Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
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Mechanism of coupling drug transport reactions located in two different membranesInward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopyCrystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sitesMechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusFTwo RND proteins involved in heavy metal efflux in Caulobacter crescentus belong to separate clusters within proteobacteria.In silico identification and characterization of the ion transport specificity for P-type ATPases in the Mycobacterium tuberculosis complexStructure and mechanism of Zn2+-transporting P-type ATPases.Small RNA Transcriptome of the Oral Microbiome during Periodontitis Progression.A new metal binding domain involved in cadmium, cobalt and zinc transportRole in metal homeostasis of CtpD, a Co²⁺ transporting P(1B4)-ATPase of Mycobacterium smegmatis.Characterization of the PIB-Type ATPases present in Thermus thermophilus.In silico approaches and chemical space of anti-P-type ATPase compounds for discovering new antituberculous drugs.Distinctive features of catalytic and transport mechanisms in mammalian sarco-endoplasmic reticulum Ca2+ ATPase (SERCA) and Cu+ (ATP7A/B) ATPasesToward a molecular understanding of metal transport by P(1B)-type ATPases.The mechanism of Cu+ transport ATPases: interaction with CU+ chaperones and the role of transient metal-binding sites.A novel P(1B)-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria.Fine-tuning of Substrate Affinity Leads to Alternative Roles of Mycobacterium tuberculosis Fe2+-ATPases.Zinc Resistance Mechanisms of P1B-type ATPases in Sinorhizobium meliloti CCNWSX0020.Mechanisms of copper homeostasis in bacteria.Iron, copper, zinc, and manganese transport and regulation in pathogenic Enterobacteria: correlations between strains, site of infection and the relative importance of the different metal transport systems for virulence.Differential roles for the Co(2+) /Ni(2+) transporting ATPases, CtpD and CtpJ, in Mycobacterium tuberculosis virulence.Metal Selectivity of a Cd-, Co-, and Zn-Transporting P1B-type ATPase.Mycobacteria and the intraphagosomal environment: take it with a pinch of salt(s)!Mycobacterium tuberculosis P-type ATPases: possible targets for drug or vaccine development.Iron Efflux by PmtA Is Critical for Oxidative Stress Resistance and Contributes Significantly to Group A Streptococcus Virulence.Bacterial Cu(+)-ATPases: models for molecular structure-function studies.Zinc Homeostasis at the Bacteria/Host Interface-From Coordination Chemistry to Nutritional Immunity.Mechanisms of charge transfer in human copper ATPases ATP7A and ATP7B.Transcriptome response to heavy metals in Sinorhizobium meliloti CCNWSX0020 reveals new metal resistance determinants that also promote bioremediation by Medicago lupulina in metal contaminated soil.The PerR-Regulated P1B-4-Type ATPase (PmtA) Acts as a Ferrous Iron Efflux Pump in Streptococcus pyogenes.The Listeria monocytogenes Fur-regulated virulence protein FrvA is an Fe(II) efflux P1B4 -type ATPase.The N-terminal degenerated metal-binding domain is involved in the heavy metal transport activity of TaHMA2.A comprehensive phylogenetic analysis of copper transporting P1B ATPases from bacteria of the Rhizobiales order uncovers multiplicity, diversity and novel taxonomic subtypes.PfeT, a P1B4 -type ATPase, effluxes ferrous iron and protects Bacillus subtilis against iron intoxicationCd(2+) extrusion by P-type Cd(2+)-ATPase of Staphylococcus aureus 17810R via energy-dependent Cd(2+)/H(+) exchange mechanism.Bacillithiol is a major buffer of the labile zinc pool in Bacillus subtilis.Iron distribution through the developmental stages of Medicago truncatula nodules.A structural model of the copper ATPase ATP7B to facilitate analysis of Wilson disease-causing mutations and studies of the transport mechanism.Selective substrate uptake: The role of ATP-binding cassette (ABC) importers in pathogenesis.Cu+-specific CopB transporter: Revising P1B-type ATPase classification.
P2860
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P2860
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
@ast
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
@en
type
label
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
@ast
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
@en
prefLabel
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
@ast
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
@en
P2093
P2860
P50
P356
P1433
P1476
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence
@en
P2093
Daniel Raimunda
José M Argüello
Manuel González-Guerrero
P2860
P304
P356
10.1021/BI201418K
P407
P577
2011-10-31T00:00:00Z