Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state - Wikidata - wikimedia - TriplyDB

Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state

Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state

http://www.wikidata.org/entity/Q27684301

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The Nucleotide-Binding Sites of SUR1: A Mechanistic Model Cryo-EM Analysis of the Conformational Landscape of Human P-glycoprotein (ABCB1) During its Catalytic Cycle.Structure and mechanism of an active lipid-linked oligosaccharide flippase Structure and Mechanism of the Sphingopyxin I Lasso Peptide Isopeptidase Transporter oligomerization: form and function ATP-dependent substrate transport by the ABC transporter MsbA is proton-coupled ABCB4 missense mutations D243A, K435T, G535D, I490T, R545C, and S978P significantly impair the lipid floppase and likely predispose to secondary pathologies in the human population.Distinct conformational spectrum of homologous multidrug ABC transporters.Full-open and closed CFTR channels, with lateral tunnels from the cytoplasm and an alternative position of the F508 region, as revealed by molecular dynamics.ATP-Binding Cassette Transporter Structure Changes Detected by Intramolecular Fluorescence Energy Transfer for High-Throughput Screening.The Heterodimeric ABC Transporter EfrCD Mediates Multidrug Efflux in Enterococcus faecalis.Structural and Functional Basis for Lipid Synergy on the Activity of the Antibacterial Peptide ABC Transporter McjD.Molecular modelling and molecular dynamics of CFTR.Transmembrane helical interactions in the CFTR channel pore.New Insights into the Biosynthetic Logic of Ribosomally Synthesized and Post-translationally Modified Peptide Natural Products.Spatial positioning of CFTR's pore-lining residues affirms an asymmetrical contribution of transmembrane segments to the anion permeation pathway A single active catalytic site is sufficient to promote transport in P-glycoprotein Exploring conformational equilibria of a heterodimeric ABC transporter.Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP.Unidirectional Transport Mechanism in an ATP Dependent Exporter.Sequential Action of MalE and Maltose Allows Coupling ATP Hydrolysis to Translocation in the MalFGK2 Transporter.Lasso peptide, a highly stable structure and designable multifunctional backbone.Mechanistic diversity in ATP-binding cassette (ABC) transporters.Structural Changes Fundamental to Gating of the Cystic Fibrosis Transmembrane Conductance Regulator Anion Channel Pore.Architecture and functional properties of the CFTR channel pore.Structure of the transporter associated with antigen processing trapped by herpes simplex virus.Effects of a detergent micelle environment on P-glycoprotein (ABCB1)-ligand interactions.Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): CLOSED AND OPEN STATE CHANNEL MODELS.The B1 Protein Guides the Biosynthesis of a Lasso Peptide.Structural basis of MsbA-mediated lipopolysaccharide transport.Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump.Expanding the chemical diversity of lasso peptide MccJ25 with genetically encoded noncanonical amino acids.Insights into the Unique Phosphorylation of the Lasso Peptide Paeninodin.Structural basis for antibacterial peptide self-immunity by the bacterial ABC transporter McjD.Global alteration of the drug-binding pocket of human P-glycoprotein (ABCB1) by substitution of fifteen conserved residues reveals a negative correlation between substrate size and transport efficiency.Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii.ATPase activity regulation by leader peptide processing of ABC transporter maturation and secretion protein, NukT, for lantibiotic nukacin ISK-1.Antibiotics from Gram-negative bacteria: a comprehensive overview and selected biosynthetic highlights.Tyrosine kinase inhibitors enhanced the efficacy of conventional chemotherapeutic agent in multidrug resistant cancer cells.Lasso-inspired peptides with distinct antibacterial mechanisms.

P2860

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P2860

Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state

http://www.wikidata.org/entity/Q27684301

description

2014 nî lūn-bûn

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2014 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2014 թվականի հունիսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Structure of an antibacterial ...... a novel outward occluded state

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Structure of an antibacterial ...... a novel outward occluded state

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Structure of an antibacterial ...... a novel outward occluded state

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type

label

Structure of an antibacterial ...... a novel outward occluded state

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Structure of an antibacterial ...... a novel outward occluded state

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Structure of an antibacterial ...... a novel outward occluded state

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Structure of an antibacterial ...... a novel outward occluded state

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Structure of an antibacterial ...... a novel outward occluded state

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Structure of an antibacterial ...... a novel outward occluded state

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PNAS.1320506111

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Structure of an antibacterial ...... a novel outward occluded state

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P2093

Hassanul G Choudhury

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

Indran Mathavan

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

So Iwata

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

Yanyan Li

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

Zhen Tong

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

P2860

Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding

Flexibility in the ABC transporter MsbA: Alternating access with a twist.

Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot

Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone

Crystal structure of a catalytic intermediate of the maltose transporter

Precursor-centric genome-mining approach for lasso peptide discovery

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides

Structure of a bacterial multidrug ABC transporter

Microcin J25, from the macrocyclic to the lasso structure: implications for biosynthetic, evolutionary and biotechnological perspectives.

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9145-50

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scholarly article

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1712468

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10.1073/PNAS.1320506111

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P433

25

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111

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Konstantinos Beis

Sylvie Rebuffat

Hendrik W van Veen

Séverine Zirah

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2014-06-24T00:00:00Z

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264635222

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24920594

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4078857

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