Author

K. Long

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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Biochemistry· 2 Cancer Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 2 Assay:proteomics· 2 Assay:bulk RNA-seq· 1 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1

Frequent Co-Authors

A. Joe· 1 shared A. L. Bohanon· 1 shared A. Piserchio· 1 shared B. E. Mendelson· 1 shared C. Adamchak· 1 shared C. J. Petzold· 1 shared D. Bhattacharjee· 1 shared D. D. Luu· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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1 shared paperMicrobiology

A. Joe

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

A drug's most potent target is not necessarily the source of its anti-cancer activity

D. Bhattacharjee, J. Bakar, E. L. Sausville, B. E. Mendelson, K. Long, J. C. Smith, J. M. Sheltzer

This study shows that ralimetinib's anti-cancer effect is due to EGFR inhibition, not p38, and highlights the need for comprehensive profiling to determine drug mechanisms.

Cell Chemical Biology · Oct 1, 2023Peer-reviewedCancer Biology

Structural Basis for the Calmodulin-Mediated Activation of eEF-2K

A. Piserchio, E. A. Isiroho, K. Long, A. L. Bohanon, E. A. Kumar, N. Will, D. Jeruzalmi, K. N. Dalby, R. Ghose

The paper determines the atomic structure of the calmodulin-eEF-2KTR complex, revealing the mechanism by which calmodulin activates eEF-2K through an allosteric spine.

bioRxiv · Jan 15, 2022 · PreprintBiochemistry

METTL3 promotes homologous recombination repair and modulates chemotherapeutic response by regulating the EGF/Rad51 axis

E. Li, M. Xia, Y. Du, K. Long, F. Ji, F. Pan, L. He, Z. Hu, Z. Guo

This study identifies METTL3's role in promoting homologous recombination repair and modulating chemotherapeutic response in breast cancer cells by regulating the EGF/RAD51 axis through m6A modification.

bioRxiv · Nov 11, 2021Biochemistry

Sulfated RaxX, which represents an unclassified group of ribosomally synthesized post-translationally modified peptides, binds a host immune receptor

D. D. Luu, A. Joe, Y. Chen, K. Parys, O. Bahar, R. Pruitt, L. J. G. Chen, C. J. Petzold, K. Long, C. Adamchak, V. Stewart, Y. Belkhadir, P. C. Ronald

The paper identifies RaxX as a sulfated RiPP that binds the rice immune receptor XA21, revealing its role in bacterial immune activation.

bioRxiv · Oct 13, 2018Microbiology