Author

C. E. Berndsen

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 3 Organism:Arabidopsis· 2 Organism:human· 2 Research Focus:cell type annotation· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

C. M. Ravenburg· 2 shared I. R. Roy· 2 shared J. D. Monroe· 2 shared A. M. White· 1 shared C. Buchholz· 1 shared C. K. Sutton· 1 shared J. E. Hayes· 1 shared M. A. Friedman· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

C. M. Ravenburg

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4 papers

Recent·Most cited

Structural and functional analysis of the human Cone-rod homeobox transcription factor

P.-M. Clanor, C. Buchholz, J. E. Hayes, M. A. Friedman, A. M. White, R. A. Enke, C. E. Berndsen

This study presents the first structural analysis of the human CRX homeodomain using bioinformatics and SAXS, revealing its monomeric structure and DNA-binding capability.

bioRxiv · Jan 9, 2022Biochemistry

The β-amylase7 gene in Zea mays encodes a protein with structural and catalytic properties similar to Arabidopsis BAM2

C. M. Ravenburg, M. B. Riney, J. D. Monroe, C. E. Berndsen

The paper investigates the structural and catalytic properties of ZmBAM7-S, suggesting it may function similarly to AtBAM2 despite being annotated as a BAM7 gene.

bioRxiv · Oct 14, 2021 · PreprintBiochemistry

Solution structure and assembly of β-amylase 2 from Arabidopsis thaliana

N. P. Chandrasekharan, C. M. Ravenburg, I. R. Roy, J. D. Monroe, C. E. Berndsen

The paper determines the solution structure and assembly of AtBAM2 from Arabidopsis thaliana using small-angle X-ray scattering, revealing a tetramer with unique features compared to BAM5 from sweet potato.

bioRxiv · Sep 17, 2019 · PreprintBiochemistry

Resilience of BST-2/Tetherin structure to single amino acid substitutions

I. R. Roy, C. K. Sutton, C. E. Berndsen

The paper investigates how single amino acid substitutions in the ectodomain of human Tetherin affect its structure and function, finding that most mutations do not disrupt structure or function.

bioRxiv · Nov 26, 2018Biochemistry