Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF - Wikidata - awgldk - TriplyDB

Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

http://www.wikidata.org/entity/Q27678845

about

A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Relating sequence encoded information to form and function of intrinsically disordered proteins Single-Cell, Time-Resolved Antimicrobial Effects of a Highly Cationic, Random Nylon-3 Copolymer on Live Escherichia coli.Supramolecular assemblies underpin turnover of outer membrane proteins in bacteria.Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake Structural and biophysical analysis of nuclease protein antibiotics Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins.Alpha-synuclein lipid-dependent membrane binding and translocation through the α-hemolysin channel Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum Digested disorder: Quarterly intrinsic disorder digest (April-May-June, 2013).Daring to be different: colicin N finds another way.C-Terminal Domain of Hemocyanin, a Major Antimicrobial Protein from Litopenaeus vannamei: Structural Homology with Immunoglobulins and Molecular Diversity Dynamic protein ligand interactions--insights from MS.The proton-motive force is required for translocation of CDI toxins across the inner membrane of target bacteria Osmoporin OmpC forms a complex with MlaA to maintain outer membrane lipid asymmetry in Escherichia coli.Conformational States of macromolecular assemblies explored by integrative structure calculation.High-resolution mass spectrometry of small molecules bound to membrane proteins Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa CdiA Effectors from Uropathogenic Escherichia coli Use Heterotrimeric Osmoporins as Receptors to Recognize Target Bacteria.Efficacy of species-specific protein antibiotics in a murine model of acute Pseudomonas aeruginosa lung infection.The Colicin E1 TolC Box: Identification of a Domain Required for Colicin E1 Cytotoxicity and TolC Binding.The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein.The role of structural proteomics in vaccine development: recent advances and future prospects.Orientation of the OmpF Porin in Planar Lipid Bilayers.Mass spectrometric identification of intermediates in the O2-driven [4Fe-4S] to [2Fe-2S] cluster conversion in FNR.Protein folding in the cell envelope of Escherichia coli.Characterization of Membrane Protein-Lipid Interactions by Mass Spectrometry Ion Mobility Mass Spectrometry.Mass spectrometry of B. subtilis CopZ: Cu(i)-binding and interactions with bacillithiol.Diversity and distribution of nuclease bacteriocins in bacterial genomes revealed using Hidden Markov Models.Antibacterial toxin colicin N and phage protein G3p compete with TolB for a binding site on TolA.The Colicin E1 TolC-Binding Conformer: Pillar or Pore Function of TolC in Colicin Import?Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement.Fourier Transform-Ion Cyclotron Resonance Mass Spectrometry as a Platform for Characterizing Multimeric Membrane Protein Complexes.The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Allosteric modulation of protein-protein interactions by individual lipid binding events.Exploitation of an iron transporter for bacterial protein antibiotic import.Native Desorption Electrospray Ionization Liberates Soluble and Membrane Protein Complexes from Surfaces.

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P2860

Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

http://www.wikidata.org/entity/Q27678845

description

2013 nî lūn-bûn

@nan

2013 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2013 թվականի հունիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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SCIENCE.1237864

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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

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Alexander Klein

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Colin Kleanthous

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Helen R Saibil

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Jonathan T S Hopper

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Justyna A Wojdyla

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Nicholas G Housden

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Renata Kaminska

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P2860

Intrinsically unstructured proteins and their functions

MolProbity: all-atom structure validation for macromolecular crystallography

Colicin biology

The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9

The structure of BtuB with bound colicin E3 R-domain implies a translocon

Molecular mimicry enables competitive recruitment by a natively disordered protein

Crystal structures of the OmpF porin: function in a colicin translocon

Allosteric β-propeller signalling in TolB and its manipulation by translocating colicins

Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF

Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide

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10.1126/SCIENCE.1237864

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6140

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340

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Carol V. Robinson

David Rodríguez-Larrea

Natalya Lukoyanova

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2013-06-28T00:00:00Z

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243968915

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23812713

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3856478

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