Cu(I) recognition via cation-π and methionine interactions in CusF - Wikidata - wikimedia - TriplyDB

Cu(I) recognition via cation-π and methionine interactions in CusF

Cu(I) recognition via cation-π and methionine interactions in CusF

http://www.wikidata.org/entity/Q27649415

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Resistance mechanisms of Mycobacterium tuberculosis against phagosomal copper overload Tryptophan Cu(I)–π interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF Crystal Structure of the Membrane Fusion Protein CusB from Escherichia coli Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport Crystal Structure of Escherichia coli CusC, the Outer Membrane Component of a Heavy Metal Efflux Pump Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli Structures of a Na+-coupled, substrate-bound MATE multidrug transporter The ins and outs of RND efflux pumps in Escherichia coli Structural biology of copper trafficking Copper metallochaperones Positive selection in octopus haemocyanin indicates functional links to temperature adaptation Tryptophan-lipid interactions in membrane protein folding probed by ultraviolet resonance Raman and fluorescence spectroscopy.Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy Insight into the cation-π interaction at the metal binding site of the copper metallochaperone CusF.Architecture and roles of periplasmic adaptor proteins in tripartite eﬄux assemblies Effect of dioxygen on copper(II) binding to alpha-synuclein.Tracking metal ions through a Cu/Ag efflux pump assigns the functional roles of the periplasmic proteins Copper transport and trafficking at the host-bacterial pathogen interface.The essential role of the Cu(II) state of Sco in the maturation of the Cu(A) center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis Sco Coordination chemistry of bacterial metal transport and sensing.Silver resistance in Gram-negative bacteria: a dissection of endogenous and exogenous mechanisms.Efflux pumps of the resistance-nodulation-division family: a perspective of their structure, function, and regulation in gram-negative bacteria.A place for thioether chemistry in cellular copper ion recognition and trafficking.Ammonium catalyzed cyclitive additions: evidence for a cation-π interaction with alkynes.Complexation and coacervation of like-charged polyelectrolytes inspired by mussels.Lumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase.Kβ Valence to Core X-ray Emission Studies of Cu(I) Binding Proteins with Mixed Methionine - Histidine Coordination. Relevance to the Reactivity of the M- and H-sites of Peptidylglycine Monooxygenase Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone.The Structure of the Periplasmic Sensor Domain of the Histidine Kinase CusS Shows Unusual Metal Ion Coordination at the Dimeric Interface.Mechanisms of copper homeostasis in bacteria.Structure and dynamics of the N-terminal domain of the Cu(I) binding protein CusB.Robust affinity standards for Cu(I) biochemistry The Cus efflux system removes toxic ions via a methionine shuttle.Structure and mechanism of the tripartite CusCBA heavy-metal efflux complex.Group-10 metal complexes of biological molecules and related ligands: structural and functional properties.Pathogenic adaptations to host-derived antibacterial copper.Bacterial multidrug efflux transporters.The cation-π interaction.Heavy metal transport by the CusCFBA efflux system.Bacterial Cu(+)-ATPases: models for molecular structure-function studies.

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P2860

Cu(I) recognition via cation-π and methionine interactions in CusF

http://www.wikidata.org/entity/Q27649415

description

2008 nî lūn-bûn

@nan

2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Cu(I) recognition via cation-π and methionine interactions in CusF

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Cu(I) recognition via cation-π and methionine interactions in CusF

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Cu(I) recognition via cation-π and methionine interactions in CusF

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type

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Cu(I) recognition via cation-π and methionine interactions in CusF

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Cu(I) recognition via cation-π and methionine interactions in CusF

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Cu(I) recognition via cation-π and methionine interactions in CusF

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Cu(I) recognition via cation-π and methionine interactions in CusF

@ast

Cu(I) recognition via cation-π and methionine interactions in CusF

@en

Cu(I) recognition via cation-π and methionine interactions in CusF

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NCHEMBIO.2007.57

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Nature Chemical Biology

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Cu(I) recognition via cation-pi and methionine interactions in CusF

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P2093

Anna V Davis

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Benjamin M Staehlin

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Gurusamy Balakrishnan

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Jay P Stasser

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Pamela Focia

http://www.w3.org/2001/XMLSchema#string

Thomas G Spiro

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Thomas V O'Halloran

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Yi Xue

http://www.w3.org/2001/XMLSchema#string

P2860

A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites

Unusual Cu(I)/Ag(I) coordination ofEscherichia coliCusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy

The Cationminus signpi Interaction

Transition metal speciation in the cell: insights from the chemistry of metal ion receptors

A novel copper-binding fold for the periplasmic copper resistance protein CusF.

The PcoC copper resistance protein coordinates Cu(I) via novel S-methionine interactions.

Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12.

A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase.

Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli.

Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza a virus.

P2888

nchembio.2007.57

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107-109

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10.1038/NCHEMBIO.2007.57

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2

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James E Penner-Hahn

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2007-12-23T00:00:00Z

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5692348

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1002785728

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18157124

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