Ask about this productRelated genes to: SNAP25 antibody
- Gene:
- SNAP25 NIH gene
- Name:
- synaptosome associated protein 25
- Previous symbol:
- SNAP
- Synonyms:
- SNAP-25, RIC-4, RIC4, SEC9, bA416N4.2, dJ1068F16.2
- Chromosome:
- 20p12.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-01-24
- Date modifiied:
- 2016-10-05
Related products to: SNAP25 antibody
Related articles to: SNAP25 antibody
- Alzheimer's disease (AD) is characterized by synaptopathy, a neuropathological feature that can contribute to underlying cognitive decline. Here, we evaluate potential cerebrospinal fluid (CSF) and blood-based synaptic biomarkers in AD dementia and its earliest clinical stage, mild cognitive impairment (MCI). - Source: PubMed
Gaur AmishWong MelissaChen Jinghan JennyKang YejinTahoulas DanielleJeor KomalpreetRaguram Keeirah HGallagher DamienRapoport MarkHerrmann NathanLanctôt Krista L - Developmental and epileptic encephalopathies (DEEs) with early burst-suppression EEG (EIDEE-BS) are among the most severe neonatal epileptic syndromes, typically presenting in the first months of life with refractory seizures and profound neurodevelopmental impairment. Although variants in the , , and genes are recognized as major causes, the full genetic spectrum remains uncertain. We aimed to delineate the electroclinical characteristics, genetic etiologies, and long-term outcomes in a large MRI-negative EIDEE-BS cohort. - Source: PubMed
Publication date: 2026/05/26
Riccardi FlorenceDesnous BéatriceBorloz EmilieLepine AnneLacoste CarolineMignon-Ravix CécileCacciagli PierreMissirian ChantalMolinari FlorenceMortreux JérémieAfenjar AlexandraAltuzarra CéciliaAuvin StéphaneBar ClaireBarth MagalieBiscaye StéphanieBourel-Ponchel EmilieCabasson SébastienCances ClaudeCastelnau PierreCaubel IsabelleCarneiro MarylineChabrol BrigitteChadie AlexandraChaussenot AnnabelleCheuret EmmanuelChouchane MondherCogné BenjaminColin EstelleDemurger FlorenceDesportes VincentDieux-Coeslier AnneDoummar DianeGoizet CyrilGoldenberg AliceGhoumid JamalGuerrot Anne-MarieHerenger YvanHeron DelphineHorvath GabriellaIlunga SergeIsidor BertrandJeanne MédéricJulia SophieKaminska AnnaLagrue EmmanuelleLambert LaetitiaLebre Anne-SophieLefranc JérémieLesca GaëtanLevrat VirginieMansour HichamMarey IsabelleMarret StéphaneMaurey HélèneMetreau JuliaMignot CyrilNaudion SophieNeveu JulienPatat OlivierPasquier LaurentPerrier Julie BoeswillwaldPetit FlorencePoulat Anne-LiseQuélin ChloéRichelme ChristianRollier PaulRondeau StéphaneRoubertie AgatheSchaefer EliseDe Saint-Martin AnneThauvin ChristelTorre StéphanieToutain AnnickVan Coster RudyVille Dorothée MVilleneuve NathalieVillard LaurentMilh Mathieu - Botulinum neurotoxins (BoNTs) act on peripheral cholinergic nerve terminals, inducing reversible muscle paralysis and profound therapeutic effects. However, their limited cell-type specificity and narrow therapeutic window have motivated the development of engineered variants. Here, a modular strategy was employed to construct full-length chimeric BoNTs, grafting receptor-binding segments from BoNT/B or BoNT/F onto the BoNT/A framework. The novel chimeras AAAF and AAFF efficiently cleaved rSNAP-25 in cell-free assays. Firstly, both toxins showed effective cellular uptake and cleaved endogenous SNAP-25 in Neuro-2a cells, with cleavage efficiencies of approximately 46% for AAAF and 73% for AAFF, highlighting the enhanced activity of AAFF. Secondly, AAAF induced faster recovery from reversible muscle paralysis compared to rBoNT/A-WT, whereas AAFF produced more sustained paralysis, with both exhibiting reduced systemic toxicity. Despite these altered pharmacological profiles, the chimeras required higher doses than rBoNT/A-WT to induce neuromuscular effects. Collectively, this study presents the design of novel chimeric BoNT/A-F proteins, characterizes their functional activities, and provides a preliminary exploration of how domain grafting affects cellular uptake, enzymatic activity, and neuromuscular pharmacodynamics. - Source: PubMed
Publication date: 2026/04/29
Pan SihanYe YuanzhiLi YangFu HongxinWang Jufang - Current proteomic analyses of presynaptic compartments largely rely on synaptosome fractions prepared from whole brain or dissected brain regions. However, the accurate identification of proteins that are truly enriched at presynaptic sites is limited by the purification efficiency and the intrinsic heterogeneity of synaptosome preparations. Alternative approaches that achieve higher spatial specificity are therefore required. Here, we established an in situ proximity biotinylation platform based on APEX2 to profile the proteomes of presynaptic boutons and their neighboring axons in living neurons. In cultured hippocampal neurons, presynaptic boutons were selectively labeled using APEX2-Synapsin 1, whereas axonal regions including presynaptic boutons were labeled using APEX2-SNAP-25, enabling compartment-resolved proteomic comparison. Through quantitative mass spectrometry and systematic analysis, we selected approximately 500 proteins that are preferentially enriched in boutons relative to axons. This bouton-enriched proteome includes canonical synaptic vesicle proteins and well-characterized active zone components, validating the spatial specificity of the approach. In addition, it reveals protein clusters suggestive of specialized signaling pathways related to ATP production and protein degradation, indicating previously underappreciated metabolic and proteostatic specialization enriched in presynaptic terminals. Together, our dataset provides a resource for the study of synaptic function under physiological and pathological conditions and establishes a generalizable strategy for spatially resolved proteomic analysis of neuronal subcompartmentation. - Source: PubMed
Publication date: 2026/05/13
Nakazawa KeitaTaoufiq ZacharieKakuda NobutoGoda YukikoTakamori Shigeo - Tumor-secreted exosomes are essential in driving tumor progression by releasing multivesicular bodies (MVBs), which are endosome organelles containing intraluminal vesicles (ILVs), as exosomes. However, the mechanisms controlling MVB biosynthesis, trafficking, and exosome exocytosis are not fully understood. - Source: PubMed
Publication date: 2026/05/12
Bai SuwenSun HexingLiu RongZhang WenjunWei YuanLuo YumeiWang MinghuaWu JingChan David WDu Juan