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Anuradha Deshmukh

Anuradha Deshmukh

Postdoctoral researcher in glycosylation and cancer therapeutics

anuradha-deshmukh
Marseille, France
Joined March 2026
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Summary

Structural biology and enzymology focus: During her PhD and early research career, Deshmukh contributed to structural and biochemical studies of apicomplexan aspartic proteases (e.g., plasmepsin X, TgASP5), using protein purification, crystallography and modeling to illuminate mechanisms of zymogen inactivation and inhibitor binding. nih+2
PhD training at IIT Bombay in protein crystallography: Listed as a former member of the Protein Crystallography Lab and as a research scholar at IIT Bombay, her graduate work produced multiple peer-reviewed papers and preprints in structural biology. ac+1
Transition to glycosylation and cancer translational research: As a postdoctoral fellow at CRCM (GLYNTHERA team), she shifted focus to O-glycosylation in cancer, cell–cell and cell–ECM interactions, and the development of glyco-specific/bispecific antibody tools for therapeutic targeting. crcm-marseille+1
Collaborative, translational orientation: Her recent work includes translational projects (e.g., antibody-tool development in collaboration with industry partners) indicating an applied, collaborative approach to moving molecular and structural findings toward therapeutic strategies. crcm-marseille

Work

Education

Projects

Writing

Inhibition of Plasmodium falciparum plasmepsins by drugs targeting HIV-1 protease: A way forward for antimalarial drug discovery

January 1, 2024

Study showing that HIV-1 protease inhibitors (ritonavir and lopinavir) inhibit plasmepsin II and plasmepsin X, with structural and biochemical analyses supporting repurposing strategies and inhibitor design for antimalarial therapy.

Favicon imagepmc.ncbi.nlm.nih.gov

Toxoplasma gondii aspartic protease 5: structural basis of substrate binding and inhibition mechanism

January 1, 2024

Structural and modeling studies of TgASP5, describing active-site architecture, substrate specificity determinants and analyses of known aspartic protease inhibitors as starting scaffolds for TgASP5-targeted inhibitor development.

Favicon imagepubmed.ncbi.nlm.nih.gov

Structures of plasmepsin X from Plasmodium falciparum reveal a novel inactivation mechanism of the zymogen and molecular basis for binding of inhibitors in mature enzyme

January 1, 2022

Structural characterization of PfPMX zymogen and mature enzyme, describing a novel inactivation mechanism and detailing substrate and inhibitor binding to inform inhibitor development against apicomplexan pepsin-like aspartic proteases.

Favicon imagepubmed.ncbi.nlm.nih.gov