Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.
about
A reduction in ribonucleotide reductase activity slows down the chromosome replication fork but does not change its localizationAllele specific synthetic lethality between priC and dnaAts alleles at the permissive temperature of 30 degrees C in E. coli K-12The G157C mutation in the Escherichia coli sliding clamp specifically affects initiation of replicationComparative analysis of glutaredoxin domains from bacterial opportunistic pathogensSolution structures of Mycobacterium tuberculosis thioredoxin C and models of intact thioredoxin system suggest new approaches to inhibitor and drug designThe clip-segment of the von Willebrand domain 1 of the BMP modulator protein Crossveinless 2 is preformedDepletion of Plasmodium berghei plasmoredoxin reveals a non-essential role for life cycle progression of the malaria parasiteFunctional studies of multiple thioredoxins from Mycobacterium tuberculosisLaboratory evolution of one disulfide isomerase to resemble anotherGenetic evidence for a link between glycolysis and DNA replication.Recombination phenotypes of Escherichia coli greA mutants.Ribonucleotide reductase and the regulation of DNA replication: an old story and an ancient heritage.Glutathione revisited: a vital function in iron metabolism and ancillary role in thiol-redox control.A novel regulatory mechanism couples deoxyribonucleotide synthesis and DNA replication in Escherichia coli.Hda-mediated inactivation of the DnaA protein and dnaA gene autoregulation act in concert to ensure homeostatic maintenance of the Escherichia coli chromosome.Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli.Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin.Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activitySHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasmFunctional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways.The reducing activity of glutaredoxin 3 toward cytoplasmic substrate proteins is restricted by methionine 43.The system biology of thiol redox system in Escherichia coli and yeast: differential functions in oxidative stress, iron metabolism and DNA synthesis.Genetic suppressors and recovery of repressed biochemical memory.Genes of Escherichia coli O157:H7 that are involved in high-pressure resistance.Physical interaction between human ribonucleotide reductase large subunit and thioredoxin increases colorectal cancer malignancy.Oxidative stress, protein damage and repair in bacteria.The tRNA thiolation pathway modulates the intracellular redox state in Escherichia coli.A residue outside the active site CXXC motif regulates the catalytic efficiency of Glutaredoxin 3.Requirements for replication restart proteins during constitutive stable DNA replication in Escherichia coli K-12.Mutations at several loci cause increased expression of ribonucleotide reductase in Escherichia coliImportance of the maintenance pathway in the regulation of the activity of Escherichia coli ribonucleotide reductase.What lies beyond uranus? Preconceptions, ignorance, serendipity and suppressors in the search for biology's secrets.Glutaredoxins are essential for stress adaptation in the cyanobacterium Synechocystis sp. PCC 6803.Determinants of activity in glutaredoxins: an in vitro evolved Grx1-like variant of Escherichia coli Grx3.Thioredoxins in redox maintenance and survival during oxidative stress of Bacteroides fragilis.Natural-Product-Inspired Aminoepoxybenzoquinones Kill Members of the Gram-Negative Pathogen Salmonella by Attenuating Cellular Stress Response.Insufficient levels of the nrdAB-encoded ribonucleotide reductase underlie the severe growth defect of the Δhda E. coli strain.AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage.The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity.DnaA and LexA Proteins Regulate Transcription of the uvrB Gene in Escherichia coli: The Role of DnaA in the Control of the SOS Regulon.
P2860
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P2860
Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.
description
2004 nî lūn-bûn
@nan
2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2004 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
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name
Interactions of glutaredoxins, ...... on system of Escherichia coli.
@ast
Interactions of glutaredoxins, ...... on system of Escherichia coli.
@en
type
label
Interactions of glutaredoxins, ...... on system of Escherichia coli.
@ast
Interactions of glutaredoxins, ...... on system of Escherichia coli.
@en
prefLabel
Interactions of glutaredoxins, ...... on system of Escherichia coli.
@ast
Interactions of glutaredoxins, ...... on system of Escherichia coli.
@en
P2093
P2860
P356
P1476
Interactions of glutaredoxins, ...... ion system of Escherichia coli
@en
P2093
Amir Porat
Jon Beckwith
Ron Ortenberg
P2860
P304
P356
10.1073/PNAS.0401965101
P407
P577
2004-04-27T00:00:00Z