SNCA & APP Protein Protein Interaction Antibody Pair
- Known as:
- SNCA & APP Protein Protein Interaction Antibody Pair
- Catalog number:
- DI0059
- Product Quantity:
- 1 Set
- Category:
- -
- Supplier:
- Abno
- Gene target:
- SNCA & APP Protein Interaction Antibody Pair
Related genes to: SNCA & APP Protein Protein Interaction Antibody Pair
- Gene:
- SNCA NIH gene
- Name:
- synuclein alpha
- Previous symbol:
- PARK1, PARK4
- Synonyms:
- NACP, PD1
- Chromosome:
- 4q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-01-24
- Date modifiied:
- 2018-04-18
Related products to: SNCA & APP Protein Protein Interaction Antibody Pair
Related articles to: SNCA & APP Protein Protein Interaction Antibody Pair
- Studying the genetic basis of human phenotypes involves two primary strategies. Model-system experiments generate interpretable gene networks but do not establish relevance to human disease. In contrast, statistical genetics identifies variant- and gene-level associations but cannot test mechanistic models. Here, we bridge these approaches by introducing NERINE, a hierarchical model-based rare variant association test that incorporates gene network topology while remaining robust to network inaccuracies. NERINE supports analysis of networks from established pathway databases and model-system screens. A comprehensive search across pathway databases reveals associations for breast cancer, cardiovascular diseases, and type 2 diabetes not detected by single-gene tests. Applied to experimental screen-derived networks in Parkinson's disease (PD), NERINE highlights autophagy-, vesicle-trafficking-, and protein-homeostasis-related gene modules. Genome-scale CRISPR interference (CRISPRi) screening in human neurons and NERINE converge on PRL, revealing an intraneuronal α-synuclein/prolactin stress response that may impact resilience to PD. - Source: PubMed
Publication date: 2026/06/22
Nazeen SumaiyaWang XinyuanMorrow Autumn RStrom RonyaEthier ElizabethRitter DylanHenderson Alexander B HAfroz JalwaCassa Christopher SStitziel Nathan OGupta Rajat MLuk Kelvin CStuder LorenzKhurana VikramSunyaev Shamil R - Genome-edited human pluripotent stem cells (hPSCs) provide a powerful platform to study complex diseases such as Parkinson's disease (PD). Here, we describe iSCORE-PD, an isogenic collection of 65 genome-edited hPSC lines carrying disease-causing or high-risk variants in 11 PD-linked genes (SNCA, PRKN, PINK1, DJ1/PARK7, LRRK2, ATP13A2, FBXO7, DNAJC6, SYNJ1, VPS13C, and GBA1). All lines are derived from a well-characterized female hESC line and subjected to extensive quality control. Whole-genome sequencing reveals that genetic variation between lines, largely confined to non-coding regions, is minimal relative to inter-individual differences in patient-derived hiPSCs, with most variation arising from random mutations acquired during cell culture rather than genome-editing-induced off-target effects. Including multiple independently derived clones per mutation can control for this random genetic drift. Our systematic approach ensures high quality of this publicly available iSCORE-PD resource, highlights the advantages of prime editing over conventional CRISPR/Cas9 methods, and establishes best practices for generating disease-modeling hPSC collections. - Source: PubMed
Publication date: 2026/06/17
Busquets OriolLi HanqinSyed Khaja MohieddinJerez Pilar AlvarezDunnack JesseLo Bu RianaVerma YogendraPangilinan Gabriella RMartin AnnikaStraub JannesDu YuXinSimon Vivien MPoser StevenBush ZipporiahDiaz JessicaSahagun AtehsaGao JianpuHong SamanthaHernandez Dena GLevine Kristin SPochet NathalieBooth Ezgi OBlanchette MarcoBateup Helen SRio Donald CBlauwendraat CornelisHockemeyer DirkSoldner Frank - Parkinson's disease (PD) is a neurodegenerative disorder characterized by alpha-synuclein (α-syn) aggregates termed Lewy bodies. To model PD pathology in vitro, preformed fibrils of α-syn (PFFs), which can be taken up by cells, provide a seed that drives misfolding and aggregation of endogenous α-syn, with new aggregates amplifying this process. External application of PFFs to dopaminergic neurons (DNs) increases aggregate formation, marked by α-syn phosphorylation at serine 129 (pS129-syn), a pathological PD marker. Building on this, we developed an automated synuclein seeding assay to quantify new α-syn aggregates in iPSC-derived DNs. Using pS129-syn as a readout, we show that PFFs elicit a time- and dose-dependent increase in pS129-syn aggregates. Our automated seeding assay further revealed that aggregate formation depends on endogenous α-syn levels. Treatment with PFFs produced a greater increase in pS129-syn aggregates in iPSC DNs derived from a PD patient with a triplication in the SNCA gene, which encodes the α-syn protein and which elevates total α-syn levels, relative to DNs from an isogenic iPSC line from the same individual, in which the SNCA gene mutation had been corrected by CRISPR/Cas9. In contrast, no pS129-syn signal was detected in neurons in which all copies of the SNCA gene had been knocked out (KO). This proof-of-principle automated high-content imaging workflow for synuclein seeding has been validated using isogenic cell lines with defined SNCA copy number variants and it offers a platform for assessing compounds and therapeutics that may impede α-syn aggregate formation. - Source: PubMed
Publication date: 2026/06/15
Han ChanshuaiNguyen-Renou EmmanuelleBenaliouad FaizaLuo WenChen Carol X-QAlluli AeshahVillegas LorenzaBeitel Lenore KShlaifer IrinaReintsch Wolfgang EKrahn Andrea ICid Pellitero Esther DelFon Edward ADurcan Thomas M - Neurodegenerative disorders such as Parkinson's disease (PD) arise from interconnected mechanisms including mitochondrial dysfunction, oxidative stress, neuroinflammation, and impaired protein homeostasis, leading to progressive dopaminergic neuron loss and limited benefit from current single target therapies. Parkin (PARK2), an E3 ubiquitin ligase central to mitochondrial quality control and mitophagy, has therefore emerged as an attractive therapeutic node, with its functional stabilization representing a promising strategy to restore mitochondrial homeostasis in PD. In this study, phytocompounds from Althaea officinalis were evaluated using an integrated in silico pipeline combining ADMET prediction, molecular docking, 100 ns molecular dynamics simulations, MM-GBSA binding free energy analysis, and network pharmacology to identify potential PARK2 modulating lead compounds relevant to Parkinson's disease. Forty bioactive constituents were screened, and computational ADMET modeling highlighted flavonoids and coumarin derivatives such as scopolin, astragalin, isoquercitrin, and quercetin derivatives as having acceptable oral absorption, limited predicted toxicity, and low risk of major metabolic or cardiotoxic liabilities. Structure-based docking against PARK2 (PDB ID: 5C23) revealed that several A. officinalis metabolites, notably scopolin, β-D-glucose, quercetin-3-glucoside, and L-arabinose, exhibit favorable binding affinities (docking scores - 7.232 to - 6.648 kcal/mol) and form energetically stable complexes with key catalytic and regulatory residues, in some cases outperforming co-crystal ligand. Subsequent 100 ns molecular dynamics simulations confirmed that the scopolin- and quercetin-3-glucoside-PARK2 complexes remain structurally stable, with low RMSD fluctuations, compact Rg profiles, and persistent hydrogen-bonding, while MM-GBSA calculations yielded consistently favorable ΔGbind values, further supporting their high-affinity interaction with PARK2. Network pharmacology analysis further showed that these phytochemicals converge on core PD-related targets such as AKT1, PIK3R1, MAPT, SNCA, PSEN2, BCL2L1, HK1, RPS6KA3, TLR1, and TLR2 within PI3K-Akt, MAPK, mTOR, HIF-1, autophagy, apoptosis, insulin, Toll-like receptor, and Parkinson disease pathways, indicating a multi-target, multi-pathway mode of action. Overall, the findings suggest that A. officinalis phytocompounds especially scopolin and quercetin glycosides possess drug-like ADMET properties, strong PARK2 binding, MD-validated complex stability with favorable MM-GBSA binding energies, and systems-level engagement with PD-relevant signaling networks, supporting their candidacy as plant-derived leads for PARK2-centered therapeutic strategies in PD. - Source: PubMed
Publication date: 2026/06/15
Heshetha MHaneesh MuthineniKarthick VenkatesanThamarai RajkumarAmalraj Singamoorthy - Obesity is recognized as a key contributor to the impaired endometrial receptivity that results in infertility; however, the molecular mechanisms underlying endometrial dysfunction remain incompletely understood. In this study, proteomic and ubiquitination analyses of secretory-phase endometrial tissue revealed a significant upregulation of SNCA/synuclein alpha and dysregulation of macroautophagy/autophagy in women with obesity. SNCA is best known for its role in neurodegenerative protein aggregation disorders. Proteomic and ubiquitination analysis of secretory-phase endometrial tissue revealed a significant upregulation of SNCA and dysregulation of autophagy in women with obesity. This study aimed to elucidate the role and mechanistic basis of SNCA and autophagy in obesity-associated endometrial receptivity defects. We demonstrated that elevated SNCA expression in endometrium and endometrial stromal cells (ESCs) correlated with impaired autophagy and disrupted decidualization in and . Mechanistically, SNCA directly interacted with the E3 ubiquitin ligase STUB1 (STIP1 homology and U-box containing protein 1) in ESCs, thereby disrupting the association between STUB1 and phosphorylated TFEB (transcription factor EB; p-TFEB). This interaction attenuated p‑TFEB degradation, leading to suppressed autophagic flux and ultimately compromised decidualization of ESCs. Conversely, knockout alleviated obesity-induced endometrial impairments in mice. Moreover, STUB1 overexpression rescued decidualization and autophagy defects. Notably, metformin intervention restored autophagic activity and endometrial receptivity in obese mice by downregulation of SNCA independent of its autophagy-modulating effects. Together, these findings uncovered a novel pathogenic mechanism in which obesity-driven SNCA overexpression impairs endometrial receptivity by inhibiting STUB1-TFEB-mediated autophagy, positioning the SNCA-STUB1-TFEB axis as a promising therapeutic target for obesity-related endometrial infertility.: BECN1: beclin 1; CCK-8: Cell Counting Kit-8; CQ: chloroquine; DEPs: differentially expressed proteins; DIO: diet-induced obese; ESCs: endometrial stromal cells; FBS: fetal bovine serum; GD7: gestational day 7; GSEA: Gene Set Enrichment Analysis; HFD: high-fat diet; HOXA10: homeobox A10; IGFBP1: insulin like growth factor binding protein 1; IPGTT: intraperitoneal glucose tolerance test; LIF: LIF interleukin 6 family cytokine; PBS: phosphate-buffered saline; PRL: prolactin; Rapa: rapamycin; SNCA/synuclein alpha; SQSTM1/p62: sequestosome 1; STUB1: STIP1 homology and U-box containing protein 1; TC: total cholesterol; TEM: transmission electron microscopy; TFEB: transcription factor EB; UPS: ubiquitin-proteasome system; WOI: window of implantation. - Source: PubMed
Publication date: 2026/06/23
Tang FeiGuo PeipeiWang LitingXie PengxiangWang YiWang YueFang YouyanLi CaihuaCao YunxiaXiang HuifenYin ZongzhiZhang DongWei ZhaolianHe Ye