Skip To Main Content
Kankana Bardhan on Muck Rack

Kankana Bardhan

As seen in: British Journal of Cancer, Nature, Science Magazine, Cell Press, The Journal of Immunology
Is this you? As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work. Claim your profile

Get in touch with Kankana

Contact Kankana, search articles and posts on X, monitor coverage, and track replies from one place.

Learn more about Muck Rack

Actions

Share this page

Is this you?

As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.
Claim your profile

Articles

Publisher Correction: Phosphorylation of PD-1-Y248 is a marker of PD-1-mediated inhibitory function in human T cells

|
By Vassiliki A Boussiotis, Kankana Bardhan, Halil-Ibrahim Aksoylar, Thibault Le Bourgeois
| Nature Verified
Correction to: Scientific Reports https://doi.org/10.1038/s41598-019-53463-0, published online 21 November 2019 In the original version of this Article, the author Thibault Le Bourgeois was incorrectly indexed. This error has now been corrected. Author information Author notes Thibault Le Bourgeois Present address: Antoine Lacassagne Cancer Institute of Nice, Medical University of Nice Sophia Antipolis, Sophia Antipolis, France Jessica D.
Open in Who Shared Issue with article?

Acquired Resistance of EGFR-Mutated Lung Cancer to Tyrosine Kinase Inhibitor Treatment Promotes PARP Inhibitor Sensitivity

|
By Kankana Bardhan, Lynnette Marcar, Liliana Gheorghiu, Patrick Dinkelborg
| Cell Press Verified
Highlights • TKI resistance promotes PARP inhibitor sensitivity of EGFR mutant lung cancer cells • PARP inhibitor sensitivity can be traced back to the initial TKI persister state • PARP inhibitor sensitivity is mediated by NOX-dependent reactive oxygen species • Abrogating PARylation of NOX activator RAC1 phenocopies PARP inhibitor effects Summary Lung cancers with oncogenic mutations in the epidermal growth factor receptor (EGFR) invariably acquire resistance to tyrosine kinase inhibitor...
Open in Who Shared Issue with article?

The adaptor molecule RIAM integrates signaling events critical for integrin-mediated control of immune function and cancer progression

|
By Nikolaos Patsoukis, Kankana Bardhan, Jessica Weaver, Duygu Sari
| Science Magazine Verified
Rap1-interacting molecule (RIAM) is a multidomain protein that regulates multiple functions in immune cells. RIAM contains an RA (RalGDS/AF-6 or Ras-association) domain, a PH (pleckstrin homology) domain, and two proline-rich regions. It also contains two putative coiled-coil regions at the amino (N) terminus. The simultaneous interaction of PH and RA domains with their partners results in relocation of RIAM to the plasma membrane upon cell activation.
Open in Who Shared Issue with article?
See all 6 articles