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

Synaptic vesicle glycoprotein 2b

SV2B, synaptic vesicle protein 2B, synaptic vesicle glycoprotein 2b
proton cotransporter; mediates the uptake of neurotransmitters into vesicles [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: SV2, CD45, Synaptophysin, CAN, Rdl
Papers on SV2B
Dynamic gene expression in the song system of zebra finches during the song learning period.
Mello et al., Portland, United States. In Dev Neurobiol, Dec 2015
SV2B, TAC1).
SV2B is essential for the integrity of the glomerular filtration barrier.
Kawachi et al., Niigata, Japan. In Lab Invest, May 2015
We have previously reported that synaptic vesicle protein 2 B (SV2B) is expressed in the podocyte and that the expression is clearly decreased in nephrotic models.
Lack of synaptic vesicle protein SV2B protects against amyloid-β₂₅₋₃₅-induced oxidative stress, cholinergic deficit and cognitive impairment in mice.
Lamberty et al., Braine-le-Comte, Belgium. In Behav Brain Res, 2014
SV2B is a synaptic protein widely distributed throughout the brain, which is part of the complex vesicle protein machinery involved in the regulation of synaptic vesicle endocytosis and exocytosis, and therefore in neurotransmitters release.
Therapeutic target for nephrotic syndrome: Identification of novel slit diaphragm associated molecules.
Kawachi et al., Niigata, Japan. In World J Nephrol, 2014
Then we have found that synaptic vesicle protein 2B, ephrin-B1 and neurexin were already downregulated at the early stage of puromycin aminonucleoside nephropathy, and that these molecules were localized close to nephrin.
Expression pattern of synaptic vesicle protein 2 (SV2) isoforms in patients with temporal lobe epilepsy and hippocampal sclerosis.
Deprez et al., Liège, Belgium. In Neuropathol Appl Neurobiol, 2014
METHODS: SV2A, SV2B and SV2C immunostaining and QuantiGene branched DNA assay were performed on biopsies from 31 consecutive TLE patients with mesial temporal sclerosis (MTS) and compared with 10 autopsy controls.
Loss of photoreceptors results in upregulation of synaptic proteins in bipolar cells and amacrine cells.
Dhingra et al., Gurgaon, India. In Plos One, 2013
The levels of SV2B, a synaptic protein expressed by photoreceptors and bipolar cells, were reduced in whole retina, but increased in the IPL of rd1 mouse.
Identification of a novel fusion gene involving RUNX1 and the antisense strand of SV2B in a BCR-ABL1-positive acute leukemia.
Hébert et al., Montréal, Canada. In Genes Chromosomes Cancer, 2013
This previously unreported rearrangement yields a fusion of RUNX1 with the antisense strand of the SV2B gene, a new translocation partner of RUNX1, resulting in the expression of out-of-frame mRNA chimeric transcripts and the production of putative truncated RUNX1 isoforms.
Double receptor anchorage of botulinum neurotoxins accounts for their exquisite neurospecificity.
Rummel, Hannover, Germany. In Curr Top Microbiol Immunol, 2012
Whereas the 50 kDa cell binding domain H(C) of BoNT/A interacts with all three SV2 isoforms, BoNT/E H(C) only binds SV2A and SV2B.
Altered balance between excitatory and inhibitory inputs onto CA1 pyramidal neurons from SV2A-deficient but not SV2B-deficient mice.
Seutin et al., Liège, Belgium. In J Neurosci Res, 2012
Synaptic vesicle protein 2 (SV2) is a glycoprotein that exists in three isoforms, SV2A, SV2B, and SV2C.
Expression of SV2 isoforms during rodent brain development.
Rogister et al., Liège, Belgium. In Bmc Neurosci, 2012
BACKGROUND: SV2A, SV2B and SV2C are synaptic vesicle proteins that are structurally related to members of the major facilitator superfamily (MFS).
Loss of the SV2-like protein SVOP produces no apparent deficits in laboratory mice.
Bajjalieh et al., Seattle, United States. In Plos One, 2012
To test this, we generated SVOP knockout mice and SVOP/SV2A/SV2B triple knockout mice.
Synaptic vesicle protein 2 (SV2) isoforms.
Lara-Padilla et al., Mexico. In Asian Pac J Cancer Prev, 2011
Furthermore, the genomic expression was consistent with protein expression for a such cell line, but in MDA-MB-231 there was no SV2B genomic expression, and the SV2C mRNA and protein were not found in the non tumoral cell line.
SV2 regulates neurotransmitter release via multiple mechanisms.
Bajjalieh et al., Seattle, United States. In Am J Physiol Cell Physiol, 2010
These results indicate that SV2 performs at least two actions at the synapse that contribute to neurotransmitter release.
SV2 acts via presynaptic calcium to regulate neurotransmitter release.
Heidelberger et al., Houston, United States. In Neuron, 2010
SV2 controls key aspects of synaptic functionality via its ability to regulate presynaptic Ca(2+).
SV2 mediates entry of tetanus neurotoxin into central neurons.
Chapman et al., Madison, United States. In Plos Pathog, 2009
Loss of synaptic vesicle glycoprotein 2b is associated with inhibition of tetanus neurotoxin into central neurons.
Slit diaphragm dysfunction in proteinuric states: identification of novel therapeutic targets for nephrotic syndrome.
Shimizu et al., Niigata, Japan. In Clin Exp Nephrol, 2009
By the subtraction hybridization techniques using glomerular cDNA of normal and proteinuric rats, we detected that synaptic vesicle protein 2B and ephrin B1 are involved in the maintenance of the barrier function of the slit diaphragm.
Therapeutic targets in the podocyte: findings in anti-slit diaphragm antibody-induced nephropathy.
Shimizu et al., Niigata, Japan. In J Nephrol, 2009
Recently, it was found that IP-10, SV2B, ephrin B1 and the receptors of angiotensin II were expressed in the podocyte, and that their expressions were clearly altered in anti-nephrin antibody-induced nephropathy.
Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons.
Chapman et al., Madison, United States. In Mol Biol Cell, 2008
Data demonstrate that glycosylated SV2A and SV2B act in conjunction with gangliosides to mediate the entry of BoNT/E into neurons.
Loss of the Synaptic Vesicle Protein SV2B results in reduced neurotransmission and altered synaptic vesicle protein expression in the retina.
Bajjalieh et al., Portland, United States. In Plos One, 2008
SV2B contributes to the modulation of synaptic vesicle exocytosis and plays a significant role in regulating synaptic protein content
SV2 is the protein receptor for botulinum neurotoxin A.
Chapman et al., Madison, United States. In Science, 2006
findings show that botulinum neurotoxin (BoNT/A) enters neurons by binding to the synaptic vesicle protein SV2 (isoforms A, B, and C);SV2 acts as the protein receptor for BoNT/A
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