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Volumn 135, Issue 1, 1996, Pages 123-137

Redox-sensitive homodimerization of Pex11p: A proposed mechanism to regulate peroxisomal division

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Indexed keywords

FUNGAL PROTEIN;

EID: 0029792856     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.135.1.123     Document Type: Article
Times cited : (93)

References (51)
  • 1
    • 0028047262 scopus 로고
    • Dynamics of mitochondria in living cells: Shape changes, dislocation, fusion, and fission of mitochondria
    • Bereiter-Hahn, J., and M. Voth. 1994. Dynamics of mitochondria in living cells: shape changes, dislocation, fusion, and fission of mitochondria. Microsc. Res. Tech. 27:198-219.
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 198-219
    • Bereiter-Hahn, J.1    Voth, M.2
  • 2
    • 0028129071 scopus 로고
    • MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria
    • Burgess, S.M., M. Delannoy, and R.E. Jensen. 1994. MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria. J. Cell Biol. 126:1375-1391.
    • (1994) J. Cell Biol. , vol.126 , pp. 1375-1391
    • Burgess, S.M.1    Delannoy, M.2    Jensen, R.E.3
  • 4
    • 0029879509 scopus 로고    scopus 로고
    • The sorting sequence of the peroxisomal integral membrane protein PMP47 is contained within a short hydrophilic loop
    • Dyer, J.M., J.A. McNew, and J.M. Goodman. 1996. The sorting sequence of the peroxisomal integral membrane protein PMP47 is contained within a short hydrophilic loop. J. Cell Biol. 133:269-280.
    • (1996) J. Cell Biol. , vol.133 , pp. 269-280
    • Dyer, J.M.1    McNew, J.A.2    Goodman, J.M.3
  • 5
    • 0028859252 scopus 로고
    • Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p
    • Erdmann, R., and G. Blobel. 1995. Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p. J. Cell Biol. 128:509-523.
    • (1995) J. Cell Biol. , vol.128 , pp. 509-523
    • Erdmann, R.1    Blobel, G.2
  • 6
    • 0026651919 scopus 로고
    • Shape changes of giant liposomes induced by an asymetric transmembrane distribution of phospholipids
    • Farge, E., and P.F. Devaux. 1992. Shape changes of giant liposomes induced by an asymetric transmembrane distribution of phospholipids. Biophys. J. 61: 347-357.
    • (1992) Biophys. J. , vol.61 , pp. 347-357
    • Farge, E.1    Devaux, P.F.2
  • 7
    • 0022998575 scopus 로고
    • The membrane proteins of the methanol-induced peroxisome of Candida boidinii: Initial characterization and generation of monoclonal antibodies
    • Goodman, J.M., J. Maher, P.A. Silver, A. Pacifico, and D. Sanders. 1986. The membrane proteins of the methanol-induced peroxisome of Candida boidinii: Initial characterization and generation of monoclonal antibodies. J. Biol. Chem. 261:3464-3468.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3464-3468
    • Goodman, J.M.1    Maher, J.2    Silver, P.A.3    Pacifico, A.4    Sanders, D.5
  • 8
    • 0025552698 scopus 로고
    • Peroxisomes induced in Candida boidinni by methanol, oleic acid and D-alanine vary in metabolic function but share common integral membrane proteins
    • Goodman, J.M., S.B. Trapp, H. Hwang, and M. Veenhuis. 1990. Peroxisomes induced in Candida boidinni by methanol, oleic acid and D-alanine vary in metabolic function but share common integral membrane proteins. J. Cell Sci. 97:193-204.
    • (1990) J. Cell Sci. , vol.97 , pp. 193-204
    • Goodman, J.M.1    Trapp, S.B.2    Hwang, H.3    Veenhuis, M.4
  • 9
    • 0029609755 scopus 로고
    • PPAR: A mediator of peroxisomal proliferator action
    • Green, S. 1995. PPAR: a mediator of peroxisomal proliferator action. Mut. Res. 333:101-109.
    • (1995) Mut. Res. , vol.333 , pp. 101-109
    • Green, S.1
  • 10
    • 0028903534 scopus 로고
    • Import of microinjected proteins bearing the SKL peroxisomal targeting sequence into the peroxisomes of a human fibroblast cell line: Evidence that virtually all peroxisomes are import-competent
    • Hill, P.E., and P.A. Walton. 1995. Import of microinjected proteins bearing the SKL peroxisomal targeting sequence into the peroxisomes of a human fibroblast cell line: evidence that virtually all peroxisomes are import-competent. J. Cell Sci. 108:1469-1476.
    • (1995) J. Cell Sci. , vol.108 , pp. 1469-1476
    • Hill, P.E.1    Walton, P.A.2
  • 11
    • 0023202281 scopus 로고
    • Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutary coenzyme A reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum
    • Jingami, H., M.S. Brown, J.L. Goldstein, R.G. Anderson, and K.L. Luskey, 1987. Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutary coenzyme A reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum. J. Cell Biol. 104: 1693-1704.
    • (1987) J. Cell Biol. , vol.104 , pp. 1693-1704
    • Jingami, H.1    Brown, M.S.2    Goldstein, J.L.3    Anderson, R.G.4    Luskey, K.L.5
  • 12
    • 0025937302 scopus 로고
    • Shape transitions and shape stability of giant phospholipid vesicles in pure water induced by area-to-volume changes
    • Käs, J., and E. Sackmann. 1991. Shape transitions and shape stability of giant phospholipid vesicles in pure water induced by area-to-volume changes. Biophys. J. 60:825-844.
    • (1991) Biophys. J. , vol.60 , pp. 825-844
    • Käs, J.1    Sackmann, E.2
  • 13
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., J.D. Roberts, and R.A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154: 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0028997684 scopus 로고
    • Targeted disruption of the alpha isoform of the peroxisome proliferator-activated receptor gene in mice results in abolishment of the pleiotropic effects of peroxisome proliferators
    • Lee, S.S., T. Pineau, J. Drago, E.J. Lee, J.W. Owens, D.L. Kroetz, P.M. Fernandez-Salguero, H. Westphal, and F.J. Gonzales. 1995. Targeted disruption of the alpha isoform of the peroxisome proliferator-activated receptor gene in mice results in abolishment of the pleiotropic effects of peroxisome proliferators. Mol. Cell. Biol. 15:3012-3022.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3012-3022
    • Lee, S.S.1    Pineau, T.2    Drago, J.3    Lee, E.J.4    Owens, J.W.5    Kroetz, D.L.6    Fernandez-Salguero, P.M.7    Westphal, H.8    Gonzales, F.J.9
  • 16
    • 0027299296 scopus 로고
    • Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus
    • Li, Y., M. Schubert, R.R. Wagner, and C.Y. Kang. 1993. Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus. J. Virol. 67:4415-4420.
    • (1993) J. Virol. , vol.67 , pp. 4415-4420
    • Li, Y.1    Schubert, M.2    Wagner, R.R.3    Kang, C.Y.4
  • 17
    • 0027524176 scopus 로고
    • RTG1 and RTG2: Two yeast genes required for a novel path of communication from mitochondria to the nucleus
    • Liao, X., and R.A. Butow. 1993. RTG1 and RTG2: two yeast genes required for a novel path of communication from mitochondria to the nucleus. Cell. 12: 61-71.
    • (1993) Cell , vol.12 , pp. 61-71
    • Liao, X.1    Butow, R.A.2
  • 18
    • 0027294580 scopus 로고
    • Domain-induced budding of fluid membranes
    • Lipowsky, R. 1993. Domain-induced budding of fluid membranes. Biophys. J. 64:1133-1138.
    • (1993) Biophys. J. , vol.64 , pp. 1133-1138
    • Lipowsky, R.1
  • 19
    • 0024509605 scopus 로고
    • Biochemical mechanisms of induction of hepatic peroxisome proliferation
    • Lock, E.A., A.M. Mitchell, and C.R. Elcombe. 1989. Biochemical mechanisms of induction of hepatic peroxisome proliferation. Annu. Rev. Pharmacol. Toxicol. 29:145-163.
    • (1989) Annu. Rev. Pharmacol. Toxicol. , vol.29 , pp. 145-163
    • Lock, E.A.1    Mitchell, A.M.2    Elcombe, C.R.3
  • 20
    • 0029080687 scopus 로고
    • Formation of membrane domains during the budding of vesicular stomatitis virus. A model for selective lipid and protein sorting in biological membranes
    • Luan, P., L. Yang, and M. Glaser. 1995. Formation of membrane domains during the budding of vesicular stomatitis virus. A model for selective lipid and protein sorting in biological membranes. Biochemistry. 34:9874-9883.
    • (1995) Biochemistry , vol.34 , pp. 9874-9883
    • Luan, P.1    Yang, L.2    Glaser, M.3
  • 21
    • 0028299317 scopus 로고
    • Formation of membrane domains by the envelope proteins of vesicular stomatitis virus
    • Luan, P.G. 1994. Formation of membrane domains by the envelope proteins of vesicular stomatitis virus. Biochemistry. 33:4483-4489.
    • (1994) Biochemistry , vol.33 , pp. 4483-4489
    • Luan, P.G.1
  • 22
    • 0027315501 scopus 로고
    • Biogenesis of peroxisomes: Isolation and characterization of two distinct peroxisomal populations from normal and regenerating rat liver
    • Lüers, G., T. Hashimoto, H.D. Fahimi, and A. Völkl. 1993. Biogenesis of peroxisomes: isolation and characterization of two distinct peroxisomal populations from normal and regenerating rat liver. J. Cell Biol. 121:1271-1280.
    • (1993) J. Cell Biol. , vol.121 , pp. 1271-1280
    • Lüers, G.1    Hashimoto, T.2    Fahimi, H.D.3    Völkl, A.4
  • 24
    • 0028231695 scopus 로고
    • An internal region of the peroxisomal membrane protein PMP47 is essential for sorting to peroxisomes
    • McCammon, M.T., J.A. McNew, P.J. Willy, and J.M. Goodman. 1994. An internal region of the peroxisomal membrane protein PMP47 is essential for sorting to peroxisomes. J. Cell Biol. 124:915-925.
    • (1994) J. Cell Biol. , vol.124 , pp. 915-925
    • McCammon, M.T.1    McNew, J.A.2    Willy, P.J.3    Goodman, J.M.4
  • 25
    • 0025046371 scopus 로고
    • Association of glyoxylate and beta-oxidation enzymes with peroxisomes of Saccharomyces cerevisiae
    • McCammon, M.T., M. Veenhuis, S.B. Trapp, and J.M. Goodman. 1990. Association of glyoxylate and beta-oxidation enzymes with peroxisomes of Saccharomyces cerevisiae. J. Bacteriol. 172:5816-5827.
    • (1990) J. Bacteriol. , vol.172 , pp. 5816-5827
    • McCammon, M.T.1    Veenhuis, M.2    Trapp, S.B.3    Goodman, J.M.4
  • 26
    • 0028033934 scopus 로고
    • An oligomeric protein is imported into peroxisomes in vivo
    • McNew, J.A., and J.M. Goodman. 1994. An oligomeric protein is imported into peroxisomes in vivo. J. Cell Biol. 127:1245-1257.
    • (1994) J. Cell Biol. , vol.127 , pp. 1245-1257
    • McNew, J.A.1    Goodman, J.M.2
  • 27
    • 0027399721 scopus 로고
    • Specific cross-linking of the proline isomerase cyclophilin to a non-proline-containing peptide
    • McNew, J.A., K. Sykes, and J.M. Goodman. 1993. Specific cross-linking of the proline isomerase cyclophilin to a non-proline-containing peptide. Mol. Biol. Cell. 4:223-232.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 223-232
    • McNew, J.A.1    Sykes, K.2    Goodman, J.M.3
  • 28
    • 0017166624 scopus 로고
    • Cytochrome P-450 induction by phenobarbital and 3-methylcholanthrene in primary cultures of hepatocytes
    • Michalopoulos, G., C.A. Sattler, G.L. Sattler, and H.C. Pitot. 1976. Cytochrome P-450 induction by phenobarbital and 3-methylcholanthrene in primary cultures of hepatocytes. Science (Wash. DC). 193:907-909.
    • (1976) Science (Wash. DC) , vol.193 , pp. 907-909
    • Michalopoulos, G.1    Sattler, C.A.2    Sattler, G.L.3    Pitot, H.C.4
  • 29
    • 0027944155 scopus 로고
    • The peroxisonial membrane proteins of Candida boidinii: Gene isolation and expression
    • Moreno, M., R. Lark, K.L. Campbell, and J.M. Goodman. 1994. The peroxisonial membrane proteins of Candida boidinii: gene isolation and expression. Yeast. 10:1447-1457.
    • (1994) Yeast , vol.10 , pp. 1447-1457
    • Moreno, M.1    Lark, R.2    Campbell, K.L.3    Goodman, J.M.4
  • 30
    • 0039720445 scopus 로고
    • Rhabdovirus membrane and maturation
    • R.R. Wagner, editor. Plenum Press, New York
    • Pal, R., and R.R. Wagner. 1987. Rhabdovirus membrane and maturation. In The Rhabdoviruses. R.R. Wagner, editor. Plenum Press, New York. 72-158.
    • (1987) The Rhabdoviruses , pp. 72-158
    • Pal, R.1    Wagner, R.R.2
  • 32
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J.E., and F.T. Wieland. 1996. Protein sorting by transport vesicles. Science (Wash. DC). 272:227-234.
    • (1996) Science (Wash. DC) , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 33
    • 0029182477 scopus 로고
    • Budding, fission, and domain formation in mixed lipid vesicles induced by lateral phase separation and macromolecular condensation
    • Sackmann, E., and T. Feder. 1995. Budding, fission, and domain formation in mixed lipid vesicles induced by lateral phase separation and macromolecular condensation. Mol. Membr. Biol. 12:21-28.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 21-28
    • Sackmann, E.1    Feder, T.2
  • 34
    • 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
    • Sakai, Y., P.A. Marshall, A. Saiganji, K. Takabe, H. Saiki, N. Kato, and J.M. Goodman. 1995. The Candida boidinii peroxisomal membrane protein Pmp30 has a role in peroxisomal proliferation and is functionally homologous to Pmp27 from Saccharomyces cerevisiae. J. Bacteriol. 177:6773-6781.
    • (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
  • 36
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner, W., and C. Weissmann. 1973. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56:502-514.
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 37
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Scheckman, R., and L. Orci. 1996. Coat proteins and vesicle budding. Science (Wash. DC). 271:1526-1533.
    • (1996) Science (Wash. DC) , vol.271 , pp. 1526-1533
    • Scheckman, R.1    Orci, L.2
  • 38
    • 0027982467 scopus 로고
    • Heterogeniety of peraxisomes in human hepatoblastoma cell line HepG2. Evidence of distinct subpopulations
    • Schrader, M., E. Baumgart, A. Völkl, and H.D. Fahimi. 1994. Heterogeniety of peraxisomes in human hepatoblastoma cell line HepG2. Evidence of distinct subpopulations. Eur. J. Cell Biol. 64:281-294.
    • (1994) Eur. J. Cell Biol. , vol.64 , pp. 281-294
    • Schrader, M.1    Baumgart, E.2    Völkl, A.3    Fahimi, H.D.4
  • 39
    • 0030071925 scopus 로고    scopus 로고
    • Interaction of microtubules with peroxisomes. Tubular and spherical peroxisomes in HepG2 cells and their alterations induced by microtubule-active drugs
    • Schrader, M., J.K. Burkhardt, E. Baumgart, G. Lüers, H. Spring, A. Völkl, and H.D. Fahimi. 1996. Interaction of microtubules with peroxisomes. Tubular and spherical peroxisomes in HepG2 cells and their alterations induced by microtubule-active drugs. Eur J. Cell Biol. 69:24-35.
    • (1996) Eur J. Cell Biol. , vol.69 , pp. 24-35
    • Schrader, M.1    Burkhardt, J.K.2    Baumgart, E.3    Lüers, G.4    Spring, H.5    Völkl, A.6    Fahimi, H.D.7
  • 40
    • 0001718634 scopus 로고
    • Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions
    • Sheetz, M.P., and S.J. Singer. 1974. Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions. Proc. Natl. Acad. Sci. USA. 71:4457-4461.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4457-4461
    • Sheetz, M.P.1    Singer, S.J.2
  • 41
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 42
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo, L.F., and M.P. Yaffe. 1994. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell. Biol. 126:1361-1373.
    • (1994) J. Cell. Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 44
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gets to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gets to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 45
    • 0017151579 scopus 로고
    • Hansenula polymorpha in a methanol-limited chemostat. Physiological responses due to the involvement of methanol oxidase as a key enzyme in methanol metabolism
    • van Dijken, J.P., R. Otto, and W. Harder. 1976. Hansenula polymorpha in a methanol-limited chemostat. Physiological responses due to the involvement of methanol oxidase as a key enzyme in methanol metabolism. Arch. Microbiol. 111:137-144.
    • (1976) Arch. Microbiol. , vol.111 , pp. 137-144
    • Van Dijken, J.P.1    Otto, R.2    Harder, W.3
  • 46
    • 0028845973 scopus 로고
    • Localization of peroxisomal 3-oxoacyl-CoA thiolase in particles of varied density in rat liver: Implications for peroxisome biogenesis
    • van Roermund, C.W.T., M. van der Berg, and R.J.A. Wanders. 1995. Localization of peroxisomal 3-oxoacyl-CoA thiolase in particles of varied density in rat liver: implications for peroxisome biogenesis. Biochim. Biophys. Acta. 1245:348-358.
    • (1995) Biochim. Biophys. Acta , vol.1245 , pp. 348-358
    • Van Roermund, C.W.T.1    Van Der Berg, M.2    Wanders, R.J.A.3
  • 47
    • 0025103805 scopus 로고
    • Peroxisomal assembly: Membrane proliferation precedes the induction of the abundant matrix proteins in the methylotrophic yeast Candida boidinii
    • Veenhuis, M., and J.M. Goodman. 1990. Peroxisomal assembly: membrane proliferation precedes the induction of the abundant matrix proteins in the methylotrophic yeast Candida boidinii. J. Cell Sci. 96:583-590.
    • (1990) J. Cell Sci. , vol.96 , pp. 583-590
    • Veenhuis, M.1    Goodman, J.M.2
  • 48
    • 0001931722 scopus 로고
    • Metabolic significance and biogenesis of microbodies in yeasts
    • H.D. Fahimi and H. Sies, editors. Springer-Verlag, Berlin
    • Veenhuis, M., and W. Harder. 1987. Metabolic significance and biogenesis of microbodies in yeasts. In Peroxisomes in Biology and Medicine. H.D. Fahimi and H. Sies, editors. Springer-Verlag, Berlin. 437-458.
    • (1987) Peroxisomes in Biology and Medicine , pp. 437-458
    • Veenhuis, M.1    Harder, W.2
  • 49
    • 0017820576 scopus 로고
    • Development of crystalline peroxisomes in methanol-grown cells of the yeast Hansenula polymoropha and its relation to environmental conditions
    • Veenhuis, M., J.P. van Dijken, S.A.F. Pilon, and W. Harder. 1978. Development of crystalline peroxisomes in methanol-grown cells of the yeast Hansenula polymoropha and its relation to environmental conditions. Arch. Microbiol. 117:153-163.
    • (1978) Arch. Microbiol. , vol.117 , pp. 153-163
    • Veenhuis, M.1    Van Dijken, J.P.2    Pilon, S.A.F.3    Harder, W.4
  • 50
    • 0028939995 scopus 로고
    • Novel peroxisomal populations in subcellular fractions from rat liver
    • Wilcke, M., K. Hultenby, and S.E.H. Alexson. 1995. Novel peroxisomal populations in subcellular fractions from rat liver. J. Biol. Chem. 270:6949-6958.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6949-6958
    • Wilcke, M.1    Hultenby, K.2    Alexson, S.E.H.3
  • 51
    • 0023571885 scopus 로고
    • Three-dimensional reconstruction of a peroxisomal reticulum in regenerating rat liver: Evidence of interconnections between heterogeneous segments
    • Yamamoto, K., and H.D. Fahimi. 1987. Three-dimensional reconstruction of a peroxisomal reticulum in regenerating rat liver: evidence of interconnections between heterogeneous segments. J. Cell Biol. 105:713-72.
    • (1987) J. Cell Biol. , vol.105 , pp. 713-772
    • Yamamoto, K.1    Fahimi, H.D.2


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