Author

C. K. Das

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

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Cancer Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:chromatin & epigenetic regulation· 2 Approach:experimental assay· 2 Approach:statistical model· 2 Organism:bacteria (other)· 1 Research Focus:cancer & tumor microenvironment· 1 Assay:ChIP-seq· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

A. M. Chinnaiyan· 1 shared A. Parolia· 1 shared B. K. Verma· 1 shared C. Hou· 1 shared E. Mitchell-Velasquez· 1 shared E. Young· 1 shared F. Altegoer· 1 shared G. Bange· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperCancer Biology

A. M. Chinnaiyan

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

NSD2 is a requisite subunit of the AR/FOXA1 neo-enhanceosome in promoting prostate tumorigenesis

A. Parolia, S. Eyunni, B. K. Verma, E. Young, L. Liu, J. George, S. Aras, C. K. Das, R. Mannan, R. ur Rasool, J. Luo, S. E. Carson, E. Mitchell-Velasquez, Y. Liu, L. Xiao, , I. A. Asangani

This study identifies NSD2 as a critical component of the AR neo-enhanceosome in prostate cancer, showing its role in AR enhancer circuitry and tumor progression.

Nature Genetics · Sep 9, 2024Peer-reviewedCancer Biology

Methyl substituted β-lactam framework based antibiotics and β-lactamase inhibitors: Proof of concept by computations

V. Thakkur, C. K. Das, S. Verma, S. Saha, N. N. Nair

This paper presents a computational proof of concept for methyl-substituted β-lactam antibiotics that slow deacylation of the acyl-enzyme complex by 109-fold without affecting binding to β-lactamase.

bioRxiv · Jan 14, 2024 · PreprintBiochemistry

The CTPase activity of ParB acts as a timing mechanism to control the dynamics and function of prokaryotic DNA partition complexes

M. Osorio-Valeriano, F. Altegoer, C. K. Das, W. Steinchen, G. Panis, L. Connolley, G. Giacomelli, H. Feddersen, L. Corrales-Guerrero, P. Giammarinaro, J. Hanssmann, M. Bramkamp, P. H. Viollier, S. Murray, L. V. Schäfer, , M. Thanbichler

This study identifies how ParB's CTPase activity regulates DNA partition complex dynamics and function by controlling clamp sliding time and spreading.

bioRxiv · May 5, 2021Microbiology