Dimethyl di-O-methylpannarate
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| Category | Others |
| Catalog number | BBF-05113 |
| CAS | 27161-99-5 |
| Molecular Weight | 372.37 |
| Molecular Formula | C20H20O7 |
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Description
Dimethyl di-O-methylpannarate is a structure from the lichen.
Specification
| Synonyms | 2,6-Dibenzofurandicarboxylic acid, 3,9-dimethoxy-1,7-dimethyl-, dimethyl ester (7CI,8CI,9CI); 2,6-Dimethyl 3,9-dimethoxy-1,7-dimethyl-2,6-dibenzofurandicarboxylate; Di-O-methylpannaric acid dimethyl ester |
| IUPAC Name | dimethyl 3,9-dimethoxy-1,7-dimethyldibenzo[b,d]furan-2,6-dicarboxylate |
Properties
| Boiling Point | 524.1±45.0°C (Predicted) |
| Melting Point | 168°C |
| Density | 1.254±0.06 g/cm3 (Predicted) |
Reference Reading
1. NSD1 promotes esophageal cancer tumorigenesis via HIF1α signaling
Feng He, Hang Xiao, Yixin Cai, Ni Zhang Cell Biol Toxicol. 2022 Dec 16. doi: 10.1007/s10565-022-09786-2. Online ahead of print.
Unlike angiogenesis in normal tissues, tumor angiogenesis is typically dysregulated, during which the HIF1/VEGFA signaling pathway plays a pivotal role. Solid tumors generate immature vessels, which promote tumor progression and treatment resistance. NSD1 can di-methylate histone 3 lysine 36 and regulate transcription factors binding to the promoters of various genes. However, the role of NSD1 in tumorigenesis remains elusive. Here, we evaluated the relationship between NSD1 signaling and HIF1 signaling. It was found that NSD1 transcriptionally regulates HIF1α expression by recruiting STAT3 molecule into the HIF1α promoter. In vivo xenograft experiments further confirmed that HIF1α and STAT3 maintenance is essential for NSD1-mediated tumor progression and angiogenesis. Therefore, the NSD1/STAT3/HIF1α signaling pathway may be a novel and effective treatment target for ESCA.
2. Structure, Activity and Function of the Protein Arginine Methyltransferase 6
Somlee Gupta, Rajashekar Varma Kadumuri, Anjali Kumari Singh, Sreenivas Chavali, Arunkumar Dhayalan Life (Basel). 2021 Sep 11;11(9):951. doi: 10.3390/life11090951.
Members of the protein arginine methyltransferase (PRMT) family methylate the arginine residue(s) of several proteins and regulate a broad spectrum of cellular functions. Protein arginine methyltransferase 6 (PRMT6) is a type I PRMT that asymmetrically dimethylates the arginine residues of numerous substrate proteins. PRMT6 introduces asymmetric dimethylation modification in the histone 3 at arginine 2 (H3R2me2a) and facilitates epigenetic regulation of global gene expression. In addition to histones, PRMT6 methylates a wide range of cellular proteins and regulates their functions. Here, we discuss (i) the biochemical aspects of enzyme kinetics, (ii) the structural features of PRMT6 and (iii) the diverse functional outcomes of PRMT6 mediated arginine methylation. Finally, we highlight how dysregulation of PRMT6 is implicated in various types of cancers and response to viral infections.
3. Discovery of novel PRMT5 inhibitors bearing a methylpiperazinyl moiety
Xinyu Bai, Zheng Zhai, Xuyang Zhao, Ridong Li, Ling Liang, Yan Jin, Yuxin Yin Future Med Chem. 2022 Jul;14(14):1071-1086. doi: 10.4155/fmc-2021-0244. Epub 2022 Jun 24.
Background: PRMT5 is an epigenetics-related enzyme, which plays a critical role in cancer development. Hence PRMT5 inhibition has been validated as a promising therapeutic strategy. Methods & Results: We synthesized a series of methylpiperazinyl derivatives as novel PRMT5 inhibitors that were achieved by scaffold-hopping from EPZ015666 by virtual screening followed by rational drug design. Among all compounds 43g, bearing a thiourea linker, showed antitumor activity across multiple cancer cell lines and reduced the level of symmetric arginine dimethylation of SmD3 dose-dependently. Moreover, 43g selectively inhibited PRMT5 among protein arginine methyltransferase isoforms. Further proteomics analysis revealed that 43g remarkably reduced the global arginine dimethylation level in a cellular context. Conclusion: This work provides new chemical templates for future structural optimization of PRMT5-related cancer treatments.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
