[go: up one dir, main page]

Andrews et al., 2012 - Google Patents

Control of iron metabolism in bacteria

Andrews et al., 2012

View PDF
Document ID
13040228786093559505
Author
Andrews S
Norton I
Salunkhe A
Goodluck H
Aly W
Mourad-Agha H
Cornelis P
Publication year
Publication venue
Metallomics and the Cell

External Links

Snippet

Bacteria depend upon iron as a vital cofactor that enables a wide range of key metabolic activities. Bacteria must therefore ensure a balanced supply of this essential metal. To do so, they invest considerable resourse into its acquisition and employ elaborate control …
Continue reading at ndl.ethernet.edu.et (PDF) (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
    • C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
    • C07K14/245—Escherichia (G)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
    • C07K14/305—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F)
    • C07K14/31—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
    • C07K14/28—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Vibrionaceae (F)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/79—Transferrins, e.g. lactoferrins, ovotransferrins

Similar Documents

Publication Publication Date Title
Andrews et al. Control of iron metabolism in bacteria
Giachino et al. Copper tolerance in bacteria requires the activation of multiple accessory pathways
Brophy et al. Manganese and microbial pathogenesis: sequestration by the Mammalian immune system and utilization by microorganisms
Wątły et al. Zinc homeostasis at the bacteria/host interface—from coordination chemistry to nutritional immunity
Rudolph et al. Beyond the Fur paradigm: iron-controlled gene expression in rhizobia
Caza et al. Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans
Rensing et al. Escherichia coli mechanisms of copper homeostasis in a changing environment
Tong et al. Bacterial heme-transport proteins and their heme-coordination modes
Blencowe et al. Zn (II) metabolism in prokaryotes
Zeth Dps biomineralizing proteins: multifunctional architects of nature
Lechowicz et al. An update on the transport and metabolism of iron in Listeria monocytogenes: the role of proteins involved in pathogenicity
Li et al. Iron acquisition strategies of Vibrio anguillarum
Sheldon et al. The iron-regulated staphylococcal lipoproteins
Kim et al. Chaperone-mediated copper handling in the periplasm
Ge et al. Iron trafficking system in Helicobacter pylori
Danielli et al. Regulatory circuits in Helicobacter pylori: network motifs and regulators involved in metal-dependent responses
Kaushik et al. Ferric uptake regulator (FUR) protein: properties and implications in cyanobacteria
Liu et al. Recent advances in the siderophore biology of Shewanella
Chakraborty et al. Iron Uptake in Bacteria with Emphasis on E. coli and Pseudomonas
Dent et al. Axial heme coordination by the tyr-his motif in the extracellular hemophore hasap is critical for the release of heme to the HasR receptor of Pseudomonas aeruginosa
Flannagan et al. In vivo growth of Staphylococcus lugdunensis is facilitated by the concerted function of heme and non-heme iron acquisition mechanisms
Grinter et al. Beware of proteins bearing gifts: protein antibiotics that use iron as a Trojan horse
Obando S et al. A cluster of five genes essential for the utilization of dihydroxamate xenosiderophores in Synechocystis sp. PCC 6803
Obisesan et al. Bacterial responses to iron withholding by calprotectin
Normant et al. How the presence of hemin affects the expression of the different iron uptake pathways in Pseudomonas aeruginosa Cells