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1 that HrtR expressed as a fusion protein is a heme-binding protein.
2 We furthermore demonstrate that BdlA is a heme-binding protein.
3 rhythms in mammals, has been identified as a heme-binding protein.
4 haride was suppressed by hemopexin, a plasma heme-binding protein.
5 HemQ is a multimeric heme-binding protein.
6 -like proteins (gb|ADZ24001.1), is in fact a heme-binding protein.
7 nd was not detectable when the medium lacked heme-binding proteins.
8 he availability and avidity of extracellular heme-binding proteins.
9 ng cassette (ABC) transporter made by GAS as heme-binding proteins.
10 Pap31, a homolog of the Bartonella quintana heme-binding protein A (HbpA), defined the high-density
11 ctional heme transfer between a cell surface heme-binding protein and the lipoprotein of a heme-speci
12 . gingivalis for the extraction of heme from heme-binding proteins and for iron transport are poorly
13 cation to a range of other systems including heme-binding proteins and proteins to which a covalently
14 inimal amino acid sequence identity to these heme-binding proteins and the structure of Shp(180) reve
15 we showed that MF6p/FhHDM-1 is a transitory heme-binding protein as protein.heme complexes can be di
18 ass of proteins that includes esterases, the heme-binding protein ChaN, and an uncharacterized domain
20 rovide further evidence that the cytoplasmic heme-binding proteins, contrary to previous reports, are
22 -family proteins) are a widespread family of heme-binding proteins for which chemical and biological
24 ggest the possibility that these cytoplasmic heme-binding proteins have multiple functions that are t
31 derived from the amino-terminal cleavage of heme-binding protein, is a potent chemoattractant for hu
32 y, several Gram-negative pathogens secrete a heme binding protein known as HasA to scavenge heme from
33 a hepatica that belongs to a broad family of heme-binding proteins (MF6p/helminth defense molecules (
34 onal study of the first purified periplasmic heme-binding protein (PBP), ShuT from Shigella dysenteri
35 functional characterization of a cytoplasmic heme-binding protein PhuS from the opportunistic pathoge
37 al rearrangement of the C-terminal domain of heme binding protein (PhuS) is required for interaction
38 eletion of the gene encoding the cytoplasmic heme-binding protein, PhuS, homologs of which have been
39 id-lipid-associated protein-fibrillins, SOUL heme-binding proteins, phytyl ester synthases, beta-caro
41 ide, mRNA II is suppressed suggesting that a heme-binding protein (responsive to oxygen) may suppress
42 ally, this organism produces a hemolymphatic heme-binding protein (RHBP) that transports heme to peri
46 d in other pathogenic bacterial cell surface heme-binding proteins, suggesting that the mechanisms of
47 Cig1 exhibited the absorbance spectrum of a heme-binding protein upon heme titration, and Cig1 may t
48 which are found in all putative periplasmic heme-binding proteins, were subjected to UV-visible, res
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