Bacterial RNase P as a potential target for novel anti-infectives

Curr Opin Investig Drugs. 2003 Aug;4(8):937-43.

Abstract

The diversity of higher-order structure in ribonucleoprotein (RNP) complexes makes them amenable to small-molecule modulation of their biological function. This review will discuss why bacterial RNase P, a simple yet essential ubiquitous and highly conserved RNP enzyme, represents an excellent target for the discovery and development of novel antimicrobials.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Anti-Infective Agents / pharmacology*
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Models, Molecular
  • Protein Subunits / metabolism
  • RNA, Bacterial / metabolism*
  • Ribonuclease P / antagonists & inhibitors*
  • Substrate Specificity

Substances

  • Anti-Infective Agents
  • Enzyme Inhibitors
  • Protein Subunits
  • RNA, Bacterial
  • Ribonuclease P