Structure‐Based Design: From Renin to HIV‐1 Protease

Lunney, Elizabeth A.; Humblet, Christine

doi:10.1002/9783527612178.ch3

Search citation statements

Order By: Relevance

Paper Sections

Select...

Carbamates With Clinical Potential1

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1999

2015

Publication Types

Select...

Article3

Relationship

Self Cite0

Independent3

Authors

Journals

Cited by 3 publications

(1 citation statement)

References 76 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…HIV protease is a C 2 -symmetric, 198-amino acid homodimeric aspartyl protease in which each protein subunit contributes one Asp-Thr-Gly motif to the single active site . The X-ray crystallographic analysis of the native protein and subsequent protein–ligand complexes and extensive research programs on other aspartyl proteases, including human renin, provided a path toward accelerated drug discovery programs targeting HIV protease. − A number of FDA-approved HIV protease inhibitor drugs contain an important carbamate functionality. In this section, currently approved protease inhibitor drugs are discussed (Figure ).…”

Section: Carbamates With Clinical Potentialmentioning

confidence: 99%

Organic Carbamates in Drug Design and Medicinal Chemistry

2015

View full text Add to dashboard Cite

The carbamate group is a key structural motif in many approved drugs and prodrugs. There is an increasing use of carbamates in medicinal chemistry and many carbamate derivatives are specifically designed to make drug-target interactions through their carbamate moiety. In this review, we present properties and stabilities of carbamates, reagents and chemical methodologies for the synthesis of carbamates, and recent application of carbamates in drug design and medicinal chemistry.

show abstract