54926-13-5

Upstream product

• 3424-93-9 4-methoxyphenylacetamide 
• 4637-24-5 N,N-dimethyl-formamide dimethyl acetal 
• 104-92-7 1-bromo-4-methoxy-benzene 
• 201230-82-2 carbon monoxide 
• 68-12-2 N,N-dimethyl-formamide 

Downstream Products

• 54926-15-7 N-formyl-(4-methoxy)benzamide 
• 58415-04-6 C₉H₉NO₂S 
• 83253-04-7 N-[1-Ethylsulfanyl-meth-(Z)-ylidene]-4-methoxy-benzamide 
• 64310-35-6 5-(4-Methoxy-phenyl)-1H-[1,2,4]triazole 
• 83253-19-4 2-(4-Methoxyphenyl)-4-phenyl-1,3,5-triazine 
• 83253-20-7 4-Amino-2-(4-Methoxyphenyl)-1,3,5-triazine 
• 83253-18-3 2-(4-Methoxyphenyl)-4-methyl-1,3,5-triazine 

Relevant academic research and scientific papers

VASCULAR ADHESION PROTEIN-1 (VAP-1) MODULATORS AND THERAPEUTIC USES THEREOF

Disclosed herein are small molecule Vascular Adhesion Protein- 1 (VAP-1) modulator compositions, pharmaceutical compositions, the use and preparation thereof.

Liganding Functional Tyrosine Sites on Proteins Using Sulfur-Triazole Exchange Chemistry

Tuning reactivity of sulfur electrophiles is key for advancing click chemistry and chemical probe discovery. To date, activation of the sulfur electrophile for protein modification has been ascribed principally to stabilization of a fluoride leaving group (LG) in covalent reactions of sulfonyl fluorides and arylfluorosulfates. We recently introduced sulfur-triazole exchange (SuTEx) chemistry to demonstrate the triazole as an effective LG for activating nucleophilic substitution reactions on tyrosine sites of proteins. Here, we probed tunability of SuTEx for fragment-based ligand discovery by modifying the adduct group (AG) and LG with functional groups of differing electron-donating and -withdrawing properties. We discovered the sulfur electrophile is highly sensitive to the position of modification (AG versus LG), which enabled both coarse and fine adjustments in solution and proteome activity. We applied these reactivity principles to identify a large fraction of tyrosine sites (～30%) on proteins (～44%) that can be liganded across >1500 probe-modified sites quantified by chemical proteomics. Our proteomic studies identified noncatalytic tyrosine and phosphotyrosine sites that can be liganded by SuTEx fragments with site specificity in lysates and live cells to disrupt protein function. Collectively, we describe SuTEx as a versatile covalent chemistry with broad applications for chemical proteomics and protein ligand discovery.

An efficient method for the preparation of N-formyl-imide via amidine using propylphosphonic anhydride (T3P)

An efficient method for the preparation of N-formyl imide via amidine using propylphosphonic anhydride (T3P) has been described. Using this method many aryl, hetero aryl, alkyl as well as amino acid imides were synthesized in high yields.