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


Top mentioned proteins: CAN, HAD, ACID, OUT, iMpact
Papers on Barrel
The structure of the β-barrel assembly machinery complex.
Noinaj et al., West Lafayette, United States. In Science, Feb 2016
β-Barrel outer membrane proteins (OMPs) are found in the outer membranes of Gram-negative bacteria and are essential for nutrient import, signaling, and adhesion.
Localized Gene Expression Analysis during Sprouting Angiogenesis in Mouse Embryoid Bodies Using a Double Barrel Carbon Probe.
Matsue et al., Sendai, Japan. In Anal Chem, Feb 2016
First, we collected localized cells from the live tissue model embedded in hydrogel using the double barrel carbon probe (DBCP) and quantified mRNA expression.
Management of the Nasal Dorsum: Construction and Maintenance of a Barrel Vault.
Gruber et al., Campbell, United States. In Clin Plast Surg, Jan 2016
The role of the spreader flap and its extension into the bony vault is stressed to re-create the barrel vaultlike nasal architecture.
The TIM Barrel Architecture Facilitated the Early Evolution of Protein-Mediated Metabolism.
Landweber et al., United States. In J Mol Evol, Jan 2016
The triosephosphate isomerase (TIM) barrel protein fold is a structurally repetitive architecture that is present in approximately 10 % of all enzymes.
The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core.
Sousa et al., Boulder, United States. In Structure, Jan 2016
UNASSIGNED: The β-barrel assembly machine (BAM) mediates folding and insertion of integral β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria.
Barrel-shaped ClpP Proteases Display Attenuated Cleavage Specificities.
Sieber et al., Garching bei München, Germany. In Acs Chem Biol, Jan 2016
Our data suggest a mechanism that implicates the barrel-shaped architecture of ClpP not only in shielding the active sites to prevent uncontrolled proteolysis but also in providing high local substrate concentrations to enable efficient proteolytic processing.
Fitting the Pieces of the β-Barrel Assembly Machinery Complex.
Buchanan et al., West Lafayette, United States. In Biochemistry, Nov 2015
β-Barrel membrane proteins are found in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria; however, exactly how they are folded and inserted remains unknown.
The β-Barrel Assembly Machinery Complex.
Lithgow et al., Canberra, Australia. In Methods Mol Biol, 2014
The outer membranes of gram-negative bacteria contain integral membrane proteins, most of which are of β-barrel structure, and critical for bacterial survival.
Structural Aspects of Bacterial Outer Membrane Protein Assembly.
Moraes et al., Toronto, Canada. In Adv Exp Med Biol, 2014
The outer membrane of Gram-negative bacteria is predominantly populated by β-Barrel proteins and lipid anchored proteins that serve a variety of biological functions.
Learning-Dependent Plasticity of the Barrel Cortex Is Impaired by Restricting GABA-Ergic Transmission.
Kossut et al., Warsaw, Poland. In Plos One, 2014
We previously reported an increase in the number of inhibitory markers in the barrel cortex of mice after fear conditioning engaging vibrissae, observed concurrently with enlargement of the cortical representational area of the row of vibrissae receiving conditioned stimulus (CS).
[Research progress on the folding and membrane-insertion mechanisms of beta-barrel outer membrane protein of gram-negative bacteria--a review].
Luo et al., In Wei Sheng Wu Xue Bao, 2014
Beta-Barrel outer membrane proteins are the major components of the outer membrane of Gram-negative bacteria, which are in contact with the extracellular environment directly.
Determination of Radical Scavenging Activity and Total Phenols of Wine and Spices: A Randomized Study.
Shaikh et al., York, United States. In Antioxidants (basel), 2012
Thirty eight bottles of red wine (Carbanet Sauvignon) were randomly selected based on vintage, region, price, and age (number of months in a barrel).
Degringolade, a SUMO-targeted ubiquitin ligase, inhibits Hairy/Groucho-mediated repression.
Orian et al., Haifa, Israel. In Embo J, 2011
In this study, the authors show that Dgrn is a negative regulator of the repressor Hairy and its corepressor Groucho (Gro/transducin-like enhancer (TLE)) during embryonic segmentation and neurogenesis.
Long- and short-range transcriptional repressors induce distinct chromatin states on repressed genes.
Arnosti et al., East Lansing, United States. In Curr Biol, 2011
Hairy induces widespread histone deacetylation and inhibits the recruitment of basal machinery without inducing chromatin compaction.
β-Barrel membrane protein assembly by the Bam complex.
Kahne et al., Cambridge, United States. In Annu Rev Biochem, 2010
β-barrel membrane proteins perform important functions in the outer membranes (OMs) of Gram-negative bacteria and of the mitochondria and chloroplasts of eukaryotes.
Introduction to theme "membrane protein folding and insertion".
von Heijne, Stockholm, Sweden. In Annu Rev Biochem, 2010
This volume of the Annual Review of Biochemistry contains three reviews on current developments in membrane protein research: Grigoryan et al. "Transmembrane Communication: General Principles and Lessons from the Structure and Function of the M2 Proton Channel, K⁺ Channels, and Integrin Receptors," Hagan et al. "β-Barrel Membrane Protein Assembly by the Bam Complex," and Dalbey et al. "Assembly of Bacterial Inner Membrane Proteins."
The bHLH transcription factor, hairy, refines the terminal cell fate in the Drosophila embryonic trachea.
Myat et al., New York City, United States. In Plos One, 2009
Studies demonstrate a novel role for Hairy in restriction of the terminal cell fate by limiting the domain of bnl expression in surrounding muscle cells such that only a single dorsal branch cell becomes specified as a terminal cell.
Genomic mapping of binding regions for the Ecdysone receptor protein complex.
White et al., Chicago, United States. In Genome Res, 2009
Results show that three direct targets of ECR/USP--hairy, vrille, and Hr4--are required for cellular differentiation in response to the hormone.
Mechanisms underlying hypoxia tolerance in Drosophila melanogaster: hairy as a metabolic switch.
Haddad et al., San Diego, United States. In Plos Genet, 2008
hypoxia-selected flies: (a) altered their gene expression and genetic code, and (b) coordinated their metabolic suppression, especially during development, with hairy acting as a metabolic switch, thus playing a crucial role in hypoxia-tolerance
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