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Volumn 184, Issue 11, 2002, Pages 2931-2939

An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; FERRITIN; GENE PRODUCT; HEME; HYDROXYL RADICAL; IRON; IRON BINDING PROTEIN; PEROXIDASE; PROTEIN DPR; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; ZINC;

EID: 0036091613     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.11.2931-2939.2002     Document Type: Article
Times cited : (100)

References (56)
  • 8
    • 0028861959 scopus 로고
    • Bacillus subtilis MrgA is a Dps (PexB) homologue: Evidence for metalloregulation of an oxidative-stress gene
    • (1995) Mol. Microbiol. , vol.18 , pp. 295-300
    • Chen, L.1    Helmann, J.D.2
  • 9
    • 0021809734 scopus 로고
    • A specific iron stain for iron-binding proteins in polyacrylamide gels: Application to transferrin and lactoferrin
    • (1985) Anal. Biochem. , vol.148 , pp. 498-502
    • Chung, M.C.1
  • 13
    • 0029785171 scopus 로고    scopus 로고
    • Insertional inactivation of Streptococcus pyogenes sod suggests that prtF is regulated in response to a superoxide signal
    • (1996) J. Bacteriol. , vol.178 , pp. 4688-4695
    • Gibson, C.M.1    Caparon, M.G.2
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0026636709 scopus 로고
    • Nucleotide sequence of Streptococcus mutans superoxide dismutase gene and isolation of insertion mutants
    • (1992) J. Bacteriol. , vol.174 , pp. 4928-4934
    • Nakayama, K.1
  • 36
    • 0029082683 scopus 로고
    • The DpsA protein of Synechococcus sp. strain PCC7942 is a DNA-binding hemoprotein. Linkage of the Dps and bacterioferritin protein families
    • (1995) J. Biol. Chem. , vol.270 , pp. 22478-22482
    • Pena, M.M.1    Bullerjahn, G.S.2
  • 38
    • 0034612366 scopus 로고    scopus 로고
    • AhpF can be dissected into two functional units: Tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC
    • (2000) Biochemistry , vol.39 , pp. 6602-6615
    • Poole, L.B.1    Godzik, A.2    Nayeem, A.3    Schmitt, J.D.4
  • 41
    • 0026059349 scopus 로고
    • Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. Structural relationship with the flavoprotein disulfide reductases
    • (1991) J. Mol. Biol. , vol.221 , pp. 857-871
    • Ross, R.P.1    Claiborne, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.