Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis. - Wikidata - awgldk - TriplyDB

Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis.

Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis.

http://www.wikidata.org/entity/Q33994946

about

Entry of Porphyromonas gingivalis outer membrane vesicles into epithelial cells causes cellular functional impairment Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization Outer membrane lipoprotein biogenesis: Lol is not the end.Contact- and Protein Transfer-Dependent Stimulation of Assembly of the Gliding Motility Machinery in Myxococcus xanthus.Identification of an iron-regulated, hemin-binding outer membrane protein in Sinorhizobium meliloti A two-component system regulates hemin acquisition in Porphyromonas gingivalis Porphyromonas gingivalis ferrous iron transporter FeoB1 influences sensitivity to oxidative stress.Metal uptake in host-pathogen interactions: role of iron in Porphyromonas gingivalis interactions with host organisms The enigma of cobalamin (Vitamin B12) biosynthesis in Porphyromonas gingivalis. Identification and characterization of a functional corrin pathway.Binding specificity of the Porphyromonas gingivalis heme and hemoglobin receptor HmuR, gingipain K, and gingipain R1 for heme, porphyrins, and metalloporphyrins Degradation of host heme proteins by lysine- and arginine-specific cysteine proteinases (gingipains) of Porphyromonas gingivalis.Determination of hemin-binding characteristics of proteins by a combinatorial peptide library approach.BhuR, a virulence-associated outer membrane protein of Bordetella avium, is required for the acquisition of iron from heme and hemoproteins.Identification of amino acid residues involved in heme binding and hemoprotein utilization in the Porphyromonas gingivalis heme receptor HmuR.Characterization of a hemophore-like protein from Porphyromonas gingivalis.Porphyrin-mediated cell surface heme capture from hemoglobin by Porphyromonas gingivalis.Comparative genome analysis of Prevotella intermedia strain isolated from infected root canal reveals features related to pathogenicity and adaptation.Antigens of bacteria associated with periodontitis.Lactoferrin and oral diseases: current status and perspective in periodontitis.Iron and heme utilization in Porphyromonas gingivalis.Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface The role of heme binding by DNA-protective protein from starved cells (Dps) in the Tolerance of Porphyromonas gingivalis to heme toxicity.Humoral responses to Porphyromonas gingivalis gingipain adhesin domains in subjects with chronic periodontitis.The nucleoid-associated protein HUβ affects global gene expression in Porphyromonas gingivalis Response of Porphyromonas gingivalis to heme limitation in continuous culture.Quantitative proteomics of intracellular Porphyromonas gingivalis Role and regulation of heme iron acquisition in gram-negative pathogens.Identification of a hemin utilization protein of Moraxella catarrhalis (HumA).Outer-membrane vesicles from Gram-negative bacteria: biogenesis and functions.Feasibility and therapeutic strategies of vaccines against Porphyromonas gingivalis.Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond Spheres of influence: Porphyromonas gingivalis outer membrane vesicles.Heme acquisition mechanisms of Porphyromonas gingivalis - strategies used in a polymicrobial community in a heme-limited host environment.Effects of non-iron metalloporphyrins on growth and gene expression of Porphyromonas gingivalis.VimA-dependent modulation of the secretome in Porphyromonas gingivalis.LuxS involvement in the regulation of genes coding for hemin and iron acquisition systems in Porphyromonas gingivalis.Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50.Hemin binding by Porphyromonas gingivalis strains is dependent on the presence of A-LPS.The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli.Hemoglobin hydrolysis and heme acquisition by Porphyromonas gingivalis.

P2860

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P2860

Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis.

http://www.wikidata.org/entity/Q33994946

description

2000 nî lūn-bûn

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2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2000 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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Characterization of a novel ou ...... n of Porphyromonas gingivalis.

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Characterization of a novel ou ...... n of Porphyromonas gingivalis.

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type

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Characterization of a novel ou ...... n of Porphyromonas gingivalis.

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Characterization of a novel ou ...... n of Porphyromonas gingivalis.

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Characterization of a novel ou ...... n of Porphyromonas gingivalis.

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Characterization of a novel ou ...... n of Porphyromonas gingivalis.

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Characterization of a novel ou ...... n of Porphyromonas gingivalis.

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P2860

DNA sequencing with chain-terminating inhibitors

Transcription termination at intrinsic terminators: the role of the RNA hairpin

Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria

Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis

Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis

WHAT IF: a molecular modeling and drug design program

Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli

The PROSITE database, its status in 1999

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6456-6462

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Porphyromonas gingivalis

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