Author

J. W. Schmidberger

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 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Organism:human· 1 Organism:plant (other)· 1 Assay:proteomics· 1

Frequent Co-Authors

C. S. Bond· 2 shared J. Haywood· 2 shared J. S. Mylne· 2 shared S. G. Nonis· 2 shared A. G. Elliott· 1 shared A. M. James· 1 shared A. P. Silva· 1 shared B. L. Parker· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiochemistry

C. S. Bond

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Author profile →

3 papers

Recent·Most cited

Structural basis for a natural circular permutation in proteins

S. G. Nonis, J. Haywood, J. W. Schmidberger, C. S. Bond, J. S. Mylne

This study elucidates the structural basis of a natural circular permutation in conA, showing how CeAEP1 catalyzes cleavage and transpeptidation to form the stable conA protein.

bioRxiv · Oct 28, 2020 · PreprintBiochemistry

The Nucleosome Remodeling and Deacetylase complex has an asymmetric, dynamic, and modular architecture

J. K. Low, A. P. Silva, M. Sharifi Tabar, M. Torrado, S. R. Webb, B. L. Parker, M. Sana, C. Smits, J. W. Schmidberger, L. Brillault, M. J. Jackman, D. C. Williams, G. A. Blobel, S. B. Hake, N. E. Shepherd, , J. P. Mackay

This study reveals the asymmetric and dynamic architecture of the NuRD complex using integrated biochemical and structural methods.

bioRxiv · Feb 17, 2020Biochemistry

The macrocyclizing protease butelase 1 remains auto-catalytic and reveals the structural basis for ligase activity

A. M. James, J. Haywood, J. Leroux, K. Ignasiak, A. G. Elliott, J. W. Schmidberger, M. F. Fisher, S. G. Nonis, R. Fenske, C. S. Bond, J. S. Mylne

The paper shows butelase 1 retains cleavage activity despite being classified as a ligase, with structural insights into its macrocyclization efficiency.

bioRxiv · Oct 21, 2018Biophysics