Short communicationIsolation and characterization of a hemin-binding cell envelope protein fromPorphyromonas gingivalis
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Cited by (22)
Four new phenylpropanoid glycosides from Clausena dunniana var. robustaand their antiinflammatory activities
2017, Phytochemistry LettersCitation Excerpt :Furthermore, fourteen previously reported compounds were also obtained. Their structures were identified by the comparison of their physical and NMR spectral data with literature values and were assigned as β-D-glucopyranoside, phenylmethyl (5) (Shu et al., 2016), 3-(4E-d-glucopyranosyloxy-3-methoxy)-phenyl-2E-prophenol (6) (Cho et al., 2011), methylsalicylate-2- O-β-d-glucopyranoside (7) (Matsumoto et al., 2017), cucumegastigmane I (8) (Hien et al., 2015), cucumegastigmane II (9) (Samy et al., 2017), 2′-deoxy-adenosine (10) (Gao et al., 2017), adenosine (11) (Tan et al., 2017), (S)-4-hydroxy-4-[(1E,3R)-3-hydroxy-1-buten-1-yl]-3,5,5-trimethyl-2-cyclohexen-1-one (12) (Liu et al., 2017), (7S, 8R)-3,5-dimethoxy-7,8-dihydroxy-phenylpropane (13) (Husain et al., 2011), octadecanoic acid (14) (Rezanka et al., 2017), 1,2-benzenedicarboxylic acid, 1,2-bis(2-methylpropyl) ester (15) (Eseyin et al., 2017), 3-buten-2-one,4-[(1R,2R,4S)-2-(β-D-glucopyranosyloxy)-4-hydroxy-2,6,6-trimethylcyclohexylidene]-3-methyl-,(3R)-(9CI) (16) (Benmerache et al., 2016), 2,4,5-trimethoxybenzaldehyde (17) (Kim et al., 1996), and 2-cyclohexen-1-one,4-[3-(β-D-glucopyranosyloxy)-1-propenyl]-4-hydroxy-3,5,5-trimethyl-, [S-(E)]-(9CI) (18) (Shang et al., 2017). The potential NF-κB inhibitory activity of the isolated compounds were evaluated by using TNF-α stimulated HeLa cells stably transfected with a NF-κB-driven luciferase reporter with parthenolide as positive control.
SigCH, an extracytoplasmic function sigma factor of Porphyromonas gingivalis regulates the expression of cdhR and hmuYR
2017, AnaerobeCitation Excerpt :In Gram-negative bacteria, TonB-dependent outer membrane receptors are implicated in iron acquisition [28]. Several putative TonB-dependent receptors were identified in P. gingivalis, including HtrE [29], IhtA [26,30,31], HmuR [32,33]. Furthermore, CdhR is a transcriptional regulator of hmu genes [34].
Heme environment in HmuY, the heme-binding protein of Porphyromonas gingivalis
2009, Biochemical and Biophysical Research CommunicationsCitation Excerpt :An identical structure of this operon was shown in P. gingivalis W50, W83, and 381 strains [6,7]. HmuY is a membrane-associated putative lipoprotein identified in P. gingivalis 381, W50, W83, and ATCC 33277 strains [6–9], and in Bacteroides fragilis and B. thetaiotaomicron[6]. We reported that HmuY bound heme in vitro and that its expression was regulated by iron [6].
Purification and initial characterization of a novel Porphyromonas gingivalis HmuY protein expressed in Escherichia coli and insect cells
2006, Protein Expression and PurificationIron and heme utilization in Porphyromonas gingivalis
2005, FEMS Microbiology ReviewsA 35-kDa co-aggregation factor is a hemin binding protein in Porphyromonas gingivalis
2003, Biochemical and Biophysical Research Communications
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