About: Regulation of the Intracellular Free Iron Pool by Dpr Provides Oxygen Tolerance to Streptococcus mutans

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About: Regulation of the Intracellular Free Iron Pool by Dpr Provides Oxygen Tolerance to Streptococcus mutans Goto Sponge NotDistinct Permalink

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scientific article (publication date: September 2004)

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rdf:type	Item
description	article scientifique publié en 2004 (fr) artículu científicu espublizáu en 2004 (ast) 2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована у вересні 2004 (uk) 2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած (hyw) 2004年學術文章 (zh) wetenschappelijk artikel (gepubliceerd op 2004/09/01) (nl) مقالة علمية (نشرت في سبتمبر 2004) (ar) scientific article (publication date: September 2004) (en) im September 2004 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q29391695-1E7D7884-9006-44E4-A239-AFE0B3DBE25E
publication date	2004-09-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q29391695-B34C418C-EC72-4C7E-8A4C-C9576744A659
language of work or name	English
cites work	wds:Q29391695-05F0E9C9-7F9B-48BA-83B2-4531E7958FB8 wds:Q29391695-0A4A5EBF-5FA4-4224-9A50-0CAD3386E774 wds:Q29391695-126477CB-342C-4CDB-BEE3-D15FDB46E74A wds:Q29391695-138928F9-3AEA-46E5-B138-DD38A4399B2F wds:Q29391695-1AC1AE5F-EB2A-4C58-B4B1-28DC56DF265E wds:Q29391695-228C0175-F2EF-45FC-952F-D6BE08BFD726 wds:Q29391695-24A9EF05-96D6-411A-A346-80823A3097D3 wds:Q29391695-2693F634-6B0D-47AC-8354-5F5ABB933128 wds:Q29391695-2BC7CBEA-6F6A-4E2F-AC19-CD1B755ABE9C wds:Q29391695-2D9FDD6F-BA82-46AB-8E61-FCB5A0094E9D wds:Q29391695-3057D0C8-7C3E-4E12-8982-5370C15F6627 wds:Q29391695-319A32E8-4733-4EBE-8A43-D72A4759B504 wds:Q29391695-3AF5ED80-1B43-4359-AD71-3965B39CFF62 wds:Q29391695-3F7B9948-E623-4B70-B5F2-8BEF75D4F951 wds:Q29391695-40788803-5BAC-495B-818A-1AAA0692C3CD wds:Q29391695-460CB668-472B-4115-A5CE-DF8B6293C008 wds:Q29391695-57F9DDB3-1B34-4B8B-BCD0-04132B17A540 wds:Q29391695-622800EA-9DCF-4A00-A079-93DA6D6EA569 wds:Q29391695-674CD4EE-C6A8-4605-887A-959AD8798A99 wds:Q29391695-6777DA0E-B38A-4188-A2FA-2A1336B1E461 wds:Q29391695-6ECCAD68-C864-44E1-8710-128D3946AE66 wds:Q29391695-73015122-1D16-4D9C-91F3-917E6E750B10 wds:Q29391695-765A46E5-F51F-44A9-9751-A94B5B08F39B wds:Q29391695-86BB91AB-8D7F-4DB6-84D2-FC350AC922B1 wds:Q29391695-8B5EF681-6F3C-42CF-A3EA-0F87AE79C165 wds:Q29391695-8CE1C053-BB5E-480A-BB1F-00E6B185116B wds:Q29391695-95E0628D-065C-4495-9C85-FD483D7A9611 wds:Q29391695-96EB054E-59B1-40C3-A464-C7CD31A378E3 wds:Q29391695-A5C599D6-5C77-4B3D-85BA-D0110C18B686 wds:Q29391695-AFB61A8D-7BD9-4CD8-9BFF-51FD94B5894A wds:Q29391695-B3A54822-CEC1-4BA7-B5B9-0F7F41428D6D wds:Q29391695-C1A4DBB6-5F70-4F7E-A7CA-E5D85FD85440 wds:Q29391695-CFB46467-682F-4D69-B0B8-61E2127050A0 wds:Q29391695-DF9D7D09-F6DD-4D0C-8B7A-E04E760E5214 wds:Q29391695-E141D621-1FDE-4D29-A2ED-2672E738D912 wds:Q29391695-EC7594A3-54DA-40B7-9DF8-5C3ACDA58807 wds:Q29391695-F6369788-62C3-4724-8B9A-236B57B99507 wds:Q29391695-FF5AAAF4-DAD2-4295-A510-1F3F73F3F67E
cites work	The labile iron pool: characterization, measurement, and participation in cellular processes(1). Superoxide accelerates DNA damage by elevating free-iron levels Role of the dpr product in oxygen tolerance in Streptococcus mutans The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure. The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni Bacterial iron homeostasis Oxygen toxicity, oxygen radicals, transition metals and disease The crystal structure of Dps, a ferritin homolog that binds and protects DNA Pathways of Oxidative Damage Role of the citrate pathway in glutamate biosynthesis by Streptococcus mutans The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site DNA protection by stress-induced biocrystallization A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua Yeast lacking superoxide dismutase(s) show elevated levels of "free iron" as measured by whole cell electron paramagnetic resonance Manganese: its acquisition by and function in the lactic acid bacteria Iron and oxidative stress in bacteria Increased production of hydrogen peroxide by Lactobacillus delbrueckii subsp. bulgaricus upon aeration: involvement of an NADH oxidase in oxidative stress Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient Quantitation of intracellular free iron by electron paramagnetic resonance spectroscopy An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro. Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the fenton reaction Molecular basis of H2O2 resistance mediated by Streptococcal Dpr. Demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis. Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: implications for iron incorporation. Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein Functions of two types of NADH oxidases in energy metabolism and oxidative stress of Streptococcus mutans. Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans Cloning, nucleotide sequence, and disruption of Streptococcus mutans glutathione reductase gene (gor). Effect of intracellular pH and potassium ions on a primary transport system for glutamate/aspartate in Streptococcus mutans Nucleotide sequence of Streptococcus mutans superoxide dismutase gene and isolation of insertion mutants Characteristics of a hydrogen peroxide-forming pyruvate oxidase from Streptococcus sanguis Oxygen toxicity in Streptococcus mutans: manganese, iron, and superoxide dismutase Microwave digestion using dual PTFE containers for analysis of trace elements in small amounts of biological samples
author name string	wds:Q29391695-35B13472-901B-47B6-94BA-765F3730AC15 wds:Q29391695-67BB0945-EFA1-4C73-B3CE-4CB8294A6600 wds:Q29391695-B602146E-7F35-412B-B942-B7D4F394BC01 wds:Q29391695-D9B59714-CA84-43C6-8B63-A2A67037CB71 wds:Q29391695-E28C8985-EC6E-4024-B967-8AB75FF86C65 wds:Q29391695-F25B93CF-3FE8-4A36-8315-CFB412B9FE98
author name string	Y. Yamamoto K. Fukui K. Kimura

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