Author

S. Doublie

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 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein structure prediction· 3 Assay:structural biology· 3 Organism:human· 2 Organism:C. elegans· 1

Frequent Co-Authors

B. E. Eckenroth· 3 shared A. Shen· 2 shared J. A. Dragon· 2 shared A. E. Rohlfing· 1 shared A. M. Averill· 1 shared B. L. Carroll· 1 shared C. Alves Feliciano· 1 shared E. R. Forster· 1 shared

Activity by Year

2018-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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3 shared papersMicrobiology

B. E. Eckenroth

Mutual co-authors in cluster

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4 papers

Recent·Most cited

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

Allosteric activation of CwlD amidase activity by the GerS lipoprotein during Clostridioides difficile spore formation

C. Alves Feliciano, B. E. Eckenroth, O. R. Diaz, S. Doublie, A. Shen

This study determines the crystal structure of the CwlD:GerS complex in C. difficile, revealing that GerS stabilizes zinc binding to CwlD, essential for its amidase activity during spore formation.

bioRxiv · Jun 21, 2021Microbiology

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

The CspC pseudoprotease regulates germination of Clostridioides difficile spores in response to multiple environmental signals

A. E. Rohlfing, B. E. Eckenroth, E. R. Forster, Y. Kevorkian, M. L. Donnelly, H. Benito de la Puebla, S. Doublie, A. Shen

This study identifies CspC as a bile salt sensor for C. difficile spore germination and shows it also responds to amino acid and calcium co-germinants through specific residues.

bioRxiv · Nov 5, 2018Microbiology