The role of arginine in interactions of microcystins with protein phosphatases 1 and 2a

Bioorganic & Medicinal Chemistry Letters
1992.0

Abstract

Comparison of the enzyme inhibition and receptor binding activity of microcystin-LR and microcystin-LA has shown that the arginine residue in microcystin-LR does not significantly contribute to biological activity. This data allows a refinement of a receptor binding model of the okadaic acid class of protein phosphatase inhibitors.

DOI： 10.1016/S0960-894X(00)80388-1

Knowledge Graph

Similar Paper

The role of arginine in interactions of microcystins with protein phosphatases 1 and 2a
Bioorganic & Medicinal Chemistry Letters 1992.0
Inhibition of protein phosphatase 2A by cyclic peptides modelled on the microcystin ring
Bioorganic & Medicinal Chemistry Letters 1996.0
Microcystin analogues comprised only of adda and a single additional amino acid retain moderate activity as PP1/PP2A inhibitors
Bioorganic & Medicinal Chemistry Letters 2003.0
Linearized and truncated microcystin analogues as inhibitors of protein phosphatases 1 and 2A
Bioorganic & Medicinal Chemistry Letters 2003.0
The conserved acid binding domain model of inhibitors of protein phosphatases 1 and 2A: Molecular modelling aspects.
Bioorganic & Medicinal Chemistry Letters 1993.0
The effects of single l-amino acid substitutions on the lethal potencies of the microcystins
Toxicon 1989.0
Microginins 299-A and -B, leucine aminopeptidase inhibitors from the cyanobacterium Microcystis aeruginosa (NIES-299)
Tetrahedron 1997.0
Identification and characterization of hydrophobic microcystins in Canadian freshwater cyanobacteria
Toxicon 1993.0
Microcystin-la from a blue-green alga belonging to the stigonematales
Phytochemistry 1992.0
[d-Leu1] microcystin-LR, a new microcystin isolated from waterbloom in a Canadian prairie lake
Toxicon 2001.0