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dc.contributor.author김화영ko
dc.contributor.author김용준[김용준]ko
dc.contributor.author곽근희[곽근희]ko
dc.contributor.author이추희ko
dc.date.accessioned2015-12-17T01:12:06Z-
dc.date.available2015-12-17T01:12:06Z-
dc.date.created2015-11-13-
dc.date.issued201110-
dc.identifier.citationBMB REPORTS, v.44, no.10, pp.669 - 673-
dc.identifier.issn1976-6696-
dc.identifier.urihttp://hdl.handle.net/YU.REPOSITORY/24435-
dc.identifier.urihttp://dx.doi.org/10.5483/BMBRep.2011.44.10.669-
dc.description.abstractHuman methionine sulfoxide reductase B3A (hMsrB3A) is an endoplasmic reticulum (ER) reductase that catalyzes the stereospecific reduction of methionine-R-sulfoxide to methionine in proteins. In this work, we identified an antimicrobial peptide from hMsrB3A protein. The N-terminal ER-targeting signal peptide (amino acids 1-31) conferred an antimicrobial effect in Escherichia coli cells. Sequence and structural analyses showed that the overall positively charged ER signal peptide had an Arg- and Pro-rich region and a potential hydrophobic a-helical segment that contains 4 cysteine residues. The potential a-helical region was essential for the antimicrobial activity within E. coli cells. A synthetic peptide, comprised of 2-26 amino acids of the signal peptide, was effective at killing Gram-negative E. colt, Klebsiella pneumoniae, and Salmonella paratyphi, but had no bactericidal activity against Gram-positive Staphylococcus aureus. [BMB reports 2011; 44(10): 669-673]-
dc.language영어-
dc.publisherKOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY-
dc.subjectMECHANISM-
dc.subjectMAMMALS-
dc.subjectLIVER-
dc.titleIdentification of an antimicrobial peptide from human methionine sulfoxide reductase B3-
dc.typeArticle-
dc.identifier.wosid000296673100008-
dc.identifier.scopusid2-s2.0-84863244017-
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의과대학 > 생화학.분자생물학교실 > Articles
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