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M

Murray D. Bailey

Researcher at Boehringer Ingelheim

Publications -  53
Citations -  4162

Murray D. Bailey is an academic researcher from Boehringer Ingelheim. The author has contributed to research in topics: NS3 & Protease. The author has an hindex of 24, co-authored 53 publications receiving 4062 citations.

Papers
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Journal ArticleDOI

An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus.

TL;DR: Administration of BILN 2061 to patients infected with HCV genotype 1 for 2 days resulted in an impressive reduction of HCV RNA plasma levels, and established proof-of-concept in humans for an HCV NS3 protease inhibitor, illustrating the potential of the viral-enzyme-targeted drug discovery approach for the development of new HCV therapeutics.
Journal ArticleDOI

Unexpected intermolecular pd-catalyzed cross-coupling reaction employing heteroaromatic carboxylic acids as coupling partners.

TL;DR: A selective transformation of carboxylic acid moiety was found to occur exclusively at the position previously occupied by the acid, even in the presence of a reactive C-H group, allowing for the preparation of a variety of aryl-substituted heteroaromatics that would be difficult to obtain via other methods.
Patent

Hepatitis C inhibitor tri-peptides

TL;DR: In this article, a compound of formula (I) is defined as an acyl derivative of formula R4-O-C(O)-; a carboxyl of the same type of compound; a thioamide of the compound.
Patent

Macrocyclic peptides active against the hepatitis C virus

TL;DR: In this article, the authors defined a pharmaceutically acceptable salt of the HCV NS3 protease, which is useful as an inhibitor of the NS3 protein-protein interaction.
Patent

Hepatitis C inhibitor peptide analogs

TL;DR: In this article, the authors proposed azalactone compounds of the formula (III) which can be reacted with an amide anion to produce the compounds of formula (I), which are useful for the treatment and prevention of hepatitis C viral infection in mammals by inhibiting HCV NS3 protease.