About: PerR acts as a switch for oxygen tolerance in the strict anaerobe Clostridium acetobutylicum

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About: PerR acts as a switch for oxygen tolerance in the strict anaerobe Clostridium acetobutylicum Goto Sponge NotDistinct Permalink

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description	artículu científicu espublizáu en 2008 (ast) vědecký článek publikovaný v roce 2008 (cs) 2008 թվականի մայիսին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в травні 2008 (uk) 2008 թուականի Մայիսին հրատարակուած գիտական յօդուած (hyw) مقالة علمية (نشرت في مايو 2008) (ar) vedecký článok (publikovaný 2008/05/01) (sk) wetenschappelijk artikel (gepubliceerd op 2008/05/01) (nl) im Mai 2008 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28485887-F94EB9D7-80D2-4D74-B26A-7D883D9FAA8C
publication date	2008-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28485887-BD6C57F2-EE86-4B17-A043-07BD369AB1E5
language of work or name	English
cites work	wds:Q28485887-061069CB-A605-425E-9A34-EB09791377DB wds:Q28485887-06E14F30-8A90-45FE-89B8-0343577314C3 wds:Q28485887-076C2864-58B2-476E-8781-B8EF983E7828 wds:Q28485887-0B826E1C-A8C7-4DAE-BC32-479E208E78ED wds:Q28485887-0C78E877-9C72-434F-B397-07ACE4013143 wds:Q28485887-0D35C8EA-1FA4-40E4-9F50-32FD74AF5EDD wds:Q28485887-16087CFC-AE6D-4080-BD3F-083A8304D7D1 wds:Q28485887-1AFEA255-0904-4BB0-B3D2-3B8F74047579 wds:Q28485887-22165885-7B7E-4A23-AFF3-252A1DE3B1F9 wds:Q28485887-2C243B1B-492B-4E25-B001-883B5FEFBCC8 wds:Q28485887-2CC835A1-B48B-4087-A278-091533B26C14 wds:Q28485887-2FC31FC1-BD2E-42D9-8F73-30DEDDC948B5 wds:Q28485887-38309AF7-59E3-49A8-B842-F1ED9E4BC2AD wds:Q28485887-461479CF-31A8-4BEE-9A7A-881C9C428534 wds:Q28485887-4AFA8B40-90B4-4961-86B3-98B2B597AFDE wds:Q28485887-51F67726-FE69-41D6-8642-A4F8948E4264 wds:Q28485887-542174B2-C92C-43EC-8DF0-5A17C1168C01 wds:Q28485887-5CC42924-BBA9-49CE-805B-D87D7576F56A wds:Q28485887-5F9E4673-7FE8-4284-94F9-8E1C8C788A5E wds:Q28485887-65220C59-C49F-4E47-AE3F-0AA56DCA96F8 wds:Q28485887-65B2CE62-28DC-4F50-8276-E6C48CF4A1FC wds:Q28485887-89766B33-7B5E-4C6A-8DBE-37E653D1847D wds:Q28485887-918460C6-D300-4296-9C82-38F6C0378312 wds:Q28485887-97B88B35-A636-4A7C-9E77-8EF9A050999D wds:Q28485887-9FA8EAD0-ACE1-490F-8FBD-49565D736EEB wds:Q28485887-9FF65CC1-C2A4-487E-9F15-05F88972C767 wds:Q28485887-A5A38A3D-C467-47DF-B93E-36323BD1CBB3 wds:Q28485887-B2D53057-A34C-4CE8-BDAD-03F26106460F wds:Q28485887-C234CD62-16A6-42B9-9915-839338DB33F9 wds:Q28485887-C3610CB6-7001-48B0-9AB9-AA741DE8BB68 wds:Q28485887-C6442E03-CEC5-40F0-9B5B-073336800297 wds:Q28485887-CE15D514-2F1E-40EF-BF61-40A3E4662B09 wds:Q28485887-D353A529-2AEB-477F-8A0D-62B4D63715D4 wds:Q28485887-D8B0ED20-DFF2-4E7F-8113-9D50EE1F887A wds:Q28485887-E01E0E8F-6E61-4F79-A143-C4C74CC63FB8 wds:Q28485887-E948F2E9-FB2D-439C-B074-1C7589BE6A42 wds:Q28485887-E986CFB7-EF8B-4A9F-9A1E-1D00E95EF9DE wds:Q28485887-F32BEEEA-CFCD-4587-AD85-69C42852B36E wds:Q28485887-F8C8EF4E-14FB-4DBC-A380-FA8E242E35DE
cites work	Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family Superoxide dismutase: improved assays and an assay applicable to acrylamide gels Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis. Aerotolerance and peroxide resistance in peroxidase and PerR mutants of Streptococcus pyogenes Identification of the Clostridium perfringens genes involved in the adaptive response to oxidative stress The rubrerythrin-like protein Hsp21 of Clostridium acetobutylicum is a general stress protein Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli Superoxide accelerates DNA damage by elevating free-iron levels CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro Pathways of Oxidative Damage Purification and characterization of the pyruvate-ferredoxin oxidoreductase from Clostridium acetobutylicum. The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation Anaerobic microbes: oxygen detoxification without superoxide dismutase. Iron-sulphur clusters and the problem with oxygen Differential gene expression in response to hydrogen peroxide and the putative PerR regulon of Synechocystis sp. strain PCC 6803. Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum Biobutanol: an attractive biofuel Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron cluster Rubredoxin:oxygen oxidoreductase enhances survival of Desulfovibrio vulgaris hildenborough under microaerophilic conditions PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: a novel oxidative stress protection system Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase Adaptive responses to oxygen stress in obligatory anaerobes Clostridium acetobutylicum and Clostridium aminovalericum The superoxide dismutase activity of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774 An Enzyme-Based Theory of Obligate Anaerobiosis: The Physiological Function of Superoxide Dismutase An O2-inducible rubrerythrin-like protein, rubperoxin, is functional as a H2O2 reductase in an obligatory anaerobe Clostridium acetobutylicum. What biological purpose is served by superoxide reductase? A Standard Operating Procedure (SOP) for the preparation of intra- and extracellular proteins of Clostridium acetobutylicum for proteome analysis. New and fast method to quantify respiration rates of bacterial and plankton communities in freshwater ecosystems by using optical oxygen sensor spots. PerR controls Mn-dependent resistance to oxidative stress in Neisseria gonorrhoeae Transcription of the pst operon of Clostridium acetobutylicum is dependent on phosphate concentration and pH Crystal structure studies on rubrerythrin: enzymatic activity in relation to the zinc movement
author name string	wds:Q28485887-4E7F47EF-C9FB-4F47-894F-98BCA2CDCFBC wds:Q28485887-5F7F3B9C-0FD8-4014-BD13-A578C3597EAC wds:Q28485887-867C99B9-FE9D-4E7A-A886-F1379E3B54CA wds:Q28485887-C7199040-E4FD-44DD-9F42-6A3B01B21828
OpenCitations bibliographic resource ID	wds:Q28485887-4595AD5E-4C85-4DD4-9A65-FF753CC8DB1A
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/717498
author name string	Hubert Bahl

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