Author

J. A. Dragon

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 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 3 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Assay:bulk RNA-seq· 1 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

S. Doublie· 2 shared A. Baraev· 1 shared A. Cao· 1 shared A. D'Amico· 1 shared A. M. Averill· 1 shared A. Veillette· 1 shared B. E. Eckenroth· 1 shared B. L. Carroll· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 11 mutual co-author links

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Curved chords = mutual co-authorship

2 shared papersBiochemistry

S. Doublie

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The Fatty Acid Binding Protein Family Represents a Novel Target in Multiple Myeloma

M. Farrell, H. Fairfield, M. Karam, A. D'Amico, C. S. Murphy, C. Falank, R. S. Pistofidi, A. Cao, C. R. Marinac, J. A. Dragon, L. McGuinness, C. G. Gartner, R. D. Iorio, E. Jachimowicz, V. DeMambro, , M. R. Reagan

This paper identifies the fatty acid binding protein (FABP) family as a novel therapeutic target in multiple myeloma, showing that FABP inhibition reduces tumor growth and alters key cellular processes.

eLife · Mar 7, 2023Peer-reviewedCancer Biology

Caught in Motion: Human NTHL1 Undergoes Interdomain Rearrangement Necessary for Catalysis

B. L. Carroll, K. E. Zahn, J. P. Hanley, S. S. Wallace, J. A. Dragon, S. Doublie

This study reports the first X-ray structure of human NTHL1, revealing an open conformation essential for catalysis and showing that interdomain rearrangement is critical for DNA binding.

bioRxiv · Aug 13, 2021Biochemistry

Unique structural features of mammalian NEIL2 DNA glycosylase prime its activity for diverse DNA substrates and environments

B. E. Eckenroth, V. Cao, A. M. Averill, J. A. Dragon, S. Doublie

This study presents the first crystal structure of NEIL2 DNA glycosylase, revealing its unique conformational dynamics and substrate preferences, along with characterization of three cancer variants.

bioRxiv · Feb 28, 2020Biochemistry

Critical role for Slam/SAP signaling in the thymic developmental programming of IL-17- and IFN-γ-producing γδ T cells

O. Dienz, V. L. DeVault, S. C. Musial, S. K. Mistri, L. Mei, A. Baraev, J. A. Dragon, D. Krementsov, A. Veillette, J. E. Boyson

This study shows that SLAM/SAP signaling is critical for thymic development of IL-17 and IFN-γ-producing γδ T cells, with subset-specific dependencies.

bioRxiv · Oct 11, 2019Immunology