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SNAP Receptor

Q: How can research on the SNAP Receptor provide insights into neurological disorders?

Research on the SNAP Receptor can provide valuable insights into the mechanisms of synaptic function and neurological disorders. By studying the SNAP Receptor, researchers can gain a better understanding of the processes involved in synaptic transmission and how disruptions in these pathways can contribute to neurological conditions.

Q: Are there different variations or types of the SNAP Receptor, and how do they differ?

The SNAP Receptor, or SV2A, is a single protein found in synaptic vesicles. However, there are some genetic variations or isoforms of the SNAP Receptor that can have slight differences in their structure and function. Understanding these variations can be important for specific applications or targeted therapies related to the SNAP Receptor.

The SNAP Receptor, also known as the Synaptic Vesicle Protein 2A (SV2A), is a transmembrane protein found in synaptic vesicles of neurons.
It plays a crucial role in the regulation of neurotransmitter release and synaptic transmission.
The SNAP Receptor is an important target for the development of antiepileptic drugs, as it is the binding site for the widely used anticonvulsant levetiracetam.
Resesearch on the SNAP Receptor can provide valuable insights into the mechanisms of synaptic function and neurological disorders, and PubCompare.ai's AI-driven platform can optimize this research by locating the best literature, pre-prints, and patents through intelligent comparisons.
Explore PubCompare.ai today and take your SNAP Receptor studies to new hights.

Most cited protocols related to «SNAP Receptor»

Drosophila Climbing and Clonal Analyses

Cited 19 times

Flies were maintained on standard yeast/cornmeal/agar media. In climbing tests, a total of 90 adults per genotype were recorded and scored in cohorts of three to six flies, after tapping them down in a plastic graduated cylinder (Juhász et al., 2007 (link)). In clonal analyses, RNAi cells were generated spontaneously in larvae carrying hs-Flp; upstream activation sequence (UAS)-Dcr2; Actin>CD2>Gal4 UAS-RNAi (and UAS-GFP or UAS-LAMP1-GFP as a knockdown cell marker), and mutant cell clones (marked by lack of GFP expression) were generated by heat shocking 2–4-h embryos of the genotype hs-Flp; ubi-GFP FRT2A/Syx17[LL] FRT2A in a 38°C water bath for 1 h (Juhász et al., 2007 (link), 2008 (link); Pircs et al., 2012 (link)). Expression of mCherry-Atg8a was driven by a fat body–specific r4 promoter in our screen (transgenic flies were provided by T. Neufeld, University of Minnesota, Minneapolis, MN; Pircs et al., 2012 (link)). We used the GFP knockin line dLAMP[CPTI001775] (Drosophila Genetic Resource Center) to label lysosomes, w[1118] as control, UAS-GFP-KDEL and Pdi[G00198] as ER reporters (Bloomington Drosophila Stock Center), Atg2[EP3697] (Berry and Baehrecke, 2007 (link)), Atg7[d77]/Atg7[d14] (Juhász et al., 2007 (link)) mutants, and SNARE loss-of-function strains listed in Table S1. Knockdown of usnp was induced by Actin-Gal4 for Western blots and collagen-Gal4 for EM in L3 stage larvae, and overexpression of UAS-p35 or UAS-DIAP1 in adult neurons was mediated by elav-Gal4 (all obtained from Bloomington Drosophila Stock Center).

Takáts S., Nagy P., Varga Á., Pircs K., Kárpáti M., Varga K., Kovács A.L., Hegedűs K, & Juhász G. (2013). Autophagosomal Syntaxin17-dependent lysosomal degradation maintains neuronal function in Drosophila. The Journal of Cell Biology, 201(4), 531-539.

Publication 2013

Actins Adult Agar Animals, Transgenic Bath Berries Cells Clone Cells Collagen Diptera Drosophila Embryo Fat Body Genotype Larva lysosomal-associated membrane protein 1, human Lysosomes Neurons RNA Interference Saccharomyces cerevisiae SNAP Receptor Strains TNFRSF10D protein, human Western Blot

Structural Determination of SNARE Complex

Cited 16 times

All SNARE monomers were separately expressed from pET28a as His₆-tagged proteins in E. coli Bl21 (DE3) cells and purified by Ni²⁺-NTA and ion exchange chromatography. SNARE complexes were then assembled from monomers and purified by ion exchange and size exclusion chromatography. Diffraction data were collected on beamline X10SA at the Swiss Light Source of the Paul Scherrer Institut (Switzerland) and processed with HKL2000. Initial phases were obtained from single-wavelength anomalous dispersion data from crystals containing selenomethionine-labelled syntaxin 1A that diffracted to 4.3 Å resolution. For the final model building native diffraction data to a resolution of 3.4 Å were used. Model building and refinement were performed using the programs COOT and Phenix, respectively.

Stein A., Weber G., Wahl M.C, & Jahn R. (2009). Helical extension of the neuronal SNARE complex into the membrane. Nature, 460(7254), 525-528.

Publication 2009

Cells Escherichia coli Proteins Gel Chromatography Ion-Exchange Chromatographies Ion Exchange Light Selenomethionine SNAP Receptor Syntaxin-1A

Limitations in Computational Protein Structure Prediction

Cited 13 times

As with any new method, it is important when interpreting the results (our large set of predicted complex structures) to keep in mind the limitations of the approach. First, our study is not comprehensive, so conclusions should not be drawn about absences; in particular we eliminated proteins that arose from recent duplication due to difficulty in identifying orthologs in other organisms, and thus only surveyed 2/3 of the entire yeast proteome. Second, the approach likely misses interactions restricted to a small set of organisms, or which vary rapidly during evolution, due to weaker co-evolutionary signals. Third, the approach likely works less well for transient interactions which generally involve smaller and weaker interfaces which may be under lower selective pressure, in particular those involving intrinsically disordered regions which are poorly represented in the PDB. The majority of known interactions identified by our approach are likely obligate assemblies and involve ordered structural elements. Fourth, interactions between single hydrophobic or amphipathic helices, such as single transmembrane helices or coiled coils, may be overpredicted (in initial studies of human complexes, interactions solely between single-pass transmembrane regions appear to be over represented). Fifth, and perhaps most importantly, for proteins that form high-order obligate protein complexes, binary complex models may be quite inaccurate, as illustrated by the SNARE example.

Humphreys I.R., Pei J., Baek M., Krishnakumar A., Anishchenko I., Ovchinnikov S., Zhang J., Ness T.J., Banjade S., Bagde S.R., Stancheva V.G., Li X.H., Liu K., Zheng Z., Barrero D.J., Roy U., Kuper J., Femández I.S., Szakal B., Branzei D., Rizo J., Kisker C., Greene E.C., Biggins S., Keeney S., Miller E.A., Fromme J.C., Hendrickson T.L., Cong Q, & Baker D. (2021). Computed Structures of core eukaryotic protein complexes. Science (New York, N.Y.), 374(6573), eabm4805.

Publication 2021

Biological Evolution Helix (Snails) Homo sapiens Hydrophobic Interactions Pressure Proteins Proteome Saccharomyces cerevisiae SNAP Receptor Transients

Reconstitution of SNARE-Mediated Membrane Fusion

Cited 13 times

The SNARE proteins were essentially isolated as previously described (Mima et al., 2008 (link)). Vti1p and Nyv1p were gel-filtered into RB150/ß-OG (20 mM HEPES, pH 7.4, 150 mM NaCl, 10% glycerol [vol/vol], 1% [wt/vol] ß-octyl glucoside) after purification using Sephacryl S-200 HR (GE Healthcare Biosciences, Pittsburgh, PA). A complete detergent exchange was confirmed by determining the 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS) concentrations in elution fractions (Urbani and Warne, 2005 (link)); only fractions with no residual amounts of CHAPS were pooled and used in the reconstitution experiments. Ypt7p (Hickey et al., 2009 (link)), Sec17p (Schwartz and Merz, 2009 (link)), His₆-Sec18p (Haas and Wickner, 1996 (link)), and HOPS (Hickey and Wickner, 2010 (link)) were isolated as previously described.

Zucchi P.C, & Zick M. (2011). Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis. Molecular Biology of the Cell, 22(23), 4635-4646.

Publication 2011

3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Detergents Glycerin HEPES Humulus Mima octyl glucoside propylsulfonic acid RB150 SNAP Receptor Sodium Chloride

Proteoliposome Preparation for Fusion Assay

Cited 11 times

Proteoliposomes for content-mixing assays were prepared by detergent dialysis in RB150/Mg²⁺ (20 mM HEPES-NaOH, pH 7.4, 150 mM NaCl, 1 mM MgCl₂, 10% glycerol [vol/vol]) as described (Zucchi and Zick, 2011 (link)) from lipid mixes mimicking the vacuolar composition (43.6 mol% 1,2-dilinoleoyl-sn-glycero-3-phosphocholine, 18 mol% 1,2-dilinoleoyl-sn-glycero-3-phosphoethanolamine, 18 mol% soy l-α-phosphatidylinositol, 4.4 mol% 1,2-dilinoleoyl-sn-glycero-3-phospho-l-serine, 2 mol% 1,2-dilinoleoyl-sn-glycero-3-phosphate, 1 mol% 16:0 1,2-dipalmitoyl-sn-glycerol [all from Avanti Polar Lipids, Alabaster, AL]; 8 mol% ergosterol [Sigma-Aldrich, St. Louis, MO], 1 mol% each of di-C16 phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate [Echelon Biosciences] and 3 mol% 7-nitrobenz-2-oxa-1,3-diazole [NBD]–1,2-dipalmitoyl-sn-glycero-3-phosphatidylethanolamine [DPPE; Life Technologies, Carlsbad, CA]) for donor liposomes or 3 mol% Marina-Blue-DPPE for acceptor, subsets of the four vacuolar SNAREs, and Ypt7p, entrapping Cy5-labeled streptavidin or biotinylated R-phycoerythrin. Molar protein:lipid ratio was 1:2500 for SNAREs and 1:2000 for Ypt7p. Isolation after reconstitution was achieved by floatation on a three-step Histodenz gradient (35, 25% Histodenz [wt/vol] and RB150/Mg²⁺). Histodenz (Sigma-Aldrich) solutions were prepared as 70% stock solution in modified RB150/Mg²⁺ with a reduced concentration (2% [vol/vol]) of glycerol to compensate for the osmotic activity of the density medium; lower-concentration solutions were obtained by dilution with RB150/Mg²⁺. RPLs for experiments based on lipid dequenching were prepared with 1.5 mol% of NBD-DPPE and rhodamine-DPPE for donor RPLs and without fluorescent lipids for acceptor RPLs. RPLs for experiments based on tethering via streptavidin were prepared with 0.1 mol% 18:1 Biotinyl Cap PE (1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(cap biotinyl) [Avanti Polar Lipids]) and without entrapped content markers.

Zick M, & Wickner W. (2013). The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes. Molecular Biology of the Cell, 24(23), 3746-3753.

Publication 2013

1,2-dipalmitoyl-3-phosphatidylethanolamine 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine-N-(7-nitro-2-1,3-benzoxadiazol-4-yl) Alabaster Biological Assay bis(diphenylphosphine)ethane Detergents Dialysis dioleoyl cephalin Ergosterol Glycerin Glycerylphosphorylcholine HEPES isolation Lipids Liposomes Magnesium Chloride Molar Osmosis Phosphates Phosphatidylethanolamines phosphatidylinositol 3-phosphate Phosphatidylinositols Phycoerythrin Proteins proteoliposomes RB150 Rhodamine Serine SNAP Receptor Sodium Chloride Streptavidin Technique, Dilution Tissue Donors Vacuole

Most recents protocols related to «SNAP Receptor»

Milk Yield and Mammary Biopsy in Sows

Feed intake of sows was recorded daily, and the litter size and live weight of piglets were recorded weekly, from which the milk yield was estimated using the equations developed by Hansen et al. [7 (link)]. On d 10 and d 17 of lactation, both milk samples and mammary biopsies were collected 4 to 5 h after morning feeding, and milk samples were collected first, while the sows were held by snare restraint. The milk samples were collected after ear vein injection of 0.3 mL (10 IU/mL) oxytocin (Løvens Kemiske Fabrik, Ballerup, Denmark). The mammary biopsies were collected from three selected glands using a Manan Pro-Mag 2.2 biopsy gun with a 14-gauge needle (Medical Device Technologies, Gainesville, FL, USA) after washing, wiping with ethanol, and application of local anesthesia according to the method described by Theil et al. [21 (link)]. Approximately 20 mg biopsy was collected, immediately frozen in liquid nitrogen, and then transferred to −80 ℃ to store for later analysis of mRNA expression.

Zhe L., Krogh U., Lauridsen C., Nielsen M.O., Fang Z, & Theil P.K. (2023). Impact of dietary fat levels and fatty acid composition on milk fat synthesis in sows at peak lactation. Journal of Animal Science and Biotechnology, 14, 42.

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Publication 2023

ARID1A protein, human Biopsy Ethanol Feed Intake Freezing Lactation Local Anesthesia Mammary Gland Medical Devices Milk Needle Biopsies Nitrogen Oxytocin RNA, Messenger SNAP Receptor Veins

Bursting Strength Analysis of Fabric Samples

Bursting strength tests were employed to investigate the mechanical properties of TC, TC-DY, and TC-DY-TA fabrics via an electronic fabric strength tester from Hongda Experiment Instructions Co. Ltd (Nantong, China). Bursting strength values were determined by the constant-rate-of-traverse (CRT) ball burst method according to GB/T 19,976 (2005). Briefly, samples were cut into 80 mm diameter circles to cover the ring snare mechanism with an inner diameter of 45 mm. A polished steel ball with a diameter of 25 mm was pressed into the fabric sample through a ring snare mechanism at 300 mm/min. The force required for penetrating each sample was recorded.

Jiang C., Dejarnette S., Chen W., Scholle F., Wang Q, & Ghiladi R.A. (2023). Color-variable dual-dyed photodynamic antimicrobial polyethylene terephthalate (PET)/cotton blended fabrics. Photochemical & Photobiological Sciences.

Publication 2023

SNAP Receptor Steel

Prepyloric Submucosal Tumor Endoscopic Resection

Endoscopic ultrasonography (EUS) was routinely performed to determine the lesion origin. Patients were maintained in the left lateral position, and general anesthesia was administered using mechanical ventilation. All procedures were carried out by three experienced endoscopists with experience with over 300 ESD cases and 300 STER cases. ESD procedure was carried out using the following steps: marking–injection–circumferential incision–submucosal dissection. Of note, the post-ESD wound was closed using metal clips if the GWD occurred during the procedure.
The P-STER procedure was carried out as follows: (1) Several milliliters of a mixture solution (100 mL saline + 2 mL indigo carmine + 1 mL epinephrine) was injected 3–4 cm proximal to the prepyloric SMTs with an injection needle (NM-4L-1, Olympus; Figures 1(a), 1(b), and 1(c)); (2) an inverted T incision as described previously was made as the tunnel entrance [5 (link)] (Figure 1(d)); (3) a tunnel was created between the mucosal and MP layer with the triangular knife and the tunnel ended at 1 cm distal to the prepyloric SMTs (Figures 1(e) and 1(f)); (4) an insulation-tip knife (KD611L, IT2, Olympus), a triangular knife, or a snare (ASM-1-S or ASJ-1-S, Cook, Limerick, Ireland) was used to remove the prepyloric SMT after it was completely exposed (Figures 1(g) and 1(h)); and (5) the incision was closed with clips (HX-610-135, Olympus) after examination of the tunnel (Figure 1(i)). Of note, the endoscopists could chose the full-thickness resection of MP if the lesion originated from the MP layer. The specimen was routinely pinned at a rubber plate for size measurement followed by fixing into formalin for histopathological evaluation.
Moreover, the snare could be used to remove the lesion at the discretion of the endoscopists in both the ESD and P-STER procedures, if operation difficulty was encountered in the final stage of the procedure.

Zhang W., Wang J., Chai N, & Linghu E. (2023). Comparison between Submucosal Tunneling Endoscopic Resection and Endoscopic Submucosal Dissection for Prepyloric Submucosal Tumors: A Case-Matched Controlled Study. Gastroenterology Research and Practice, 2023, 5931360.

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Publication 2023

Clip Dissection Epinephrine Formalin General Anesthesia Indigo Carmine Mechanical Ventilation Metals Mucous Membrane Needles Patients Reproduction Rubber Saline Solution SNAP Receptor Wounds

Phylogenetic Analysis of C. elegans SNARE Proteins

For this study, about 30 C. elegans SNARE and SNARE-associated protein sequences were retrieved directly from WormBase based on previous annotation (https://wormbase.org) (accessed on 11 May 2022) [28 (link)]. The protein sequences of their closest human orthologs were retrieved from UniProt (https://www.uniprot.org) (accessed on 11 May 2022). Initially, the protein sequences obtained were aligned using Clustal Omega, which also gave a neighbor-joining tree without distance corrections (https://www.ebi.ac.uk/Tools/msa/clustalo/) (accessed on 12 May 2022) [66 (link)]. The phylogenetic tree data obtained from Clustal Omega were then further annotated using iTOL (https://itol.embl.de) (accessed on 8 August 2022). Particularly, the unrooted display mode was selected using the equal-angle algorithm by default [29 (link)].

Gkikas I., Daskalaki I., Kounakis K., Tavernarakis N, & Lionaki E. (2023). MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging in C. elegans. International Journal of Molecular Sciences, 24(4), 4230.

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Publication 2023

Amino Acid Sequence Homo sapiens NR4A2 protein, human SNAP Receptor Trees

Subcellular Localization of SNARE Proteins

To predict subcellular localization and mitochondrial targeting signals between SNARE proteins we analyzed protein sequences retrieved from WormBase using DeepLoc 2.0(DTU Health Tech, Lyngby, Denmark) (https://services.healthtech.dtu.dk/service.php?DeepLoc-2.0) (accessed on 16 July 2022), MitoProt II (Institute of Human Genetics, Munich, Germany) (https://ihg.helmholtz-muenchen.de/ihg/mitoprot.html) (accessed on 29 July 2022) and iMLP Technical University of Kaiserslautern, Kaiserslautern, Germany) (http://imlp.bio.uni-kl.de/) (accessed on 26 August 2022) tools [35 (link),36 (link),37 (link)].

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Publication 2023

Amino Acid Sequence Mitochondria Mitochondrial Proteins SNAP Receptor

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What is the SNAP Receptor and what is its function?

How can research on the SNAP Receptor provide insights into neurological disorders?

What are some common challenges in SNAP Receptor research, and how can PubCompare.ai help?

One of the key challenges in SNAP Receptor research is efficiently screening and comparing the vast amount of available literature, preprints, and patents to identify the most relevant and effective protocols. PubCompare.ai's AI-driven platform can assist researchers by helping them screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform's intelligent comparisons can highlight key differences in protocol effectiveness, enabling researchers to choose the best option for reproducibility and accuracy in their SNAP Receptor studies.

Are there different variations or types of the SNAP Receptor, and how do they differ?

How can PubCompare.ai help optimize SNAP Receptor research protocols?

PubCompare.ai's AI-driven platform can help optimize SNAP Receptor research protocols in several ways. Firstly, it allows researchers to screen the protocol literature more efficiently, saving time and resources. Secondly, the platform's AI-powered analysis can help identify the most effective protocols by highlighting key differences in their effectiveness. This enables researchers to choose the best option for reproducibility and accuracy in their SNAP Receptor studies. By leveraging PubCompare.ai, researchers can take their SNAP Receptor studies to new hights and unlock the full potential of their research.

More about "SNAP Receptor"

The Synaptic Vesicle Protein 2A (SV2A), also known as the SNAP Receptor, is a crucial transmembrane protein found in the synaptic vesicles of neurons.
It plays a pivotal role in regulating neurotransmitter release and synaptic transmission, making it an essential component of neuronal communication and function.
Researchers have a keen interest in the SNAP Receptor as it is a prime target for the development of antiepileptic drugs.
The widely used anticonvulsant levetiracetam, for instance, binds to the SNAP Receptor, highlighting its therapeutic potential.
By understanding the mechanisms and dynamics of the SNAP Receptor, scientists can gain valuable insights into the underlying processes of synaptic function and neurological disorders.
To optimize SNAP Receptor research, PubCompare.ai's AI-driven platform offers an innovative solution.
This cutting-edge technology can help researchers locate the best available literature, pre-prints, and patents through intelligent comparisons.
By utilizing PubCompare.ai, researchers can streamline their SNAP Receptor studies and uncover new avenues for exploration.
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These components and technologies can provide complementary insights and tools for advancing SNAP Receptor research.
By leveraging the power of PubCompare.ai and exploring the broader landscape of related topics, researchers can take their SNAP Receptor studies to new hights and unlock the full potential of this critical synaptic protein.