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

MAX gene associated

Mga
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Top mentioned proteins: ACID, HAD, CAN, C5a, V1a
Papers on Mga
The Mga Regulon but Not Deoxyribonuclease Sda1 of Invasive M1T1 Group A Streptococcus Contributes to In Vivo Selection of CovRS Mutations and Resistance to Innate Immune Killing Mechanisms.
New
Lei et al., Bozeman, United States. In Infect Immun, Nov 2015
The deletion of emm and a spontaneous Mga mutation in MGAS2221 reduced and prevented in vivo selection for CovRS mutants, respectively.
The Streptococcus pyogenes orphan protein tyrosine phosphatase, SP-PTP, possesses dual specificity and essential virulence regulatory functions.
New
Pancholi et al., Columbus, United States. In Mol Microbiol, Aug 2015
SP-PTP also differentially regulates the expression of ∼50% of the total GAS genes, including several virulence genes potentially through the two-component regulators, CovR, WalR and PTS/HPr regulation of Mga.
Phosphorylation events in the multiple gene regulator of group A Streptococcus significantly influence global gene expression and virulence.
New
Kumaraswami et al., Houston, United States. In Infect Immun, Jun 2015
Whole-genome sequencing analysis of ∼800 strains of group A Streptococcus (GAS) found that the gene encoding the multiple virulence gene regulator of GAS (mga) is highly polymorphic in serotype M59 strains but not in strains of other serotypes.
A naturally occurring single amino acid replacement in multiple gene regulator of group A Streptococcus significantly increases virulence.
New
Olsen et al., Monterrey, Mexico. In Am J Pathol, Feb 2015
Whole-genome sequencing of approximately 800 serotype M59 group A Streptococcus strains, recovered during an outbreak of severe invasive infections across North America, identified a disproportionate number of SNPs in the gene encoding multiple gene regulator of group A Streptococcus (mga).
Mga is essential for the survival of pluripotent cells during peri-implantation development.
Papaioannou et al., New York City, United States. In Development, 2015
The dual specificity T-box/basic-helix-loop-helix-zipper transcription factor Mga is expressed in the pluripotent cells of the inner cell mass (ICM) and epiblast of the peri-implantation mouse embryo, but its function has not been investigated previously.
PTS-Mediated Regulation of the Transcription Activator MtlR from Different Species: Surprising Differences despite Strong Sequence Conservation.
Deutscher et al., Jouy-le-Moutier, France. In J Mol Microbiol Biotechnol, 2014
MtlR contains an N-terminal helix-turn-helix motif followed by an Mga-like domain, two PTS regulation domains (PRDs), an EIIB(Gat)- and an EIIA(Mtl)-like domain.
Natural variation in the promoter of the gene encoding the Mga regulator alters host-pathogen interactions in group a Streptococcus carrier strains.
Musser et al., Houston, United States. In Infect Immun, 2013
We previously reported that two epidemiologically unassociated serotype M3 group A Streptococcus (GAS) carrier strains had an identical 12-bp deletion in the promoter of the gene encoding Mga, a global positive gene regulator.
The pneumococcal MgaSpn virulence transcriptional regulator generates multimeric complexes on linear double-stranded DNA.
Bravo et al., Madrid, Spain. In Nucleic Acids Res, 2013
It is thought to be a member of the Mga/AtxA family of global regulators.
PTS phosphorylation of Mga modulates regulon expression and virulence in the group A streptococcus.
McIver et al., College Park, United States. In Mol Microbiol, 2013
In the group A streptococcus (GAS), the virulence regulator Mga contains homology to phosphotransferase system (PTS) regulatory domains (PRDs) found in sugar operon regulators.
The regulation of jejunal induction of the maltase-glucoamylase gene by a high-starch/low-fat diet in mice.
GeneRIF
Goda et al., Shizuoka, Japan. In Mol Nutr Food Res, 2010
investigation of dietary control of Mgam expression in jejunum: high starch diet induces Mgam through mechanism involving increased acetylation of histones and increased binding of CREBBP, CDX2, and HNF1 to Mgam gene
Mucosal maltase-glucoamylase plays a crucial role in starch digestion and prandial glucose homeostasis of mice.
GeneRIF
Sterchi et al., Houston, United States. In J Nutr, 2009
mucosal alpha-glucogenic activity of Mgam plays a crucial role in the regulation of prandial glucose homeostasis
Correlations between carbon metabolism and virulence in bacteria.
Review
Deutscher et al., Paris, France. In Contrib Microbiol, 2008
For example, expression of the gene encoding the Streptococcus pyogenes virulence regulator Mga is controlled by the classical carbon catabolite repression (CCR) mechanism operative in Firmicutes.
Stand-alone response regulators controlling global virulence networks in streptococcus pyogenes.
Review
McIver, College Park, United States. In Contrib Microbiol, 2008
The 'stand-alone' regulators Mga, RofA-like proteins (RALPs), and RopB/Rgg control important and diverse virulence regulons in response to growth-related signals and other environmental conditions in GAS.
The Mga virulence regulon: infection where the grass is greener.
Review
McIver et al., College Park, United States. In Mol Microbiol, 2007
Mga represents a ubiquitous stand-alone virulence regulator that controls genes (Mga regulon) whose products are necessary for adherence, internalization and host immune evasion.
Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis.
GeneRIF
Nichols et al., San Luis Potosí, Mexico. In J Nutr, 2007
The alpha-glucogenic activities of the jejunal mucosa with and without added recombinant pancreatic alpha-amylase, using a range of food starch substrates are reported.
P-Ser-HPr--a link between carbon metabolism and the virulence of some pathogenic bacteria.
Review
Poncet et al., France. In Biochim Biophys Acta, 2006
In S. pyogenes, the expression of several virulence genes depends on the transcription activator Mga.
The Mad side of the Max network: antagonizing the function of Myc and more.
Review
Lüscher et al., Aachen, Germany. In Curr Top Microbiol Immunol, 2005
Mad family members, including Mad1, Mxi1, Mad3, Mad4, Mnt, and Mga, function in part as antagonists of Myc oncoproteins.
A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells.
Impact
Nakatani et al., Boston, United States. In Science, 2002
E2F-6 is found in a multimeric protein complex that contains Mga and Max, and thus the complex can bind not only to the E2F-binding site but also to Myc- and Brachyury-binding sites.
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