Author

V. Dharmarajan

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:biophysical modeling· 1 Assay:ChIP-seq· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

P. R. Griffin· 3 shared A. L. Burlingame· 1 shared B. D. Pascal· 1 shared C. E. Fowler· 1 shared C. G. Mayne· 1 shared D. J. Hosfield· 1 shared D. J. Kojetin· 1 shared D. P. Marciano· 1 shared

Activity by Year

2018-2018 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiophysics

P. R. Griffin

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Author profile →

3 papers

Recent·Most cited

Disorganization of the histone core promotes organization of heterochromatin into phase-separated droplets

S. Sanulli, M. J. Trnka, V. Dharmarajan, R. W. Tibble, B. D. Pascal, A. L. Burlingame, P. R. Griffin, J. D. Gross, G. J. Narlikar

This study shows that the S. pombe HP1 protein Swi6 promotes chromatin compaction through phase-separated droplets by disorganizing the histone core and increasing histone residue accessibility.

bioRxiv · Nov 18, 2018 · PreprintBiophysics

The SERM/SERD Bazedoxifene Disrupts ESR1 Helix 12 to Overcome Acquired Hormone Resistance in Breast Cancer Cells

S. W. Fanning, R. Jeselsohn, V. Dharmarajan, C. G. Mayne, M. Karimi, G. Buchwalter, R. Houtman, W. Toy, C. E. Fowler, M. Laine, K. E. Carlson, T. A. Martin, J. Nowak, J. C. Nwachukwu, D. J. Hosfield, , G. L. Greene

This study shows that bazedoxifene disrupts ESR1 helix 12 to overcome acquired hormone resistance in breast cancer cells by inhibiting Y537S and D538G ER mutants more effectively than tamoxifen.

bioRxiv · Apr 23, 2018Cancer Biology

Defining a canonical ligand-binding pocket in the orphan nuclear receptor Nurr1

I. M. S. de Vera, P. Munoz-Tello, V. Dharmarajan, D. P. Marciano, E. Matta-Camacho, P. K. Giri, J. Shang, T. S. Hughes, M. Rance, P. R. Griffin, D. J. Kojetin

This study shows the Nurr1 ligand-binding domain has a dynamic, solvent-accessible pocket that can bind unsaturated fatty acids, challenging the notion that it lacks a canonical ligand-binding pocket.

bioRxiv · Apr 17, 2018Biophysics