Author

A. M. Spring

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

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:differential expression· 1 Organism:Drosophila· 1

Frequent Co-Authors

A. C. Raimer· 2 shared A. G. Matera· 2 shared G. D. Van Duyne· 2 shared K. Gupta· 2 shared Y. Wen· 2 shared A. D. Ebert· 1 shared A. I. Lamond· 1 shared C. L. Lorson· 1 shared

Activity by Year

2016-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersBiochemistry

A. C. Raimer

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Author profile →

2 papers

Recent·Most cited

Assembly of higher-order SMN oligomers is essential for metazoan viability and requires an exposed structural motif present in the YG zipper dimer

K. Gupta, Y. Wen, N. S. Ninan, A. C. Raimer, R. Sharp, A. M. Spring, K. L. Sarachan, M. C. Johnson, G. D. Van Duyne, A. G. Matera

This study identifies a structural motif in the SMN YG box essential for higher-order oligomerization, which is critical for viability and linked to SMA in animal models.

bioRxiv · Nov 7, 2020Biochemistry

Self-oligomerization regulates stability of Survival Motor Neuron (SMN) protein isoforms by sequestering an SCFSlmb degron

K. M. Gray, K. A. Kaifer, D. Baillat, Y. Wen, T. R. Bonacci, A. D. Ebert, A. C. Raimer, A. M. Spring, S. ten Have, J. J. Glascock, K. Gupta, G. D. Van Duyne, M. J. Emanuele, A. I. Lamond, E. J. Wagner, , A. G. Matera

The paper identifies SCFSlmb as a regulator of SMN protein stability through a degron, showing that self-oligomerization stabilizes SMN isoforms and mitigates SMA severity.

bioRxiv · Sep 30, 2016Biochemistry