55930-23-9

Upstream product

• 99-94-5 p-Toluic acid 
• 79-37-8 oxalyl dichloride 
• 934-67-8 trans-4-methylcyclohexanecarboxylic acid 

Downstream Products

• 111055-01-7 4-(4-Methyl-cyclohexanecarbonyloxy)-benzoic acid 4-ethyl-phenyl ester 
• 3937-49-3 (trans-4-methylcyclohexyl)methanol 
• 195138-41-1 ethyl 4-(4-methylcyclohexyl)-4-oxobutyrate 
• 960521-55-5 ethyl 2-[[(trans-4-methylcyclohexyl)carbonyl](1-methylethyl)amino]-5-phenyl-3-furancarboxylate 
• 960521-59-9 ethyl 5-(4-bromophenyl)-2-[[(trans-4-methylcyclohexyl)carbonyl](1-methylethyl)amino]-3-furancarboxylate 
• 960522-01-4 ethyl 5-(4-bromophenyl)-2-{[(trans-4-methylcyclohexyl)carbonyl]amino}-3-furancarboxylate 
• 1007374-15-3 C₂₆H₃₃NO₄ 
• 865868-86-6 ethyl 3-{[(trans-4-methylcyclohexyl)carbonyl]amino}-1-phenyl-1H-pyrazole-4-carboxylate 
• 865868-15-1 ethyl 3-[[(trans-4-methylcyclohexyl)carbonyl](1-methylethyl)amino]-1-phenyl-1H-pyrazole-4-carboxylate 
• 865868-90-2 1,1-dimethylethyl 4-{{4-[(ethyloxy)carbonyl]-1-phenyl-1H-pyrazol-3-yl}[(trans-4-methylcyclohexyl)carbonyl]amino}-1-piperidinecarboxylate 
• 712353-28-1 5-bromo-3-[(1,4-dioxa-spiro[4.5]dec-8-yl)-(trans-4-methyl-cyclohexanecarbonyl)-amino]-thiophene-2-carboxylic acid methyl ester 

Relevant academic research and scientific papers

Palladium-Catalyzed Migratory Insertion of Carbenes and C-C Cleavage of Cycloalkanecarboxamides

A palladium catalyzed reaction of cycloalkanecarboxamides and diazomalonates or bis(phenylsulfonyl)diazomethane has been developed. The reaction proceeds via carbene migratory insertion and cascade C-C cleavage pathways. Cycloalkanecarboxamides with four to seven membered rings are applicable in the transformation. A series of ring opening products were prepared with moderate yields. The finding provides valuable clues for the development of new reactions involving carbene migratory insertion and the cleavage of unstrained C(sp3)-C(sp3) bonds.

Discovery of Novel Thiophene-Based, Thumb Pocket 2 Allosteric Inhibitors of the Hepatitis C NS5B Polymerase with Improved Potency and Physicochemical Profiles

The hepatitis C viral proteins NS3/4A protease, NS5B polymerase, and NS5A are clinically validated targets for direct-acting antiviral therapies. The NS5B polymerase may be inhibited directly through the action of nucleosides or nucleotide analogues or al

γ,δ,ε-C(sp3)-H Functionalization through Directed Radical H-Abstraction

Aliphatic amides are selectively functionalized at the γ- and δ-positions through directed radical 1,5 and 1,6 H-abstractions, respectively. The initially formed γ- or δ-lactams are intercepted by N-iodosuccinimide and trimethylsilyl azide, leading to double and triple C-H functionalizations at the γ-, δ-, and ε-positions. This new reactivity is exploited to convert alkyls into amino alcohols and allylic amines.

Discovery of GS-9669, a thumb site II non-nucleoside inhibitor of NS5B for the treatment of genotype 1 chronic hepatitis C infection

Investigation of thiophene-2-carboxylic acid HCV NS5B site II inhibitors, guided by measurement of cell culture medium binding, revealed the structure-activity relationships for intrinsic cellular potency. The pharmacokinetic profile was enhanced through incorporation of heterocyclic ethers on the N-alkyl substituent. Hydroxyl groups were incorporated to modulate protein binding. Intrinsic potency was further improved through enantiospecific introduction of an olefin in the N-acyl motif, resulting in the discovery of the phase 2 clinical candidate GS-9669. The unexpected activity of this compound against the clinically relevant NS5B M423T mutant, relative to the wild type, was shown to arise from both the N-alkyl substituent and the N-acyl group.

Discovery of dual death-associated protein related apoptosis inducing protein kinase 1 and 2 inhibitors by a scaffold hopping approach

DRAK2 emerged as a promising drug target for the treatment of autoimmune diseases and to prevent graft rejection after organ transplantation. Screening of a compound library in a DRAK2 binding assay led to the identification of an isothiazolo[5,4-b]pyridine derivative as a novel ligand for DRAK2, displaying a Kdvalue of 1.6 μM. Subsequent medicinal chemistry work led to the discovery of a thieno[2,3-b]pyridine derivative with strong DRAK2 binding affinity (Kd= 9 nM). Moreover, this compound also behaves as a functional inhibitor of DRAK2 enzymatic activity, displaying an IC50value of 0.82 μM, although lacking selectivity, when tested against DRAK1. This paper describes for the first time functionally active dual DRAK1 and DRAK2 inhibitors that can be used as starting point for the synthesis of chemical tool compounds to study DRAK1 and DRAK2 biology, or they can be considered as hit compounds for hit-to-lead optimization campaigns in drug discovery programs.

THIOPHENE COMPOUNDS

Polymorph Forms M, H, P, X, and ZA of Compound (1) represented by the following structural formula: are described. A method of preparing polymorph Form M of Compound (1) includes stirring a mixture of Compound (1) and a solvent system that includes isopro

IMIDAZOPYRROLIDINONE COMPOUNDS

The invention relates to compounds of formula (I): (I) as described herein, pharmaceutical preparations comprising such compounds, uses and methods of use for such compounds in the treatment of a disorder or a disease mediated by the activity of MDM2 and/or MDM4, and combinations comprising such compounds.

VIRAL POLYMERASE INHIBITORS

Compounds of formula I: wherein X, R2, R3, R3a, R3b,R5 and R6 are defined herein, are useful as inhibitors of the hepatitis C virus NS5B polymerase.

Viral Polymerase Inhibitors

Compounds of formula I: wherein X, R2, R3, R5 and R6 are defined herein, are useful as inhibitors of the hepatitis C virus NS5B polymerase.

VIRAL POLYMERASE INHIBITORS

Compounds of formula (I): wherein X, R2, R3, R5 and R6 are defined herein, are useful as inhibitors of the hepatitis C virus NS5B polymerase.