CITED1 Mouse Monoclonal Antibody
- Known as:
- CITED1 Mouse Monoclonal Antibody
- Catalog number:
- BIN-004435-M03
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- CITED1 Mouse Monoclonal Antibody
Related genes to: CITED1 Mouse Monoclonal Antibody
- Gene:
- CITED1 NIH gene
- Name:
- Cbp/p300 interacting transactivator with Glu/Asp rich carboxy-terminal domain 1
- Previous symbol:
- MSG1
- Synonyms:
- -
- Chromosome:
- Xq13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-03-27
- Date modifiied:
- 2016-02-24
Related products to: CITED1 Mouse Monoclonal Antibody
Related articles to: CITED1 Mouse Monoclonal Antibody
- Recent advances in predicting and modeling conformational ensembles of intrinsically disordered proteins (IDPs) have provided much needed insights into sequence-ensemble relationships. It is thought that conservation of physicochemical properties, but not the exact identity or order of the amino acids, maintains IDP ensemble properties that are crucial for function. However, detailed experimental studies are still required to fully understand the relationships between sequence and function in IDPs. The human CITED proteins, which are fully disordered transcriptional regulators, share conserved C-terminal transactivation domains (CTADs) that interact with the TAZ1 domain of the transcriptional coactivators CBP/p300. The conserved CTADs harbor amino acid substitutions in regions that are known to be important for interactions of CITED2 with TAZ1, but the effects of these substitutions on TAZ1 binding for the other CITED proteins are unknown. Here, we use solution NMR spectroscopy, circular dichroism, and surface plasmon resonance to characterize the conformational ensembles, dynamics, and interactions of the CITED CTADs. The CTADs are disordered in isolation, although the CITED2 CTAD uniquely displays residual helical structure that is sensitive to ionic strength and protein concentration. In contrast, the CITED1 and CITED4 CTADs remain largely disordered and exhibit more uniform dynamics. Quantitative binding measurements reveal differences in thermodynamics and kinetics for the CTADs' interactions with TAZ1, with CITED2 binding most tightly and CITED4 exhibiting significantly weaker affinity. Our results highlight the sensitivity of IDP conformational ensembles to minor sequence changes and the impacts that changes in IDP structures and dynamics can have on biological functions. - Source: PubMed
Do To UyenKraft Emma JChappell Garrett FParnham StuartBerlow Rebecca B - Oocyte maturation defect (OMD) is a rare cause of female infertility characterized by the persistent arrest of oocytes at immature stages. While biallelic PATL2 variants have been associated with OMD, the underlying molecular mechanisms remain unclear. This study aimed to identify novel PATL2 variants in OMD patients and investigate their functional consequences using a Patl2 knockout (KO) mouse model. - Source: PubMed
Publication date: 2026/04/30
Yu LiWang LinPan BaishenWang BeiliDong XiGuo WeiChe Qi - BACKGROUND: BRAF V600E mutation is insufficient for accurate diagnosis of thyroid neoplasms, although it has been widely used in clinical settings. We aimed to construct a messenger RNA (mRNA)-based model to identify thyroid cancer in indeterminate thyroid nodules in the absence of BRAF mutation. METHODS: Our cohort consisted of 88 papillary thyroid cancer (PTC) patients with BRAF V600E substitution, 103 BRAF mutation negative PTC cases, and 96 subjects with benign thyroid nodules. Based on the mRNA levels of MET proto-oncogene, receptor tyrosine kinase (MET), TIMP metallopeptidase inhibitor 1 (TIMP1), transforming growth factor alpha (TGFA), Cbp/p300 interacting transactivator with Glu/Asp rich carboxy-terminal domain 1 (CITED1), and fibronectin 1 (FN1) in thyroid specimens, model building was conducted to develop a gene expression-based classifier to differentiate benign from malignant thyroid nodules. In addition, external validation was performed using the thyroid carcinoma (THCA) dataset from the Cancer Genome Atlas (TCGA). RESULTS: Dataset-based bioinformatic analysis confirmed the elevated expression levels of these five genes in PTC compared to normal thyroid tissue. Overall, the binary classified model correctly identified 84 of 88 BRAF-mutated PTC and 75 of 103 BRAF mutation negative PTC as malignant tumors, respectively. For PTC carrying BRAF V600E mutation, the sensitivity, specificity, positive predictive value (PPV), negative predictive value (NPV), and area under the curve (AUC) were 0.955, 0.969, 0.966, 0.959 and 0.987, respectively. More importantly, the diagnostic performance of the approach in determining PTC without BRAF mutation was presented as the sensitivity of 0.728, specificity of 0.969, PPV of 0.962, NPV of 0.769, and AUC of 0.871. CONCLUSION: We developed and validated a gene expression classifier to assist in the diagnosis of BRAF V600E-negative PTC cases. This tool is poised to become a useful adjunct to individualized management of thyroid cancer in clinical practice. - Source: PubMed
Publication date: 2026/03/10
Wang LiangMao WuDeng HuaZhou Wei-PingZhang LiangLi Jie - Recent advances in predicting and modeling conformational ensembles of intrinsically disordered proteins (IDPs) have provided much needed insights into sequence-ensemble relationships. It is thought that conservation of physicochemical properties, but not the exact identity or order of the amino acids, maintains IDP ensemble properties that are crucial for function. However, detailed experimental studies are still required to fully understand the relationships between sequence and function in IDPs. The human CITED proteins, which are fully disordered transcriptional regulators, share conserved C-terminal transactivation domains (CTADs) that interact with the TAZ1 domain of the transcriptional coactivators CBP/p300. The conserved CTADs harbor amino acid substitutions in regions that are known to be important for interactions of CITED2 with TAZ1, but the effects of these substitutions on TAZ1 binding for the other CITED proteins are unknown. Here, we use solution NMR spectroscopy, circular dichroism, and surface plasmon resonance to characterize the conformational ensembles, dynamics, and interactions of the CITED CTADs. The CTADs are disordered in isolation, although the CITED2 CTAD uniquely displays residual helical structure that is sensitive to ionic strength and protein concentration. In contrast, the CITED1 and CITED4 CTADs remain largely disordered and exhibit more uniform dynamics. Quantitative binding measurements reveal differences in thermodynamics and kinetics for the CTADs' interactions with TAZ1, with CITED2 binding most tightly and CITED4 exhibiting significantly weaker affinity. Our results highlight the sensitivity of IDP conformational ensembles to minor sequence changes and the impacts that changes in IDP structures and dynamics can have on biological functions. - Source: PubMed
Publication date: 2026/01/21
Do To UyenKraft Emma JChappell Garrett FParnham StuartBerlow Rebecca B - The CITED proteins function as transcriptional modulators that are essential for vertebrate development. These proteins interact with numerous partners, notably transcription factors and co-activators. The hallmark of the CITED family is their conserved carboxy-terminal domain, which interacts strongly with the CBP/p300 co-activators. The expression of CITED genes is detected early during embryogenesis within embryonic and foetal regions critical for cardiac morphogenesis, among other developmental processes. Notably, CITED2 loss of function is strongly associated with congenital heart malformations in mice and zebrafish embryos, as well as congenital heart disease (CHD) in humans, whereas other CITED family members are not critical for cardiogenesis. Emerging evidence implicates CITED2 and CITED4 in regulating heart physiological adaptations and protective responses to pathological stress. This review provides a detailed analysis of CITED proteins and their interactors, focusing on CITED-target genes relevant for cardiogenesis and heart disease. We also highlight recent findings indicating that CITED2 and CITED4 may be instrumental for the development of novel therapeutic strategies to mitigate CHD and preserve adult cardiac function. - Source: PubMed
Publication date: 2025/11/07
Bragança JoséCabrita Pinto Rute LuísaVentura IgorFerreira SilvanaMarreiros António