The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
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Ruffling of Metalloporphyrins Bound to IsdG and IsdI, Two Heme-degrading Enzymes in Staphylococcus aureusUnusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosisThe IsdG-family of haem oxygenases degrades haem to a novel chromophoreIn vitro heme biotransformation by the HupZ enzyme from Group A streptococcusHeme degrading protein HemS is involved in oxidative stress response of Bartonella henselaeIron homeostasis in the Rhodobacter genusBacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases.Functional identification of HugZ, a heme oxygenase from Helicobacter pylori.A bacterial iron exporter for maintenance of iron homeostasisNutritional immunity: transition metals at the pathogen-host interface.Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.The crimson conundrum: heme toxicity and tolerance in GAS.Staphylococcus lugdunensis IsdG liberates iron from host heme.The bhuQ gene encodes a heme oxygenase that contributes to the ability of Brucella abortus 2308 to use heme as an iron source and is regulated by Irr.A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO.The Bradyrhizobium japonicum Irr protein is a transcriptional repressor with high-affinity DNA-binding activity.Positive control of ferric siderophore receptor gene expression by the Irr protein in Bradyrhizobium japonicum.A battle for iron: host sequestration and Staphylococcus aureus acquisitionBacteria capture iron from heme by keeping tetrapyrrol skeleton intactMetal acquisition and virulence in Brucella.Chlamydomonas reinhardtii LFO1 Is an IsdG Family Heme Oxygenase.Iron homeostasis in Brucella abortus: the role of bacterioferritin.Ironing Out the Unconventional Mechanisms of Iron Acquisition and Gene Regulation in Chlamydia.Comparative analysis of hmuO function and expression in Corynebacterium species.HmuP is a coactivator of Irr-dependent expression of heme utilization genes in Bradyrhizobium japonicum.The ChrA-ChrS and HrrA-HrrS signal transduction systems are required for activation of the hmuO promoter and repression of the hemA promoter in Corynebacterium diphtheriae.Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes.
P2860
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P2860
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
description
2006 nî lūn-bûn
@nan
2006 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
@ast
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
@en
type
label
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
@ast
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
@en
prefLabel
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
@ast
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
@en
P2860
P356
P1476
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
@en
P2093
Mark R O'Brian
Sumant Puri
P2860
P304
P356
10.1128/JB.00737-06
P407
P577
2006-09-01T00:00:00Z