57188-76-8

Upstream product

• 52323-98-5 4,4-dimethylpent-2-yn-1-ol 
• 98-59-9 p-toluenesulfonyl chloride 
• 917-92-0 3,3-Dimethylbut-1-yne 

Downstream Products

• 22585-31-5 3-(tert-butyl)-4,4-dimethylpenta-1,2-diene 
• 1041847-91-9 [NMe₂(4,4-dimethyl-2-pentynyl)(CH=C(CH₃)2)][OTS] 
• 145942-60-5 N-(4,4-dimethyl-2-pentynyl)-N-methyl-[(2R,3R)-3-(2,4-difluorophenyl)-3-hydroxy-4-(1H-1,2,4-triazol-1-yl)-2-butane]sulfonamide 

Relevant academic research and scientific papers

RECEPTOR INHIBITOR, PHARMACEUTICAL COMPOSITION COMPRISING SAME, AND USE THEREOF

The present invention discloses a receptor inhibitor of formula (I), a pharmaceutical composition comprising the same and the use thereof.

HETEROARYL COMPOUNDS USEFUL AS INHIBITORS OF SUMO ACTIVATING ENZYME

Disclosed are compounds of formula (I): or a pharmaceutically acceptable salt thereof; wherein Y, Ra, Ra', Rc, Rf, X2, Rd, Rd', Re, Re', m, and G have the values described herein and stereochemical configurations depicted at asterisked positions indicate absolute stereochemistry, useful as inhibitors of Sumo Activating Enzyme (SAE). Further provided are pharmaceutical compositions comprising a compound of the disclosure and methods of using the compositions in the treatment of proliferative, inflammatory, cardiovascular and neurodegenerative diseases or disorders.

Aza cope rearrangement of propargyl enammonium cations catalyzed by a self-assembled "nanozyme"

The tetrahedral assembly [Ga4L6]12- [L = N,N-bis(2,3-dihydroxybenzoyl)-1,5-diaminonaphthalene) encapsulates a variety of cations, including propargyl enammonium cations capable of undergoing the aza Cope rearrangement. For propargyl enammonium substrates that are encapsulated in the [Ga4L6]12- assembly, rate accelerations by factors of up to 184 compared with the background reaction rate were observed. After rearrangement, the product iminium ion is released into solution and hydrolyzed, allowing for catalytic turnover. The activation parameters for the catalyzed and uncatalyzed reaction were determined, revealing that a decrease in the entropy of activation is responsible for the observed rate enhancements. The catalyzed reaction exhibits saturation kinetics: the rate data obeyed the Michaelis-Menten model of enzyme kinetics, and competitive inhibition using a nonreactive guest was demonstrated.