PDZD2 Antibody (OAAF02010)
- Known as:
- PDZD2 Antibody (OAAF02010)
- Catalog number:
- oaaf02010
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- PDZD2 Antibody (OAAF02010)
Related genes to: PDZD2 Antibody (OAAF02010)
- Gene:
- PDZD2 NIH gene
- Name:
- PDZ domain containing 2
- Previous symbol:
- PDZK3
- Synonyms:
- KIAA0300
- Chromosome:
- 5p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2002-04-10
- Date modifiied:
- 2016-10-25
Related products to: PDZD2 Antibody (OAAF02010)
Related articles to: PDZD2 Antibody (OAAF02010)
- While the venetoclax-based VD-CAG regimen has shown promising efficacy in acute myeloid leukemia (AML), its underlying molecular response mechanisms remain poorly understood, and robust prognostic biomarkers for non-M3 AML treated with this regimen are lacking. This study aimed to elucidate the molecular alterations associated with VD-CAG treatment response, and to identify and validate robust prognostic biomarkers to improve risk stratification for non-M3 AML patients. - Source: PubMed
Publication date: 2026/05/19
Tang JiruiYang KunZhang YingTang YuqianYang YankunLi QinWang XuemeiGong Yuping - The cooperative nature of protein folding limits the experimental dissection of the reaction mechanism. PDZ domains, with conserved folds, numerous homologs, and accessible folding intermediates, offer an ideal model to study folding pathways. Here, we present a detailed structural and kinetic characterization of the folding pathway of PDZ6 from PDZD2. Using kinetic folding experiments under different salt conditions combined with φ-value analysis, we revealed a complex energy landscape for PDZ6, featuring three distinct transition states (TS1-TS3) and the progressive acquisition of native-like structure along the reaction coordinate. Taking advantage of the large number of homologous PDZ domains, we compared φ-values at conserved structural positions with those previous obtained for PDZ3 of PSD-95 and PDZ2 of PTP-BL. This analysis revealed a shared, conserved folding mechanism among PDZ domains, in which the central β-strands act as nucleation cores for folding. Overall, this work provides the first structural dissection of the three transition states governing PDZ6 folding and highlights a conserved, hierarchical folding mechanism among PDZ domains. These findings expand our understanding of PDZ folding principles and may inform studies on their functional modulation and evolutionary adaptation. - Source: PubMed
Publication date: 2025/12/19
Obreja Cosmin MarianMarinidis DimitriosPennacchietti ValeriaDi Matteo SaraIppoliti RodolfoMalagrinò Francesca - Alzheimer's disease (AD) is the most common cause of dementia in the elderly. However, the particular cause of AD development has not been fully elucidated. Currently, cellular senescence is recognized as a contributing factor to the aging process and age-related diseases. - Source: PubMed
Publication date: 2025/05/21
Sha DujuanZhang JingxuanFang XuWang XinyuHe XuanShu Xin - Adenosine, an ATP degradation product, is a sleep pressure factor. The adenosine 1 receptor (A1R) reports sleep need. Histaminergic neurons (HN) of the tuberomamillary nucleus (TMN) fire exclusively during wakefulness and promote arousal. All of them express GABA receptors and are inhibited by GABA. Does adenosine contribute to their silencing? - Source: PubMed
Publication date: 2025/01/08
Wegmann LeaHaas Helmut LSergeeva Olga A - Tetralogy of Fallot (TOF) is the most common cyanotic heart defect in newborns, with a complex etiology and genetic variation considered to be one of the main pathogenic factors. Identifying genetic variations associated with TOF has important clinical value for understanding its pathogenesis, patient susceptibility, and prognosis of patients with TOF. Therefore, this study aimed to identify potential pathogenic genes of TOF through comprehensive genetic analysis. In this study, we employed whole exome sequencing (WES) of the DNA of 47 Chinese children who received surgical TOF treatment at the Children's Hospital of Zhejiang University of Medicine and processed for DNA extraction and quantification of the DNA following WES using the Illumina NovaSeq platform. WES data undergo strict quality control and analysis processes including alignment, postprocessing, variant calling, annotation, and prioritization. Key tools, such as GATK's haplotype calling module and Annotate Variation, were used for variant annotation. In addition, by combining bioinformatics tools such as SIFT, Polyphen2, and Clin Pred, we evaluated the potential impact of nonsynonymous mutations on protein function and referred to relevant literature to support our prediction. Comprehensive data analysis and quality assessment analysis corroborated the data generated from the WES dataset of 47 patients with TOF. Interpreting variants from the perspective of clinical pathogenicity results revealed a novel polymorphism and variant associated with TOF. The identified genetic results revealed evidence for a major contribution of MUTYH, RARB, GFM1, PDZD2, CEP57, DCPS, POMT2, BUB1B, CYP19A1, MAZ, USP10, and TCF3 and provided novel findings for functionally interacting proteins associated with the pathomechanism of TOF. Seven pathogenic variants related to TOF were detected, most of which were previously unreported in this cohort. The genetic variations discovered in this study emphasize the importance of genetic factors in the pathogenesis of TOF, revealing its complex molecular pathways and protein-protein interactions. The study of genetic diversity provides a new perspective for understanding the etiology of TOF and promotes an in-depth exploration of its pathological mechanisms. These findings lay the foundation for subsequent clinical research and the development of treatment strategies. - Source: PubMed
Publication date: 2024/12/09
Abdullahi Khalid MohamoudAli Ahmed FaisalAdan Mohamed MohamoudShu Qiang