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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Cholinergic receptor, nicotinic, beta polypeptide 1

The muscle acetylcholine receptor is composed of five subunits: two alpha subunits and one beta, one gamma, and one delta subunit. This gene encodes the beta subunit of the acetylcholine receptor. The acetylcholine receptor changes conformation upon acetylcholine binding leading to the opening of an ion-conducting channel across the plasma membrane. Mutations in this gene are associated with slow-channel congenital myasthenic syndrome. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, HAD, OUT, V1a
Papers using CHRNB1 antibodies
Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances.
Sandler Steve J., In PLoS ONE, 2007
... The custom polyclonal rabbit anti-AcrB was ordered from GenScript (Piscataway, NJ), produced following ...
Papers on CHRNB1
Aminoacyl β-naphthylamides as substrates and modulators of AcrB multidrug efflux pump.
Nikaido et al., Monserrato, Italy. In Proc Natl Acad Sci U S A, Feb 2016
UNASSIGNED: Efflux pumps of the resistance-nodulation division superfamily, such as AcrB, make a major contribution to multidrug resistance in Gram-negative bacteria.
Pseudoatomic Structure of the Tripartite Multidrug Efflux Pump AcrAB-TolC Reveals the Intermeshing Cogwheel-like Interaction between AcrA and TolC.
Ha et al., Taejŏn, South Korea. In Structure, Feb 2016
The three essential components, AcrA, AcrB, and TolC, must function in concert with each respective binding partner within the complex.
Transcriptional feedback regulation of efflux protein expression for increased tolerance to and production of n-butanol.
Tullman-Ercek et al., Berkeley, United States. In Metab Eng, Jan 2016
We test the promoter in the context of the efflux pump AcrB and its butanol-secreting variant, AcrBv2.
Differential impact of ramRA mutations on both ramA transcription and decreased antimicrobial susceptibility in Salmonella Typhimurium.
Vila et al., Barcelona, Spain. In J Antimicrob Chemother, Jan 2016
Moreover, the impact of such mutations on impairing the transcription of ramA, acrB, tolC and acrF was also assessed as was the impact on the resistance or decreased susceptibility phenotype.
Binding site feature description of 2-substituted benzothiazoles as potential AcrAB-TolC efflux pump inhibitors in E. coli.
Yalcin et al., Ankara, Turkey. In Sar Qsar Environ Res, Oct 2015
In order to describe the binding site features of these BSN compounds with AcrB, docking studies were performed using the CDocker method.
The pseudo-atomic structure of an RND-type tripartite multidrug efflux pump.
Luisi et al., In Biol Chem, Sep 2015
We describe recent structural and functional data that have provided insights into the architecture and transport mechanism of the AcrA-AcrB-TolC pump of Escherichia coli.
RND-type drug efflux pumps from Gram-negative bacteria: molecular mechanism and inhibition.
Ma et al., Adelaide, Australia. In Front Microbiol, 2014
Recent successes on the structure determination and functional analysis of the AcrB and MexB components of the AcrAB-TolC and MexAB-OprM drug efflux systems as well as the structure of the fully assembled, functional triparted AcrAB-TolC complex significantly contributed to our understanding of the mechanism of substrate transport and the options for inhibition of efflux.
Structure of the AcrAB-TolC multidrug efflux pump.
Luisi et al., Houston, United States. In Nature, 2014
This pump assembly comprises the outer-membrane channel TolC, the secondary transporter AcrB located in the inner membrane, and the periplasmic AcrA, which bridges these two integral membrane proteins.
Efflux pump-mediated antibiotics resistance: insights from computational structural biology.
Kandt et al., Bonn, Germany. In Interdiscip Sci, 2014
Here we review the employment of molecular dynamics computer simulations to investigate RND efflux pumps focusing on our group's recent contributions to this field studying questions of energy conversion and substrate transport in the inner membrane antiporter AcrB in Escherichia coli as well as access regulation and gating mechanism in the outer membrane efflux ducts TolC and OprM in E. coli and Pseudomonas aeruginosa.
Structural basis for the inhibition of bacterial multidrug exporters.
Yamaguchi et al., Ibaraki, Japan. In Nature, 2013
The multidrug efflux transporter AcrB and its homologues are important in the multidrug resistance of Gram-negative pathogens.
RND efflux pumps: structural information translated into function and inhibition mechanisms.
Vargiu et al., Monserrato, Italy. In Curr Top Med Chem, 2012
Most of these studies focused on the RND drug/proton antiporter AcrB, part of the AcrAB-TolC efflux pump actively recognizing and expelling noxious agents from the interior of bacteria.
Broad-specificity efflux pumps and their role in multidrug resistance of Gram-negative bacteria.
Pagès et al., Berkeley, United States. In Fems Microbiol Rev, 2012
The recent investigation on the efflux pump AcrB at its structural and physiological levels, including the identification of drug affinity sites and kinetic parameters for various antibiotics, may pave the way towards the rational development of an improved new generation of antibacterial agents as well as efflux inhibitors in order to efficiently combat efflux-based resistance mechanisms.
Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket.
Yamaguchi et al., Ibaraki, Japan. In Nature, 2012
AcrB and its homologues are the principal multidrug transporters in Gram-negative bacteria and are important in antibiotic drug tolerance.
The local anaesthetics proadifen and adiphenine inhibit nicotinic receptors by different molecular mechanisms.
Bouzat et al., Bahía Blanca, Argentina. In Br J Pharmacol, 2009
The local anaesthetics proadifen and adiphenine inhibit nicotinic receptors by different molecular mechanisms.
Binding to gating transduction in nicotinic receptors: Cys-loop energetically couples to pre-M1 and M2-M3 regions.
Sine et al., Rochester, United States. In J Neurosci, 2009
Extracellular beta1-beta2 and cysteine-loops bridge the pre-M1 transmembrane domain and M2-M3 linker to transduce agonist binding into channel gating.
Decremental response to high-frequency trains of acetylcholine pulses but unaltered fractional Ca2+ currents in a panel of "slow-channel syndrome" nicotinic receptor mutants.
Grosman et al., Champaign, United States. In J Gen Physiol, 2009
In V266M mutant the peak-current amplitude decreases along trains of nearly saturating ACh pulses delivered at physiologically relevant frequencies, consistent with enhanced entry into desensitization in congenital myasthenic syndrome.
Mutation analysis of CHRNA1, CHRNB1, CHRND, and RAPSN genes in multiple pterygium syndrome/fetal akinesia patients.
Maher et al., Birmingham, United Kingdom. In Am J Hum Genet, 2008
No CHRNA1, CHRNB1, or CHRND mutations were detected, but a homozygous RAPSN frameshift mutation, c.1177-1178delAA, was identified in a family with three children affected with lethal fetal akinesia sequence.
Synaptic differentiation is defective in mice lacking acetylcholine receptor beta-subunit tyrosine phosphorylation.
Burden et al., New York City, United States. In Development, 2007
Tyrosine phosphorylation of the acetylcholine receptor (AChR) beta-subunit is important in organizing AChRs and regulating synaptic differentiation.
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism.
Yamaguchi et al., Ibaraki, Japan. In Nature, 2006
AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA.
Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump.
Koshland et al., Berkeley, United States. In Science, 2003
We obtained x-ray crystallographic structures of the trimeric AcrB pump from Escherichia coli with four structurally diverse ligands.
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