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ProteomicsIdentification of a FimA protein in a crude lysate SDS-PAGE gel of a P. gingivalis heme-uptake mutant
Porphyromonas gingivalis is one of the main etiological agents responsible for initiating and progressing periodontal diseases in humans. P. gingivalis does not synthesize heme, and it uses host hemoproteins as a source of this molecule. The main heme uptake mechanism utilized by P. gingivalis is th...
ORGANISM(S): Porphyromonas gingivalis A7436 
2024-12-28 | PXD054703 | Pride
Pili Sds-page Gel band analysis Pilus Bottom-up Heme-uptake mutant Mse Hmur Lc-ms Major fimbrium Fima Hmuy Porphyromonas gingivalis 
TranscriptomicsPorphyromonas gingivalis 33277 wild-type vs Fur orthologue Har isogenic mutant ECR455
Porphyromonas gingivalis is a major pathogen associated with the microbial biofilm-mediated disease chronic periodontitis. P. gingivalis has an obligate requirement for iron and protoporphyrin IX which it satisfies by transporting heme and iron liberated from the human host. The level of cellular ir...
ORGANISM(S): Porphyromonas gingivalis ATCC 33277 
2015-04-01 | E-GEOD-37099 | biostudies-arrayexpress
UnknownDirect Heme Uptake by Phytoplankton-Associated Roseobacter Bacteria.
Not available
S-EPMC5225302 | biostudies-literature
UnknownThe PAS Domain-Containing Protein HeuR Regulates Heme Uptake in Campylobacter jejuni.
Not available
S-EPMC5111405 | biostudies-literature
TranscriptomicsRNAseq of Staphylococcus aureus wildtype and ppGpp0 mutant reveals rolen of alarmon (p)ppGpp confering tolerance to oxidative stress and antibiotics during the stationary phase in Staphylococcus aureus
RNAseq of coding RNA in Staphylococcus aureus wildtype and ppGpp0 mutant shows transcription of the Fe-storage ferritin (ftnA) and miniferritin (dps) was elevated in the ppGpp0 mutant, while Fur-regulated iron transporters for uptake of heme or siderophores were repressed, including the isdABCDEFG, ...
ORGANISM(S): Staphylococcus aureus subsp. aureus USA300 
2020-08-31 | E-MTAB-9368 | biostudies-arrayexpress
UnknownControl of hmu Heme Uptake Genes in Yersinia pseudotuberculosis in Response to Iron Sources.
Not available
S-EPMC5827684 | biostudies-literature
UnknownHeme Uptake in Lactobacillus sakei Evidenced by a New Energy Coupling Factor (ECF)-Like Transport System.
Not available
S-EPMC7480364 | biostudies-literature
ProteomicsFree rather than total iron content is critically linked to the Fur physiology in Shewanella oneidensis
Ferric uptake regulator (Fur) is a transcriptional regulator playing a central role in iron homeostasis of many bacteria and Fur inactivation commonly results in pleiotropic phenotypes. In Shewanella oneidensis, a representative of dissimilatory metal-reducing -proteobacteria capable of respiring a...
ORGANISM(S): Shewanella Oneidensis Mr-1 
2020-09-29 | PXD021732 |
TranscriptomicsTranscriptome analysis of wt and PerR mutant Group A streptococcus (GAS), strain 003Sm in THB medium, with and without hydrogen peroxide
Transcriptome analysis of of wt and PerR mutant Group A streptococcus strain 003Sm grown in the presence or absence of hydrogen peroxide, at early and late log
ORGANISM(S): Streptococcus pyogenes 
2011-11-18 | E-MTAB-646 | biostudies-arrayexpress
TranscriptomicsPorphyromonas gingivalis 33277 wild-type vs Fur orthologue Har isogenic mutant ECR455
Porphyromonas gingivalis is a major pathogen associated with the microbial biofilm-mediated disease chronic periodontitis. P. gingivalis has an obligate requirement for iron and protoporphyrin IX which it satisfies by transporting heme and iron liberated from the human host. The level of cellular ir...
ORGANISM(S): Porphyromonas gingivalis ATCC 33277 Porphyromonas gingivalis W83 
2015-04-01 | GSE37099 | GEO
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