메뉴 건너뛰기




Volumn 443, Issue 2, 2012, Pages 535-547

Novel structural arrangement of nematode cystathionine β-synthases: Characterization of Caenorhabditis elegans CBS-1

Author keywords

Caenorhabditis elegans; Cystathionine synthase (CBS); Domain architecture; Homocysteine; Hydrogen sulfide; Knockdown

Indexed keywords

CYSTATHIONINE BETA SYNTHASE; CYSTATHIONINE BETA SYNTHASE 1; ENZYME VARIANT; HEME; HOMOCYSTEINE; HYDROGEN SULFIDE; MONOMER; MUTANT PROTEIN; POLYPEPTIDE; PYRIDOXAL 5 PHOSPHATE; S ADENOSYLMETHIONINE; SULFUR AMINO ACID; UNCLASSIFIED DRUG;

EID: 84859464714     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111478     Document Type: Article
Times cited : (31)

References (59)
  • 1
    • 0031748093 scopus 로고    scopus 로고
    • The metabolism of homocysteine: Pathways and regulation
    • Finkelstein, J. D. (1998) The metabolism of homocysteine: pathways and regulation. Eur. J. Pediatr. 157, S40-S44
    • (1998) Eur. J. Pediatr. , vol.157
    • Finkelstein, J.D.1
  • 2
    • 0032566713 scopus 로고    scopus 로고
    • Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity
    • Taoka, S., Ohja, S., Shan, X., Kruger, W. D. and Banerjee, R. (1998) Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity. J. Biol. Chem. 273, 25179-25184
    • (1998) J. Biol. Chem. , vol.273 , pp. 25179-25184
    • Taoka, S.1    Ohja, S.2    Shan, X.3    Kruger, W.D.4    Banerjee, R.5
  • 3
    • 9744276776 scopus 로고    scopus 로고
    • Redox regulation and reaction mechanism of human cystathionine-beta- synthase: A PLP-dependent hemesensor protein
    • DOI 10.1016/j.abb.2004.08.037, PII S0003986104004680
    • Banerjee, R. and Zou, C. G. (2005) Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor protein. Arch. Biochem. Biophys. 433, 144-156 (Pubitemid 39586589)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 144-156
    • Banerjee, R.1    Zou, C.-G.2
  • 4
    • 36049049474 scopus 로고    scopus 로고
    • Ferrous human cystathionine beta-synthase loses activity during enzyme assay due to a ligand switch process
    • DOI 10.1021/bi701159y
    • Cherney, M. M., Pazicni, S., Frank, N., Marvin, K. A., Kraus, J. P. and Burstyn, J. N. (2007) Ferrous human cystathionine beta-synthase loses activity during enzyme assay due to a ligand switch process. Biochemistry 46, 13199-13210 (Pubitemid 350086238)
    • (2007) Biochemistry , vol.46 , Issue.45 , pp. 13199-13210
    • Cherney, M.M.1    Pazicni, S.2    Frank, N.3    Marvin, K.A.4    Kraus, J.P.5    Burstyn, J.N.6
  • 5
    • 79955870491 scopus 로고    scopus 로고
    • Cobalt cystathionine beta-synthase: Acobalt-substituted heme protein with a unique thiolate ligation motif
    • Smith, A. T., Majtan, T., Freeman, K. M., Su, Y., Kraus, J. P. and Burstyn, J. N. (2011) Cobalt cystathionine beta-synthase: acobalt-substituted heme protein with a unique thiolate ligation motif. Inorg. Chem. 50, 4417-4427
    • (2011) Inorg. Chem. , vol.50 , pp. 4417-4427
    • Smith, A.T.1    Majtan, T.2    Freeman, K.M.3    Su, Y.4    Kraus, J.P.5    Burstyn, J.N.6
  • 6
    • 0033649909 scopus 로고    scopus 로고
    • The molecular evolution of pyridoxal-5′- phosphate-dependent enzymes
    • Mehta, P. K. and Christen, P. (2000) The molecular evolution of pyridoxal-5′- phosphate-dependent enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 74, 129-184
    • (2000) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.74 , pp. 129-184
    • Mehta, P.K.1    Christen, P.2
  • 7
    • 0032528375 scopus 로고    scopus 로고
    • Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: Structural and functional consequences
    • DOI 10.1006/abbi.1998.0723
    • Kery, V., Poneleit, L. and Kraus, J. P. (1998) Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: structural and functional consequences. Arch. Biochem. Biophys. 355, 222-232 (Pubitemid 28364373)
    • (1998) Archives of Biochemistry and Biophysics , vol.355 , Issue.2 , pp. 222-232
    • Kery, V.1    Poneleit, L.2    Kraus, J.P.3
  • 8
    • 0032848774 scopus 로고    scopus 로고
    • Assignment of enzymatic functions to specific regions of the PLP-dependent heme protein cystathionine beta-synthase
    • Taoka, S., Widjaja, L. and Banerjee, R. (1999) Assignment of enzymatic functions to specific regions of the PLP-dependent heme protein cystathionine beta-synthase. Biochemistry 38, 13155-13161
    • (1999) Biochemistry , vol.38 , pp. 13155-13161
    • Taoka, S.1    Widjaja, L.2    Banerjee, R.3
  • 9
    • 0021354796 scopus 로고
    • Biosynthesis and proteolytic activation of cystathionine beta-synthase in rat liver
    • Skovby, F., Kraus, J. P. and Rosenberg, L. E. (1984) Biosynthesis and proteolytic activation of cystathionine beta-synthase in rat liver. J. Biol. Chem. 259, 588-593 (Pubitemid 14177681)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.1 , pp. 588-593
    • Skovby, F.1    Kraus, J.P.2    Rosenberg, L.E.3
  • 10
    • 0038269014 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-induced targeted proteolysis of cystathionine beta-synthase modulates redox homeostasis
    • Zou, C. G. and Banerjee, R. (2003) Tumor necrosis factor-α-induced targeted proteolysis of cystathionine beta-synthase modulates redox homeostasis. J. Biol. Chem. 278, 16802-16808
    • (2003) J. Biol. Chem. , vol.278 , pp. 16802-16808
    • Zou, C.G.1    Banerjee, R.2
  • 11
    • 0034697356 scopus 로고    scopus 로고
    • Yeast cystathionine beta-synthase is a pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein
    • DOI 10.1074/jbc.C000056200
    • Jhee, K. H., McPhie, P. and Miles, E. W. (2000) Yeast cystathionine beta-synthase isa pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein. J. Biol. Chem. 275, 11541-11544 (Pubitemid 30237709)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 11541-11544
    • Jhee, K.-H.1    McPhie, P.2    Miles, E.W.3
  • 12
    • 0035794209 scopus 로고    scopus 로고
    • Characterization of transsulfuration and cysteine biosynthetic pathways in the protozoan hemoflagellate, Trypanosoma cruzi. Isolation and molecular characterization of cystathionine beta-synthase and serine acetyltransferase from Trypanosoma
    • Nozaki, T., Shigeta, Y., Saito-Nakano, Y., Imada, M. and Kruger, W. D. (2001) Characterization of transsulfuration and cysteine biosynthetic pathways in the protozoan hemoflagellate, Trypanosoma cruzi. Isolation and molecular characterization of cystathionine beta-synthase and serine acetyltransferase from Trypanosoma. J. Biol. Chem. 276, 6516-6523
    • (2001) J. Biol. Chem. , vol.276 , pp. 6516-6523
    • Nozaki, T.1    Shigeta, Y.2    Saito-Nakano, Y.3    Imada, M.4    Kruger, W.D.5
  • 13
    • 78650504604 scopus 로고    scopus 로고
    • Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine beta-synthase
    • Koutmos, M., Kabil, O., Smith, J. L. and Banerjee, R. (2010) Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine beta-synthase. Proc. Natl. Acad. Sci. U.S.A. 107, 20958-20963
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 20958-20963
    • Koutmos, M.1    Kabil, O.2    Smith, J.L.3    Banerjee, R.4
  • 14
    • 0034730104 scopus 로고    scopus 로고
    • Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation
    • DOI 10.1021/bi001020g
    • Jhee, K. H., McPhie, P. and Miles, E. W. (2000) Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation. Biochemistry 39, 10548-10556 (Pubitemid 30655932)
    • (2000) Biochemistry , vol.39 , Issue.34 , pp. 10548-10556
    • Jhee, K.-H.1    McPhie, P.2    Miles, E.W.3
  • 15
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. (1974) The genetics of Caenorhabditis elegans. Genetics 77, 71-94
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 16
    • 0035421273 scopus 로고    scopus 로고
    • Structure of human cystathionine beta-synthase: A unique pyridoxal 5′-phosphate-dependent heme protein
    • DOI 10.1093/emboj/20.15.3910
    • Meier, M., Janosik, M., Kery, V., Kraus, J. P. and Burkhard, P. (2001) Structure of human cystathionine beta-synthase: a unique pyridoxal 5′-phosphate-dependent heme protein. EMBO J. 20, 3910-3916 (Pubitemid 32751807)
    • (2001) EMBO Journal , vol.20 , Issue.15 , pp. 3910-3916
    • Meier, M.1    Janosik, M.2    Kery, V.3    Kraus, J.P.4    Burkhard, P.5
  • 17
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • Wiederstein, M. and Sippl, M. J. (2007) ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res. 35, W407-W410
    • (2007) Nucleic Acids Res. , vol.35
    • Wiederstein, M.1    Sippl, M.J.2
  • 18
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex, N. and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 21
    • 0242578620 scopus 로고    scopus 로고
    • A Simple, Fast, and Accurate Algorithm to Estimate Large Phylogenies by Maximum Likelihood
    • DOI 10.1080/10635150390235520
    • Guindon, S. and Gascuel, O. (2003) A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol. 52, 696-704 (Pubitemid 37365050)
    • (2003) Systematic Biology , vol.52 , Issue.5 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 23
    • 38449099892 scopus 로고    scopus 로고
    • Reporter gene fusions
    • The C. elegans Research Community, ed., 1-23, doi/10.1895/wormbook.1.106. 1
    • Boulin, T., Etchberger, J. F. and Hobert, O. (2006) Reporter gene fusions. In WormBook (The C. elegans Research Community, ed.), pp. 1-23, doi/10.1895/wormbook.1.106.1
    • (2006) WormBook
    • Boulin, T.1    Etchberger, J.F.2    Hobert, O.3
  • 24
    • 38349053999 scopus 로고    scopus 로고
    • Purification and characterization of the wild type and truncated human cystathionine beta-synthase enzymes expressed in E. coli
    • Frank, N., Kent, J. O., Meier, M. and Kraus, J. P. (2008) Purification and characterization of the wild type and truncated human cystathionine beta-synthase enzymes expressed in E. coli. Arch. Biochem. Biophys. 470, 64-72
    • (2008) Arch. Biochem. Biophys. , vol.470 , pp. 64-72
    • Frank, N.1    Kent, J.O.2    Meier, M.3    Kraus, J.P.4
  • 25
    • 0035124772 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of the active core of human recombinant cystathionine beta-synthase: An enzyme involved in vascular disease
    • DOI 10.1107/S0907444900017893
    • Janosik, M., Meier, M., Kery, V., Oliveriusova, J., Burkhard, P. and Kraus, J. P. (2001) Crystallization and preliminary X-ray diffraction analysis of the active core of human recombinant cystathionine beta-synthase: an enzyme involved in vascular disease. Acta Crystallogr. Sect. D Biol. Crystallogr. 57, 289-291 (Pubitemid 32145416)
    • (2001) Acta Crystallographica Section D: Biological Crystallography , vol.57 , Issue.2 , pp. 289-291
    • Janosik, M.1    Meier, M.2    Kery, V.3    Oliveriusova, J.4    Burkhard, P.5    Kraus, J.P.6
  • 26
    • 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 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 78650101391 scopus 로고    scopus 로고
    • Cross-talk between the catalytic core and the regulatory domain in cystathionine beta-synthase: Study by differential covalent labeling and computational modeling
    • Hnizda, A., Spiwok, V., Jurga, V., Kozich, V., Kodicek, M. and Kraus, J. P. (2010) Cross-talk between the catalytic core and the regulatory domain in cystathionine beta-synthase: study by differential covalent labeling and computational modeling. Biochemistry 49, 10526-10534
    • (2010) Biochemistry , vol.49 , pp. 10526-10534
    • Hnizda, A.1    Spiwok, V.2    Jurga, V.3    Kozich, V.4    Kodicek, M.5    Kraus, J.P.6
  • 29
    • 77957241706 scopus 로고    scopus 로고
    • Cystathionine beta-synthase null homocystinuric mice fail to exhibit altered hemostasis or lowering of plasma homocysteine in response to betaine treatment
    • Maclean, K. N., Sikora, J., Kozich, V., Jiang, H., Greiner, L. S., Kraus, E., Krijt, J., Crnic, L. S., Allen, R. H., Stabler, S. P. et al. (2010) Cystathionine beta-synthase null homocystinuric mice fail to exhibit altered hemostasis or lowering of plasma homocysteine in response to betaine treatment. Mol. Genet. Metab. 101, 163-171
    • (2010) Mol. Genet. Metab. , vol.101 , pp. 163-171
    • Maclean, K.N.1    Sikora, J.2    Kozich, V.3    Jiang, H.4    Greiner, L.S.5    Kraus, E.6    Krijt, J.7    Crnic, L.S.8    Allen, R.H.9    Stabler, S.P.10
  • 30
    • 79951685530 scopus 로고    scopus 로고
    • Determination of cystathionine beta-synthase activity in human plasma by LC-MS/MS: Potential use in diagnosis of CBS deficiency
    • Krijt, J., Kopecka, J., Hnizda, A., Moat, S., Kluijtmans, L. A., Mayne, P. and Kozich, V. (2011) Determination of cystathionine beta-synthase activity in human plasma by LC-MS/MS: potential use in diagnosis of CBS deficiency. J. Inherited Metab. Dis. 34, 49-55
    • (2011) J. Inherited Metab. Dis. , vol.34 , pp. 49-55
    • Krijt, J.1    Kopecka, J.2    Hnizda, A.3    Moat, S.4    Kluijtmans, L.A.5    Mayne, P.6    Kozich, V.7
  • 31
  • 35
    • 0029844625 scopus 로고    scopus 로고
    • A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst
    • DOI 10.1021/bi961517j
    • Rege, V. D., Kredich, N. M., Tai, C. H., Karsten, W. E., Schnackerz, K. D. and Cook, P. F. (1996) A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst. Biochemistry 35, 13485-13493 (Pubitemid 26349445)
    • (1996) Biochemistry , vol.35 , Issue.41 , pp. 13485-13493
    • Rege, V.D.1    Kredich, N.M.2    Tai, C.-H.3    Karsten, W.E.4    Schnackerz, K.D.5    Cook, P.F.6
  • 36
    • 58749087051 scopus 로고    scopus 로고
    • Kinetic characterization of recombinant human cystathionine beta-synthase purified from E. coli
    • Belew, M. S., Quazi, F. I., Willmore, W. G. and Aitken, S. M. (2009) Kinetic characterization of recombinant human cystathionine beta-synthase purified from E. coli. Protein Expression Purif. 64, 139-145
    • (2009) Protein Expression Purif. , vol.64 , pp. 139-145
    • Belew, M.S.1    Quazi, F.I.2    Willmore, W.G.3    Aitken, S.M.4
  • 37
    • 0033532324 scopus 로고    scopus 로고
    • Janus kinases and their role in growth and disease
    • DOI 10.1016/S0024-3205(98)00538-4, PII S0024320598005384
    • Aringer, M., Cheng, A., Nelson, J. W., Chen, M., Sudarshan, C., Zhou, Y. J. and O'Shea, J. J. (1999) Janus kinases and their role in growth and disease. Life Sci. 64, 2173-2186 (Pubitemid 29254037)
    • (1999) Life Sciences , vol.64 , Issue.24 , pp. 2173-2186
    • Aringer, M.1    Cheng, A.2    Nelson, J.W.3    Chen, M.4    Sudarshan, C.5    Zhou, Y.-J.6    O'Shea, J.J.7
  • 38
    • 33751027683 scopus 로고    scopus 로고
    • Human cystathionine beta-synthase is a target for sumoylation
    • DOI 10.1021/bi0615644
    • Kabil, O., Zhou, Y. and Banerjee, R. (2006) Human cystathionine beta-synthase isa target for sumoylation. Biochemistry 45, 13528-13536 (Pubitemid 44753822)
    • (2006) Biochemistry , vol.45 , Issue.45 , pp. 13528-13536
    • Kabil, O.1    Zhou, Y.2    Banerjee, R.3
  • 39
  • 40
    • 38549139094 scopus 로고    scopus 로고
    • Alternative splicing in C. elegans
    • The C. elegans Research Community, ed., doi/10.1895/wormbook.1.31.1
    • Zahler, A. M. (2005) Alternative splicing in C. elegans. In WormBook (The C. elegans Research Community, ed.), pp. 1-13, doi/10.1895/wormbook.1.31.1
    • (2005) WormBook , pp. 1-13
    • Zahler, A.M.1
  • 41
    • 38449094605 scopus 로고    scopus 로고
    • The C. elegans intestine
    • The C. elegans Research Community, ed.. doi/ 10.1895/wormbook.1.133.1
    • McGhee, J. D. (2007) The C. elegans intestine. In WormBook (The C. elegans Research Community, ed.). pp. 1-36, doi/10.1895/wormbook.1.133.1
    • (2007) WormBook , pp. 1-36
    • McGhee, J.D.1
  • 42
    • 0033818441 scopus 로고    scopus 로고
    • Pathways and regulation of homocysteine metabolism in mammals
    • Finkelstein, J. D. (2000) Pathways and regulation of homocysteine metabolism in mammals. Semin. Thromb. Hemostasis 26, 219-225
    • (2000) Semin. Thromb. Hemostasis , vol.26 , pp. 219-225
    • Finkelstein, J.D.1
  • 43
    • 38449121369 scopus 로고    scopus 로고
    • The cuticle
    • The C. elegans Research Community, ed.. doi/ 10.1895/wormbook.1.138.1
    • Page, A. P. and Johnstone, I. L. (2007) The cuticle. In WormBook (The C. elegans Research Community, ed.). pp. 1-15, doi/10.1895/wormbook.1.138.1
    • (2007) WormBook , pp. 1-15
    • Page, A.P.1    Johnstone, I.L.2
  • 44
    • 78651457395 scopus 로고    scopus 로고
    • Hydrogen sulfide: Its production, release and functions
    • Kimura, H. (2011) Hydrogen sulfide: its production, release and functions. Amino Acids 41, 113-121
    • (2011) Amino Acids , vol.41 , pp. 113-121
    • Kimura, H.1
  • 45
    • 75649150459 scopus 로고    scopus 로고
    • Hydrogen sulfide increases hypoxia-inducible factor-1 activity independently of von Hippel-Lindau tumor suppressor-1 in C. elegans
    • Budde, M. W. and Roth, M. B. (2010) Hydrogen sulfide increases hypoxia-inducible factor-1 activity independently of von Hippel-Lindau tumor suppressor-1 in C. elegans. Mol. Biol. Cell 21, 212-217
    • (2010) Mol. Biol. Cell , vol.21 , pp. 212-217
    • Budde, M.W.1    Roth, M.B.2
  • 46
    • 0029876402 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous neuromodulator
    • Abe, K. and Kimura, H. (1996) The possible role of hydrogen sulfide as an endogenous neuromodulator. J. Neurosci. 16, 1066-1071 (Pubitemid 26140863)
    • (1996) Journal of Neuroscience , vol.16 , Issue.3 , pp. 1066-1071
    • Abe, K.1    Kimura, H.2
  • 47
    • 0034999073 scopus 로고    scopus 로고
    • The use of functional genomics in C. elegans for studying human development and disease
    • DOI 10.1023/A:1010306731764
    • Kuwabara, P. E. and O'Neil, N. (2001) The use of functional genomics in C. elegans for studying human development and disease. J. Inherited Metab. Dis. 24, 127-138 (Pubitemid 32479411)
    • (2001) Journal of Inherited Metabolic Disease , vol.24 , Issue.2 , pp. 127-138
    • Kuwabara, P.E.1    O'Neil, N.2
  • 48
    • 33746982979 scopus 로고    scopus 로고
    • Propionyl-CoA and adenosylcobalamin metabolism in Caenorhabditis elegans: Evidence for a role of methylmalonyl-CoA epimerase in intermediary metabolism
    • DOI 10.1016/j.ymgme.2006.06.001, PII S1096719206002149
    • Chandler, R. J., Aswani, V., Tsai, M. S., Falk, M., Wehrli, N., Stabler, S., Allen, R., Sedensky, M., Kazazian, H. H. and Venditti, C. P. (2006) Propionyl-CoA and adenosylcobalamin metabolism in Caenorhabditis elegans: evidence for a role of methylmalonyl-CoA epimerase in intermediary metabolism. Mol. Genet. Metab. 89, 64-73 (Pubitemid 44205483)
    • (2006) Molecular Genetics and Metabolism , vol.89 , Issue.1-2 , pp. 64-73
    • Chandler, R.J.1    Aswani, V.2    Tsai, M.S.3    Falk, M.4    Wehrli, N.5    Stabler, S.6    Allen, R.7    Sedensky, M.8    Kazazian, H.H.9    Venditti, C.P.10
  • 49
    • 48749129833 scopus 로고    scopus 로고
    • Anabolic function of phenylalanine hydroxylase in Caenorhabditis elegans
    • Calvo, A. C., Pey, A. L., Ying, M., Loer, C. M. and Martinez, A. (2008) Anabolic function of phenylalanine hydroxylase in Caenorhabditis elegans. FASEB J. 22, 3046-3058
    • (2008) FASEB J. , vol.22 , pp. 3046-3058
    • Calvo, A.C.1    Pey, A.L.2    Ying, M.3    Loer, C.M.4    Martinez, A.5
  • 50
    • 44049105102 scopus 로고    scopus 로고
    • The Caenorhabditis elegans K10C2.4 gene encodes a member of the fumarylacetoacetate hydrolase family: A Caenorhabditis elegans model of type I tyrosinemia
    • Fisher, A. L., Page, K. E., Lithgow, G. J. and Nash, L. (2008) The Caenorhabditis elegans K10C2.4 gene encodes a member of the fumarylacetoacetate hydrolase family: a Caenorhabditis elegans model of type I tyrosinemia. J. Biol. Chem. 283, 9127-9135
    • (2008) J. Biol. Chem. , vol.283 , pp. 9127-9135
    • Fisher, A.L.1    Page, K.E.2    Lithgow, G.J.3    Nash, L.4
  • 52
    • 33745223646 scopus 로고    scopus 로고
    • Finding function innovel targets: C. elegans as a model organism
    • Kaletta, T. and Hengartner, M. O. (2006) Finding function innovel targets: C. elegans as a model organism. Nat. Rev. 5, 387-398
    • (2006) Nat. Rev. , vol.5 , pp. 387-398
    • Kaletta, T.1    Hengartner, M.O.2
  • 54
    • 0042250902 scopus 로고    scopus 로고
    • Cystathionine-β-synthase and its deficiency
    • Carmel, R. and Jacobsen, D. W., eds, . Cambridge University Press, Cambridge
    • Kraus, J. P. and Kožich, V. (2001) Cystathionine-β-synthase and its deficiency. In Homocysteine in Health and Disease (Carmel, R. and Jacobsen, D. W., eds), pp. 223-243, Cambridge University Press, Cambridge
    • (2001) Homocysteine in Health and Disease , pp. 223-243
    • Kraus, J.P.1    Kožich, V.2
  • 56
    • 70349411509 scopus 로고    scopus 로고
    • Defective responses tooxidative stress in protein l-isoaspartyl repair-deficient Caenorhabditis elegans
    • Khare, S., Gomez, T., Linster, C. L. and Clarke, S. G. (2009) Defective responses tooxidative stress in protein l-isoaspartyl repair-deficient Caenorhabditis elegans. Mech. Ageing Dev. 130, 670-680
    • (2009) Mech. Ageing Dev. , vol.130 , pp. 670-680
    • Khare, S.1    Gomez, T.2    Linster, C.L.3    Clarke, S.G.4
  • 57
    • 77957223318 scopus 로고    scopus 로고
    • A novel transgenic mouse model of CBS-deficient homocystinuria does not incur hepatic steatosis or fibrosis and exhibits a hypercoagulative phenotype that is ameliorated by betaine treatment
    • Maclean, K. N., Sikora, J., Kozich, V., Jiang, H., Greiner, L. S., Kraus, E., Krijt, J., Overdier, K. H., Collard, R., Brodsky, G. L. et al. (2010) A novel transgenic mouse model of CBS-deficient homocystinuria does not incur hepatic steatosis or fibrosis and exhibits a hypercoagulative phenotype that is ameliorated by betaine treatment. Mol. Genet. Metab. 101, 153-162
    • (2010) Mol. Genet. Metab. , vol.101 , pp. 153-162
    • Maclean, K.N.1    Sikora, J.2    Kozich, V.3    Jiang, H.4    Greiner, L.S.5    Kraus, E.6    Krijt, J.7    Overdier, K.H.8    Collard, R.9    Brodsky, G.L.10
  • 58
    • 69249100078 scopus 로고    scopus 로고
    • Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions
    • Singh, S., Padovani, D., Leslie, R. A., Chiku, T. and Banerjee, R. (2009) Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions. J. Biol. Chem. 284, 22457-22466
    • (2009) J. Biol. Chem. , vol.284 , pp. 22457-22466
    • Singh, S.1    Padovani, D.2    Leslie, R.A.3    Chiku, T.4    Banerjee, R.5
  • 59
    • 80053303036 scopus 로고    scopus 로고
    • The response of Caenorhabditis elegans to hydrogen sulfide and hydrogen cyanide
    • Budde, M. W. and Roth, M. B. (2011) The response of Caenorhabditis elegans to hydrogen sulfide and hydrogen cyanide. Genetics 189, 521-532
    • (2011) Genetics , vol.189 , pp. 521-532
    • Budde, M.W.1    Roth, M.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.