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Volumn 28, Issue 5, 2004, Pages 603-643

Biogenesis of peroxisomes and glycosomes: Trypanosomatid glycosome assembly is a promising new drug target

Author keywords

Drug design; Glycosome and peroxisome biogenesis; Peroxin; Protein protein interaction; Trypanosomatids

Indexed keywords

GLYCOLYTIC ENZYME; MATRIX PROTEIN; MEMBRANE PROTEIN; PEROXIN;

EID: 7944224890     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsre.2004.06.004     Document Type: Review
Times cited : (91)

References (310)
  • 1
    • 0035900653 scopus 로고    scopus 로고
    • Reconstructing/deconstructing the earliest eukaryotes: How comparative genomics can help
    • J.B. Dacks, and W.F. Doolittle Reconstructing/deconstructing the earliest eukaryotes: how comparative genomics can help Cell 107 2001 419 425
    • (2001) Cell , vol.107 , pp. 419-425
    • Dacks, J.B.1    Doolittle, W.F.2
  • 2
    • 0037025197 scopus 로고    scopus 로고
    • Rooting the eukaryote tree by using a derived gene fusion
    • A. Stechmann, and T. Cavalier-Smith Rooting the eukaryote tree by using a derived gene fusion Science 297 2002 89 91
    • (2002) Science , vol.297 , pp. 89-91
    • Stechmann, A.1    Cavalier-Smith, T.2
  • 3
    • 0028607296 scopus 로고
    • The evolutionary expansion of the trypanosomatid flagellates
    • K. Vickerman The evolutionary expansion of the trypanosomatid flagellates Int. J. Parasitol. 24 1994 1317 1331
    • (1994) Int. J. Parasitol. , vol.24 , pp. 1317-1331
    • Vickerman, K.1
  • 4
    • 0036242661 scopus 로고    scopus 로고
    • Basic cell biology of Trypanosoma cruzi
    • W. De Souza Basic cell biology of Trypanosoma cruzi Curr. Pharm. Des. 8 2002 269 285
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 269-285
    • De Souza, W.1
  • 5
    • 0017366999 scopus 로고
    • Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei: The glycosome
    • F.R. Opperdoes, and P. Borst Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei: the glycosome FEBS Lett. 80 1977 360 364
    • (1977) FEBS Lett. , vol.80 , pp. 360-364
    • Opperdoes, F.R.1    Borst, P.2
  • 6
    • 0023464501 scopus 로고
    • Compartmentation of carbohydrate metabolism in trypanosomes
    • F.R. Opperdoes Compartmentation of carbohydrate metabolism in trypanosomes Annu. Rev. Microbiol. 41 1987 127 151
    • (1987) Annu. Rev. Microbiol. , vol.41 , pp. 127-151
    • Opperdoes, F.R.1
  • 7
    • 0028180653 scopus 로고
    • Structure, function, and biogenesis of glycosomes in Kinetoplastida
    • V. Hannaert, and P.A.M. Michels Structure, function, and biogenesis of glycosomes in Kinetoplastida J. Bioenerg. Biomembr. 26 1994 205 212
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 205-212
    • Hannaert, V.1    Michels, P.A.M.2
  • 8
    • 0034333236 scopus 로고    scopus 로고
    • Metabolic aspects of glycosomes in Trypanosomatidae - New data and views
    • P.A.M. Michels, V. Hannaert, and F. Bringaud Metabolic aspects of glycosomes in Trypanosomatidae - new data and views Parasitol. Today 16 2000 482 489
    • (2000) Parasitol. Today , vol.16 , pp. 482-489
    • Michels, P.A.M.1    Hannaert, V.2    Bringaud, F.3
  • 11
    • 0142258170 scopus 로고    scopus 로고
    • Chemotherapy of human African trypanosomiasis: Current and future prospects
    • A.H. Fairlamb Chemotherapy of human African trypanosomiasis: current and future prospects Trends Parasitol. 19 2003 488 494
    • (2003) Trends Parasitol. , vol.19 , pp. 488-494
    • Fairlamb, A.H.1
  • 13
    • 0142227145 scopus 로고    scopus 로고
    • Specific chemotherapy of Chagas disease: Controversies and advances
    • J.A. Urbina, and R. Docampo Specific chemotherapy of Chagas disease: controversies and advances Trends Parasitol. 19 2003 495 501
    • (2003) Trends Parasitol. , vol.19 , pp. 495-501
    • Urbina, J.A.1    Docampo, R.2
  • 14
    • 0142258171 scopus 로고    scopus 로고
    • Leishmaniasis - Current chemotherapy and recent advances in the search for novel drugs
    • S.L. Croft, and G.H. Coombs Leishmaniasis - current chemotherapy and recent advances in the search for novel drugs Trends Parasitol. 19 2003 502 508
    • (2003) Trends Parasitol. , vol.19 , pp. 502-508
    • Croft, S.L.1    Coombs, G.H.2
  • 15
    • 0035222844 scopus 로고    scopus 로고
    • Antigenic variation in trypanosomes: Enhanced phenotypic variation in a eukaryotic parasite
    • J.D. Barry, and R. McCulloch Antigenic variation in trypanosomes: enhanced phenotypic variation in a eukaryotic parasite Adv. Parasitol. 49 2001 1 70
    • (2001) Adv. Parasitol. , vol.49 , pp. 1-70
    • Barry, J.D.1    McCulloch, R.2
  • 16
    • 0036853070 scopus 로고    scopus 로고
    • Evasion of innate immunity by parasitic protozoa
    • D. Sacks, and A. Sher Evasion of innate immunity by parasitic protozoa Nat. Immunol. 3 2002 1041 1047
    • (2002) Nat. Immunol. , vol.3 , pp. 1041-1047
    • Sacks, D.1    Sher, A.2
  • 17
    • 0033083293 scopus 로고    scopus 로고
    • Recent advances in identifying and validating drug targets in trypanosomes and leishmanias
    • M.P. Barrett, J.C. Mottram, and G.H. Coombs Recent advances in identifying and validating drug targets in trypanosomes and leishmanias Trends Microbiol. 7 1999 82 88
    • (1999) Trends Microbiol. , vol.7 , pp. 82-88
    • Barrett, M.P.1    Mottram, J.C.2    Coombs, G.H.3
  • 18
    • 0033927095 scopus 로고    scopus 로고
    • Target-based drug discovery for malaria, leishmaniasis, and trypanosomiasis
    • K.A. Werbovetz Target-based drug discovery for malaria, leishmaniasis, and trypanosomiasis Curr. Med. Chem. 7 2000 835 860
    • (2000) Curr. Med. Chem. , vol.7 , pp. 835-860
    • Werbovetz, K.A.1
  • 20
    • 0023812484 scopus 로고
    • Compartmentation of glycolysis in trypanosomes: A potential target for new trypanocidal drugs
    • P.A.M. Michels Compartmentation of glycolysis in trypanosomes: a potential target for new trypanocidal drugs Biol. Cell 64 1988 157 164
    • (1988) Biol. Cell , vol.64 , pp. 157-164
    • Michels, P.A.M.1
  • 21
    • 0028949538 scopus 로고
    • Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis
    • C.C. Wang Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis Annu. Rev. Pharmacol. Toxicol. 35 1995 93 127
    • (1995) Annu. Rev. Pharmacol. Toxicol. , vol.35 , pp. 93-127
    • Wang, C.C.1
  • 22
    • 0033977087 scopus 로고    scopus 로고
    • Metabolic control analysis of glycolysis in trypanosomes as an approach to improve selectivity and effectiveness of drugs
    • B.M. Bakker, H.V. Westerhoff, F.R. Opperdoes, and P.A.M. Michels Metabolic control analysis of glycolysis in trypanosomes as an approach to improve selectivity and effectiveness of drugs Mol. Biochem. Parasitol. 106 2000 1 10
    • (2000) Mol. Biochem. Parasitol. , vol.106 , pp. 1-10
    • Bakker, B.M.1    Westerhoff, H.V.2    Opperdoes, F.R.3    Michels, P.A.M.4
  • 23
    • 0035339822 scopus 로고    scopus 로고
    • Enzymes of carbohydrate metabolism as potential drug targets
    • F.R. Opperdoes, and P.A.M. Michels Enzymes of carbohydrate metabolism as potential drug targets Int. J. Parasitol. 31 2001 482 490
    • (2001) Int. J. Parasitol. , vol.31 , pp. 482-490
    • Opperdoes, F.R.1    Michels, P.A.M.2
  • 25
    • 0022538521 scopus 로고
    • Inhibition of glyceraldehyde-3-phosphate dehydrogenase by pentalenolactone in Trypanosoma brucei
    • M. Duszenko, and D. Mecke Inhibition of glyceraldehyde-3-phosphate dehydrogenase by pentalenolactone in Trypanosoma brucei Mol. Biochem. Parasitol. 19 1986 223 229
    • (1986) Mol. Biochem. Parasitol. , vol.19 , pp. 223-229
    • Duszenko, M.1    Mecke, D.2
  • 26
    • 0029589663 scopus 로고
    • The inhibition of pyruvate transport across the plasma membrane of the bloodstream form of Trypanosoma brucei and its metabolic implications
    • E.A.C. Wiemer, P.A.M. Michels, and F.R. Opperdoes The inhibition of pyruvate transport across the plasma membrane of the bloodstream form of Trypanosoma brucei and its metabolic implications Biochem. J. 312 1995 479 484
    • (1995) Biochem. J. , vol.312 , pp. 479-484
    • Wiemer, E.A.C.1    Michels, P.A.M.2    Opperdoes, F.R.3
  • 27
    • 0032548073 scopus 로고    scopus 로고
    • Selective tight binding inhibitors of trypanosomal glyceraldehyde-3- phosphate dehydrogenase via structure-based drug design
    • A.M. Aronov, C.L.M.J. Verlinde, W.G.J. Hol, and M.H. Gelb Selective tight binding inhibitors of trypanosomal glyceraldehyde-3-phosphate dehydrogenase via structure-based drug design J. Med. Chem. 41 1998 4790 4799
    • (1998) J. Med. Chem. , vol.41 , pp. 4790-4799
    • Aronov, A.M.1    Verlinde, C.L.M.J.2    Hol, W.G.J.3    Gelb, M.H.4
  • 29
    • 0019641689 scopus 로고
    • Respiration of Leishmania mexicana amastigotes and promastigotes
    • D.T. Hart, K. Vickerman, and G.H. Coombs Respiration of Leishmania mexicana amastigotes and promastigotes Mol. Biochem. Parasitol. 4 1981 39 51
    • (1981) Mol. Biochem. Parasitol. , vol.4 , pp. 39-51
    • Hart, D.T.1    Vickerman, K.2    Coombs, G.H.3
  • 30
    • 0021248130 scopus 로고
    • Enzymes of carbohydrate metabolism in Leishmania donovani amastigotes
    • J.C. Meade, T.A. Glaser, P.F. Bonventre, and A.J. Mukkada Enzymes of carbohydrate metabolism in Leishmania donovani amastigotes J. Protozool. 31 1984 156 161
    • (1984) J. Protozool. , vol.31 , pp. 156-161
    • Meade, J.C.1    Glaser, T.A.2    Bonventre, P.F.3    Mukkada, A.J.4
  • 31
    • 0021986626 scopus 로고
    • Leishmania mexicana: Enzyme activities of amastigotes and promastigotes and their inhibition by antimonials and arsenicals
    • J.C. Mottram, and G.H. Coombs Leishmania mexicana: enzyme activities of amastigotes and promastigotes and their inhibition by antimonials and arsenicals Exp. Parasitol. 59 1985 151 160
    • (1985) Exp. Parasitol. , vol.59 , pp. 151-160
    • Mottram, J.C.1    Coombs, G.H.2
  • 32
    • 0022260611 scopus 로고
    • Leishmania mexicana: Subcellular distribution of enzymes in amastigotes and promastigotes
    • J.C. Mottram, and G.H. Coombs Leishmania mexicana: subcellular distribution of enzymes in amastigotes and promastigotes Exp. Parasitol. 59 1985 265 274
    • (1985) Exp. Parasitol. , vol.59 , pp. 265-274
    • Mottram, J.C.1    Coombs, G.H.2
  • 33
    • 0034825692 scopus 로고    scopus 로고
    • Life in vacuoles - Nutrient acquisition by Leishmania amastigotes
    • R.J. Burchmore, and M.P. Barrett Life in vacuoles - nutrient acquisition by Leishmania amastigotes Int. J. Parasitol. 31 2001 1311 1320
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1311-1320
    • Burchmore, R.J.1    Barrett, M.P.2
  • 34
    • 0020103971 scopus 로고
    • A comparative study of Leishmania mexicana amastigotes and promastigotes. Enzyme activities and subcellular locations
    • G.H. Coombs, J.A. Craft, and D.T. Hart A comparative study of Leishmania mexicana amastigotes and promastigotes. Enzyme activities and subcellular locations Mol. Biochem. Parasitol. 5 1982 199 211
    • (1982) Mol. Biochem. Parasitol. , vol.5 , pp. 199-211
    • Coombs, G.H.1    Craft, J.A.2    Hart, D.T.3
  • 35
    • 0021869320 scopus 로고
    • Enhanced metabolism of Leishmania donovani amastigotes at acid pH: An adaptation for intracellular growth
    • A.J. Mukkada, J.C. Meade, T.A. Glaser, and P.F. Bonventre Enhanced metabolism of Leishmania donovani amastigotes at acid pH: an adaptation for intracellular growth Science 229 1985 1099 1101
    • (1985) Science , vol.229 , pp. 1099-1101
    • Mukkada, A.J.1    Meade, J.C.2    Glaser, T.A.3    Bonventre, P.F.4
  • 37
    • 0023445305 scopus 로고
    • Aerobic glucose fermentation by Trypanosoma cruzi axenic culture amastigote-like forms during growth and differentiation to epimastigotes
    • J.C. Engel, B.M. Franke de Cazzulo, A.O. Stoppani, J.J. Cannata, and J.J. Cazzulo Aerobic glucose fermentation by Trypanosoma cruzi axenic culture amastigote-like forms during growth and differentiation to epimastigotes Mol. Biochem. Parasitol. 26 1987 1 10
    • (1987) Mol. Biochem. Parasitol. , vol.26 , pp. 1-10
    • Engel, J.C.1    Franke De Cazzulo, B.M.2    Stoppani, A.O.3    Cannata, J.J.4    Cazzulo, J.J.5
  • 38
    • 0026699609 scopus 로고
    • Aerobic fermentation of glucose by trypanosomatids
    • J.J. Cazzulo Aerobic fermentation of glucose by trypanosomatids FASEB J. 6 1992 3153 3161
    • (1992) FASEB J. , vol.6 , pp. 3153-3161
    • Cazzulo, J.J.1
  • 39
    • 0032125880 scopus 로고    scopus 로고
    • Differences in energy metabolism between Trypanosomatidae
    • A.G.M. Tielens, and J.J. Van Hellemond Differences in energy metabolism between Trypanosomatidae Parasitol. Today 14 1998 265 271
    • (1998) Parasitol. Today , vol.14 , pp. 265-271
    • Tielens, A.G.M.1    Van Hellemond, J.J.2
  • 41
    • 0029166451 scopus 로고
    • Protein trafficking in kinetoplastid protozoa
    • C. Clayton, T. Häusler, and J. Blattner Protein trafficking in kinetoplastid protozoa Microbiol. Rev. 59 1995 325 344
    • (1995) Microbiol. Rev. , vol.59 , pp. 325-344
    • Clayton, C.1    Häusler, T.2    Blattner, J.3
  • 45
    • 84985444559 scopus 로고
    • Peroxisomes and related particles in historical perspective
    • C. de Duve Peroxisomes and related particles in historical perspective Ann. N. Y. Acad. Sci. 386 1982 1 4
    • (1982) Ann. N. Y. Acad. Sci. , vol.386 , pp. 1-4
    • De Duve, C.1
  • 46
    • 0024369688 scopus 로고
    • Peroxisome biogenesis revisited
    • P. Borst Peroxisome biogenesis revisited Biochim. Biophys. Acta 1008 1989 1 13
    • (1989) Biochim. Biophys. Acta , vol.1008 , pp. 1-13
    • Borst, P.1
  • 47
    • 0025974987 scopus 로고
    • Recognition of a peroxisomal tripeptide entry signal by the glycosomes of Trypanosoma brucei
    • K. Fung, and C. Clayton Recognition of a peroxisomal tripeptide entry signal by the glycosomes of Trypanosoma brucei Mol. Biochem. Parasitol. 45 1991 261 264
    • (1991) Mol. Biochem. Parasitol. , vol.45 , pp. 261-264
    • Fung, K.1    Clayton, C.2
  • 48
    • 0027506960 scopus 로고
    • The C-terminal tripeptide of glycosomal phosphoglycerate kinase is both necessary and sufficient for import into the glycosomes of Trypanosoma brucei
    • J.M. Sommer, G. Peterson, G.A. Keller, M. Parsons, and C.C. Wang The C-terminal tripeptide of glycosomal phosphoglycerate kinase is both necessary and sufficient for import into the glycosomes of Trypanosoma brucei FEBS Lett. 316 1993 53 58
    • (1993) FEBS Lett. , vol.316 , pp. 53-58
    • Sommer, J.M.1    Peterson, G.2    Keller, G.A.3    Parsons, M.4    Wang, C.C.5
  • 49
    • 0032578490 scopus 로고    scopus 로고
    • Compartmentation of phosphoglycerate kinase in Trypanosoma brucei plays a critical role in parasite energy metabolism
    • J. Blattner, S. Helfert, P. Michels, and C. Clayton Compartmentation of phosphoglycerate kinase in Trypanosoma brucei plays a critical role in parasite energy metabolism Proc. Natl. Acad. Sci. USA 95 1998 11596 11600
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11596-11600
    • Blattner, J.1    Helfert, S.2    Michels, P.3    Clayton, C.4
  • 50
    • 0035397515 scopus 로고    scopus 로고
    • Roles of triosephosphate isomerase and aerobic metabolism in Trypanosoma brucei
    • S. Helfert, A.M. Estevez, B. Bakker, P. Michels, and C. Clayton Roles of triosephosphate isomerase and aerobic metabolism in Trypanosoma brucei Biochem. J. 357 2001 117 125
    • (2001) Biochem. J. , vol.357 , pp. 117-125
    • Helfert, S.1    Estevez, A.M.2    Bakker, B.3    Michels, P.4    Clayton, C.5
  • 52
    • 0029587512 scopus 로고
    • Regulation and control of compartmentalized glycolysis in bloodstream form Trypanosoma brucei
    • B.M. Bakker, H.V. Westerhoff, and P.A.M. Michels Regulation and control of compartmentalized glycolysis in bloodstream form Trypanosoma brucei J. Bioenerg. Biomembr. 27 1995 513 525
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 513-525
    • Bakker, B.M.1    Westerhoff, H.V.2    Michels, P.A.M.3
  • 54
    • 0019469031 scopus 로고
    • Subcellular compartmentation of glycolytic intermediates in Trypanosoma brucei
    • N. Visser, F.R. Opperdoes, and P. Borst Subcellular compartmentation of glycolytic intermediates in Trypanosoma brucei Eur. J. Biochem. 118 1981 521 526
    • (1981) Eur. J. Biochem. , vol.118 , pp. 521-526
    • Visser, N.1    Opperdoes, F.R.2    Borst, P.3
  • 55
    • 0022423164 scopus 로고
    • The aerobic/anaerobic transition of glucose metabolism in Trypanosoma brucei
    • R. Eisenthal, and A. Panes The aerobic/anaerobic transition of glucose metabolism in Trypanosoma brucei FEBS Lett. 181 1985 23 27
    • (1985) FEBS Lett. , vol.181 , pp. 23-27
    • Eisenthal, R.1    Panes, A.2
  • 56
    • 7944236195 scopus 로고    scopus 로고
    • Lipid metabolism in relation to human disease. Chapter 7, Permeability properties of peroxisomes
    • R.J.A. Wanders, and J.M. Tager Lipid metabolism in relation to human disease. Chapter 7, Permeability properties of peroxisomes Molec. Aspects Med. 19 1998 113 120
    • (1998) Molec. Aspects Med. , vol.19 , pp. 113-120
    • Wanders, R.J.A.1    Tager, J.M.2
  • 57
    • 0029064219 scopus 로고
    • The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions
    • C.W. Van Roermund, Y. Elgersma, N. Singh, R.J.A. Wanders, and H.F. Tabak The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions EMBO J. 14 1995 3480 3486
    • (1995) EMBO J. , vol.14 , pp. 3480-3486
    • Van Roermund, C.W.1    Elgersma, Y.2    Singh, N.3    Wanders, R.J.A.4    Tabak, H.F.5
  • 58
    • 0034717895 scopus 로고    scopus 로고
    • Transport of fatty acids and metabolites across the peroxisomal membrane
    • E.H. Hettema, and H.F. Tabak Transport of fatty acids and metabolites across the peroxisomal membrane Biochim. Biophys. Acta 1486 2000 18 27
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 18-27
    • Hettema, E.H.1    Tabak, H.F.2
  • 60
    • 0033832732 scopus 로고    scopus 로고
    • The structural properties of plant peroxisomes and their metabolic significance
    • S. Reumann The structural properties of plant peroxisomes and their metabolic significance Biol. Chem. 381 2000 639 648
    • (2000) Biol. Chem. , vol.381 , pp. 639-648
    • Reumann, S.1
  • 61
    • 0020108137 scopus 로고
    • Regulation of glycolysis in Trypanosoma brucei: Hexokinase and phosphofructokinase activity
    • M. Nwagwu, and F.R. Opperdoes Regulation of glycolysis in Trypanosoma brucei: hexokinase and phosphofructokinase activity Acta Trop. 39 1982 61 72
    • (1982) Acta Trop. , vol.39 , pp. 61-72
    • Nwagwu, M.1    Opperdoes, F.R.2
  • 63
    • 0021874922 scopus 로고
    • Purification and regulatory properties of phosphofructokinase from Trypanosoma (Trypanozoon) brucei brucei
    • C.N. Cronin, and K.F. Tipton Purification and regulatory properties of phosphofructokinase from Trypanosoma (Trypanozoon) brucei brucei Biochem. J. 227 1985 113 124
    • (1985) Biochem. J. , vol.227 , pp. 113-124
    • Cronin, C.N.1    Tipton, K.F.2
  • 64
    • 0036038938 scopus 로고    scopus 로고
    • Leishmania donovani phosphofructokinase. Gene characterization, biochemical properties and structure-modeling studies
    • C. López, N. Chevalier, V. Hannaert, D.J. Rigden, P.A.M. Michels, and J.L. Ramirez Leishmania donovani phosphofructokinase. Gene characterization, biochemical properties and structure-modeling studies Eur. J. Biochem. 269 2002 3978 3989
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3978-3989
    • López, C.1    Chevalier, N.2    Hannaert, V.3    Rigden, D.J.4    Michels, P.A.M.5    Ramirez, J.L.6
  • 66
    • 0031021873 scopus 로고    scopus 로고
    • Glycolysis in bloodstream form Trypanosoma brucei can be understood in terms of the kinetics of the glycolytic enzymes
    • B.M. Bakker, P.A.M. Michels, F.R. Opperdoes, and H.V. Westerhoff Glycolysis in bloodstream form Trypanosoma brucei can be understood in terms of the kinetics of the glycolytic enzymes J. Biol. Chem. 272 1997 3207 3215
    • (1997) J. Biol. Chem. , vol.272 , pp. 3207-3215
    • Bakker, B.M.1    Michels, P.A.M.2    Opperdoes, F.R.3    Westerhoff, H.V.4
  • 67
    • 0018977225 scopus 로고
    • Glycolysis in Trypanosoma brucei
    • N. Visser, and F.R. Opperdoes Glycolysis in Trypanosoma brucei Eur. J. Biochem. 103 1980 623 632
    • (1980) Eur. J. Biochem. , vol.103 , pp. 623-632
    • Visser, N.1    Opperdoes, F.R.2
  • 73
    • 0023361695 scopus 로고
    • Proliferation of microbodies in Saccharomyces cerevisiae
    • M. Veenhuis, M. Mateblowski, W.H. Kunau, and W. Harder Proliferation of microbodies in Saccharomyces cerevisiae Yeast 3 1987 77 84
    • (1987) Yeast , vol.3 , pp. 77-84
    • Veenhuis, M.1    Mateblowski, M.2    Kunau, W.H.3    Harder, W.4
  • 74
    • 0025342563 scopus 로고
    • Isolation and characterization of Chinese hamster ovary cell mutants defective in assembly of peroxisomes
    • T. Tsukamoto, S. Yokota, and Y. Fujiki Isolation and characterization of Chinese hamster ovary cell mutants defective in assembly of peroxisomes J. Cell Biol. 110 1990 651 660
    • (1990) J. Cell Biol. , vol.110 , pp. 651-660
    • Tsukamoto, T.1    Yokota, S.2    Fujiki, Y.3
  • 76
    • 0026769928 scopus 로고
    • Targeting efficiencies of various permutations of the consensus C-terminal tripeptide peroxisomal targeting signal
    • B.W. Swinkels, S.J. Gould, and S. Subramani Targeting efficiencies of various permutations of the consensus C-terminal tripeptide peroxisomal targeting signal FEBS Lett. 305 1992 133 136
    • (1992) FEBS Lett. , vol.305 , pp. 133-136
    • Swinkels, B.W.1    Gould, S.J.2    Subramani, S.3
  • 77
  • 78
    • 0032509362 scopus 로고    scopus 로고
    • The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it
    • G. Lametschwandtner, C. Brocard, M. Fransen, P. Van Veldhoven, J. Berger, and A. Hartig The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it J. Biol. Chem. 273 1998 33635 33643
    • (1998) J. Biol. Chem. , vol.273 , pp. 33635-33643
    • Lametschwandtner, G.1    Brocard, C.2    Fransen, M.3    Van Veldhoven, P.4    Berger, J.5    Hartig, A.6
  • 79
    • 0037414447 scopus 로고    scopus 로고
    • Motif refinement of the peroxisomal targeting signal 1 and evaluation of taxon-specific differences
    • G. Neuberger, S. Maurer-Stroh, B. Eisenhaber, A. Hartig, and F. Eisenhaber Motif refinement of the peroxisomal targeting signal 1 and evaluation of taxon-specific differences J. Mol. Biol. 328 2003 567 579
    • (2003) J. Mol. Biol. , vol.328 , pp. 567-579
    • Neuberger, G.1    Maurer-Stroh, S.2    Eisenhaber, B.3    Hartig, A.4    Eisenhaber, F.5
  • 81
    • 0027168271 scopus 로고
    • The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells - The PAS8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family
    • D. McCollum, S. Monosov, and S. Subramini The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells - the PAS8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family J. Cell Biol. 121 1993 761 774
    • (1993) J. Cell Biol. , vol.121 , pp. 761-774
    • McCollum, D.1    Monosov, S.2    Subramini, S.3
  • 82
    • 0027138676 scopus 로고
    • PAS10 is a tetratricopeptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae
    • I. Van der Leij, M.M. Franse, Y. Elgersma, B. Distel, and H.F. Tabak PAS10 is a tetratricopeptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae Proc. Natl. Acad. Sci. USA 90 1993 11782 11786
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11782-11786
    • Van Der Leij, I.1    Franse, M.M.2    Elgersma, Y.3    Distel, B.4    Tabak, H.F.5
  • 83
    • 0028817372 scopus 로고
    • Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders
    • G. Dodt, N. Braverman, C. Wong, A. Moser, H.W. Moser, P. Watkins, D. Valle, and S.J. Gould Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders Nat. Genet. 9 1995 115 125
    • (1995) Nat. Genet. , vol.9 , pp. 115-125
    • Dodt, G.1    Braverman, N.2    Wong, C.3    Moser, A.4    Moser, H.W.5    Watkins, P.6    Valle, D.7    Gould, S.J.8
  • 85
    • 0028982056 scopus 로고
    • The PAH2 gene is required for peroxisome sssembly in the methylotrophic yeast Hansenula polymorpha and encodes a member of the tetratricopeptide repeat family of proteins
    • W.M. Nuttley, R.K. Szilard, J.J. Smith, M. Veenhuis, and R.A. Rachubinski The PAH2 gene is required for peroxisome sssembly in the methylotrophic yeast Hansenula polymorpha and encodes a member of the tetratricopeptide repeat family of proteins Gene 160 1995 33 39
    • (1995) Gene , vol.160 , pp. 33-39
    • Nuttley, W.M.1    Szilard, R.K.2    Smith, J.J.3    Veenhuis, M.4    Rachubinski, R.A.5
  • 86
    • 0029591563 scopus 로고
    • Pay32p of the yeast Yarrowia lipolytica is an intraperoxisomal component of the matrix protein translocation machinery
    • R.K. Szilard, V.I. Titorenko, M. Veenhuis, and R.A. Rachubinski Pay32p of the yeast Yarrowia lipolytica is an intraperoxisomal component of the matrix protein translocation machinery J. Cell Biol. 131 1995 1453 1469
    • (1995) J. Cell Biol. , vol.131 , pp. 1453-1469
    • Szilard, R.K.1    Titorenko, V.I.2    Veenhuis, M.3    Rachubinski, R.A.4
  • 90
    • 0032213098 scopus 로고    scopus 로고
    • The plant PTS-1 receptor: Similarities and differences to its human and yeast counterparts
    • C. Wimmer, M. Schmid, M. Veenhuis, and C. Gietl The plant PTS-1 receptor: similarities and differences to its human and yeast counterparts Plant J. 16 1998 453 464
    • (1998) Plant J. , vol.16 , pp. 453-464
    • Wimmer, C.1    Schmid, M.2    Veenhuis, M.3    Gietl, C.4
  • 91
    • 0030459304 scopus 로고    scopus 로고
    • Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: Evidence that PTS1 protein import is mediated by a cycling receptor
    • G. Dodt, and S.J. Gould Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: evidence that PTS1 protein import is mediated by a cycling receptor J. Cell Biol. 135 1996 1763 1774
    • (1996) J. Cell Biol. , vol.135 , pp. 1763-1774
    • Dodt, G.1    Gould, S.J.2
  • 92
    • 0029840399 scopus 로고    scopus 로고
    • The SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane protein Pex13p functions as a docking site for Pex5p, a mobile receptor for the import of PTS1-containing proteins
    • Y. Elgersma, L. Kwast, A. Klein, T. Voorn-Brouwer, M. Van den Berg, B. Metzig, T. America, H.F. Tabak, and B. Distel The SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane protein Pex13p functions as a docking site for Pex5p, a mobile receptor for the import of PTS1-containing proteins J. Cell Biol. 135 1996 97 109
    • (1996) J. Cell Biol. , vol.135 , pp. 97-109
    • Elgersma, Y.1    Kwast, L.2    Klein, A.3    Voorn-Brouwer, T.4    Van Den Berg, M.5    Metzig, B.6    America, T.7    Tabak, H.F.8    Distel, B.9
  • 93
    • 0029795686 scopus 로고    scopus 로고
    • Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTS1 receptor
    • S.J. Gould, J.E. Kalish, J.C. Morrell, J. Bjorkman, A.J. Urquhart, and D.I. Crane Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTS1 receptor J. Cell Biol. 135 1996 85 95
    • (1996) J. Cell Biol. , vol.135 , pp. 85-95
    • Gould, S.J.1    Kalish, J.E.2    Morrell, J.C.3    Bjorkman, J.4    Urquhart, A.J.5    Crane, D.I.6
  • 94
    • 0029087571 scopus 로고
    • The Pichia pastoris peroxisomal protein Pas8p is the receptor for the C-terminal tripeptide peroxisomal targeting signal
    • S.R. Terlecky, W.M. Nuttley, D. McCollum, E. Sock, and S. Subramani The Pichia pastoris peroxisomal protein Pas8p is the receptor for the C-terminal tripeptide peroxisomal targeting signal EMBO J. 14 1995 3627 3634
    • (1995) EMBO J. , vol.14 , pp. 3627-3634
    • Terlecky, S.R.1    Nuttley, W.M.2    McCollum, D.3    Sock, E.4    Subramani, S.5
  • 95
    • 0027996438 scopus 로고
    • The tetratricopeptide repeat-domain of the PAS10 protein of Saccharomyces cerevisiae is essential for binding the peroxisomal targeting signal -SKL
    • C. Brocard, F. Kragler, M.M. Simon, T. Schuster, and A. Hartig The tetratricopeptide repeat-domain of the PAS10 protein of Saccharomyces cerevisiae is essential for binding the peroxisomal targeting signal -SKL Biochem. Biophys. Res. Commun. 204 1994 1016 1022
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 1016-1022
    • Brocard, C.1    Kragler, F.2    Simon, M.M.3    Schuster, T.4    Hartig, A.5
  • 96
    • 0033664345 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5
    • G.J. Gatto Jr., B.V. Geisbrecht, S.J. Gould, and J.M. Berg Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5 Nat. Struct. Biol. 7 2000 1091 1095
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1091-1095
    • Gatto Jr., G.J.1    Geisbrecht, B.V.2    Gould, S.J.3    Berg, J.M.4
  • 97
  • 98
    • 0031854532 scopus 로고    scopus 로고
    • An isoform of Pex5p, the human PTS1 receptor, is required for the import of PTS2 proteins into peroxisomes
    • N. Braverman, G. Dodt, S.J. Gould, and D. Valle An isoform of Pex5p, the human PTS1 receptor, is required for the import of PTS2 proteins into peroxisomes Hum. Mol. Genet. 7 1998 1195 1205
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1195-1205
    • Braverman, N.1    Dodt, G.2    Gould, S.J.3    Valle, D.4
  • 100
    • 0029795490 scopus 로고    scopus 로고
    • Identification of Pex13p, a peroxisomal membrane receptor for the PTS1 recognition factor
    • R. Erdmann, and G. Blobel Identification of Pex13p, a peroxisomal membrane receptor for the PTS1 recognition factor J. Cell Biol. 135 1996 111 121
    • (1996) J. Cell Biol. , vol.135 , pp. 111-121
    • Erdmann, R.1    Blobel, G.2
  • 102
    • 0034383397 scopus 로고    scopus 로고
    • The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction
    • P. Barnett, G. Bottger, A.T.J. Klein, H.F. Tabak, and B. Distel The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction EMBO J. 19 2000 6382 6391
    • (2000) EMBO J. , vol.19 , pp. 6382-6391
    • Barnett, P.1    Bottger, G.2    Klein, A.T.J.3    Tabak, H.F.4    Distel, B.5
  • 103
    • 0033739464 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae PTS1 receptor Pex5p interacts with the SH3 domain of the peroxisomal membrane protein Pex13p in an unconventional, non-PXXP-related manner
    • G. Bottger, P. Barnett, A.T.J. Klein, A. Kragt, H.F. Tabak, and B. Distel Saccharomyces cerevisiae PTS1 receptor Pex5p interacts with the SH3 domain of the peroxisomal membrane protein Pex13p in an unconventional, non-PXXP-related manner Mol. Biol. Cell 11 2000 3963 3976
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3963-3976
    • Bottger, G.1    Barnett, P.2    Klein, A.T.J.3    Kragt, A.4    Tabak, H.F.5    Distel, B.6
  • 104
    • 0034635364 scopus 로고    scopus 로고
    • Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p
    • A.J. Urquhart, D. Kennedy, S.J. Gould, and D.I. Crane Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p J. Biol. Chem. 11 2000 4127 4136
    • (2000) J. Biol. Chem. , vol.11 , pp. 4127-4136
    • Urquhart, A.J.1    Kennedy, D.2    Gould, S.J.3    Crane, D.I.4
  • 105
    • 0034647937 scopus 로고    scopus 로고
    • The mammalian peroxin Pex5pL, the longer isoform of the mobile peroxisome targeting signal (PTS) type 1 transporter, translocates the Pex7p.PTS2 protein complex into peroxisomes via its initial docking site, Pex14p
    • H. Otera, T. Harano, M. Honsho, K. Ghaedi, S. Mukai, A. Tanaka, A. Kawai, N. Shimizu, and Y. Fujiki The mammalian peroxin Pex5pL, the longer isoform of the mobile peroxisome targeting signal (PTS) type 1 transporter, translocates the Pex7p.PTS2 protein complex into peroxisomes via its initial docking site, Pex14p J. Biol. Chem. 275 2000 21703 21714
    • (2000) J. Biol. Chem. , vol.275 , pp. 21703-21714
    • Otera, H.1    Harano, T.2    Honsho, M.3    Ghaedi, K.4    Mukai, S.5    Tanaka, A.6    Kawai, A.7    Shimizu, N.8    Fujiki, Y.9
  • 106
    • 0030890954 scopus 로고    scopus 로고
    • Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways
    • M. Albertini, P. Rehling, R. Erdmann, W. Girzalsky, J.A.K.W. Kiel, M. Veenhuis, and W.H. Kunau Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways EMBO J. 89 1997 83 92
    • (1997) EMBO J. , vol.89 , pp. 83-92
    • Albertini, M.1    Rehling, P.2    Erdmann, R.3    Girzalsky, W.4    Kiel, J.A.K.W.5    Veenhuis, M.6    Kunau, W.H.7
  • 107
    • 0030767309 scopus 로고    scopus 로고
    • Pex14p is a member of the protein linkage map of Pex5p
    • C. Brocard, G. Lametschwandtner, R. Koudelka, and A. Hartig Pex14p is a member of the protein linkage map of Pex5p EMBO J. 16 1997 5491 5500
    • (1997) EMBO J. , vol.16 , pp. 5491-5500
    • Brocard, C.1    Lametschwandtner, G.2    Koudelka, R.3    Hartig, A.4
  • 108
    • 0032493298 scopus 로고    scopus 로고
    • Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import
    • M. Fransen, S.R. Terlecky, and S. Subramani Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import Proc. Natl. Acad. Sci. USA 95 1998 8087 8092
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8087-8092
    • Fransen, M.1    Terlecky, S.R.2    Subramani, S.3
  • 109
    • 0033617195 scopus 로고    scopus 로고
    • The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis
    • N. Shimizu, R. Itoh, Y. Hirono, H. Otera, K. Ghaedi, K. Tateishi, S. Tamura, K. Okumoto, T. Harano, S. Mukai, and Y. Fujiki The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis J. Biol. Chem. 274 1999 12593 12604
    • (1999) J. Biol. Chem. , vol.274 , pp. 12593-12604
    • Shimizu, N.1    Itoh, R.2    Hirono, Y.3    Otera, H.4    Ghaedi, K.5    Tateishi, K.6    Tamura, S.7    Okumoto, K.8    Harano, T.9    Mukai, S.10    Fujiki, Y.11
  • 111
    • 0035860787 scopus 로고    scopus 로고
    • The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14
    • J. Saidowsky, G. Dodt, K. Kirchberg, A. Wegner, W. Nastainczyk, W.H. Kunau, and W. Schliebs The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14 J. Biol. Chem. 276 2001 34524 34529
    • (2001) J. Biol. Chem. , vol.276 , pp. 34524-34529
    • Saidowsky, J.1    Dodt, G.2    Kirchberg, K.3    Wegner, A.4    Nastainczyk, W.5    Kunau, W.H.6    Schliebs, W.7
  • 112
    • 0033571690 scopus 로고    scopus 로고
    • PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import
    • C.C. Chang, D.S. Warren, K.A. Sacksteder, and S.J. Gould PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import J. Cell Biol. 147 1999 761 773
    • (1999) J. Cell Biol. , vol.147 , pp. 761-773
    • Chang, C.C.1    Warren, D.S.2    Sacksteder, K.A.3    Gould, S.J.4
  • 113
    • 0034682844 scopus 로고    scopus 로고
    • Molecular anatomy of the peroxin Pex12p - Ring finger domain is essential for Pex12p function and interacts with the peroxisome-targeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p
    • K. Okumoto, I. Abe, and Y. Fujiki Molecular anatomy of the peroxin Pex12p - ring finger domain is essential for Pex12p function and interacts with the peroxisome-targeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p J. Biol. Chem. 275 2000 25700 25710
    • (2000) J. Biol. Chem. , vol.275 , pp. 25700-25710
    • Okumoto, K.1    Abe, I.2    Fujiki, Y.3
  • 116
    • 0025941962 scopus 로고
    • A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase
    • B.W. Swinkels, S.J. Gould, A.G. Bodnar, R.A. Rachubinski, and S. Subramani A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase EMBO J. 10 1991 3255 3262
    • (1991) EMBO J. , vol.10 , pp. 3255-3262
    • Swinkels, B.W.1    Gould, S.J.2    Bodnar, A.G.3    Rachubinski, R.A.4    Subramani, S.5
  • 117
    • 0028723252 scopus 로고
    • Protein import deficiencies in human peroxisomal disorders
    • E.A.C. Wiemer, and S. Subramani Protein import deficiencies in human peroxisomal disorders Mol. Genet. Med. 4 1994 119 152
    • (1994) Mol. Genet. Med. , vol.4 , pp. 119-152
    • Wiemer, E.A.C.1    Subramani, S.2
  • 118
    • 0036305188 scopus 로고    scopus 로고
    • Cellular and molecular aspects of Zellweger syndrome and other peroxisome biogenesis disorders
    • U. Brosius, and J. Gärtner Cellular and molecular aspects of Zellweger syndrome and other peroxisome biogenesis disorders Cell. Mol. Life Sci. 59 2002 1058 1069
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1058-1069
    • Brosius, U.1    Gärtner, J.2
  • 119
    • 0029903045 scopus 로고    scopus 로고
    • The import receptor for the peroxisomal targeting signal 2 (PTS2) in Saccharomyces cerevisiae is encoded by the PAS7 gene
    • P. Rehling, M. Marzioch, F. Niesen, E. Wittke, M. Veenhuis, and W.H. Kunau The import receptor for the peroxisomal targeting signal 2 (PTS2) in Saccharomyces cerevisiae is encoded by the PAS7 gene EMBO J. 15 1996 2901 2913
    • (1996) EMBO J. , vol.15 , pp. 2901-2913
    • Rehling, P.1    Marzioch, M.2    Niesen, F.3    Wittke, E.4    Veenhuis, M.5    Kunau, W.H.6
  • 120
    • 0031941276 scopus 로고    scopus 로고
    • Components involved in peroxisome import, biogenesis, proliferation, turnover, and movement
    • S. Subramani Components involved in peroxisome import, biogenesis, proliferation, turnover, and movement Physiol. Rev. 78 1998 171 188
    • (1998) Physiol. Rev. , vol.78 , pp. 171-188
    • Subramani, S.1
  • 121
    • 0028278166 scopus 로고
    • Mutagenesis of the amino targeting signal of Saccharomyces cerevisiae 3-ketoacyl-CoA thiolase reveals conserved amino acids required for import into peroxisomes in vivo
    • J.R. Glover, D.W. Andrews, S. Subramani, and R.A. Rachubinski Mutagenesis of the amino targeting signal of Saccharomyces cerevisiae 3-ketoacyl-CoA thiolase reveals conserved amino acids required for import into peroxisomes in vivo J. Biol. Chem. 269 1994 7558 7563
    • (1994) J. Biol. Chem. , vol.269 , pp. 7558-7563
    • Glover, J.R.1    Andrews, D.W.2    Subramani, S.3    Rachubinski, R.A.4
  • 123
    • 0032419134 scopus 로고    scopus 로고
    • Mutational analyses of a type 2 peroxisomal targeting signal that is capable of directing oligomeric protein import into tobacco BY-2 glyoxysomes
    • C.R. Flynn, R.T. Mullen, and R.N. Trelease Mutational analyses of a type 2 peroxisomal targeting signal that is capable of directing oligomeric protein import into tobacco BY-2 glyoxysomes Plant J. 16 1998 709 720
    • (1998) Plant J. , vol.16 , pp. 709-720
    • Flynn, C.R.1    Mullen, R.T.2    Trelease, R.N.3
  • 124
    • 0028053931 scopus 로고
    • PAS7 encodes a novel yeast member of the WD 40 protein family essential for import of 3-oxoacyl-CoA thiolase, a PTS2-containing protein, into peroxisomes
    • M. Marzioch, R. Erdmann, M. Veenhuis, and W.H. Kunau PAS7 encodes a novel yeast member of the WD 40 protein family essential for import of 3-oxoacyl-CoA thiolase, a PTS2-containing protein, into peroxisomes EMBO J. 13 1994 4908 4918
    • (1994) EMBO J. , vol.13 , pp. 4908-4918
    • Marzioch, M.1    Erdmann, R.2    Veenhuis, M.3    Kunau, W.H.4
  • 125
    • 0028927819 scopus 로고
    • Peb1 (Pas7) in Saccharomyces cerevisiae encodes a hydrophilic, intraperoxisomal protein that is a member of the WD repeat family and is essential for the import of thiolase into peroxisomes
    • J.W. Zhang, and P.B. Lazarow Peb1 (Pas7) in Saccharomyces cerevisiae encodes a hydrophilic, intraperoxisomal protein that is a member of the WD repeat family and is essential for the import of thiolase into peroxisomes J. Cell Biol. 129 1995 65 80
    • (1995) J. Cell Biol. , vol.129 , pp. 65-80
    • Zhang, J.W.1    Lazarow, P.B.2
  • 126
    • 0030946632 scopus 로고    scopus 로고
    • Human Pex7 encodes the peroxisomal PTS2 receptor and is responsible for Rhizomelic chondrodysplasia punctata
    • N. Braverman, G. Steel, C. Obie, A. Moser, H. Moser, S.J. Gould, and D. Valle Human Pex7 encodes the peroxisomal PTS2 receptor and is responsible for Rhizomelic chondrodysplasia punctata Nat. Genet. 15 1997 369 376
    • (1997) Nat. Genet. , vol.15 , pp. 369-376
    • Braverman, N.1    Steel, G.2    Obie, C.3    Moser, A.4    Moser, H.5    Gould, S.J.6    Valle, D.7
  • 128
    • 1842335689 scopus 로고    scopus 로고
    • Rhizomelic chondrodysplasia punctata is caused by deficiency of human Pex7, a homologue of the yeast PTS2 receptor
    • P.E. Purdue, J.W. Zhang, M. Skoneczny, and P.B. Lazarow Rhizomelic chondrodysplasia punctata is caused by deficiency of human Pex7, a homologue of the yeast PTS2 receptor Nat. Genet. 15 1997 381 384
    • (1997) Nat. Genet. , vol.15 , pp. 381-384
    • Purdue, P.E.1    Zhang, J.W.2    Skoneczny, M.3    Lazarow, P.B.4
  • 130
    • 0034231261 scopus 로고    scopus 로고
    • Caenorhabditis elegans has a single pathway to target matrix proteins to peroxisomes
    • A.M. Motley, E.H. Hettema, R. Ketting, R. Plasterk, and H.F. Tabak Caenorhabditis elegans has a single pathway to target matrix proteins to peroxisomes EMBO Rep. 1 2000 40 46
    • (2000) EMBO Rep. , vol.1 , pp. 40-46
    • Motley, A.M.1    Hettema, E.H.2    Ketting, R.3    Plasterk, R.4    Tabak, H.F.5
  • 131
    • 0035834711 scopus 로고    scopus 로고
    • Domain mapping of human PEX5 reveals functional and structural similarities to Saccharomyces cerevisiae Pex18p and Pex21p
    • G. Dodt, D. Warren, E. Becker, P. Rehling, and S.J. Gould Domain mapping of human PEX5 reveals functional and structural similarities to Saccharomyces cerevisiae Pex18p and Pex21p J. Biol. Chem. 276 2001 41769 41781
    • (2001) J. Biol. Chem. , vol.276 , pp. 41769-41781
    • Dodt, G.1    Warren, D.2    Becker, E.3    Rehling, P.4    Gould, S.J.5
  • 132
    • 0036646057 scopus 로고    scopus 로고
    • Functional studies on human Pex7p: Subcellular localization and interaction with proteins containing a peroxisome-targeting signal type 2 and other peroxins
    • K. Ghys, M. Fransen, G.P. Mannaerts, and P.P. Van Veldhoven Functional studies on human Pex7p: subcellular localization and interaction with proteins containing a peroxisome-targeting signal type 2 and other peroxins Biochem. J. 365 2002 41 50
    • (2002) Biochem. J. , vol.365 , pp. 41-50
    • Ghys, K.1    Fransen, M.2    Mannaerts, G.P.3    Van Veldhoven, P.P.4
  • 133
    • 0037088664 scopus 로고    scopus 로고
    • Intracellular localization, function, and dysfunction of the peroxisome-targeting signal type 2 receptor, Pex7p, in mammalian cells
    • S. Mukai, K. Ghaedi, and Y. Fujiki Intracellular localization, function, and dysfunction of the peroxisome-targeting signal type 2 receptor, Pex7p, in mammalian cells J. Biol. Chem. 277 2002 9548 9561
    • (2002) J. Biol. Chem. , vol.277 , pp. 9548-9561
    • Mukai, S.1    Ghaedi, K.2    Fujiki, Y.3
  • 134
    • 0033594103 scopus 로고    scopus 로고
    • Involvement of Pex13p in Pex14p localization and peroxisomal targeting signal 2-dependent protein import into peroxisomes
    • W. Girzalsky, P. Rehling, K. Stein, J. Kipper, L. Blank, W.H. Kunau, and R. Erdmann Involvement of Pex13p in Pex14p localization and peroxisomal targeting signal 2-dependent protein import into peroxisomes J. Cell Biol. 144 1999 1151 1162
    • (1999) J. Cell Biol. , vol.144 , pp. 1151-1162
    • Girzalsky, W.1    Rehling, P.2    Stein, K.3    Kipper, J.4    Blank, L.5    Kunau, W.H.6    Erdmann, R.7
  • 135
    • 0036337231 scopus 로고    scopus 로고
    • Interactions of Pex7p and Pex18p/Pex21p with the peroxisomal docking machinery: Implications for the first steps in PTS2 protein import
    • K. Stein, A. Schell-Steven, R. Erdmann, and H. Rottensteiner Interactions of Pex7p and Pex18p/Pex21p with the peroxisomal docking machinery: implications for the first steps in PTS2 protein import Mol. Cell. Biol. 22 2002 6056 6069
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6056-6069
    • Stein, K.1    Schell-Steven, A.2    Erdmann, R.3    Rottensteiner, H.4
  • 136
    • 0032576614 scopus 로고    scopus 로고
    • Pex18p and Pex21p, a novel pair of related peroxins essential for peroxisomal targeting by the PTS2 pathway
    • P.E. Purdue, X.D. Yang, and P.B. Lazarow Pex18p and Pex21p, a novel pair of related peroxins essential for peroxisomal targeting by the PTS2 pathway J. Cell Biol. 143 1998 1859 1869
    • (1998) J. Cell Biol. , vol.143 , pp. 1859-1869
    • Purdue, P.E.1    Yang, X.D.2    Lazarow, P.B.3
  • 137
    • 0036013390 scopus 로고    scopus 로고
    • Direct interaction and determination of binding domains among peroxisomal import factors in Arabidopsis thaliana
    • K. Nito, M. Hayashi, and M. Nishimura Direct interaction and determination of binding domains among peroxisomal import factors in Arabidopsis thaliana Plant Cell Physiol. 43 2002 355 366
    • (2002) Plant Cell Physiol. , vol.43 , pp. 355-366
    • Nito, K.1    Hayashi, M.2    Nishimura, M.3
  • 138
    • 0032572580 scopus 로고    scopus 로고
    • Pex20p of the yeast Yarrowia lipolytica is required for the oligomerization of thiolase in the cytosol and for its targeting to the peroxisome
    • V.I. Titorenko, J.J. Smith, R.K. Szilard, and R.A. Rachubinski Pex20p of the yeast Yarrowia lipolytica is required for the oligomerization of thiolase in the cytosol and for its targeting to the peroxisome J. Cell Biol. 142 1998 403 420
    • (1998) J. Cell Biol. , vol.142 , pp. 403-420
    • Titorenko, V.I.1    Smith, J.J.2    Szilard, R.K.3    Rachubinski, R.A.4
  • 139
    • 0035203058 scopus 로고    scopus 로고
    • Yarrowia lipolytica Pex20p, Saccharomyces cerevisiae Pex18p/Pex21p and mammalian Pex5pL fulfil a common function in the early steps of the peroxisomal PTS2 import pathway
    • H. Einwächter, S. Sowinski, W.H. Kunau, and W. Schliebs Yarrowia lipolytica Pex20p, Saccharomyces cerevisiae Pex18p/Pex21p and mammalian Pex5pL fulfil a common function in the early steps of the peroxisomal PTS2 import pathway EMBO Rep. 2 2001 1035 1039
    • (2001) EMBO Rep. , vol.2 , pp. 1035-1039
    • Einwächter, H.1    Sowinski, S.2    Kunau, W.H.3    Schliebs, W.4
  • 140
    • 0037326247 scopus 로고    scopus 로고
    • Pex7p and Pex20p of Neurospora crassa function together in PTS2-dependent protein import into peroxisomes
    • M. Sichting, A. Schell-Steven, H. Prokisch, R. Erdmann, and H. Rottensteiner Pex7p and Pex20p of Neurospora crassa function together in PTS2-dependent protein import into peroxisomes Mol. Biol. Cell 14 2003 810 821
    • (2003) Mol. Biol. Cell , vol.14 , pp. 810-821
    • Sichting, M.1    Schell-Steven, A.2    Prokisch, H.3    Erdmann, R.4    Rottensteiner, H.5
  • 141
    • 0023991404 scopus 로고
    • Acyl-CoA oxidase contains two targeting sequences each of which can mediate protein import into peroxisomes
    • G.M. Small, J. Szabo, and P.B. Lazarow Acyl-CoA oxidase contains two targeting sequences each of which can mediate protein import into peroxisomes EMBO J. 7 1988 1167 1173
    • (1988) EMBO J. , vol.7 , pp. 1167-1173
    • Small, G.M.1    Szabo, J.2    Lazarow, P.B.3
  • 142
    • 0037067768 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non-PTS1, import pathway into peroxisomes that is dependent on Pex5p
    • A.T.J. Klein, M. Van den Berg, G. Bottger, H.F. Tabak, and B. Distel Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non-PTS1, import pathway into peroxisomes that is dependent on Pex5p J. Biol. Chem. 277 2002 25011 25019
    • (2002) J. Biol. Chem. , vol.277 , pp. 25011-25019
    • Klein, A.T.J.1    Van Den Berg, M.2    Bottger, G.3    Tabak, H.F.4    Distel, B.5
  • 143
    • 0028033934 scopus 로고
    • An oligomeric protein is imported into peroxisomes in vivo
    • J.A. McNew, and J.M. Goodman An oligomeric protein is imported into peroxisomes in vivo J. Cell Biol. 127 1994 1245 1257
    • (1994) J. Cell Biol. , vol.127 , pp. 1245-1257
    • McNew, J.A.1    Goodman, J.M.2
  • 144
    • 0031080512 scopus 로고    scopus 로고
    • Oilseed isocitrate lyases lacking their essential type 1 peroxisomal targeting signal are piggybacked to glyoxysomes
    • M.S. Lee, R.T. Mullen, and R.N. Trelease Oilseed isocitrate lyases lacking their essential type 1 peroxisomal targeting signal are piggybacked to glyoxysomes Plant Cell 9 1997 185 197
    • (1997) Plant Cell , vol.9 , pp. 185-197
    • Lee, M.S.1    Mullen, R.T.2    Trelease, R.N.3
  • 145
    • 0028783455 scopus 로고
    • How proteins penetrate peroxisomes
    • R.A. Rachubinski, and S. Subramani How proteins penetrate peroxisomes Cell 83 1995 525 528
    • (1995) Cell , vol.83 , pp. 525-528
    • Rachubinski, R.A.1    Subramani, S.2
  • 146
    • 0030606021 scopus 로고    scopus 로고
    • Proteins involved in peroxisome biogenesis and functioning
    • Y. Elgersma, and H.F. Tabak Proteins involved in peroxisome biogenesis and functioning Biochim. Biophys. Acta 1286 1996 269 283
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 269-283
    • Elgersma, Y.1    Tabak, H.F.2
  • 147
    • 0035115053 scopus 로고    scopus 로고
    • Eci1p uses a PTS1 to enter peroxisomes: Either its own or that of a partner, Dci1p
    • X.D. Yang, P.E. Purdue, and P.B. Lazarow Eci1p uses a PTS1 to enter peroxisomes: either its own or that of a partner, Dci1p Eur. J. Cell Biol. 80 2001 126 138
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 126-138
    • Yang, X.D.1    Purdue, P.E.2    Lazarow, P.B.3
  • 148
    • 0031023643 scopus 로고    scopus 로고
    • The Hansenula polymorpha PEX14 gene encodes a novel peroxisomal membrane protein essential for peroxisome biogenesis
    • M. Komori, S.W. Rasmussen, J.A.K.W. Kiel, R.J. Baerends, J.M. Cregg, I.J. Van der Klei, and M. Veenhuis The Hansenula polymorpha PEX14 gene encodes a novel peroxisomal membrane protein essential for peroxisome biogenesis EMBO J. 16 1997 44 53
    • (1997) EMBO J. , vol.16 , pp. 44-53
    • Komori, M.1    Rasmussen, S.W.2    Kiel, J.A.K.W.3    Baerends, R.J.4    Cregg, J.M.5    Van Der Klei, I.J.6    Veenhuis, M.7
  • 149
    • 0034989953 scopus 로고    scopus 로고
    • Pichia pastoris Pex14p, a phosphorylated peroxisomal membrane protein, is part of a PTS-receptor docking complex and interacts with many peroxins
    • M.A. Johnson, W.B. Snyder, J.L. Cereghino, M. Veenhuis, S. Subramani, and J.M. Cregg Pichia pastoris Pex14p, a phosphorylated peroxisomal membrane protein, is part of a PTS-receptor docking complex and interacts with many peroxins Yeast 18 2001 621 641
    • (2001) Yeast , vol.18 , pp. 621-641
    • Johnson, M.A.1    Snyder, W.B.2    Cereghino, J.L.3    Veenhuis, M.4    Subramani, S.5    Cregg, J.M.6
  • 150
    • 0032883925 scopus 로고    scopus 로고
    • Antibodies against Pex14p block ATP-independent binding of matrix proteins to peroxisomes in vitro
    • E. Lopez-Huertas, J.S. Oh, and A. Baker Antibodies against Pex14p block ATP-independent binding of matrix proteins to peroxisomes in vitro FEBS Lett. 459 1999 227 229
    • (1999) FEBS Lett. , vol.459 , pp. 227-229
    • Lopez-Huertas, E.1    Oh, J.S.2    Baker, A.3
  • 151
    • 0034331230 scopus 로고    scopus 로고
    • AtPex14p maintains peroxisomal functions by determining protein targeting to three kinds of plant peroxisomes
    • M. Hayashi, K. Nito, K. Toriyama-Kato, M. Kondo, T. Yamaya, and M. Nishimura AtPex14p maintains peroxisomal functions by determining protein targeting to three kinds of plant peroxisomes EMBO J. 19 2000 5701 5710
    • (2000) EMBO J. , vol.19 , pp. 5701-5710
    • Hayashi, M.1    Nito, K.2    Toriyama-Kato, K.3    Kondo, M.4    Yamaya, T.5    Nishimura, M.6
  • 153
    • 0031953256 scopus 로고    scopus 로고
    • Pex17p of Saccharomyces cerevisiae is a novel peroxin and component of the peroxisomal protein translocation machinery
    • B. Huhse, P. Rehling, M. Albertini, L. Blank, K. Meller, and W.H. Kunau Pex17p of Saccharomyces cerevisiae is a novel peroxin and component of the peroxisomal protein translocation machinery J. Cell Biol. 140 1998 49 60
    • (1998) J. Cell Biol. , vol.140 , pp. 49-60
    • Huhse, B.1    Rehling, P.2    Albertini, M.3    Blank, L.4    Meller, K.5    Kunau, W.H.6
  • 154
    • 0032738908 scopus 로고    scopus 로고
    • Pex17p is required for import of both peroxisome membrane and lumenal protein and interacts with Pex19p and the peroxisome targeting signal-receptor docking complex in Pichia pastoris
    • W.B. Snyder, A. Koller, A.J. Choy, M.A. Johnson, J.M. Cregg, L. Rangell, G.A. Keller, and S. Subramani Pex17p is required for import of both peroxisome membrane and lumenal protein and interacts with Pex19p and the peroxisome targeting signal-receptor docking complex in Pichia pastoris Mol. Biol. Cell 10 1999 4005 4019
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4005-4019
    • Snyder, W.B.1    Koller, A.2    Choy, A.J.3    Johnson, M.A.4    Cregg, J.M.5    Rangell, L.6    Keller, G.A.7    Subramani, S.8
  • 156
    • 0036179374 scopus 로고    scopus 로고
    • Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: Conserved Pex5p WXXXF/Y motifs are critical for matrix protein import
    • H. Otera, K. Setoguchi, M. Hamasaki, T. Kumashiro, N. Shimizu, and Y. Fujiki Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import Mol. Cell. Biol. 22 2002 1639 1655
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1639-1655
    • Otera, H.1    Setoguchi, K.2    Hamasaki, M.3    Kumashiro, T.4    Shimizu, N.5    Fujiki, Y.6
  • 158
    • 0029281993 scopus 로고
    • SH3 domains: Minding your PS and QS
    • B.J. Mayer, and M.J. Eck SH3 domains: minding your PS and QS Curr. Biol. 5 1995 364 367
    • (1995) Curr. Biol. , vol.5 , pp. 364-367
    • Mayer, B.J.1    Eck, M.J.2
  • 160
    • 0030897576 scopus 로고    scopus 로고
    • The peroxin Pex17p of the yeast Yarrowia lipolytica is associated peripherally with the peroxisomal membrane and is required for the import of a subset of matrix proteins
    • J.J. Smith, R.K. Szilard, M. Marelli, and R.A. Rachubinski The peroxin Pex17p of the yeast Yarrowia lipolytica is associated peripherally with the peroxisomal membrane and is required for the import of a subset of matrix proteins Mol. Cell. Biol. 17 1997 2511 2520
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2511-2520
    • Smith, J.J.1    Szilard, R.K.2    Marelli, M.3    Rachubinski, R.A.4
  • 161
    • 0037053374 scopus 로고    scopus 로고
    • Peroxisomal membrane protein import does not require Pex17p
    • C.C. Harper, S.T. South, J.M. McCaffery, and S.J. Gould Peroxisomal membrane protein import does not require Pex17p J. Biol. Chem. 277 2002 16498 16504
    • (2002) J. Biol. Chem. , vol.277 , pp. 16498-16504
    • Harper, C.C.1    South, S.T.2    McCaffery, J.M.3    Gould, S.J.4
  • 162
    • 0034677197 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Pex3p and Pex19p are required for proper localization and stability of peroxisomal membrane proteins
    • E.H. Hettema, W. Girzalsky, M. Van den Berg, R. Erdmann, and B. Distel Saccharomyces cerevisiae Pex3p and Pex19p are required for proper localization and stability of peroxisomal membrane proteins EMBO J. 19 2000 223 233
    • (2000) EMBO J. , vol.19 , pp. 223-233
    • Hettema, E.H.1    Girzalsky, W.2    Van Den Berg, M.3    Erdmann, R.4    Distel, B.5
  • 163
    • 0030951104 scopus 로고    scopus 로고
    • Isolation of the human PEX12 gene, mutated in group 3 of the peroxisome biogenesis disorders
    • C.C. Chang, W.H. Lee, H. Moser, D. Valle, and S.J. Gould Isolation of the human PEX12 gene, mutated in group 3 of the peroxisome biogenesis disorders Nat. Genet. 15 1997 385 388
    • (1997) Nat. Genet. , vol.15 , pp. 385-388
    • Chang, C.C.1    Lee, W.H.2    Moser, H.3    Valle, D.4    Gould, S.J.5
  • 165
    • 0032782346 scopus 로고    scopus 로고
    • Transmembrane topology of the peroxin, Pex2p, an essential component for the peroxisome assembly
    • T. Harano, N. Shimizu, H. Otera, and Y. Fujiki Transmembrane topology of the peroxin, Pex2p, an essential component for the peroxisome assembly J. Biochem. 125 1999 1168 1174
    • (1999) J. Biochem. , vol.125 , pp. 1168-1174
    • Harano, T.1    Shimizu, N.2    Otera, H.3    Fujiki, Y.4
  • 166
    • 0034696786 scopus 로고    scopus 로고
    • A missense mutation in the RING finger motif of PEX2 protein disturbs the import of peroxisome targeting signal 1 (PTS1)-containing protein but not the PTS2-containing protein
    • Y. Huang, R. Ito, S. Miura, T. Hashimoto, and M. Ito A missense mutation in the RING finger motif of PEX2 protein disturbs the import of peroxisome targeting signal 1 (PTS1)-containing protein but not the PTS2-containing protein Biochem. Biophys. Res. Commun. 270 2000 717 721
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 717-721
    • Huang, Y.1    Ito, R.2    Miura, S.3    Hashimoto, T.4    Ito, M.5
  • 167
    • 0026782393 scopus 로고
    • The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes
    • F.F. Wiebel, and W.H. Kunau The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes Nature 359 1992 73 76
    • (1992) Nature , vol.359 , pp. 73-76
    • Wiebel, F.F.1    Kunau, W.H.2
  • 168
    • 0028110821 scopus 로고
    • The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly
    • D.I. Crane, J.E. Kalish, and S.J. Gould The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly J. Biol. Chem. 269 1994 21835 21844
    • (1994) J. Biol. Chem. , vol.269 , pp. 21835-21844
    • Crane, D.I.1    Kalish, J.E.2    Gould, S.J.3
  • 169
    • 0026706469 scopus 로고
    • Development of the yeast Pichia pastoris as a model organism for a genetic and molecular analysis of peroxisome assembly
    • S.J. Gould, D. McCollum, A.P. Spong, J.A. Heyman, and S. Subramani Development of the yeast Pichia pastoris as a model organism for a genetic and molecular analysis of peroxisome assembly Yeast 8 1992 613 628
    • (1992) Yeast , vol.8 , pp. 613-628
    • Gould, S.J.1    McCollum, D.2    Spong, A.P.3    Heyman, J.A.4    Subramani, S.5
  • 170
    • 0033549487 scopus 로고    scopus 로고
    • Pex22p of Pichia pastoris, essential for peroxisomal matrix protein import, anchors the ubiquitin-conjugating enzyme, Pex4p, on the peroxisomal membrane
    • A. Koller, W.B. Snyder, K.N. Faber, T.J. Wenzel, L. Rangell, G.A. Keller, and S. Subramani Pex22p of Pichia pastoris, essential for peroxisomal matrix protein import, anchors the ubiquitin-conjugating enzyme, Pex4p, on the peroxisomal membrane J. Cell Biol. 146 1999 99 112
    • (1999) J. Cell Biol. , vol.146 , pp. 99-112
    • Koller, A.1    Snyder, W.B.2    Faber, K.N.3    Wenzel, T.J.4    Rangell, L.5    Keller, G.A.6    Subramani, S.7
  • 171
    • 0041827355 scopus 로고    scopus 로고
    • Pex10p links the ubiquitin conjugating enzyme Pex4p to the protein import machinery of the peroxisome
    • J.H. Eckert, and N. Johnsson Pex10p links the ubiquitin conjugating enzyme Pex4p to the protein import machinery of the peroxisome J. Cell Science 116 2003 3623 3634
    • (2003) J. Cell Science , vol.116 , pp. 3623-3634
    • Eckert, J.H.1    Johnsson, N.2
  • 172
    • 0033800536 scopus 로고    scopus 로고
    • The peroxisome biogenesis factors Pex4p, Pex22p, Pex1p, and Pex6p act in the terminal steps of peroxisomal matrix protein import
    • C.S. Collins, J.E. Kalish, J.C. Morrell, J.M. McCaffery, and S.J. Gould The peroxisome biogenesis factors Pex4p, Pex22p, Pex1p, and Pex6p act in the terminal steps of peroxisomal matrix protein import Mol. Cell. Biol. 20 2000 7516 7526
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7516-7526
    • Collins, C.S.1    Kalish, J.E.2    Morrell, J.C.3    McCaffery, J.M.4    Gould, S.J.5
  • 173
    • 0032127487 scopus 로고    scopus 로고
    • The ubiquitin-conjugating enzyme Pex4p of Hansenula polymorpha is required for efficient functioning of the PTS1 import machinery
    • I.J. Van der Klei, R.E. Hilbrands, J.A.K.W. Kiel, S.W. Rasmussen, J.M. Cregg, and M. Veenhuis The ubiquitin-conjugating enzyme Pex4p of Hansenula polymorpha is required for efficient functioning of the PTS1 import machinery EMBO J. 17 1998 3608 3618
    • (1998) EMBO J. , vol.17 , pp. 3608-3618
    • Van Der Klei, I.J.1    Hilbrands, R.E.2    Kiel, J.A.K.W.3    Rasmussen, S.W.4    Cregg, J.M.5    Veenhuis, M.6
  • 174
    • 0035861688 scopus 로고    scopus 로고
    • Pex18p is constitutively degraded during peroxisome biogenesis
    • P.E. Purdue, and P.B. Lazarow Pex18p is constitutively degraded during peroxisome biogenesis J. Biol. Chem. 276 2001 47684 47689
    • (2001) J. Biol. Chem. , vol.276 , pp. 47684-47689
    • Purdue, P.E.1    Lazarow, P.B.2
  • 175
    • 0035846962 scopus 로고    scopus 로고
    • A role for the peroxin Pex8p in Pex20p-dependent thiolase import into peroxisomes of the yeast Yarrowia lipolytica
    • J.J. Smith, and R.A. Rachubinski A role for the peroxin Pex8p in Pex20p-dependent thiolase import into peroxisomes of the yeast Yarrowia lipolytica J. Biol. Chem. 276 2001 1618 1625
    • (2001) J. Biol. Chem. , vol.276 , pp. 1618-1625
    • Smith, J.J.1    Rachubinski, R.A.2
  • 177
    • 0025965277 scopus 로고
    • PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases
    • R. Erdmann, F.F. Wiebel, A. Flesseau, J. Rytka, A. Beyer, K.U. Frohlich, and W.H. Kunau PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases Cell 64 1991 499 510
    • (1991) Cell , vol.64 , pp. 499-510
    • Erdmann, R.1    Wiebel, F.F.2    Flesseau, A.3    Rytka, J.4    Beyer, A.5    Frohlich, K.U.6    Kunau, W.H.7
  • 178
    • 0027299142 scopus 로고
    • Two complementary approaches to study peroxisome biogenesis in Saccharomyces cerevisiae: Forward and reversed genetics
    • W.H. Kunau, A. Beyer, T. Franken, K. Gotte, M. Marzioch, J. Saidowsky, A. Skaletzrorowski, and F.F. Wiebel Two complementary approaches to study peroxisome biogenesis in Saccharomyces cerevisiae: forward and reversed genetics Biochimie 75 1993 209 224
    • (1993) Biochimie , vol.75 , pp. 209-224
    • Kunau, W.H.1    Beyer, A.2    Franken, T.3    Gotte, K.4    Marzioch, M.5    Saidowsky, J.6    Skaletzrorowski, A.7    Wiebel, F.F.8
  • 179
    • 0031930956 scopus 로고    scopus 로고
    • Two AAA family peroxins, PpPex1p and PpPex6p, interact with each other in an ATP-dependent manner and are associated with different subcellular membranous structures distinct from peroxisomes
    • K.N. Faber, J.A. Heyman, and S. Subramani Two AAA family peroxins, PpPex1p and PpPex6p, interact with each other in an ATP-dependent manner and are associated with different subcellular membranous structures distinct from peroxisomes Mol. Cell. Biol. 18 1998 936 943
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 936-943
    • Faber, K.N.1    Heyman, J.A.2    Subramani, S.3
  • 180
    • 0032555273 scopus 로고    scopus 로고
    • Disruption of a PEX1-PEX6 interaction is the most common cause of the neurologic disorders Zellweger syndrome, neonatal adrenoleukodystrophy, and infantile refsum disease
    • B.V. Geisbrecht, C.S. Collins, B.E. Reuber, and S.J. Gould Disruption of a PEX1-PEX6 interaction is the most common cause of the neurologic disorders Zellweger syndrome, neonatal adrenoleukodystrophy, and infantile refsum disease Proc. Natl. Acad. Sci. USA 95 1998 8630 8635
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8630-8635
    • Geisbrecht, B.V.1    Collins, C.S.2    Reuber, B.E.3    Gould, S.J.4
  • 183
    • 0029888487 scopus 로고    scopus 로고
    • The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor
    • T. Yahraus, N. Braverman, G. Dodt, J.E. Kalish, J.C. Morrell, H.W. Moser, D. Valle, and S.J. Gould The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor EMBO J. 15 1996 2914 2923
    • (1996) EMBO J. , vol.15 , pp. 2914-2923
    • Yahraus, T.1    Braverman, N.2    Dodt, G.3    Kalish, J.E.4    Morrell, J.C.5    Moser, H.W.6    Valle, D.7    Gould, S.J.8
  • 185
    • 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
    • V.I. Titorenko, H. Chan, and R.A. Rachubinski 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 2000 29 43
    • (2000) J. Cell Biol. , vol.148 , pp. 29-43
    • Titorenko, V.I.1    Chan, H.2    Rachubinski, R.A.3
  • 186
    • 0034698778 scopus 로고    scopus 로고
    • Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p
    • V.I. Titorenko, and R.A. Rachubinski Peroxisomal membrane fusion requires two AAA family ATPases, Pex1p and Pex6p J. Cell Biol. 150 2000 881 886
    • (2000) J. Cell Biol. , vol.150 , pp. 881-886
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 187
    • 0034515057 scopus 로고    scopus 로고
    • The genetics of peroxisome biogenesis
    • K.A. Sacksteder, and S.J. Gould The genetics of peroxisome biogenesis Annu. Rev. Genet. 34 2000 623 652
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 623-652
    • Sacksteder, K.A.1    Gould, S.J.2
  • 188
    • 0345403569 scopus 로고    scopus 로고
    • Characterization of intermediates in the process of plant peroxisomal protein import
    • M.R. Pool, E. Lopez-Huertas, and A. Baker Characterization of intermediates in the process of plant peroxisomal protein import EMBO J. 17 1998 6854 6862
    • (1998) EMBO J. , vol.17 , pp. 6854-6862
    • Pool, M.R.1    Lopez-Huertas, E.2    Baker, A.3
  • 191
  • 192
    • 0028861712 scopus 로고
    • The Yarrowia lipolytica gene PAY2 encodes a 42-kDa peroxisomal integral membrane-protein essential for matrix protein import and peroxisome enlargement but not for peroxisome proliferation
    • G.A. Eitzen, J.D. Aitchison, R.K. Szilard, M. Veenhuis, W.M. Nuttley, and R.A. Rachubinski The Yarrowia lipolytica gene PAY2 encodes a 42-kDa peroxisomal integral membrane-protein essential for matrix protein import and peroxisome enlargement but not for peroxisome proliferation J. Biol. Chem. 270 1995 1429 1436
    • (1995) J. Biol. Chem. , vol.270 , pp. 1429-1436
    • Eitzen, G.A.1    Aitchison, J.D.2    Szilard, R.K.3    Veenhuis, M.4    Nuttley, W.M.5    Rachubinski, R.A.6
  • 193
    • 0033979368 scopus 로고    scopus 로고
    • Mutants of the Yarrowia lipolytica PEX23 gene encoding an integral peroxisomal membrane peroxin mislocalize matrix proteins and accumulate vesicles containing peroxisomal matrix and membrane proteins
    • T.W. Brown, V.I. Titorenko, and R.A. Rachubinski Mutants of the Yarrowia lipolytica PEX23 gene encoding an integral peroxisomal membrane peroxin mislocalize matrix proteins and accumulate vesicles containing peroxisomal matrix and membrane proteins Mol. Biol. Cell 11 2000 141 152
    • (2000) Mol. Biol. Cell , vol.11 , pp. 141-152
    • Brown, T.W.1    Titorenko, V.I.2    Rachubinski, R.A.3
  • 194
    • 0036677434 scopus 로고    scopus 로고
    • Yarrowia lipolytica cells mutant for the PEX24 gene encoding a peroxisomal membrane peroxin mislocalize peroxisomal proteins and accumulate membrane structures containing both peroxisomal matrix and membrane proteins
    • Y.Y.C. Tam, and R.A. Rachubinski Yarrowia lipolytica cells mutant for the PEX24 gene encoding a peroxisomal membrane peroxin mislocalize peroxisomal proteins and accumulate membrane structures containing both peroxisomal matrix and membrane proteins Mol. Biol. Cell 13 2002 2681 2691
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2681-2691
    • Tam, Y.Y.C.1    Rachubinski, R.A.2
  • 195
    • 0043167793 scopus 로고    scopus 로고
    • Mutations in novel peroxin gene PEX26 that cause peroxisome-biogenesis disorders of complementation group 8 provide a genotype-phenotype correlation
    • N. Matsumoto, S. Tamura, S. Furuki, N. Miyata, A. Moser, N. Shimozawa, H.W. Moser, Y. Suzuki, N. Kondo, and Y. Fujiki Mutations in novel peroxin gene PEX26 that cause peroxisome-biogenesis disorders of complementation group 8 provide a genotype-phenotype correlation Am. J. Hum. Genet. 73 2003 233 246
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 233-246
    • Matsumoto, N.1    Tamura, S.2    Furuki, S.3    Miyata, N.4    Moser, A.5    Shimozawa, N.6    Moser, H.W.7    Suzuki, Y.8    Kondo, N.9    Fujiki, Y.10
  • 196
    • 0038394714 scopus 로고    scopus 로고
    • The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes
    • N. Matsumoto, S. Tamura, and Y. Fujiki The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes Nat. Cell Biol. 5 2003 454 460
    • (2003) Nat. Cell Biol. , vol.5 , pp. 454-460
    • Matsumoto, N.1    Tamura, S.2    Fujiki, Y.3
  • 197
    • 0037632981 scopus 로고    scopus 로고
    • Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes
    • I. Birschmann, A.K. Stroobants, M. Van den Berg, A. Schafer, K. Rosenkranz, W.H. Kunau, and H.F. Tabak Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes Mol. Biol. Cell 14 2003 2226 2236
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2226-2236
    • Birschmann, I.1    Stroobants, A.K.2    Van Den Berg, M.3    Schafer, A.4    Rosenkranz, K.5    Kunau, W.H.6    Tabak, H.F.7
  • 198
    • 0035917528 scopus 로고    scopus 로고
    • The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol
    • V. Dammai, and S. Subramani The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol Cell 105 2001 187 196
    • (2001) Cell , vol.105 , pp. 187-196
    • Dammai, V.1    Subramani, S.2
  • 200
    • 85047669202 scopus 로고    scopus 로고
    • The targeting and assembly of peroxisomal proteins: Some old rules do not apply
    • J.A. McNew, and J.M. Goodman The targeting and assembly of peroxisomal proteins: some old rules do not apply Trends Biochem. Sci. 21 1996 54 58
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 54-58
    • McNew, J.A.1    Goodman, J.M.2
  • 201
    • 0030034571 scopus 로고    scopus 로고
    • Import of a DHFR hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue aminopterin
    • T. Häusler, Y.D. Stierhof, E. Wirtz, and C. Clayton Import of a DHFR hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue aminopterin J. Cell Biol. 132 1996 311 324
    • (1996) J. Cell Biol. , vol.132 , pp. 311-324
    • Häusler, T.1    Stierhof, Y.D.2    Wirtz, E.3    Clayton, C.4
  • 202
    • 0035018777 scopus 로고    scopus 로고
    • PTS2 protein import into mammalian peroxisomes
    • J.E. Legakis, and S.R. Terlecky PTS2 protein import into mammalian peroxisomes Traffic 2 2001 252 260
    • (2001) Traffic , vol.2 , pp. 252-260
    • Legakis, J.E.1    Terlecky, S.R.2
  • 203
    • 0037017402 scopus 로고    scopus 로고
    • Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing complex into peroxisomes of Yarrowia lipolytica
    • V.I. Titorenko, J.M. Nicaud, H.J. Wang, H. Chan, and R.A. Rachubinski Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing complex into peroxisomes of Yarrowia lipolytica J. Cell Biol. 156 2002 481 494
    • (2002) J. Cell Biol. , vol.156 , pp. 481-494
    • Titorenko, V.I.1    Nicaud, J.M.2    Wang, H.J.3    Chan, H.4    Rachubinski, R.A.5
  • 204
    • 0037135706 scopus 로고    scopus 로고
    • Import of assembled PTS1 proteins into peroxisomes of the yeast Hansenula polymorpha: Yes and no! Biochim
    • K.N. Faber, R. Van Dijk, I. Keizer-Gunnink, A. Koek, I.J. Van der Klei, and M. Veenhuis Import of assembled PTS1 proteins into peroxisomes of the yeast Hansenula polymorpha: yes and no! Biochim Biophys. Acta 1591 2002 157 162
    • (2002) Biophys. Acta , vol.1591 , pp. 157-162
    • Faber, K.N.1    Van Dijk, R.2    Keizer-Gunnink, I.3    Koek, A.4    Van Der Klei, I.J.5    Veenhuis, M.6
  • 206
    • 0029010680 scopus 로고
    • Import of stably folded proteins into peroxisomes
    • P.A. Walton, P.E. Hill, and S. Subramani Import of stably folded proteins into peroxisomes Mol. Biol. Cell 6 1995 675 683
    • (1995) Mol. Biol. Cell , vol.6 , pp. 675-683
    • Walton, P.A.1    Hill, P.E.2    Subramani, S.3
  • 208
    • 0036273592 scopus 로고    scopus 로고
    • Peroxisomal-protein import: Is it really that complex?
    • S.J. Gould, and C.S. Collins Peroxisomal-protein import: is it really that complex? Nat. Rev. Mol. Cell. Biol. 3 2002 382 389
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 382-389
    • Gould, S.J.1    Collins, C.S.2
  • 209
    • 0023632725 scopus 로고
    • Proton ionophores prevent assembly of a peroxisomal protein
    • E. Bellion, and J.M. Goodman Proton ionophores prevent assembly of a peroxisomal protein Cell 48 1987 165 173
    • (1987) Cell , vol.48 , pp. 165-173
    • Bellion, E.1    Goodman, J.M.2
  • 210
    • 0023809656 scopus 로고
    • Peroxisomal integral membrane proteins in control and Zellweger fibroblasts
    • M.J. Santos, T. Imanaka, H. Shio, and P.B. Lazarow Peroxisomal integral membrane proteins in control and Zellweger fibroblasts J. Biol. Chem. 263 1988 10502 10509
    • (1988) J. Biol. Chem. , vol.263 , pp. 10502-10509
    • Santos, M.J.1    Imanaka, T.2    Shio, H.3    Lazarow, P.B.4
  • 211
    • 0023932509 scopus 로고
    • Peroxisomal membrane ghosts in Zellweger syndrome-aberrant organelle assembly
    • M.J. Santos, T. Imanaka, H. Shio, G.M. Small, and P.B. Lazarow Peroxisomal membrane ghosts in Zellweger syndrome-aberrant organelle assembly Science 239 1988 1536 1538
    • (1988) Science , vol.239 , pp. 1536-1538
    • Santos, M.J.1    Imanaka, T.2    Shio, H.3    Small, G.M.4    Lazarow, P.B.5
  • 212
    • 0033544923 scopus 로고    scopus 로고
    • Formation of peroxisomes from peroxisomal ghosts in a peroxisome-deficient mammalian cell mutant upon complementation by protein microinjection
    • M. Yamasaki, N. Hashiguchi, C. Fujiwara, T. Imanaka, T. Tsukamoto, and T. Osumi Formation of peroxisomes from peroxisomal ghosts in a peroxisome-deficient mammalian cell mutant upon complementation by protein microinjection J. Biol. Chem. 274 1999 35293 35296
    • (1999) J. Biol. Chem. , vol.274 , pp. 35293-35296
    • Yamasaki, M.1    Hashiguchi, N.2    Fujiwara, C.3    Imanaka, T.4    Tsukamoto, T.5    Osumi, T.6
  • 213
    • 0028859252 scopus 로고
    • Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p
    • R. Erdmann, and G. Blobel Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p J. Cell Biol. 128 1995 509 523
    • (1995) J. Cell Biol. , vol.128 , pp. 509-523
    • Erdmann, R.1    Blobel, G.2
  • 214
    • 0242609876 scopus 로고    scopus 로고
    • Peroxisomal remnant structures in Hansenula polymorpha Pex5 cells can develop into normal peroxisomes upon induction of the PTS2 protein amine oxidase
    • F.A. Salomons, K.N. Faber, M. Veenhuis, and I.J. Van der Klei Peroxisomal remnant structures in Hansenula polymorpha Pex5 cells can develop into normal peroxisomes upon induction of the PTS2 protein amine oxidase J. Biol. Chem. 276 2001 4190 4198
    • (2001) J. Biol. Chem. , vol.276 , pp. 4190-4198
    • Salomons, F.A.1    Faber, K.N.2    Veenhuis, M.3    Van Der Klei, I.J.4
  • 215
    • 0021722336 scopus 로고
    • Synthesis of a major integral membrane polypeptide of rat liver peroxisomes on free polysomes
    • Y. Fujiki, R.A. Rachubinski, and P.B. Lazarow Synthesis of a major integral membrane polypeptide of rat liver peroxisomes on free polysomes Proc. Natl. Acad. Sci. USA 81 1984 7127 7131
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7127-7131
    • Fujiki, Y.1    Rachubinski, R.A.2    Lazarow, P.B.3
  • 217
    • 0027965618 scopus 로고
    • Peroxisome assembly factor 1: Nonsense mutation in a peroxisome deficient Chinese hamster ovary cell mutant and deletion analysis
    • T. Tsukamoto, N. Shimozawa, and Y. Fujiki Peroxisome assembly factor 1: nonsense mutation in a peroxisome deficient Chinese hamster ovary cell mutant and deletion analysis Mol. Cell. Biol. 14 1994 5458 5465
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5458-5465
    • Tsukamoto, T.1    Shimozawa, N.2    Fujiki, Y.3
  • 218
    • 16944363061 scopus 로고    scopus 로고
    • Protein translocation into peroxisomes
    • S. Subramani Protein translocation into peroxisomes J. Biol. Chem. 271 1996 32483 32486
    • (1996) J. Biol. Chem. , vol.271 , pp. 32483-32486
    • Subramani, S.1
  • 219
    • 0041810193 scopus 로고    scopus 로고
    • Peroxisomes start their life in the endoplasmic reticulum
    • H.F. Tabak, J.L. Murk, I. Braakman, and H.J. Geuze Peroxisomes start their life in the endoplasmic reticulum Traffic 4 2003 512 518
    • (2003) Traffic , vol.4 , pp. 512-518
    • Tabak, H.F.1    Murk, J.L.2    Braakman, I.3    Geuze, H.J.4
  • 220
    • 0029879509 scopus 로고    scopus 로고
    • The sorting sequence of the peroxisomal integral membrane protein PMP47 is contained within a short hydrophilic loop
    • J.M. Dyer, J.A. McNew, and J.M. Goodman The sorting sequence of the peroxisomal integral membrane protein PMP47 is contained within a short hydrophilic loop J. Cell Biol. 133 1996 269 280
    • (1996) J. Cell Biol. , vol.133 , pp. 269-280
    • Dyer, J.M.1    McNew, J.A.2    Goodman, J.M.3
  • 221
    • 0031448780 scopus 로고    scopus 로고
    • Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S. cerevisiae, causes proliferation of the endoplasmic reticulum membrane
    • Y. Elgersma, L. Kwast, M. Van den Berg, W.B. Snyder, B. Distel, S. Subramani, and H.F. Tabak Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S. cerevisiae, causes proliferation of the endoplasmic reticulum membrane EMBO J. 16 1997 7326 7341
    • (1997) EMBO J. , vol.16 , pp. 7326-7341
    • Elgersma, Y.1    Kwast, L.2    Van Den Berg, M.3    Snyder, W.B.4    Distel, B.5    Subramani, S.6    Tabak, H.F.7
  • 222
    • 0026080044 scopus 로고
    • PAS3, a Saccharomyces cerevisiae gene encoding a peroxisomal integral membrane protein essential for peroxisome biogenesis
    • J. Höhfeld, M. Veenhuis, and W.H. Kunau PAS3, a Saccharomyces cerevisiae gene encoding a peroxisomal integral membrane protein essential for peroxisome biogenesis J. Cell Biol. 114 1991 1167 1178
    • (1991) J. Cell Biol. , vol.114 , pp. 1167-1178
    • Höhfeld, J.1    Veenhuis, M.2    Kunau, W.H.3
  • 224
    • 0029744977 scopus 로고    scopus 로고
    • Isolation and characterization of Pas2p, a peroxisomal membrane protein essential for peroxisome biogenesis in the methylotrophic yeast Pichia pastoris
    • E.A.C. Wiemer, G.H. Luers, K.N. Faber, T. Wenzel, M. Veenhuis, and S. Subramani Isolation and characterization of Pas2p, a peroxisomal membrane protein essential for peroxisome biogenesis in the methylotrophic yeast Pichia pastoris J. Biol. Chem. 271 1996 18973 18980
    • (1996) J. Biol. Chem. , vol.271 , pp. 18973-18980
    • Wiemer, E.A.C.1    Luers, G.H.2    Faber, K.N.3    Wenzel, T.4    Veenhuis, M.5    Subramani, S.6
  • 225
    • 0032486364 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding the human peroxisomal assembly protein Pex3p
    • S. Kammerer, A. Holzinger, U. Welsch, and A.A. Roscher Cloning and characterization of the gene encoding the human peroxisomal assembly protein Pex3p FEBS Lett. 429 1998 53 60
    • (1998) FEBS Lett. , vol.429 , pp. 53-60
    • Kammerer, S.1    Holzinger, A.2    Welsch, U.3    Roscher, A.A.4
  • 227
    • 0034122564 scopus 로고    scopus 로고
    • The peroxin Pex3p initiates membrane assembly in peroxisome biogenesis
    • K. Ghaedi, S. Tamura, K. Okumoto, Y. Matsuzono, and Y. Fujiki The peroxin Pex3p initiates membrane assembly in peroxisome biogenesis Mol. Biol. Cell 11 2000 2085 2102
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2085-2102
    • Ghaedi, K.1    Tamura, S.2    Okumoto, K.3    Matsuzono, Y.4    Fujiki, Y.5
  • 228
    • 0033794897 scopus 로고    scopus 로고
    • Defective peroxisome membrane synthesis due to mutations in human PEX3 causes Zellweger syndrome, complementation group G
    • A.C. Muntau, P.U. Mayerhofer, B.C. Paton, S. Kammerer, and A.A. Roscher Defective peroxisome membrane synthesis due to mutations in human PEX3 causes Zellweger syndrome, complementation group G Am. J. Hum. Genet. 67 2000 967 975
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 967-975
    • Muntau, A.C.1    Mayerhofer, P.U.2    Paton, B.C.3    Kammerer, S.4    Roscher, A.A.5
  • 229
    • 0036668807 scopus 로고    scopus 로고
    • Peroxisome remnants in pex3Δ cells and the requirement of Pex3p for interactions between the peroxisomal docking and translocation subcomplexes
    • P.P. Hazra, I. Suriapranata, W.B. Snyder, and S. Subramani Peroxisome remnants in pex3Δ cells and the requirement of Pex3p for interactions between the peroxisomal docking and translocation subcomplexes Traffic 3 2002 560 574
    • (2002) Traffic , vol.3 , pp. 560-574
    • Hazra, P.P.1    Suriapranata, I.2    Snyder, W.B.3    Subramani, S.4
  • 233
    • 0034611003 scopus 로고    scopus 로고
    • PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis
    • K.A. Sacksteder, J.M. Jones, S.T. South, X.L. Li, Y.F. Liu, and S.J. Gould PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis J. Cell Biol. 148 2000 931 944
    • (2000) J. Cell Biol. , vol.148 , pp. 931-944
    • Sacksteder, K.A.1    Jones, J.M.2    South, S.T.3    Li, X.L.4    Liu, Y.F.5    Gould, S.J.6
  • 234
    • 0034641098 scopus 로고    scopus 로고
    • The peroxin Pex19p interacts with multiple, integral membrane proteins at the peroxisomal membrane
    • W.B. Snyder, A. Koller, A.J. Choy, and S. Subramani The peroxin Pex19p interacts with multiple, integral membrane proteins at the peroxisomal membrane J. Cell Biol. 149 2000 1171 1177
    • (2000) J. Cell Biol. , vol.149 , pp. 1171-1177
    • Snyder, W.B.1    Koller, A.2    Choy, A.J.3    Subramani, S.4
  • 235
    • 0034972812 scopus 로고    scopus 로고
    • Human Pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences
    • M. Fransen, T. Wylin, C. Brees, G.P. Mannaerts, and P.P. Van Veldhoven Human Pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences Mol. Cell. Biol. 21 2001 4413 4424
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4413-4424
    • Fransen, M.1    Wylin, T.2    Brees, C.3    Mannaerts, G.P.4    Van Veldhoven, P.P.5
  • 236
    • 0034615921 scopus 로고    scopus 로고
    • A stretch of positively charged amino acids at the N-terminus of Hansenula polymorpha Pex3p is involved in incorporation of the protein into the peroxisomal membrane
    • R.J.S. Baerends, K.N. Faber, A.M. Kram, J.A.K.W. Kiel, I.J. Van der Klei, and M. Veenhuis A stretch of positively charged amino acids at the N-terminus of Hansenula polymorpha Pex3p is involved in incorporation of the protein into the peroxisomal membrane J. Biol. Chem. 275 2000 9986 9995
    • (2000) J. Biol. Chem. , vol.275 , pp. 9986-9995
    • Baerends, R.J.S.1    Faber, K.N.2    Kram, A.M.3    Kiel, J.A.K.W.4    Van Der Klei, I.J.5    Veenhuis, M.6
  • 237
    • 0034717704 scopus 로고    scopus 로고
    • Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis
    • S.T. South, K.A. Sacksteder, X.L. Li, Y.F. Liu, and S.J. Gould Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis J. Cell Biol. 149 2000 1345 1359
    • (2000) J. Cell Biol. , vol.149 , pp. 1345-1359
    • South, S.T.1    Sacksteder, K.A.2    Li, X.L.3    Liu, Y.F.4    Gould, S.J.5
  • 238
    • 0032471611 scopus 로고    scopus 로고
    • Mutation in PEX16 is causal in the peroxisome-deficient Zellweger syndrome of complementation group D
    • M. Honsho, S. Tamura, N. Shimozawa, Y. Suzuki, N. Kondo, and Y. Fujiki Mutation in PEX16 is causal in the peroxisome-deficient Zellweger syndrome of complementation group D Am. J. Hum. Genet. 63 1998 1622 1630
    • (1998) Am. J. Hum. Genet. , vol.63 , pp. 1622-1630
    • Honsho, M.1    Tamura, S.2    Shimozawa, N.3    Suzuki, Y.4    Kondo, N.5    Fujiki, Y.6
  • 239
    • 0033601767 scopus 로고    scopus 로고
    • Peroxisome synthesis in the absence of preexisting peroxisomes
    • S.T. South, and S.J. Gould Peroxisome synthesis in the absence of preexisting peroxisomes J. Cell Biol. 144 1999 255 266
    • (1999) J. Cell Biol. , vol.144 , pp. 255-266
    • South, S.T.1    Gould, S.J.2
  • 240
    • 0037113975 scopus 로고    scopus 로고
    • The membrane biogenesis peroxin Pex16p: Topogenesis and functional roles in peroxisomal membrane assembly
    • M. Honsho, T. Hiroshige, and Y. Fujiki The membrane biogenesis peroxin Pex16p: topogenesis and functional roles in peroxisomal membrane assembly J. Biol. Chem. 277 2002 44513 44524
    • (2002) J. Biol. Chem. , vol.277 , pp. 44513-44524
    • Honsho, M.1    Hiroshige, T.2    Fujiki, Y.3
  • 241
    • 0031007808 scopus 로고    scopus 로고
    • Enlarged peroxisomes are present in oleic acid-grown Yarrowia lipolytica overexpressing the PEX16 gene encoding an intraperoxisomal peripheral membrane peroxin
    • G.A. Eitzen, R.K. Szilard, and R.A. Rachubinski Enlarged peroxisomes are present in oleic acid-grown Yarrowia lipolytica overexpressing the PEX16 gene encoding an intraperoxisomal peripheral membrane peroxin J. Cell Biol. 137 1997 1265 1278
    • (1997) J. Cell Biol. , vol.137 , pp. 1265-1278
    • Eitzen, G.A.1    Szilard, R.K.2    Rachubinski, R.A.3
  • 242
    • 0033231876 scopus 로고    scopus 로고
    • Peroxisomes: Simple in function but complex in maintenance
    • H.F. Tabak, I. Braakman, and B. Distel Peroxisomes: simple in function but complex in maintenance Trends Cell Biol. 9 1999 447 453
    • (1999) Trends Cell Biol. , vol.9 , pp. 447-453
    • Tabak, H.F.1    Braakman, I.2    Distel, B.3
  • 243
    • 0028783419 scopus 로고
    • The Candida boidinii peroxisomal membrane-protein PMP30 has a role in peroxisomal proliferation and is functionally homologous to PMP27 from Saccharomyces cerevisiae
    • Y. Sakai, P.A. Marshall, A. Saiganji, K. Takabe, H. Saiki, N. Kato, and J.M. Goodman The Candida boidinii peroxisomal membrane-protein PMP30 has a role in peroxisomal proliferation and is functionally homologous to PMP27 from Saccharomyces cerevisiae J. Bacteriol. 177 1995 6773 6781
    • (1995) J. Bacteriol. , vol.177 , pp. 6773-6781
    • Sakai, Y.1    Marshall, P.A.2    Saiganji, A.3    Takabe, K.4    Saiki, H.5    Kato, N.6    Goodman, J.M.7
  • 244
    • 0029792856 scopus 로고    scopus 로고
    • Redox-sensitive homodimerization of Pex11p: A proposed mechanism to regulate peroxisomal division
    • P.A. Marshall, J.M. Dyer, M.E. Quick, and J.M. Goodman Redox-sensitive homodimerization of Pex11p: a proposed mechanism to regulate peroxisomal division J. Cell Biol. 135 1996 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
  • 247
    • 0034617992 scopus 로고    scopus 로고
    • Pex11p plays a primary role in medium-chain fatty acid oxidation, a process that affects peroxisome number and size in Saccharomyces cerevisiae
    • C.W.T. Van Roermund, H.F. Tabak, M. Van den Berg, R.J.A. Wanders, and E.H. Hettema Pex11p plays a primary role in medium-chain fatty acid oxidation, a process that affects peroxisome number and size in Saccharomyces cerevisiae J. Cell Biol. 150 2000 489 497
    • (2000) J. Cell Biol. , vol.150 , pp. 489-497
    • Van Roermund, C.W.T.1    Tabak, H.F.2    Van Den Berg, M.3    Wanders, R.J.A.4    Hettema, E.H.5
  • 248
    • 0036882106 scopus 로고    scopus 로고
    • PEX11α is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation
    • X. Li, E. Baumgart, G.X. Dong, J.C. Morrell, G. Jimenez-Sanchez, D. Valle, K.D. Smith, and S.J. Gould PEX11α 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. 22 2002 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
  • 249
    • 0036261777 scopus 로고    scopus 로고
    • PEX11β deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function
    • X. Li, E. Baumgart, J.C. Morrell, G. Jimenez-Sanchez, D. Valle, and S.J. Gould PEX11β deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function Mol. Cell. Biol. 22 2002 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
  • 251
    • 0141541655 scopus 로고    scopus 로고
    • Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis
    • H. Rottensteiner, K. Stein, E. Sonnenhol, and R. Erdmann Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis Mol. Biol. Cell 14 2003 4316 4328
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4316-4328
    • Rottensteiner, H.1    Stein, K.2    Sonnenhol, E.3    Erdmann, R.4
  • 252
    • 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
    • Y.Y. Tam, J.C. Torres-Guzman, F.J. Vizeacoumar, J.J. Smith, M. Marelli, J.D. Aitchison, and R.A. Rachubinski 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 14 2003 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
  • 253
    • 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
    • F.J. Vizeacoumar, J.C. Torres-Guzman, Y.Y. Tam, J.D. Aitchison, and R.A. Rachubinski YHR150w and YDR479c encode peroxisomal integral membrane proteins involved in the regulation of peroxisome number, size, and distribution in Saccharomyces cerevisiae J. Cell Biol. 161 2003 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
  • 254
    • 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
    • F.J. Vizeacoumar, J.C. Torres-Guzman, D. Bouard, J.D. Aitchison, and R.A. Rachubinski Pex30p, Pex31p, and Pex32p form a family of peroxisomal integral membrane proteins regulating peroxisome size and number in Saccharomyces cerevisiae Mol. Biol. Cell 15 2004 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
  • 256
    • 0026511317 scopus 로고
    • Peroxisomal protein import. in vivo evidence for a novel translocation competent compartment
    • P. Heinemann, and W.W. Just Peroxisomal protein import. In vivo evidence for a novel translocation competent compartment FEBS Lett. 300 1992 179 182
    • (1992) FEBS Lett. , vol.300 , pp. 179-182
    • Heinemann, P.1    Just, W.W.2
  • 257
    • 0035842904 scopus 로고    scopus 로고
    • A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae
    • D. Hoepfner, M. Van den Berg, P. Philippsen, H.F. Tabak, and E.H. Hettema A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae J. Cell Biol. 155 2001 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
  • 258
    • 0033804750 scopus 로고    scopus 로고
    • PEX3 is the causal gene responsible for peroxisome membrane assembly-defective Zellweger syndrome of complementation group G
    • K. Ghaedi, M. Honsho, N. Shimozawa, Y. Suzuki, N. Kondo, and Y. Fujiki PEX3 is the causal gene responsible for peroxisome membrane assembly-defective Zellweger syndrome of complementation group G Am. J. Hum. Genet. 67 2000 976 981
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 976-981
    • Ghaedi, K.1    Honsho, M.2    Shimozawa, N.3    Suzuki, Y.4    Kondo, N.5    Fujiki, Y.6
  • 259
    • 0034641604 scopus 로고    scopus 로고
    • Identification of PEX3 as the gene mutated in a Zellweger syndrome patient lacking peroxisomal remnant structures
    • N. Shimozawa, Y. Suzuki, Z.Y. Zhang, A. Imamura, K. Ghaedi, Y. Fujiki, and N. Kondo Identification of PEX3 as the gene mutated in a Zellweger syndrome patient lacking peroxisomal remnant structures Hum. Mol. Genet. 9 2000 1995 1999
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1995-1999
    • Shimozawa, N.1    Suzuki, Y.2    Zhang, Z.Y.3    Imamura, A.4    Ghaedi, K.5    Fujiki, Y.6    Kondo, N.7
  • 260
    • 0035196588 scopus 로고    scopus 로고
    • Yarrowia lipolytica cells mutant for the peroxisomal peroxin Pex19p contain structures resembling wild-type peroxisomes
    • G.R. Lambkin, and R.A. Rachubinski Yarrowia lipolytica cells mutant for the peroxisomal peroxin Pex19p contain structures resembling wild-type peroxisomes Mol. Biol. Cell 12 2001 3353 3364
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3353-3364
    • Lambkin, G.R.1    Rachubinski, R.A.2
  • 262
    • 0029786673 scopus 로고    scopus 로고
    • Mutations in the PAY5 gene of the yeast Yarrowia lipolytica cause the accumulation of multiple subpopulations of peroxisomes
    • V.I. Titorenko, G.A. Eitzen, and R.A. Rachubinski Mutations in the PAY5 gene of the yeast Yarrowia lipolytica cause the accumulation of multiple subpopulations of peroxisomes J. Biol. Chem. 271 1996 20307 20314
    • (1996) J. Biol. Chem. , vol.271 , pp. 20307-20314
    • Titorenko, V.I.1    Eitzen, G.A.2    Rachubinski, R.A.3
  • 264
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • R. Schneiter, B. Brugger, R. Sandhoff, G. Zellnig, A. Leber, M. Lampl, K. Athenstaedt, C. Hrastnik, S. Eder, G. Daum, F. Paltauf, F.T. Wieland, and S.D. Kohlwein Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane J. Cell Biol. 146 1999 741 754
    • (1999) J. Cell Biol. , vol.146 , pp. 741-754
    • Schneiter, R.1    Brugger, B.2    Sandhoff, R.3    Zellnig, G.4    Leber, A.5    Lampl, M.6    Athenstaedt, K.7    Hrastnik, C.8    Eder, S.9    Daum, G.10    Paltauf, F.11    Wieland, F.T.12    Kohlwein, S.D.13
  • 266
    • 0023336255 scopus 로고
    • Biogenesis of the glycosome in Trypanosoma brucei: The synthesis, translocation and turnover of glycosomal polypeptides
    • D.T. Hart, P. Baudhuin, F.R. Opperdoes, and C. de Duve Biogenesis of the glycosome in Trypanosoma brucei: the synthesis, translocation and turnover of glycosomal polypeptides EMBO J. 6 1987 1403 1411
    • (1987) EMBO J. , vol.6 , pp. 1403-1411
    • Hart, D.T.1    Baudhuin, P.2    Opperdoes, F.R.3    De Duve, C.4
  • 267
    • 0023605611 scopus 로고
    • Import of fructose bisphosphate aldolase into the glycosomes of Trypanosoma brucei
    • C.E. Clayton Import of fructose bisphosphate aldolase into the glycosomes of Trypanosoma brucei J. Cell Biol. 105 1987 2649 2654
    • (1987) J. Cell Biol. , vol.105 , pp. 2649-2654
    • Clayton, C.E.1
  • 268
    • 0023957631 scopus 로고
    • Most proteins, including fructose bisphosphate aldolase, are stable in the procyclic trypomastigote form of Trypanosoma brucei
    • C.E. Clayton Most proteins, including fructose bisphosphate aldolase, are stable in the procyclic trypomastigote form of Trypanosoma brucei Mol. Biochem. Parasitol. 28 1988 43 46
    • (1988) Mol. Biochem. Parasitol. , vol.28 , pp. 43-46
    • Clayton, C.E.1
  • 269
    • 0026488195 scopus 로고
    • Glycosome assembly in trypanosomes: Variations in the acceptable degeneracy of a COOH-terminal microbody targeting signal
    • J. Blattner, B. Swinkels, H. Dörsam, T. Prospero, S. Subramani, and C. Clayton Glycosome assembly in trypanosomes: variations in the acceptable degeneracy of a COOH-terminal microbody targeting signal J. Cell Biol. 119 1992 1129 1136
    • (1992) J. Cell Biol. , vol.119 , pp. 1129-1136
    • Blattner, J.1    Swinkels, B.2    Dörsam, H.3    Prospero, T.4    Subramani, S.5    Clayton, C.6
  • 270
    • 0027054829 scopus 로고
    • In vivo import of firefly luciferase into the glycosomes of Trypanosoma brucei and mutational analysis of the C-terminal targeting signal
    • J.M. Sommer, Q.L. Cheng, G.A. Keller, and C.C. Wang In vivo import of firefly luciferase into the glycosomes of Trypanosoma brucei and mutational analysis of the C-terminal targeting signal Mol. Biol. Cell 3 1992 749 759
    • (1992) Mol. Biol. Cell , vol.3 , pp. 749-759
    • Sommer, J.M.1    Cheng, Q.L.2    Keller, G.A.3    Wang, C.C.4
  • 271
    • 0028929650 scopus 로고
    • Function of N-terminal import signals in trypanosome microbodies
    • J. Blattner, H. Dörsam, and C.E. Clayton Function of N-terminal import signals in trypanosome microbodies FEBS Lett. 360 1995 310 314
    • (1995) FEBS Lett. , vol.360 , pp. 310-314
    • Blattner, J.1    Dörsam, H.2    Clayton, C.E.3
  • 272
    • 0030635499 scopus 로고    scopus 로고
    • Trypanosoma brucei: Identification of an internal region of phosphoglycerate kinase required for targeting to glycosomal microbodies
    • G.C. Peterson, J.M. Sommer, S. Klosterman, C.C. Wang, and M. Parsons Trypanosoma brucei: identification of an internal region of phosphoglycerate kinase required for targeting to glycosomal microbodies Exp. Parasitol. 85 1997 16 23
    • (1997) Exp. Parasitol. , vol.85 , pp. 16-23
    • Peterson, G.C.1    Sommer, J.M.2    Klosterman, S.3    Wang, C.C.4    Parsons, M.5
  • 273
    • 0025785056 scopus 로고
    • Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. a comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex
    • R.K. Wierenga, M.E. Noble, G. Vriend, S. Nauche, and W.G.J. Hol Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex J. Mol. Biol. 220 1991 995 1015
    • (1991) J. Mol. Biol. , vol.220 , pp. 995-1015
    • Wierenga, R.K.1    Noble, M.E.2    Vriend, G.3    Nauche, S.4    Hol, W.G.J.5
  • 274
    • 0022435186 scopus 로고
    • Topogenesis of microbody enzymes: A sequence comparison of the genes for the glycosomal (microbody) and cytosolic phosphoglycerate kinases of Trypanosoma brucei
    • K.A. Osinga, B.W. Swinkels, W.C. Gibson, P. Borst, G.H. Veeneman, J.H. Van Boom, P.A.M. Michels, and F.R. Opperdoes Topogenesis of microbody enzymes: a sequence comparison of the genes for the glycosomal (microbody) and cytosolic phosphoglycerate kinases of Trypanosoma brucei EMBO J. 4 1985 3811 3817
    • (1985) EMBO J. , vol.4 , pp. 3811-3817
    • Osinga, K.A.1    Swinkels, B.W.2    Gibson, W.C.3    Borst, P.4    Veeneman, G.H.5    Van Boom, J.H.6    Michels, P.A.M.7    Opperdoes, F.R.8
  • 275
    • 0025763679 scopus 로고
    • The cytosolic and glycosomal isoenzymes of glyceraldehyde-3-phosphate dehydrogenase in Trypanosoma brucei have a distant evolutionary relationship
    • P.A.M. Michels, M. Marchand, L. Kohl, S. Allert, R.K. Wierenga, and F.R. Opperdoes The cytosolic and glycosomal isoenzymes of glyceraldehyde-3-phosphate dehydrogenase in Trypanosoma brucei have a distant evolutionary relationship Eur. J. Biochem. 198 1991 421 428
    • (1991) Eur. J. Biochem. , vol.198 , pp. 421-428
    • Michels, P.A.M.1    Marchand, M.2    Kohl, L.3    Allert, S.4    Wierenga, R.K.5    Opperdoes, F.R.6
  • 276
    • 0028080428 scopus 로고
    • Subcellular distribution and characterization of glucosephosphate isomerase in Leishmania mexicana mexicana
    • K. Nyame, C.D. Do-Thi, F.R. Opperdoes, and P.A.M. Michels Subcellular distribution and characterization of glucosephosphate isomerase in Leishmania mexicana mexicana Mol. Biochem. Parasitol. 67 1994 269 279
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 269-279
    • Nyame, K.1    Do-Thi, C.D.2    Opperdoes, F.R.3    Michels, P.A.M.4
  • 277
    • 0034623222 scopus 로고    scopus 로고
    • Molecular characterization of the first two enzymes of the pentose-phosphate pathway of Trypanosoma brucei. Glucose-6-phosphate dehydrogenase and 6-phosphogluconolactonase
    • F. Duffieux, J. Van Roy, P.A.M. Michels, and F.R. Opperdoes Molecular characterization of the first two enzymes of the pentose-phosphate pathway of Trypanosoma brucei. Glucose-6-phosphate dehydrogenase and 6- phosphogluconolactonase J. Biol. Chem. 275 2000 27559 27565
    • (2000) J. Biol. Chem. , vol.275 , pp. 27559-27565
    • Duffieux, F.1    Van Roy, J.2    Michels, P.A.M.3    Opperdoes, F.R.4
  • 278
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • M. Eilers, and G. Schatz Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria Nature 322 1986 228 232
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 279
    • 0031018416 scopus 로고    scopus 로고
    • Functional identification of a Leishmania gene related to the peroxin 2 gene reveals common ancestry of glycosomes and peroxisomes
    • J.A. Flaspohler, W.L. Rickoll, S.M. Beverley, and M. Parsons Functional identification of a Leishmania gene related to the peroxin 2 gene reveals common ancestry of glycosomes and peroxisomes Mol. Cell. Biol. 17 1997 1093 1101
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1093-1101
    • Flaspohler, J.A.1    Rickoll, W.L.2    Beverley, S.M.3    Parsons, M.4
  • 280
    • 0033525540 scopus 로고    scopus 로고
    • A dominant negative mutation in the GIM1 gene of Leishmania donovani is responsible for defects in glycosomal protein localization
    • J.A. Flaspohler, K. Lemley, and M. Parsons A dominant negative mutation in the GIM1 gene of Leishmania donovani is responsible for defects in glycosomal protein localization Mol. Biochem. Parasitol. 99 1999 117 128
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 117-128
    • Flaspohler, J.A.1    Lemley, K.2    Parsons, M.3
  • 282
    • 0036629337 scopus 로고    scopus 로고
    • Compartmentation of enzymes in a microbody, the glycosome, is essential in Trypanosoma brucei
    • C. Guerra-Giraldez, L. Quijada, and C.E. Clayton Compartmentation of enzymes in a microbody, the glycosome, is essential in Trypanosoma brucei J. Cell Sci. 115 2002 2651 2658
    • (2002) J. Cell Sci. , vol.115 , pp. 2651-2658
    • Guerra-Giraldez, C.1    Quijada, L.2    Clayton, C.E.3
  • 283
    • 0023236008 scopus 로고
    • Identification of two integral glycosomal membrane proteins in Trypanosoma brucei
    • R.A. Aman, and C.C. Wang Identification of two integral glycosomal membrane proteins in Trypanosoma brucei Mol. Biochem. Parasitol. 25 1987 83 92
    • (1987) Mol. Biochem. Parasitol. , vol.25 , pp. 83-92
    • Aman, R.A.1    Wang, C.C.2
  • 284
    • 0032125799 scopus 로고    scopus 로고
    • Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p
    • P. Lorenz, A.G. Maier, E. Baumgart, R. Erdmann, and C. Clayton Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p EMBO J. 17 1998 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
  • 285
    • 0035062359 scopus 로고    scopus 로고
    • An essential dimeric membrane protein of trypanosome glycosomes
    • A. Maier, P. Lorenz, F. Voncken, and C. Clayton An essential dimeric membrane protein of trypanosome glycosomes Mol. Microbiol. 39 2001 1443 1451
    • (2001) Mol. Microbiol. , vol.39 , pp. 1443-1451
    • Maier, A.1    Lorenz, P.2    Voncken, F.3    Clayton, C.4
  • 286
    • 0041816190 scopus 로고    scopus 로고
    • Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes
    • F. Voncken, J.J. Van Hellemond, I. Pfisterer, A. Maier, S. Hillmer, and C. Clayton Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes J. Biol. Chem. 278 2003 35299 35310
    • (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
  • 288
    • 0034607980 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 receptor protein PEX5 from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization
    • A. Jardim, W. Liu, E. Zheleznova, and B. Ullman Peroxisomal targeting signal-1 receptor protein PEX5 from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization J. Biol. Chem. 275 2000 13637 13644
    • (2000) J. Biol. Chem. , vol.275 , pp. 13637-13644
    • Jardim, A.1    Liu, W.2    Zheleznova, E.3    Ullman, B.4
  • 289
    • 0035896043 scopus 로고    scopus 로고
    • An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei
    • A. Kumar, C. Roach, I.S. Hirsh, S. Turley, S. de Walque, P.A.M. Michels, and W.G.J. Hol An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei J. Mol. Biol. 307 2001 271 282
    • (2001) J. Mol. Biol. , vol.307 , pp. 271-282
    • Kumar, A.1    Roach, C.2    Hirsh, I.S.3    Turley, S.4    De Walque, S.5    Michels, P.A.M.6    Hol, W.G.J.7
  • 291
    • 0037691903 scopus 로고    scopus 로고
    • Characterization of Trypanosoma brucei PEX14 and its role in the import of glycosomal matrix proteins
    • J. Moyersoen, J. Choe, A. Kumar, F.G.J. Voncken, W.G.J. Hol, and P.A.M. Michels Characterization of Trypanosoma brucei PEX14 and its role in the import of glycosomal matrix proteins Eur. J. Biochem. 270 2003 2059 2067
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2059-2067
    • Moyersoen, J.1    Choe, J.2    Kumar, A.3    Voncken, F.G.J.4    Hol, W.G.J.5    Michels, P.A.M.6
  • 292
    • 0037057080 scopus 로고    scopus 로고
    • Peroxisomal targeting protein 14 (PEX14) from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization
    • A. Jardim, N. Rager, W. Liu, and B. Ullman Peroxisomal targeting protein 14 (PEX14) from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization Mol. Biochem. Parasitol. 124 2002 51 62
    • (2002) Mol. Biochem. Parasitol. , vol.124 , pp. 51-62
    • Jardim, A.1    Rager, N.2    Liu, W.3    Ullman, B.4
  • 293
    • 0033525539 scopus 로고    scopus 로고
    • Purification, localisation and characterisation of glucose-6-phosphate dehydrogenase of Trypanosoma brucei
    • N. Heise, and F.R. Opperdoes Purification, localisation and characterisation of glucose-6-phosphate dehydrogenase of Trypanosoma brucei Mol. Biochem. Parasitol. 99 1999 21 32
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 21-32
    • Heise, N.1    Opperdoes, F.R.2
  • 295
    • 0141557547 scopus 로고    scopus 로고
    • The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization
    • W.C. Voegtli, A.Y. Madrona, and D.K. Wilson The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization J. Biol. Chem. 278 2003 34373 34379
    • (2003) J. Biol. Chem. , vol.278 , pp. 34373-34379
    • Voegtli, W.C.1    Madrona, A.Y.2    Wilson, D.K.3
  • 296
    • 0034697983 scopus 로고    scopus 로고
    • Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases
    • D.M. Chudzik, P.A.M. Michels, S. de Walque, and W.G.J. Hol Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases J. Mol. Biol. 300 2000 697 707
    • (2000) J. Mol. Biol. , vol.300 , pp. 697-707
    • Chudzik, D.M.1    Michels, P.A.M.2    De Walque, S.3    Hol, W.G.J.4
  • 297
    • 0141431060 scopus 로고    scopus 로고
    • Analysis of the sequence motifs responsible for the interactions of peroxins 14 and 5, which are involved in glycosome biogenesis in Trypanosoma brucei
    • J. Choe, J. Moyersoen, C. Roach, T.L. Carter, E. Fan, P.A.M. Michels, and W.G.J. Hol Analysis of the sequence motifs responsible for the interactions of peroxins 14 and 5, which are involved in glycosome biogenesis in Trypanosoma brucei Biochemistry 42 2003 10915 10922
    • (2003) Biochemistry , vol.42 , pp. 10915-10922
    • Choe, J.1    Moyersoen, J.2    Roach, C.3    Carter, T.L.4    Fan, E.5    Michels, P.A.M.6    Hol, W.G.J.7
  • 300
  • 301
    • 0035630691 scopus 로고    scopus 로고
    • Protein-protein interfaces: Mimics and inhibitors
    • A.G. Cochran Protein-protein interfaces: mimics and inhibitors Curr. Opin. Chem. Biol. 5 2001 654 659
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 654-659
    • Cochran, A.G.1
  • 302
    • 0035210089 scopus 로고    scopus 로고
    • How are peroxisomes formed. the role of the endoplasmic reticulum and peroxins
    • R.T. Mullen, C.R. Flynn, and R.N. Trelease How are peroxisomes formed. The role of the endoplasmic reticulum and peroxins Trends Plant Sci. 6 2001 256 261
    • (2001) Trends Plant Sci. , vol.6 , pp. 256-261
    • Mullen, R.T.1    Flynn, C.R.2    Trelease, R.N.3
  • 303
    • 0035815693 scopus 로고    scopus 로고
    • Discrete targeting signals direct PMP47 to oleate-induced peroxisomes in Saccharomyces cerevisiae
    • X.D. Wang, M.J. Unruh, and J.M. Goodman Discrete targeting signals direct PMP47 to oleate-induced peroxisomes in Saccharomyces cerevisiae J. Biol. Chem. 276 2001 10897 10905
    • (2001) J. Biol. Chem. , vol.276 , pp. 10897-10905
    • Wang, X.D.1    Unruh, M.J.2    Goodman, J.M.3
  • 304
    • 1642423544 scopus 로고    scopus 로고
    • Multiple targeting modules on peroxisomal proteins are not redundant: Discrete functions of targeting signals within Pmp47 and Pex8p
    • X. Wang, M.A. McMahon, S.N. Shelton, M. Nampaisansuk, J.L. Ballard, and J.M. Goodman Multiple targeting modules on peroxisomal proteins are not redundant: discrete functions of targeting signals within Pmp47 and Pex8p Mol. Biol. Cell 15 2004 1702 1710
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1702-1710
    • Wang, X.1    McMahon, M.A.2    Shelton, S.N.3    Nampaisansuk, M.4    Ballard, J.L.5    Goodman, J.M.6
  • 305
    • 0035937842 scopus 로고    scopus 로고
    • Topogenesis of peroxisomal membrane protein requires a short, positively charged intervening-loop sequence and flanking hydrophobic segments. Study using human membrane protein PMP34
    • M. Honsho, and Y. Fujiki Topogenesis of peroxisomal membrane protein requires a short, positively charged intervening-loop sequence and flanking hydrophobic segments. Study using human membrane protein PMP34 J. Biol. Chem. 276 2001 9375 9382
    • (2001) J. Biol. Chem. , vol.276 , pp. 9375-9382
    • Honsho, M.1    Fujiki, Y.2
  • 306
    • 0035844874 scopus 로고    scopus 로고
    • Multiple distinct targeting signals in integral peroxisomal membrane proteins
    • J.M. Jones, J.C. Morell, and S.J. Gould Multiple distinct targeting signals in integral peroxisomal membrane proteins J. Cell Biol. 153 2001 1141 1149
    • (2001) J. Cell Biol. , vol.153 , pp. 1141-1149
    • Jones, J.M.1    Morell, J.C.2    Gould, S.J.3
  • 307
  • 308
    • 0037016760 scopus 로고    scopus 로고
    • Two different targeting signals direct human peroxisomal membrane protein 22 to peroxisomes
    • U. Brosius, T. Dehmel, and J. Gartner Two different targeting signals direct human peroxisomal membrane protein 22 to peroxisomes J. Biol. Chem. 277 2002 774 784
    • (2002) J. Biol. Chem. , vol.277 , pp. 774-784
    • Brosius, U.1    Dehmel, T.2    Gartner, J.3
  • 309
    • 4243357938 scopus 로고    scopus 로고
    • Targeting of green fluorescent protein to peroxisomes and peroxisome membranes in S. cerevisiae
    • K. Huang, and P.B. Lazarow Targeting of green fluorescent protein to peroxisomes and peroxisome membranes in S. cerevisiae Mol. Biol. Cell 7 1996 2871
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2871
    • Huang, K.1    Lazarow, P.B.2
  • 310
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 24 1997 4876 4882
    • (1997) Nucleic Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


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