메뉴 건너뛰기




Volumn 17, Issue 3, 2000, Pages 188-200

Predicting the function and subcellular location of Caenorhabditis elegans proteins similar to Saccharomyces cerevisiae β-oxidation enzymes

Author keywords

Caenorhabditis clegans; Peroxisome; PEX 5; PTS1; Saccharomyces cercrisiae; Tetratricopeptide repeat (TPR); Two hybrid; oxidation

Indexed keywords


EID: 33749199662     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0061(20000930)17:3<188::AID-YEA27>3.3.CO;2-5     Document Type: Article
Times cited : (27)

References (59)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, cl al. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 2
    • 0027255909 scopus 로고
    • Elimination of false positives that arise in using the two-hybrid system
    • Bartel P, Chien CT, Sternglanz R, Fields S. 1993. Elimination of false positives that arise in using the two-hybrid system. Biotechniques 14: 920-924.
    • (1993) Biotechniques , vol.14 , pp. 920-924
    • Bartel, P.1    Chien, C.T.2    Sternglanz, R.3    Fields, S.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochcm 72: 248-254.
    • (1976) Anal Biochcm , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0019961172 scopus 로고
    • β-Hydroxyisobutyryl-coenzyme a deacylase deficiency: A defect in valine metabolism associated with physical malformations
    • Brown GK, Hunt SM, Scholem R, et al. 1982. β-Hydroxyisobutyryl-coenzyme A deacylase deficiency: a defect in valine metabolism associated with physical malformations. Pediatrics 70: 532-538.
    • (1982) Pediatrics , vol.70 , pp. 532-538
    • Brown, G.K.1    Hunt, S.M.2    Scholem, R.3
  • 5
    • 0030950139 scopus 로고    scopus 로고
    • A second isoform of 3-ketoacyl-CoA thiolase found in Caenorhabditis elegans, which is similar to sterol carrier protein x but lacks the sequence of sterol carrier protein 2
    • Bun-Ya M, Maebuchi M, Hashimoto T, Yokota S, Kamiryo T. 1997. A second isoform of 3-ketoacyl-CoA thiolase found in Caenorhabditis elegans, which is similar to sterol carrier protein x but lacks the sequence of sterol carrier protein 2. Eur J Biochcm 245: 252-259.
    • (1997) Eur J Biochcm , vol.245 , pp. 252-259
    • Bun-Ya, M.1    Maebuchi, M.2    Hashimoto, T.3    Yokota, S.4    Kamiryo, T.5
  • 6
    • 0026599048 scopus 로고
    • One-step transformation of yeast in stationary phase
    • Chen D-C, Yang B-C, Kuo T-T. 1992. One-step transformation of yeast in stationary phase. Curr Genet 21: 83-84.
    • (1992) Curr Genet , vol.21 , pp. 83-84
    • Chen, D.-C.1    Yang, B.-C.2    Kuo, T.-T.3
  • 7
    • 0032509179 scopus 로고    scopus 로고
    • Comparison of the complete protein sets of worm and yeast: Orthology and divergence
    • Chervitz SA, Aravind L, Sherlock G, et al. 1998. Comparison of the complete protein sets of worm and yeast: orthology and divergence. Science 282: 2022-2028.
    • (1998) Science , vol.282 , pp. 2022-2028
    • Chervitz, S.A.1    Aravind, L.2    Sherlock, G.3
  • 8
    • 0026639625 scopus 로고
    • Protein interaction cloning in yeast: Identification of mammalian proteins that react with the leucine zipper of Jun
    • Chevray PM, Nathans D. 1992. Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun. Proc Nail Acad Sci US AW: 5789-5793.
    • (1992) Proc Nail Acad Sci US AW , pp. 5789-5793
    • Chevray, P.M.1    Nathans, D.2
  • 9
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • Consortium. 1998. Genome sequence of the nematode C. elegans: a platform for investigating biology. Science 282: 2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 10
    • 0033968614 scopus 로고    scopus 로고
    • The yeast proteome database. YPD and Caenorhabditis elegans proteome database. WormPD: Comprehensive resources for the organization and comparison of model organism protein information
    • Costanzo MC, Hogan JD, Cusick ME, et al. 2000. The yeast proteome database. YPD and Caenorhabditis elegans proteome database. WormPD: comprehensive resources for the organization and comparison of model organism protein information. Nucleic Acids Res 28: 73-76.
    • (2000) Nucleic Acids Res , vol.28 , pp. 73-76
    • Costanzo, M.C.1    Hogan, J.D.2    Cusick, M.E.3
  • 11
    • 0013897667 scopus 로고
    • Peroxisomes. Microbodies and related particles
    • de Duve C, Baudhuin P. 1966. Peroxisomes. Microbodies and related particles. Physiol Rev 46: 323-357.
    • (1966) Physiol Rev , vol.46 , pp. 323-357
    • De Duve, C.1    Baudhuin, P.2
  • 12
    • 0026598115 scopus 로고
    • Targeting signal of the peroxisomal catalase in the methylotrophic yeast Hanscnula polymorpha
    • Didion T, Roggenkamp R. 1992. Targeting signal of the peroxisomal catalase in the methylotrophic yeast Hanscnula polymorpha. FEES Lett 303: 113-116.
    • (1992) FEES Lett , vol.303 , pp. 113-116
    • Didion, T.1    Roggenkamp, R.2
  • 13
    • 0025335782 scopus 로고
    • Structure and transcriptional control of the Saccharoniyces cererisiae POX1 gene encoding acyl-coenzyme a oxidase
    • Dmochowska A, Dignard D, Maleszka R, Thomas DY. 1990. Structure and transcriptional control of the Saccharoniyces cererisiae POX1 gene encoding acyl-coenzyme A oxidase. Gene 88: 247-252.
    • (1990) Gene , vol.88 , pp. 247-252
    • Dmochowska, A.1    Dignard, D.2    Maleszka, R.3    Thomas, D.Y.4
  • 14
    • 0025767818 scopus 로고
    • Regulation of transcription of the gene coding for peroxisomal 3-oxoacyl-CoA thiolase of Saccharomyces cererisiae
    • Einerhand AW, Voorn-Brouwer TM, Erdmann R, Kunau W-H, Tabak HF. 1991. Regulation of transcription of the gene coding for peroxisomal 3-oxoacyl-CoA thiolase of Saccharomyces cererisiae. Eur J Biochcm 200: 113-122.
    • (1991) Eur J Biochcm , vol.200 , pp. 113-122
    • Einerhand, A.W.1    Voorn-Brouwer, T.M.2    Erdmann, R.3    Kunau, W.-H.4    Tabak, H.F.5
  • 15
    • 0029058992 scopus 로고
    • Peroxisomal and mitochondrial carnitine acetyltransferases of Saccharomyces cererisiae are encoded by a single gene
    • Elgersma Y, van Roermund CW, Wanders RJ, Tabak HF. 1995. Peroxisomal and mitochondrial carnitine acetyltransferases of Saccharomyces cererisiae are encoded by a single gene. EMBO J 14: 3472-3479.
    • (1995) EMBO J , vol.14 , pp. 3472-3479
    • Elgersma, Y.1    Van Roermund, C.W.2    Wanders, R.J.3    Tabak, H.F.4
  • 16
    • 0029912063 scopus 로고    scopus 로고
    • Analysis of the carboxy-terminal peroxisomal targeting signal 1 in a homologous context in Saccharomyces cererisiae
    • Elgersma Y, Vos A, van den Berg M, van Roermund CW, et al. 1996. Analysis of the carboxy-terminal peroxisomal targeting signal 1 in a homologous context in Saccharomyces cererisiae. J Biol Chem 271: 26375-26382.
    • (1996) J Biol Chem , vol.271 , pp. 26375-26382
    • Elgersma, Y.1    Vos, A.2    Van Den Berg, M.3    Van Roermund, C.W.4
  • 18
    • 0033153285 scopus 로고    scopus 로고
    • Identification of peroxisomal proteins by using M13 phage protein VI phage display: Molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase
    • Fransen M, Van Veldhoven PP, Subramani S. 1999. Identification of peroxisomal proteins by using M13 phage protein VI phage display: molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase. Biochem J 340: 561-568.
    • (1999) Biochem J , vol.340 , pp. 561-568
    • Fransen, M.1    Van Veldhoven, P.P.2    Subramani, S.3
  • 22
    • 0023548002 scopus 로고
    • Identification of a peroxisomal targeting signal at the carboxy-terminus of firefly lueiferase
    • Gould SJ, Keller GA, Subramani S. 1987. Identification of a peroxisomal targeting signal at the carboxy-terminus of firefly lueiferase. J Cell Biol 105: 2923-2931.
    • (1987) J Cell Biol , vol.105 , pp. 2923-2931
    • Gould, S.J.1    Keller, G.A.2    Subramani, S.3
  • 23
    • 0025191059 scopus 로고
    • Peroxisomal protein import is conserved between yeast, plants, insects and mammals
    • Gould SJ, Keller GA, Schneider M, et al. 1990. Peroxisomal protein import is conserved between yeast, plants, insects and mammals. EMBO J 9: 85-90.
    • (1990) EMBO J , vol.9 , pp. 85-90
    • Gould, S.J.1    Keller, G.A.2    Schneider, M.3
  • 24
    • 0030848850 scopus 로고    scopus 로고
    • The Saccharomyces cercrisiac peroxisomal 2,4-dienoyl-CoA reductase is encoded by the oleate-inducible gene SPS19
    • Gurvitz A, Rottensteiner H, KilpelUinen SH, cl al. 1997. The Saccharomyces cercrisiac peroxisomal 2,4-dienoyl-CoA reductase is encoded by the oleate-inducible gene SPS19. J Biol Chem 272: 22140-22147.
    • (1997) J Biol Chem , vol.272 , pp. 22140-22147
    • Gurvitz, A.1    Rottensteiner, H.2    Kilpeluinen, S.H.3
  • 25
    • 0032553124 scopus 로고    scopus 로고
    • 2-trans-enoyl-CoA isomerase encoded by ECH is required for growth of the yeast Saccharomyces ccrevisiae on unsaturated fatty acids
    • 2-trans-enoyl-CoA isomerase encoded by ECH is required for growth of the yeast Saccharomyces ccrevisiae on unsaturated fatty acids. J Biol Chem 273: 31366-31374.
    • (1998) J Biol Chem , vol.273 , pp. 31366-31374
    • Gurvitz, A.1    Mursula, A.M.2    Firzinger, A.3
  • 27
    • 0033572998 scopus 로고    scopus 로고
    • 2-enoyl-CoA isomerase during peroxisomal β-oxidation in Saccharomyces cerevisiae
    • I999b.
    • 2-enoyl-CoA isomerase during peroxisomal β-oxidation in Saccharomyces cerevisiae. Biochem J 344: 903-914.
    • Biochem J , vol.344 , pp. 903-914
    • Gurvitz, A.1    Wabnegger, L.2    Yagi, A.I.3
  • 29
    • 0027166223 scopus 로고
    • The existence of two mitochondrial isoforms of 2,4-dienoyl-CoA reductase in the rat
    • Hakkola EH, Hiltunen JK. 1993. The existence of two mitochondrial isoforms of 2,4-dienoyl-CoA reductase in the rat. Eur J Biochem 215: 199-204.
    • (1993) Eur J Biochem , vol.215 , pp. 199-204
    • Hakkola, E.H.1    Hiltunen, J.K.2
  • 30
    • 0029860144 scopus 로고    scopus 로고
    • Primary structure and tissue-specific expression of human -hydroxyisobutyryl-coenzyme a hydrolase
    • Hawes JW, Jaskicwicz J, Shimomura Y, et al. 1996. Primary structure and tissue-specific expression of human -hydroxyisobutyryl-coenzyme A hydrolase. J Biol Chem 271: 26430-26434.
    • (1996) J Biol Chem , vol.271 , pp. 26430-26434
    • Hawes, J.W.1    Jaskicwicz, J.2    Shimomura, Y.3
  • 31
    • 0026713679 scopus 로고
    • Peroxisomal multifunctional /5-oxidation protein of Saccharomyces cercvisiae. Molecular analysis of the FOX2 gene and gene product
    • Hiltunen JK, Wenzel B, Beyer A, Erdmann R, Fossa A, Kunau W-H. 1992. Peroxisomal multifunctional /5-oxidation protein of Saccharomyces cercvisiae. Molecular analysis of the FOX2 gene and gene product. J Biol Chem 267: 6646-6653.
    • (1992) J Biol Chem , vol.267 , pp. 6646-6653
    • Hiltunen, J.K.1    Wenzel, B.2    Beyer, A.3    Erdmann, R.4    Fossa, A.5    Kunau, W.-H.6
  • 32
    • 0025877056 scopus 로고
    • A new glucose-repressible gene identified from the analysis of chromatin structure in deletion mutants of yeast SUC2 locus
    • Igual JC, Matallana E, Gonzalez-Bosch C, Franco L, PerezOrtin JE. 1991. A new glucose-repressible gene identified from the analysis of chromatin structure in deletion mutants of yeast SUC2 locus. Yeast 7: 379-389.
    • (1991) Yeast , vol.7 , pp. 379-389
    • Igual, J.C.1    Matallana, E.2    Gonzalez-Bosch, C.3    Franco, L.4    Perezortin, J.E.5
  • 33
    • 0033952584 scopus 로고    scopus 로고
    • Developmental and pathological expression of peroxisomal enzymes: Their relationship of o-bifunctional protein deficiency and Zellweger syndrome
    • Itoh M, Suzuki Y, Akaboshi S, Zhang Z, Miyabara S, Takashima S. 2000. Developmental and pathological expression of peroxisomal enzymes: their relationship of o-bifunctional protein deficiency and Zellweger syndrome. Brain Res 858: 40-47.
    • (2000) Brain Res , vol.858 , pp. 40-47
    • Itoh, M.1    Suzuki, Y.2    Akaboshi, S.3    Zhang, Z.4    Miyabara, S.5    Takashima, S.6
  • 35
    • 0034002621 scopus 로고    scopus 로고
    • Evidence for a novel pathway for the targeting of a Saccharomyces cerevisiae peroxisomal protein belonging to the isomerase/hydratasc family
    • Karpichev IV, Small GM. 2000. Evidence for a novel pathway for the targeting of a Saccharomyces cerevisiae peroxisomal protein belonging to the isomerase/hydratasc family. J Cell Sci 113:533-544.
    • (2000) J Cell Sci , vol.113 , pp. 533-544
    • Karpichev, I.V.1    Small, G.M.2
  • 36
    • 0028577805 scopus 로고
    • Isolation and characterization of cDNA for human 120kDa mitochondrial 2,4-dienoyl-coenzyme a reductase
    • Koivuranta KT, Hakkola EH, Hiltunen JK. 1994. Isolation and characterization of cDNA for human 120kDa mitochondrial 2,4-dienoyl-coenzyme A reductase. Biochcm J 304: 787-792.
    • (1994) Biochcm J , vol.304 , pp. 787-792
    • Koivuranta, K.T.1    Hakkola, E.H.2    Hiltunen, J.K.3
  • 38
    • 0027507025 scopus 로고
    • Two independent peroxisomal targeting signals in catalase a of Saccliaromyccs ccrevisiae
    • Kragler F, Langcder A, Raupachova J, Binder M, Hartig A. 1993. Two independent peroxisomal targeting signals in catalase A of Saccliaromyccs ccrevisiae. J Cell Biol 120: 665-673.
    • (1993) J Cell Biol , vol.120 , pp. 665-673
    • Kragler, F.1    Langcder, A.2    Raupachova, J.3    Binder, M.4    Hartig, A.5
  • 39
    • 0029416813 scopus 로고
    • Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of continued progress
    • Kunau W-H, Dommes V, Schulz H. 1995. β-Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: a century of continued progress. Prog Lipicl Res 34: 267-342.
    • (1995) Prog Lipicl Res , vol.34 , pp. 267-342
    • Kunau, W.-H.1    Dommes, V.2    Schulz, H.3
  • 40
    • 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 PexSp to the cognate signal and to residues adjacent to it
    • Lametschwandtner G, Brocard C, Fransen M, Van Veldhoven P, Berger J, Hartig A. 1998. The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor PexSp to the cognate signal and to residues adjacent to it. J Biol Clicm 273: 33635-33643.
    • (1998) J Biol Clicm , vol.273 , pp. 33635-33643
    • Lametschwandtner, G.1    Brocard, C.2    Fransen, M.3    Van Veldhoven, P.4    Berger, J.5    Hartig, A.6
  • 41
    • 0033200199 scopus 로고    scopus 로고
    • Typc-II 3-oxoacyl-CoA thiolase of the nematode Cacnorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced by clofibrate
    • Maebuchi M, Togo SH, Yokota S, Ghenea S, Bun-Ya M, Kamiryo T, Kawahara A. 1999. Typc-II 3-oxoacyl-CoA thiolase of the nematode Cacnorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced by clofibrate. EUT J Biochcm 264: 509-515.
    • (1999) EUT J Biochcm , vol.264 , pp. 509-515
    • Maebuchi, M.1    Togo, S.H.2    Yokota, S.3    Ghenea, S.4    Bun-Ya, M.5    Kamiryo, T.6    Kawahara, A.7
  • 42
    • 0028053931 scopus 로고
    • PAS7 encodes a novel yeast member of the WD-40 protein family essential for import of 3-oxoacyl-CoA thiolase, a PTS2containing protein, into peroxisomes
    • Marzioch M, Erdmann R, Vcenhuis M, Kunau W-H. 1994. PAS7 encodes a novel yeast member of the WD-40 protein family essential for import of 3-oxoacyl-CoA thiolase, a PTS2containing protein, into peroxisomes. EMBO J 13: 4908-4918.
    • (1994) EMBO J , vol.13 , pp. 4908-4918
    • Marzioch, M.1    Erdmann, R.2    Vcenhuis, M.3    Kunau, W.-H.4
  • 43
    • 85047669202 scopus 로고    scopus 로고
    • The targeting and assembly of peroxisomal proteins: Some old rules do not apply
    • McNew JA, Goodman JM. 1996. The targeting and assembly of peroxisomal proteins: some old rules do not apply. Trends Biochcm Sci 21: 54-58.
    • (1996) Trends Biochcm Sci , vol.21 , pp. 54-58
    • McNew, J.A.1    Goodman, J.M.2
  • 45
    • 0028890344 scopus 로고
    • Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue
    • Müller-Newen G, Janssen U, Stoffel W. 1995. Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue. Eur J Biochem 228: 68-73.
    • (1995) Eur J Biochem , vol.228 , pp. 68-73
    • Müller-Newen, G.1    Janssen, U.2    Stoffel, W.3
  • 47
    • 0029903045 scopus 로고    scopus 로고
    • The import receptor for the peroxisomal targeting signal 2. PTS2 in Saccharomyccs cerevisiae is encoded by the PAS7 gene
    • Rehling P, Marzioch M, Niesen F, Wittke E, Veenhuis M, Kunau W-H. 1996. The import receptor for the peroxisomal targeting signal 2. PTS2 in Saccharomyccs cerevisiae is encoded by the PAS7 gene. EMBO J 15: 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
  • 48
    • 0025277176 scopus 로고
    • 2,4-Dienoylcoenzyme a reductase deficiency: A possible new disorder of fatty acid oxidation
    • Roe CR, Millington DS, Norwood DL, et al. 1990. 2,4-Dienoylcoenzyme A reductase deficiency: a possible new disorder of fatty acid oxidation. J Clin Invest 85: 1703-1707.
    • (1990) J Clin Invest , vol.85 , pp. 1703-1707
    • Roe, C.R.1    Millington, D.S.2    Norwood, D.L.3
  • 50
    • 0026625826 scopus 로고
    • NADPHdependent β-oxidation of unsaturated fatty acids with double bonds extending from odd-numbered carbon atoms
    • Smeland TE, Nada M, Cuebas D, Schulz H. 1992. NADPHdependent β-oxidation of unsaturated fatty acids with double bonds extending from odd-numbered carbon atoms. Proc Natl AcadSci USA 89: 6673-6677.
    • (1992) Proc Natl AcadSci USA , vol.89 , pp. 6673-6677
    • Smeland, T.E.1    Nada, M.2    Cuebas, D.3    Schulz, H.4
  • 51
    • 0027054829 scopus 로고
    • In vivo import of firefly luciferase into the glycosomes of Trypanosoma brucci and mutational analysis of the C-terminal targeting signal
    • Sommer JM, Cheng QL, Keller G-A, Wang CC. 1992. In vivo import of firefly luciferase into the glycosomes of Trypanosoma brucci and mutational analysis of the C-terminal targeting signal. Mol Biol Cell 3: 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
  • 52
    • 0027333416 scopus 로고
    • Protein import into pcroxisomes and biogenesis of the organelle
    • Subramani S. 1993. Protein import into pcroxisomes and biogenesis of the organelle. Ann Rev Cell Biol 9: 445-478.
    • (1993) Ann Rev Cell Biol , vol.9 , pp. 445-478
    • Subramani, S.1
  • 53
    • 0030909686 scopus 로고    scopus 로고
    • PEX genes on the rise
    • Subramani S. 1997. PEX genes on the rise. Nature Genet 15: 331-333.
    • (1997) Nature Genet , vol.15 , pp. 331-333
    • Subramani, S.1
  • 54
    • 0020858899 scopus 로고
    • The embryonic cell lineage of the nematodc Caenorhabditis elegans
    • Sulston JE, Schierenberg E, White JG, Thomson JN. 1983. The embryonic cell lineage of the nematodc Caenorhabditis elegans. Dev Biol 100: 64-119.
    • (1983) Dev Biol , vol.100 , pp. 64-119
    • Sulston, J.E.1    Schierenberg, E.2    White, J.G.3    Thomson, J.N.4
  • 55
    • 16144362266 scopus 로고    scopus 로고
    • The valine catabolic pathway in human liver: Effect of cirrhosis on enzyme activities
    • Taniguchi K, Nonami T, Nakao A, et al. 1996. The valine catabolic pathway in human liver: effect of cirrhosis on enzyme activities. Hepatology 24: 1395-1398.
    • (1996) Hepatology , vol.24 , pp. 1395-1398
    • Taniguchi, K.1    Nonami, T.2    Nakao, A.3
  • 57
    • 0027138676 scopus 로고
    • PAS10 is a tetratricopcptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae
    • Van der Leij I, Franse MM, Elgersma Y, Distel B, Tabak HF. 1993. PAS10 is a tetratricopcptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae. Proc Natl Acad Sci USA 90: 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
  • 58
    • 0032620723 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of five genes coding for acyl-CoA oxidase isozymes in the yeast Yarronïa lipolytica
    • Wang H, Le Dali MT, Wache Y, Laroche C, Belin JM, Nicaud JM. 1999. Cloning, sequencing, and characterization of five genes coding for acyl-CoA oxidase isozymes in the yeast Yarronïa lipolytica. Cell Biochem Biophys 31: 165-174.
    • (1999) Cell Biochem Biophys , vol.31 , pp. 165-174
    • Wang, H.1    Le Dali, M.T.2    Wache, Y.3    Laroche, C.4    Belin, J.M.5    Nicaud, J.M.6
  • 59
    • 0028924171 scopus 로고
    • Protein-peptide interactions analyzed with the yeast two-hybrid system
    • Yang M, Wu Z, Fields S. 1995. Protein-peptide interactions analyzed with the yeast two-hybrid system. Nucleic Acids Res 23: 1152-1156.
    • (1995) Nucleic Acids Res , vol.23 , pp. 1152-1156
    • Yang, M.1    Wu, Z.2    Fields, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.