Structure based inhibitor design studies on angiotensin converting enzyme homologues

@inproceedings{Harrison2015StructureBI,
  title={Structure based inhibitor design studies on angiotensin converting enzyme homologues},
  author={Charlotte Harrison},
  year={2015}
}
Angiotensin converting enzyme, ACE (EC number 3. 4. 15. 1), is a zinc dependent dipeptidyl carboxypeptidase that has an essential role in mammalian blood pressure regulation as part of the renin-angiotensin aldosterone system. ACE acts to increase blood pressure through its actions on two peptides: angiotensin I and bradykinin. In light of this role ACE is a key target in the treatment of hypertension and ACE inhibitors have been widely used since the 1980s. Although these are effective drugs… CONTINUE READING

References

Publications referenced by this paper.
SHOWING 1-10 OF 177 REFERENCES

RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 1999
VIEW 5 EXCERPTS
HIGHLY INFLUENTIAL

REFMAC5 for the refinement of macromolecular crystal structures

  • Acta crystallographica. Section D, Biological crystallography
  • 2011
VIEW 7 EXCERPTS
HIGHLY INFLUENTIAL

LigPlot+: Multiple Ligand-Protein Interaction Diagrams for Drug Discovery

  • Journal of Chemical Information and Modeling
  • 2011
VIEW 4 EXCERPTS
HIGHLY INFLUENTIAL

Overview of the CCP4 suite and current developments

  • Acta crystallographica. Section D, Biological crystallography
  • 2011
VIEW 4 EXCERPTS
HIGHLY INFLUENTIAL

MolProbity: all-atom structure validation for macromolecular crystallography

  • Acta crystallographica. Section D, Biological crystallography
  • 2010
VIEW 6 EXCERPTS
HIGHLY INFLUENTIAL