메뉴 건너뛰기




Volumn 60, Issue 1, 2006, Pages 209-218

Oxidative stress promotes degradation of the Irr protein to regulate haem biosynthesis in Bradyrhizobium japonicum

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CATALASE; FERROUS ION; HEME; HYDROGEN PEROXIDE; IRON; IRR PROTEIN; MUTANT PROTEIN; OXYGEN; PEROXIDASE; PORPHOBILINOGEN SYNTHASE; REACTIVE OXYGEN METABOLITE; REDUCING AGENT; UNCLASSIFIED DRUG;

EID: 33644838945     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05087.x     Document Type: Article
Times cited : (51)

References (49)
  • 1
    • 0021322523 scopus 로고
    • Hemin-mediated oxidative degradation of proteins
    • Aft RL. Mueller GC. 1984 Hemin-mediated oxidative degradation of proteins J Biol Chem 259 301 305
    • (1984) J Biol Chem , vol.259 , pp. 301-305
    • Aft, R.L.1    Mueller, G.C.2
  • 2
    • 0028200484 scopus 로고
    • The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase
    • Altuvia S. Almiron M. Huisman G. Kolter R. Storz G. 1994 The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase Mol Microbiol 13 265 272
    • (1994) Mol Microbiol , vol.13 , pp. 265-272
    • Altuvia, S.1    Almiron, M.2    Huisman, G.3    Kolter, R.4    Storz, G.5
  • 3
    • 0031459386 scopus 로고    scopus 로고
    • A small, stable RNA induced by oxidative stress: Role as a pleiotropic regulator and antimutator
    • Altuvia S. Weinstein-Fischer D. Zhang A. Postow L. Storz G. 1997 A small, stable RNA induced by oxidative stress: role as a pleiotropic regulator and antimutator Cell 90 43 53
    • (1997) Cell , vol.90 , pp. 43-53
    • Altuvia, S.1    Weinstein-Fischer, D.2    Zhang, A.3    Postow, L.4    Storz, G.5
  • 4
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease and oxidative stress
    • Berlett BS. Stadtman ER. 1997 Protein oxidation in aging, disease and oxidative stress J Biol Chem 272 20313 20316
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 5
    • 0348111398 scopus 로고    scopus 로고
    • The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2
    • Bourdon E. Kang DK. Ghosh MC. Drake SK. Wey J. Levine RL. Rouault TA. 2003 The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2 Blood Cells Mol Dis 31 247 255
    • (2003) Blood Cells Mol Dis , vol.31 , pp. 247-255
    • Bourdon, E.1    Kang, D.K.2    Ghosh, M.C.3    Drake, S.K.4    Wey, J.5    Levine, R.L.6    Rouault, T.A.7
  • 6
    • 0029121431 scopus 로고
    • A mutant Bradyrhizobium japonicumδ-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules
    • Chauhan S. O'Brian MR. 1995 A mutant Bradyrhizobium japonicumδ- aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules J Biol Chem 270 19823 19827
    • (1995) J Biol Chem , vol.270 , pp. 19823-19827
    • Chauhan, S.1    O'Brian, M.R.2
  • 7
    • 0031007110 scopus 로고    scopus 로고
    • Transcriptional regulation of δ-aminolevulinic acid dehydratase synthesis by oxygen in Bradyrhizobium japonicum and evidence for developmental control of the hemB gene
    • Chauhan S. O'Brian MR. 1997 Transcriptional regulation of δ-aminolevulinic acid dehydratase synthesis by oxygen in Bradyrhizobium japonicum and evidence for developmental control of the hemB gene J Bacteriol 179 3706 3710
    • (1997) J Bacteriol , vol.179 , pp. 3706-3710
    • Chauhan, S.1    O'Brian, M.R.2
  • 8
    • 0030885964 scopus 로고    scopus 로고
    • Metals control activity and expression of the heme biosynthesis enzyme δ-aminolevulinic acid dehydratase in Bradyrhizobium japonicum
    • Chauhan S. Titus DE. O'Brian MR. 1997 Metals control activity and expression of the heme biosynthesis enzyme δ-aminolevulinic acid dehydratase in Bradyrhizobium japonicum J Bacteriol 179 5516 5520
    • (1997) J Bacteriol , vol.179 , pp. 5516-5520
    • Chauhan, S.1    Titus, D.E.2    O'Brian, M.R.3
  • 9
    • 0029152774 scopus 로고
    • Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions
    • Chen L. Keramati L. Helmann JD. 1995 Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions Proc Natl Acad Sci USA 92 8190 8194
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8190-8194
    • Chen, L.1    Keramati, L.2    Helmann, J.D.3
  • 10
    • 0342333739 scopus 로고
    • OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins
    • Christman MF. Storz G. Ames BN. 1989 OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins Proc Natl Acad Sci USA 86 3484 3488
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3484-3488
    • Christman, M.F.1    Storz, G.2    Ames, B.N.3
  • 11
    • 0024443449 scopus 로고
    • Derivatization of gamma-glutamyl semialdehyde residues in oxidized proteins by fluoresceinamine
    • Climent I. Tsai L. Levine RL. 1989 Derivatization of gamma-glutamyl semialdehyde residues in oxidized proteins by fluoresceinamine Anal Biochem 182 226 232
    • (1989) Anal Biochem , vol.182 , pp. 226-232
    • Climent, I.1    Tsai, L.2    Levine, R.L.3
  • 13
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. 1995 Superoxide radical and superoxide dismutases Annu Rev Biochem 64 97 112
    • (1995) Annu Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 14
    • 0026071003 scopus 로고
    • Aerobic growth and respiration of a δ-aminolevulinic acid synthase (hemA) mutant of Bradyrhizobium japonicum
    • Frustaci JM. Sangwan I. O'Brian MR. 1991 Aerobic growth and respiration of a δ-aminolevulinic acid synthase (hemA) mutant of Bradyrhizobium japonicum J Bacteriol 173 1145 1150
    • (1991) J Bacteriol , vol.173 , pp. 1145-1150
    • Frustaci, J.M.1    Sangwan, I.2    O'Brian, M.R.3
  • 15
    • 0032582814 scopus 로고    scopus 로고
    • Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation
    • Gitan RS. Luo H. Rodgers J. Broderius M. Eide D. 1998 Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation J Biol Chem 273 28617 28624
    • (1998) J Biol Chem , vol.273 , pp. 28617-28624
    • Gitan, R.S.1    Luo, H.2    Rodgers, J.3    Broderius, M.4    Eide, D.5
  • 16
    • 0032524657 scopus 로고    scopus 로고
    • Involvement of heme in the degradation of iron-regulatory protein 2
    • Goessling LS. Mascotti DP. Thach RE. 1998 Involvement of heme in the degradation of iron-regulatory protein 2 J Biol Chem 273 12555 12557
    • (1998) J Biol Chem , vol.273 , pp. 12555-12557
    • Goessling, L.S.1    Mascotti, D.P.2    Thach, R.E.3
  • 17
    • 0022516509 scopus 로고
    • Bacterial δ-aminolevulinic acid synthase is not essential for leghemoglobin formation in the soybean/Bradyrhizobium japonicum symbiosis
    • Guerinot ML. Chelm BK. 1986 Bacterial δ-aminolevulinic acid synthase is not essential for leghemoglobin formation in the soybean/Bradyrhizobium japonicum symbiosis Proc Natl Acad Sci USA 83 1837 1841
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1837-1841
    • Guerinot, M.L.1    Chelm, B.K.2
  • 18
    • 0032555562 scopus 로고    scopus 로고
    • The bacterial irr protein is required for coordination of heme biosynthesis with iron availability
    • Hamza I. Chauhan S. Hassett R. O'Brian MR. 1998 The bacterial irr protein is required for coordination of heme biosynthesis with iron availability J Biol Chem 273 21669 21674
    • (1998) J Biol Chem , vol.273 , pp. 21669-21674
    • Hamza, I.1    Chauhan, S.2    Hassett, R.3    O'Brian, M.R.4
  • 19
    • 0034062506 scopus 로고    scopus 로고
    • Fur-independent regulation of iron metabolism by Irr in Bradyrhizobium japonicum
    • Hamza I. Qi Z. King ND. O'Brian MR. 2000 Fur-independent regulation of iron metabolism by Irr in Bradyrhizobium japonicum Microbiology 146 669 676
    • (2000) Microbiology , vol.146 , pp. 669-676
    • Hamza, I.1    Qi, Z.2    King, N.D.3    O'Brian, M.R.4
  • 20
    • 0035723780 scopus 로고    scopus 로고
    • Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA
    • Herbig AF. Helmann JD. 2001 Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA Mol Microbiol 41 849 859
    • (2001) Mol Microbiol , vol.41 , pp. 849-859
    • Herbig, A.F.1    Helmann, J.D.2
  • 21
    • 0029830431 scopus 로고    scopus 로고
    • Cloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase
    • Herouart D. Sigaud S. Moreau S. Frendo P. Touati D. Puppo A. 1996 Cloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase J Bacteriol 178 6802 6809
    • (1996) J Bacteriol , vol.178 , pp. 6802-6809
    • Herouart, D.1    Sigaud, S.2    Moreau, S.3    Frendo, P.4    Touati, D.5    Puppo, A.6
  • 22
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay JA. 2003 Pathways of oxidative damage Annu Rev Microbiol 57 395 418
    • (2003) Annu Rev Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 23
    • 0032574765 scopus 로고    scopus 로고
    • Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: Implications for degradation of oxidized proteins
    • Iwai K. Drake SK. Wehr NB. Weissman AM. LaVaute T. Minato N. et al. 1998 Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: implications for degradation of oxidized proteins Proc Natl Acad Sci USA 95 4924 4928
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4924-4928
    • Iwai, K.1    Drake, S.K.2    Wehr, N.B.3    Weissman, A.M.4    Lavaute, T.5    Minato, N.6
  • 24
    • 0037370853 scopus 로고    scopus 로고
    • Expression of the bacterial catalase genes during Sinorhizobium meliloti-Medicago sativa symbiosis and their crucial role during the infection process
    • Jamet A. Sigaud S. Van de Sype G. Puppo A. Herouart D. 2003 Expression of the bacterial catalase genes during Sinorhizobium meliloti-Medicago sativa symbiosis and their crucial role during the infection process Mol Plant Microbe Interact 16 217 225
    • (2003) Mol Plant Microbe Interact , vol.16 , pp. 217-225
    • Jamet, A.1    Sigaud, S.2    Van De Sype, G.3    Puppo, A.4    Herouart, D.5
  • 26
    • 0035930564 scopus 로고    scopus 로고
    • Copper-induced proteolysis of the CopZ copper chaperone of Enterococcus hirae
    • Lu ZH. Solioz M. 2001 Copper-induced proteolysis of the CopZ copper chaperone of Enterococcus hirae J Biol Chem 276 47822 47827
    • (2001) J Biol Chem , vol.276 , pp. 47822-47827
    • Lu, Z.H.1    Solioz, M.2
  • 27
    • 0036047508 scopus 로고    scopus 로고
    • Regulation of inducible peroxide stress responses
    • Mongkolsuk S. Helmann JD. 2002 Regulation of inducible peroxide stress responses Mol Microbiol 45 9 15
    • (2002) Mol Microbiol , vol.45 , pp. 9-15
    • Mongkolsuk, S.1    Helmann, J.D.2
  • 28
    • 0031899593 scopus 로고    scopus 로고
    • Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli
    • Mongkolsuk S. Praituan W. Loprasert S. Fuangthong M. Chamnongpol S. 1998 Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli J Bacteriol 180 2636 2643
    • (1998) J Bacteriol , vol.180 , pp. 2636-2643
    • Mongkolsuk, S.1    Praituan, W.2    Loprasert, S.3    Fuangthong, M.4    Chamnongpol, S.5
  • 29
    • 0029994433 scopus 로고    scopus 로고
    • Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis
    • Ooi CE. Rabinovich E. Dancis A. Bonifacino JS. Klausner RD. 1996 Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis EMBO J 15 3515 3523
    • (1996) EMBO J , vol.15 , pp. 3515-3523
    • Ooi, C.E.1    Rabinovich, E.2    Dancis, A.3    Bonifacino, J.S.4    Klausner, R.D.5
  • 30
    • 0036667415 scopus 로고    scopus 로고
    • A whole genome view of prokaryotic heme biosynthesis
    • Panek H. O'Brian MR. 2002 A whole genome view of prokaryotic heme biosynthesis Microbiology 148 2273 2282
    • (2002) Microbiology , vol.148 , pp. 2273-2282
    • Panek, H.1    O'Brian, M.R.2
  • 31
    • 9244247620 scopus 로고    scopus 로고
    • KatG is the primary detoxifier of hydrogen peroxide produced by aerobic metabolism in Bradyrhizobium japonicum
    • Panek HR. O'Brian MR. 2004 KatG is the primary detoxifier of hydrogen peroxide produced by aerobic metabolism in Bradyrhizobium japonicum J Bacteriol 186 7874 7880
    • (2004) J Bacteriol , vol.186 , pp. 7874-7880
    • Panek, H.R.1    O'Brian, M.R.2
  • 32
    • 0038957365 scopus 로고    scopus 로고
    • Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress
    • Prieto-Alamo MJ. Jurado J. Gallardo-Madueno R. Monje-Casas F. Holmgren A. Pueyo C. 2000 Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress J Biol Chem 275 13398 13405
    • (2000) J Biol Chem , vol.275 , pp. 13398-13405
    • Prieto-Alamo, M.J.1    Jurado, J.2    Gallardo-Madueno, R.3    Monje-Casas, F.4    Holmgren, A.5    Pueyo, C.6
  • 33
    • 0036161801 scopus 로고    scopus 로고
    • Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis
    • Qi Z. O'Brian MR. 2002 Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis Mol Cell 9 155 162
    • (2002) Mol Cell , vol.9 , pp. 155-162
    • Qi, Z.1    O'Brian, M.R.2
  • 34
    • 0033539642 scopus 로고    scopus 로고
    • Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein
    • Qi Z. Hamza I. O'Brian MR. 1999 Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein Proc Natl Acad Sci USA 96 13056 13061
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13056-13061
    • Qi, Z.1    Hamza, I.2    O'Brian, M.R.3
  • 35
    • 0034723199 scopus 로고    scopus 로고
    • Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli
    • Ritz D. Patel H. Doan B. Zheng M. Aslund F. Storz G. Beckwith J. 2000 Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli J Biol Chem 275 2505 2512
    • (2000) J Biol Chem , vol.275 , pp. 2505-2512
    • Ritz, D.1    Patel, H.2    Doan, B.3    Zheng, M.4    Aslund, F.5    Storz, G.6    Beckwith, J.7
  • 36
    • 0017170804 scopus 로고
    • Induction of globin mRNA accumulation by hemin in cultured erythroleukemic cells
    • Ross J. Sautner D. 1976 Induction of globin mRNA accumulation by hemin in cultured erythroleukemic cells Cell 8 513 520
    • (1976) Cell , vol.8 , pp. 513-520
    • Ross, J.1    Sautner, D.2
  • 37
    • 0035212036 scopus 로고    scopus 로고
    • Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli
    • Seaver LC. Imlay JA. 2001 Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli J Bacteriol 183 7182 7189
    • (2001) J Bacteriol , vol.183 , pp. 7182-7189
    • Seaver, L.C.1    Imlay, J.A.2
  • 38
    • 0032929263 scopus 로고    scopus 로고
    • Differential regulation of two divergent Sinorhizobium meliloti genes for HPII-like catalases during free-living growth and protective role of both catalases during symbiosis
    • Sigaud S. Becquet V. Frendo P. Puppo A. Herouart D. 1999 Differential regulation of two divergent Sinorhizobium meliloti genes for HPII-like catalases during free-living growth and protective role of both catalases during symbiosis J Bacteriol 181 2634 2639
    • (1999) J Bacteriol , vol.181 , pp. 2634-2639
    • Sigaud, S.1    Becquet, V.2    Frendo, P.3    Puppo, A.4    Herouart, D.5
  • 39
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman ER. 1993 Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions Annu Rev Biochem 62 797 821
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 40
    • 0024448362 scopus 로고
    • Molecular cloning and nucleotide sequencing of oxyR, the positive regulatory gene of a regulon for an adaptive response to oxidative stress in Escherichia coli: Homologies between OxyR protein and a family of bacterial activator proteins
    • Tao K. Makino K. Yonei S. Nakata A. Shinagawa H. 1989 Molecular cloning and nucleotide sequencing of oxyR, the positive regulatory gene of a regulon for an adaptive response to oxidative stress in Escherichia coli: homologies between OxyR protein and a family of bacterial activator proteins Mol Gen Genet 218 371 376
    • (1989) Mol Gen Genet , vol.218 , pp. 371-376
    • Tao, K.1    Makino, K.2    Yonei, S.3    Nakata, A.4    Shinagawa, H.5
  • 41
    • 0024785396 scopus 로고
    • Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress
    • Tartaglia LA. Storz G. Ames BN. 1989 Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress J Mol Biol 210 709 719
    • (1989) J Mol Biol , vol.210 , pp. 709-719
    • Tartaglia, L.A.1    Storz, G.2    Ames, B.N.3
  • 42
    • 0033985228 scopus 로고    scopus 로고
    • Iron and oxidative stress in bacteria
    • Touati D. 2000 Iron and oxidative stress in bacteria Arch Biochem Biophys 373 1 6
    • (2000) Arch Biochem Biophys , vol.373 , pp. 1-6
    • Touati, D.1
  • 43
    • 0037854380 scopus 로고    scopus 로고
    • Only one catalase, katG, is detectable in Rhizobium etli, and is encoded along with the regulator OxyR on a plasmid replicon
    • Vargas Mdel C. Encarnacion S. Davalos A. Reyes-Perez A. Mora Y. Garcia-de los Santos A. et al. 2003 Only one catalase, katG, is detectable in Rhizobium etli, and is encoded along with the regulator OxyR on a plasmid replicon Microbiology 149 1165 1176
    • (2003) Microbiology , vol.149 , pp. 1165-1176
    • Vargas Mdel, C.1    Encarnacion, S.2    Davalos, A.3    Reyes-Perez, A.4    Mora, Y.5    Garcia-De Los Santos, A.6
  • 45
    • 14844355242 scopus 로고    scopus 로고
    • Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein
    • Yang J. Ishimori K. O'Brian MR. 2005 Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein J Biol Chem 280 7671 7676
    • (2005) J Biol Chem , vol.280 , pp. 7671-7676
    • Yang, J.1    Ishimori, K.2    O'Brian, M.R.3
  • 46
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M. Aslund F. Storz G. 1998 Activation of the OxyR transcription factor by reversible disulfide bond formation Science 279 1718 1721
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 48
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng M. Wang X. Templeton LJ. Smulski DR. LaRossa RA. Storz G. 2001 DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide J Bacteriol 183 4562 4570
    • (2001) J Bacteriol , vol.183 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    Larossa, R.A.5    Storz, G.6
  • 49
    • 0031893254 scopus 로고    scopus 로고
    • Copper differentially regulates the activity and degradation of yeast Mac1 transcription factor
    • Zhu Z. Labbe S. Pena MM. Thiele DJ. 1998 Copper differentially regulates the activity and degradation of yeast Mac1 transcription factor J Biol Chem 273 1277 1280
    • (1998) J Biol Chem , vol.273 , pp. 1277-1280
    • Zhu, Z.1    Labbe, S.2    Pena, M.M.3    Thiele, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.