Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
about
More than 200 genes required for methane formation from H₂ and CO₂ and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicusAllosteric Inhibition of a Zinc-Sensing Transcriptional Repressor: Insights into the Arsenic Repressor (ArsR) FamilySolution Structure of Mycobacterium tuberculosis NmtR in the Apo State: Insights into Ni(II)-Mediated AllosteryStructural basis for regulation of rhizobial nodulation and symbiosis gene expression by the regulatory protein NolRRoles of Escherichia coli ZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanismParalogous Regulators ArsR1 and ArsR2 of Pseudomonas putida KT2440 as a Basis for Arsenic Biosensor DevelopmentMining genomes of marine cyanobacteria for elements of zinc homeostasis.CorE from Myxococcus xanthus is a copper-dependent RNA polymerase sigma factor.Advances in the molecular understanding of biological zinc transport.Metalloregulatory proteins: metal selectivity and allosteric switching.Identification and characterization of the transcriptional regulator ChrB in the chromate resistance determinant of Ochrobactrum tritici 5bvl1.Construction of a self-luminescent cyanobacterial bioreporter that detects a broad range of bioavailable heavy metals in aquatic environments.Identification of a lineage specific zinc responsive genomic island in Mycobacterium avium ssp. paratuberculosis.Metalloregulation of Gram-positive pathogen physiology.Metal site occupancy and allosteric switching in bacterial metal sensor proteins.NrcR, a New Transcriptional Regulator of Rhizobium tropici CIAT 899 Involved in the Legume Root-Nodule SymbiosisTranscriptional and posttranscriptional regulation of Bacillus sp. CDB3 arsenic-resistance operon ars1.Fur-type transcriptional repressors and metal homeostasis in the cyanobacterium Synechococcus sp. PCC 7002.The Effectors and Sensory Sites of Formaldehyde-responsive Regulator FrmR and Metal-sensing VariantExtracellular Ribonuclease from Bacillus licheniformis (Balifase), a New Member of the N1/T1 RNase SuperfamilyBacterial metallothioneins: past, present, and questions for the future.Specific metal recognition in nickel trafficking.How prokaryotes deal with arsenic(†).Zinc'ing sensibly: controlling zinc homeostasis at the transcriptional level.Zinc sensing by metal-responsive transcription factor 1 (MTF1) controls metallothionein and ZnT1 expression to buffer the sensitivity of the transcriptome response to zinc.Activation of archaeal transcription mediated by recruitment of transcription factor B.Nickel-responsive transcriptional regulators.Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.Glutamate Ligation in the Ni(II)- and Co(II)-Responsive Escherichia coli Transcriptional Regulator, RcnR.Effects of trace metal ions on secondary metabolism and the morphological development of streptomycetes.Zinc Homeostasis at the Bacteria/Host Interface-From Coordination Chemistry to Nutritional Immunity.Metal homeostasis in bacteria: the role of ArsR-SmtB family of transcriptional repressors in combating varying metal concentrations in the environment.Mycobacterium tuberculosis NmtR harbors a nickel sensing site with parallels to Escherichia coli RcnR.Listeria monocytogenes CadC Regulates Cadmium Efflux and Fine-tunes Lipoprotein Localization to Escape the Host Immune Response and Promote Infection.Comparative Genomics of Bacillus amyloliquefaciens Strains Reveals a Core Genome with Traits for Habitat Adaptation and a Secondary Metabolites Rich Accessory Genome.An ArsR/SmtB family member is involved in the regulation by arsenic of the arsenite oxidase operon in Thiomonas arsenitoxydans.Bacillithiol is a major buffer of the labile zinc pool in Bacillus subtilis.Organization and regulation of the arsenite oxidase operon of the moderately acidophilic and facultative chemoautotrophic Thiomonas arsenitoxydans.An ArsR/SmtB family member regulates arsenic resistance genes unusually arranged in Thermus thermophilus HB27.Zinc acquisition mechanisms differ between environmental and virulent Francisella species.
P2860
Q21296736-14E56BA5-5EA4-4B97-A4CA-CA9FC873C6FDQ27676010-ECE8AC48-5DA9-4B20-8D2F-6B89834C97ADQ27677867-59822C82-8427-412B-9FFB-0342F083BBCEQ27683372-8696A68D-0B37-433D-8F07-1080AF557F78Q27703600-A1A76DA3-F5E1-466A-B44D-A02E80DF28EFQ28595925-E98E1E8E-9DBB-495B-936F-71300543900EQ30512952-33E14E1F-4402-4978-B516-3A96561C38C9Q33926855-52FEB7D8-3C21-476A-8CE4-6310BF4432B5Q34459994-4D86F874-0DBC-4100-B76C-F5AF2CF5558DQ34990148-D1A812DA-5BE6-4449-B89E-8E4BD024991FQ35040727-1BEDBE5C-DC78-48AC-98A2-F619F5267092Q35158093-DFF30664-1BAA-4BC6-969D-821C6FB94FFBQ35496664-F06D7DE1-5EC6-4683-8553-C001E5006B41Q35836646-E5F85D22-8928-4E09-973B-550E985C106DQ35851912-F7A92A4B-089D-41DE-B51F-67B1FC0A4470Q35994758-F9091297-F6F8-44AF-94CA-D82A86B195D1Q36035253-CB564C77-C4A0-4CA1-A5CE-1D23CFE4C88DQ36234481-12F8A922-EC94-48D1-9138-31AC03055B2FQ37243251-0D7DE2C2-8EB7-4A79-B4CF-972C356031CEQ37253105-17A26B57-F428-42EC-937E-23F3D7FA36F1Q37877170-21EE4BEE-3DD9-4A28-A431-3778F541BF0BQ38042673-DE93F2E6-9FCE-4FED-9AAA-175893B5F463Q38113999-9247762B-B752-435C-9F79-0C9A0E2C2F39Q38203812-DAFF327F-C16D-450C-8AB8-E9983554DE9BQ38294094-19D565BE-4925-4ACF-A781-87BCBC167F92Q38326186-2BB3CA62-B627-49ED-9525-468423E9D5C0Q38534594-E6E2A799-D032-4820-8FD1-A038958F7A83Q38600139-DD53F2FE-3780-4B6F-BDDB-9F6217E0BC6AQ38778229-CA819D9D-D39C-4D3E-9B67-BEE232C088D1Q38816452-08513E53-CE94-40AB-A697-4AA0CFAF85EDQ38935738-E58A94E7-2EDB-461C-9891-0AB44FB1CBF4Q39312476-C0945FF3-428F-4E7D-A0C7-4FF6610A2059Q39407946-A78C0F88-30E6-40FD-A349-2CB071690B1FQ40268156-674C5E53-ABB1-43D8-8B8A-0A9B73D21184Q41222156-9644F65B-87C8-4949-857E-1F034E6E6203Q41851868-4B801636-50DB-48AF-8B33-0061A98FCFCEQ42999727-A1179D72-CC69-4603-A73F-364439EEAFE0Q43019185-4A52BEF9-76CF-4D30-95D5-77FBEA41B8F2Q43647378-0403016E-B33A-4B84-87C5-5EAE2C50159CQ45072111-1FEB12C9-0204-455F-B3EF-932BF34CCBF8
P2860
Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 25 March 2010
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
@en
Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
@nl
type
label
Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
@en
Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
@nl
prefLabel
Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
@en
Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
@nl
P2860
P356
P1476
Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
@en
P2860
P304
P356
10.1039/B906682A
P577
2010-03-25T00:00:00Z