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

Pannexin 2

PX2, Panx2, Pannexin2
The protein encoded by this gene belongs to the innexin family. Innexin family members are the structural components of gap junctions. This protein and pannexin 1 are abundantly expressed in central nervous system (CNS) and are coexpressed in various neuronal populations. Studies in Xenopus oocytes suggest that this protein alone and in combination with pannexin 1 may form cell type-specific gap junctions with distinct properties. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2009] (from NCBI)
Top mentioned proteins: GAP, CAN, HAD, V1a, OUT
Papers on PX2
Reactivity, characterization of reaction products and immobilization of lead in water and sediments using quercetin pentaphosphate.
New
Sadik et al., Binghamton, United States. In Environ Sci Process Impacts, Feb 2016
The fluorimetric limit of detection was found to be 3.46 × 10(-4) M. The QPP-Pb complex exhibited a corresponding stoichiometry with the predominant complex PX2.
Integrated analysis of gene expression and DNA methylation changes induced by hepatocyte growth factor in human hepatocytes.
New
Yin et al., Xiamen, China. In Mol Med Report, Sep 2015
Furthermore, integration analysis of gene expression and DNA methylation changes revealed novel potential tumor suppressor genes TSGs including MYOCD, PANX2 and LHX9.
Connexins and pannexins in the skeleton: gap junctions, hemichannels and more.
Review
New
Stains et al., Indianapolis, United States. In Cell Mol Life Sci, Aug 2015
Similarly, although the expression of pannexin1, pannexin2 and pannexin3 has been demonstrated in bone and cartilage cells, their function in these tissues is not fully understood.
The role of Pannexin gene variants in schizophrenia: systematic analysis of phenotypes.
New
Stöber et al., Würzburg, Germany. In Eur Arch Psychiatry Clin Neurosci, Aug 2015
We got evidence for linkage of a catatonic phenotype to the PANX2 locus in a family study.
Identification of the Molecular and Genetic Basis of PX2, a Glycosphingolipid Blood Group Antigen Lacking on Globoside-deficient Erythrocytes.
New
Olsson et al., Lund, Sweden. In J Biol Chem, Aug 2015
Based on this linkage, we proposed that x2 joins P in the GLOB blood group system (ISBT 028) and is renamed PX2 (GLOB2).
Pannexin-2 is expressed in the human colon with extensive localization in the enteric nervous system.
New
Liu et al., Sydney, Australia. In Neurogastroenterol Motil, May 2015
BACKGROUND: Pannexin-2 (Panx2) is a member of the novel group of membrane spanning protein channels present in the central nervous system.
Pannexin 1 and pannexin 3 channels regulate skeletal muscle myoblast proliferation and differentiation.
Cowan et al., Ottawa, Canada. In J Biol Chem, 2014
We show here that Panx1 and Panx3, but not Panx2, are present in human and rodent skeletal muscle, and their various species are differentially expressed in fetal versus adult human skeletal muscle tissue.
Molecular cloning, characterization, and expression of pannexin genes in chicken.
Lee et al., Taegu, South Korea. In Poult Sci, 2014
Moreover, expression of the Panx family has been reported in several rodent tissues: Panx1 is ubiquitously expressed in mammals, whereas Panx2 and Panx3 expressions are more restricted.
Pannexin channels and their links to human disease.
Review
Laird et al., London, Canada. In Biochem J, 2014
Although the pannexin family consists of only three members (Panx1, Panx2 and Panx3), one or more of these pannexins are expressed in virtually every mammalian organ, implicating their potential role in a diverse array of pathophysiologies.
Amplification of human platelet activation by surface pannexin-1 channels.
Mahaut-Smith et al., Leicester, United Kingdom. In J Thromb Haemost, 2014
RESULTS: PANX1, but not PANX2 or PANX3, mRNA was detected in human platelets.
Regulation of pannexin channels by post-translational modifications.
Review
Thompson et al., London, Canada. In Febs Lett, 2014
Post-translational modifications have been postulated as some of the regulating mechanisms for Panx1, while Panx2 and Panx3 have not been as well characterized.
The pannexins: past and present.
Review
Naus et al., Bethesda, United States. In Front Physiol, 2013
Three distinct Panx paralogs (Panx1, Panx2, and Panx3) are shared among the major vertebrate phyla, but they appear to have suppressed (or even lost) their ability to directly couple adjacent cells.
Pannexin2 oligomers localize in the membranes of endosomal vesicles in mammalian cells while Pannexin1 channels traffic to the plasma membrane.
Sosinsky et al., San Diego, United States. In Front Cell Neurosci, 2013
Pannexin2 (Panx2) is the largest of three members of the pannexin proteins.
Pannexin 2 protein expression is not restricted to the CNS.
Naus et al., Vancouver, Canada. In Front Cell Neurosci, 2013
Three distinct Panx paralogs (Panx1, Panx2 and Panx3) have been identified in vertebrates but previous reports on Panx expression and functionality focused primarily on Panx1 and Panx3 proteins.
An update on the GLOB blood group system and collection.
Review
Olsson et al., Lund, Sweden. In Immunohematology, 2012
Other related glycolipid structures, the LKE and PX2 antigens, remain in the GLOB blood group collection pending further evidence about the genes and gene products responsible for their synthesis.
Pannexins in ischemia-induced neurodegeneration.
GeneRIF
Schwaninger et al., Lübeck, Germany. In Proc Natl Acad Sci U S A, 2012
Px1 and Px2 underlie channel function in neurons and contribute to ischemic brain damage
Pannexin protein expression in the rat middle cerebral artery.
GeneRIF
Sokoya et al., Houston, United States. In J Vasc Res, 2011
pannexin 2 is expressed in both endothelium and smooth muscle of middle cerebral arteries.
Expression and roles of pannexins in ATP release in the pituitary gland.
GeneRIF
Stojilkovic et al., Bethesda, United States. In Endocrinology, 2011
Overexpression of pannexins 1 and 2 in pituitary cells enhanced the release of ATP.
Pannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other.
GeneRIF
Sosinsky et al., San Diego, United States. In J Biol Chem, 2010
Pannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other
Pannexin 2 is expressed by postnatal hippocampal neural progenitors and modulates neuronal commitment.
GeneRIF
Bennett et al., Ottawa, Canada. In J Biol Chem, 2010
Pannexin 2 is expressed by postnatal hippocampal neural progenitors and modulates neuronal commitment
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