.3    Erdmann, R.4    Meyer, H.E.5
  • 164
    • 77957758512 scopus 로고    scopus 로고
    • Genome-wide analysis of effectors of peroxisome biogenesis
    • Saleem, R. A. et al. Genome-wide analysis of effectors of peroxisome biogenesis. PLoS ONE 5, e11953 (2010
    • (2010) PLoS ONE , vol.5
    • Saleem, R.A.1
  • 165
    • 60849129470 scopus 로고    scopus 로고
    • Imaging-based live cell yeast screen identifies novel factors involved in peroxisome assembly
    • Wolinski, H. et al. Imaging-based live cell yeast screen identifies novel factors involved in peroxisome assembly. J. Proteome Res. 8, 20-27 (2009
    • (2009) J. Proteome Res. , vol.8 , pp. 20-27
    • Wolinski, H.1
  • 166
    • 80053404632 scopus 로고    scopus 로고
    • A regression model approach to enable cell morphology correction in high-Throughput flow cytometry
    • Knijnenburg, T. A. et al. A regression model approach to enable cell morphology correction in high-Throughput flow cytometry. Mol. Syst. Biol. 7, 531 (2011
    • (2011) Mol. Syst. Biol. , vol.7 , Issue.531
    • Knijnenburg, T.A.1
  • 167
    • 33746072623 scopus 로고    scopus 로고
    • Targeting of the tail-Anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-Terminal PEX19-binding sites
    • Halbach, A. et al. Targeting of the tail-Anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-Terminal PEX19-binding sites. J. Cell Sci. 119, 2508-2517 (2006
    • (2006) J. Cell Sci. , vol.119 , pp. 2508-2517
    • Halbach, A.1
  • 168
    • 78149407181 scopus 로고    scopus 로고
    • Identification of PEX33, a novel component of the peroxisomal docking complex in the filamentous fungus Neurospora crassa
    • Managadze, D. et al. Identification of PEX33, a novel component of the peroxisomal docking complex in the filamentous fungus Neurospora crassa. Eur. J. Cell Biol. 89, 955-964 (2010
    • (2010) Eur. J. Cell Biol. , vol.89 , pp. 955-964
    • Managadze, D.1
  • 169
    • 33750447941 scopus 로고    scopus 로고
    • Dynamin-related proteins Vps1p and Dnm1p control peroxisome abundance in Saccharomyces cerevisiae
    • Kuravi, K. et al. Dynamin-related proteins Vps1p and Dnm1p control peroxisome abundance in Saccharomyces cerevisiae. J. Cell Sci. 119, 3994-4001 (2006
    • (2006) J. Cell Sci. , vol.119 , pp. 3994-4001
    • Kuravi, K.1
  • 170
    • 33750072352 scopus 로고    scopus 로고
    • Phosphoinositide synthesis and degradation in isolated rat liver peroxisomes
    • Jeynov, B., Lay, D., Schmidt, F., Tahirovic, S. & Just, W. W. Phosphoinositide synthesis and degradation in isolated rat liver peroxisomes. FEBS Lett. 580, 5917-5924 (2006
    • (2006) FEBS Lett. , vol.580 , pp. 5917-5924
    • Jeynov, B.1    Lay, D.2    Schmidt, F.3    Tahirovic, S.4    Just, W.W.5


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