R. Banerjee

Plasmepsin II, an Acidic Hemoglobinase from thePlasmodium falciparum Food Vacuole, Is Active at Neutral pH on the Host Erythrocyte Membrane Skeleton*

D. Goldberg, P. Grellier, D E Goldberg, 1999, The Journal of Biological Chemistry.

Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine

Jun Liu, D. Goldberg, M. Klemba, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain.

R. Matthews, R. Banerjee, P. Datta, 1989, The Journal of biological chemistry.

Biosynthesis and Maturation of the Malaria Aspartic Hemoglobinases Plasmepsins I and II*

D. Goldberg, S. Francis, R. Banerjee, 1997, The Journal of Biological Chemistry.

The Plasmodium Food Vacuole

D. Goldberg, R. Banerjee, Ritu Banerjee, 2001 .

Plasmodium Food Vacuole Plasmepsins Are Activated by Falcipains*

P. Rosenthal, D. Goldberg, S. Gilbertson, 2008, Journal of Biological Chemistry.

Food vacuole plasmepsins are processed at a conserved site by an acidic convertase activity in Plasmodium falciparum.

D. Goldberg, S. Francis, R. Banerjee, 2003, Molecular and biochemical parasitology.