DPF3 antibody - middle region (ARP34293_P050)
- Known as:
- DPF3 (anti-) - middle region (ARP34293_P050)
- Catalog number:
- arp34293_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- DPF3 antibody - middle region (ARP34293_P050)
Related genes to: DPF3 antibody - middle region (ARP34293_P050)
- Gene:
- DPF3 NIH gene
- Name:
- double PHD fingers 3
- Previous symbol:
- -
- Synonyms:
- cer-d4, Cerd4, FLJ14079, BAF45c
- Chromosome:
- 14q24.2
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-28
- Date modifiied:
- 2017-03-21
Related products to: DPF3 antibody - middle region (ARP34293_P050)
Related articles to: DPF3 antibody - middle region (ARP34293_P050)
- Amyloids refer to a diverse group of highly ordered proteinaceous structures conserved across all of the domains of life that not only are involved in severe proteinopathies but also serve as unique functional platforms. They are notably organized around a cross-β sheet core arranged into a dry steric zipper. Identifying regions promoting such type of assembly requires investigating, usually at the atomistic level, their structural and morphological properties. Although more amyloid structures are being solved and described by means of high-resolution experimental techniques, most amyloidogenic systems remain experimentally elusive or uncharacterized. To overcome such limitations, we propose a multilevel sequence-based computational approach taking advantage of aggregation-oriented predictors and modelers coupled with all-atom equilibrium molecular dynamics (MD) simulations. As an example of this approach, we introduced our protein of interest, the intrinsically disordered zinc finger DPF3a, to the pipeline, thus identifying a hit hexapeptide (NCYIWM) exhibiting remarkable pro-amyloid features. Indeed, this peptide was shown to stabilize different steric zipper topologies, spontaneously self-assemble into β-sheeted oligomers, and to act as an amyloid seed enabling the conversion and addition of β-sheet multimers for fibril elongation, which echoes the pathological repertoire of DPF3a. In comparison, simulations performed on a peptide sequence consensually predicted as nonamyloid (AERSVR) congruently underscored its inability to maintain a steric zipper configuration and nucleate into oligomers enriched in β character. Using only the sequence of a target protein as starting input, our methodology noteworthily proved to be reliable for detecting aggregation-prone regions, assessing their amyloidogenicity, and elucidating their fibrillation mechanisms while holding promise for the design of new anti-amyloid drugs and amyloid-inspired biomaterials. - Source: PubMed
Publication date: 2026/04/16
Mignon JulienLeyder TanguyBâlon HugoMonari AntonioMottet DenisMichaux Catherine - Renal cell carcinoma (RCC) is a heterogeneous malignancy influenced by genetic and environmental factors. Previous genome-wide association studies (GWAS) have identified risk single nucleotide polymorphisms (SNPs) associated with RCC susceptibility, particularly within genes such as , , , , and . These SNPs are in regions implicated in key cellular processes like calcium signaling, chromatin remodeling, hypoxia response and oncogenesis. These pathways are highly relevant to RCC pathogenesis, although the functional significance of these genetic variations in sporadic RCC remains insufficiently characterized. - Source: PubMed
Publication date: 2026/03/11
Morales-Álvarez C MJiménez-Domínguez A CRios-Pelegrina R MArance EMarín-Benesiu FVázquez-Alonso FMartínez-González L JÁlvarez-Cubero M J - Antipsychotic drugs elicit complex cellular responses in neurons, yet the molecular mechanisms underlying their actions remain incompletely understood. Here, we employed deep proteomic profiling (DDA/DIA-MS) in LUHMES-derived dopaminergic neurons to explore the distinct proteomic profile induced by clozapine and risperidone. Pathway analysis revealed that clozapine robustly upregulated lipid metabolic pathways, particularly those involved in cholesterol and fatty acid biosynthesis. Conversely, risperidone primarily enhanced oxidative phosphorylation and modulated synaptic architecture and protein metabolic-pathways. Functional enrichment further indicated that clozapine promotes sterol metabolism, neuronal viability, and neurite outgrowth-hallmarks of neurotrophic activity - while simultaneously suppressing neurotransmission. Importantly, quantitative analysis of the nuclear subproteome enabled us to map these opposing regulatory hubs with high precision. Mechanistically, clozapine induced a transcriptionally repressive state, marked by downregulation of chromatin-opening factors CHD5 and DPF3 (BAF complex components) and HMGN1. In parallel, upregulation of the transcriptional repressor CIC reinforced this repressive signature, suggesting diminished chromatin accessibility. Furthermore, downregulation of activity-dependent regulators CRTC3 and JUNB pointed to an attenuation of excitability-driven gene expression. In contrast, risperidone upregulated TCF4, TCF7L1, FOS, HMGN1, and coactivators RREB1 and NCOA3, promoting Wnt signaling, chromatin accessibility and synaptic plasticity. Taken together, our data unveil distinct proteomic, transcriptional and epigenetic programs orchestrated by clozapine and risperidone, providing novel molecular insights into their divergent clinical actions. - Source: PubMed
Publication date: 2025/11/26
Rybczyński PiotrCacala RadoslawCepil ZuzannaFic EwelinaRomanska WeronikaMarczak LukaszPustelny KatarzynaKedracka-Krok Sylwia - Dipeptidyl peptidase IV (DPPIV) family proteases are classically defined by their strict removal of N-terminal dipeptides from substrates bearing a proline or alanine at the P position. Here, we report that both Caenorhabditis elegans DPF-3 and human DPP4 (hDPP4) possess previously unrecognized tripeptidyl peptidase activity in addition to dipeptidyl peptidase activity. This activity plays a key role in the processing of the WAGO-1 protein N-terminus, which is essential for proper small-RNA loading, germline genome defense, and fertility. Kinetic analyses using the fluorogenic substrate H-Met-Gly-Pro-AMC further demonstrated that, in vitro, DPF-3 and hDPP4 can liberate AMC. These findings potentially expand the substrate repertoire of DPPIV proteases, suggesting that these proteases could function as versatile N-terminal processors, with important implications for nascent protein maturation. - Source: PubMed
Publication date: 2025/11/14
Trivedi AdityaGudipati Rajani Kanth - Proteases are enzymes that catalyse the hydrolysis of peptide bonds in proteins for their functional, modification or degradation. Members of the Dipeptidyl Peptidase IV (DPPIV) family are exopeptidases that cleave dipeptides off the N-termini of their substrate peptides, typically after proline or alanine. Recently, we showed that human DPP4 and DPF-3 have a larger target repertoire , permitting cleavage after additional amino acids. Here, we use TAILS (Terminal Amine Isotopic Labelling of Substrates) to identify DPF-3 targets and observe cleavage of MEP-1 after threonine, confirming a broader substrate specificity of DPF-3 also . Demonstrating physiological relevance, we show that rendering MEP-1 resistant to cleavage disrupts its stability, leading to developmental abnormalities such as defective gonadal migration and reproductive issues. Collectively, our findings highlight a previously unappreciated complexity in the substrate specificity of DPPIV family proteases and suggest that their physiological roles may extend beyond what is currently known. - Source: PubMed
Publication date: 2025/09/28
Aygün IlkinAmanullah AfzalSeebacher JanHess DanielSoneson CharlotteGroßhans HelgeGudipati Rajani Kanth