Author

A. K. Aggarwal

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:experimental assay· 3 Research Focus:chromatin & epigenetic regulation· 2 Organism:human· 2 Assay:structural biology· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. Bonucci· 1 shared D.-D. Vu· 1 shared E. P. Reddy· 1 shared F. Ferrage· 1 shared G. Bouvignies· 1 shared J. Kottur· 1 shared J. M. STARK· 1 shared L. Carlier· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

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1 shared paperBiophysics

A. Bonucci

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Author profile →

3 papers

Recent·Most cited

Nucleic Acid Mediated Activation of a Short Prokaryotic Argonaute Immune System

A. K. Aggarwal, J. Kottur, R. Malik

This study resolves crystal and cryo-EM structures of the SPARTA system to elucidate its activation mechanism involving nucleic acid binding and oligomerization.

bioRxiv · Sep 17, 2023Biophysics

Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro

D.-D. Vu, A. Bonucci, M. Breniere, M. Cisneros-Aguirre, P. Pelupessy, Z. Wang, L. Carlier, G. Bouvignies, P. Cortes, A. K. Aggarwal, M. Blackledge, Z. Gueroui, V. Belle, J. M. STARK, M. M. Modesti, F. Ferrage

This study characterizes the multivalent interactions of XRCC4 and XLF CTRs, showing they form condensates that enhance DNA ligation in vitro and suggest roles in NHEJ dynamics and cancer biology.

bioRxiv · Jul 12, 2023Biophysics

Mechanism of action of rigosertib does not involve tubulin binding

S. J. Baker, S. C. Cosenza, S. Athuluri-Divakar, M. V. R. Reddy, R. Vasquez-Del Carpio, R. Jain, A. K. Aggarwal, E. P. Reddy

This paper investigates the mechanism of action of rigosertib and finds that it does not involve tubulin binding, as clinical grade rigosertib lacks the impurity responsible for this activity.

bioRxiv · Dec 12, 2019 · PreprintCancer Biology