Arsenate reductase of Staphylococcus aureus plasmid pI258.
about
A tale of two oxidation states: bacterial colonization of arsenic-rich environmentsThe ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite.Microbial methylation of metalloids: arsenic, antimony, and bismuth.Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase functionArsenate reductases in prokaryotes and eukaryotes.Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatasesAll intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascadeConformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilisCrystal structure of anapoform ofShigella flexneriArsH protein with an NADPH-dependent FMN reductase activityPathways of As(III) detoxification in Saccharomyces cerevisiae.Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase.Solution structures and backbone dynamics of arsenate reductase from Bacillus subtilis: reversible conformational switch associated with arsenate reductionArsenic binding to proteinsHow thioredoxin dissociates its mixed disulfideA Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate ReductionAn arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristicsThe chromosomal arsenic resistance genes of Thiobacillus ferrooxidans have an unusual arrangement and confer increased arsenic and antimony resistance to Escherichia coli.Families of soft-metal-ion-transporting ATPases.Identification of antimony- and arsenic-oxidizing bacteria associated with antimony mine tailingReactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9.Microbial arsenic: from geocycles to genes and enzymes.Resistance determinants of a highly arsenic-resistant strain of Leptospirillum ferriphilum isolated from a commercial biooxidation tankBiochemistry of arsenic detoxification.Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchangeVirulence and arsenic resistance in Yersiniae.Genes and enzymes involved in bacterial oxidation and reduction of inorganic arsenicEarth Abides Arsenic BiotransformationsArginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) productAdventitious arsenate reductase activity of the catalytic domain of the human Cdc25B and Cdc25C phosphatases.Role of arsenic and its resistance in nature.Bacterial metabolism of environmental arsenic--mechanisms and biotechnological applications.Growth of Strain SES-3 with Arsenate and Other Diverse Electron AcceptorsCellular Response of Sinorhizobium sp. Strain A2 during Arsenite Oxidation.Construction and purification of His-tagged staphylococcal ArsB protein, an integral membrane protein that is involved in arsenical salt resistance.Validation of arsenic resistance in Bacillus cereus strain AG27 by comparative protein modeling of arsC gene product.The conserved active site tryptophan of thioredoxin has no effect on its redox properties.The phosphatase C(X)5R motif is required for catalytic activity of the Saccharomyces cerevisiae Acr2p arsenate reductase.Molecular characterization of Alr1105 a novel arsenate reductase of the diazotrophic cyanobacterium Anabaena sp. PCC7120 and decoding its role in abiotic stress management in Escherichia coli.Arsenic-resistant proteobacterium from the phyllosphere of arsenic-hyperaccumulating fern (Pteris vittata L.) reduces arsenate to arsenite.
P2860
Q21145233-3BBAA3A9-658A-4EEC-988B-C3EC4784C947Q24520730-9A64CBB2-5294-4928-8959-49963730E8A9Q24533232-975CF981-289A-4B36-9338-28859FF4BA9CQ24805132-F8C42599-8F3E-4345-AE2D-968EBB57AABCQ24812431-4F51178F-A02E-4499-9234-75DAF2FD1BADQ27636058-B882B228-00A0-47F9-AAAF-7849D008C66FQ27639193-C7A63F37-9D94-4192-A752-00D6617826DEQ27643830-21A50F70-CC2C-434C-9C1B-FA9531D9E0F0Q27648905-6690D82D-8B40-4131-AD80-59D61691C001Q27931719-3F44E410-4DC8-4145-8DDD-6A4C43197DECQ27939130-03735327-C397-40B6-BFCD-CA689615F80FQ28274552-DAE9F943-13E3-4803-86E9-9A6018073A76Q28389752-FB636F80-C392-4971-A7EA-65AEA73DF96DQ28475852-E82700C8-CFBA-4849-AF70-582968A8D31FQ28607586-41C564CE-55C2-4706-B412-648633B3B181Q28776688-1FD2CE6D-E37F-4932-8EAE-5E00E33BEB6BQ33588905-11AC3AE5-9337-47B8-8D07-8F2004CCBC6EQ33635719-FC81FF7B-1327-4E09-AC5E-62982F11D820Q33805666-709EE3E7-F892-420A-A175-BC59E335B47DQ33883304-48D73614-25EB-4227-8434-FDF2265696FDQ34027820-CAFCF4E9-BB17-408B-8FE9-EF456C9666DCQ34143180-4736DBAA-0C0E-4CA7-8BA9-77D4B38E4F41Q34432205-D5AED57F-A44F-4C53-8668-916B2216A1E1Q34922203-38FB7D4E-6534-4AD1-8603-1F84052B91EEQ34962642-2158C5C9-D458-4F47-A690-D3D46609414AQ35619204-CB815A82-CC06-40B8-9FA6-AA75C0804149Q36030281-3184690B-21C0-4023-8AF7-EFF7593CD049Q36462027-6F41875A-4A2C-4E19-BD84-FBFEF5456DECQ36519451-2CA02666-E03A-4FCE-AEBB-861139ECB511Q37338838-BA09616E-B933-42B5-9D95-7B8B5A8154F5Q37936450-E8D2CAA9-8DE5-470F-8129-20D04797B84AQ38094953-E37CAB69-D789-44D8-B92D-419BB8F3C285Q41849516-11319013-2A5B-43DA-80C7-1C531AFF1B6EQ41981740-9DBD75C8-FD9F-4E4D-B9A3-62F52DFC0334Q42326998-0EE5FEBC-5A3D-46F7-8635-CC0061295D19Q42687278-53AD6509-A2A1-48A0-8535-A8B6071F12DBQ42727690-8467CDD1-E9A9-4BD8-B2BE-13C6FE30E52FQ43680910-C09AF590-D596-409D-AB14-0D1A9720619AQ44280108-EFFFD7B6-2797-45D8-8621-B65A21705A96Q48085250-2E5A3267-B90F-42EA-806C-50269D30682F
P2860
Arsenate reductase of Staphylococcus aureus plasmid pI258.
description
1994 nî lūn-bûn
@nan
1994 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@ast
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@en
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@nl
type
label
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@ast
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@en
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@nl
prefLabel
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@ast
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@en
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@nl
P2093
P356
P1433
P1476
Arsenate reductase of Staphylococcus aureus plasmid pI258.
@en
P2093
P304
P356
10.1021/BI00189A034
P407
P577
1994-06-01T00:00:00Z