Usheer Kanjee, Ph.D.

Affiliations: 
2012 Biochemistry University of Toronto, Toronto, ON, Canada 
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Walid Houry grad student 2012 University of Toronto
 (Structural and Functional Studies on the Escherichia coli Inducible Lysine Decarboxylase: Linking the Acid Stress and Stringent Responses.)
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Publications

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Kanjee U, Rangel GW, Clark MA, et al. (2018) Molecular and cellular interactions defining the tropism of Plasmodium vivax for reticulocytes. Current Opinion in Microbiology. 46: 109-115
Gruszczyk J, Kanjee U, Chan LJ, et al. (2018) Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax. Science (New York, N.Y.). 359: 48-55
Wong W, Huang R, Menant S, et al. (2018) Structure of Plasmodium falciparum Rh5-CyRPA-Ripr invasion complex. Nature. 565: 118-121
Kanjee U, Grüring C, Chaand M, et al. (2017) CRISPR/Cas9 knockouts reveal genetic interaction between strain-transcendent erythrocyte determinants of Plasmodium falciparum invasion. Proceedings of the National Academy of Sciences of the United States of America
Dankwa S, Chaand M, Kanjee U, et al. (2017) Genetic evidence for erythrocyte receptor glycophorin B expression levels defining a dominant Plasmodium falciparum invasion pathway into human erythrocytes. Infection and Immunity
Hostetler JB, Lo E, Kanjee U, et al. (2016) Independent Origin and Global Distribution of Distinct Plasmodium vivax Duffy Binding Protein Gene Duplications. Plos Neglected Tropical Diseases. 10: e0005091
Niang M, Bei AK, Madnani KG, et al. (2014) STEVOR is a Plasmodium falciparum erythrocyte binding protein that mediates merozoite invasion and rosetting. Cell Host & Microbe. 16: 81-93
Kanjee U, Houry WA. (2013) Mechanisms of acid resistance in Escherichia coli. Annual Review of Microbiology. 67: 65-81
Kanjee U, Ogata K, Houry WA. (2012) Direct binding targets of the stringent response alarmone (p)ppGpp. Molecular Microbiology. 85: 1029-43
Kanjee U, Gutsche I, Ramachandran S, et al. (2011) The enzymatic activities of the Escherichia coli basic aliphatic amino acid decarboxylases exhibit a pH zone of inhibition. Biochemistry. 50: 9388-98
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