Author

S. L. Lundstrom

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· 3

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 3 Assay:proteomics· 3 Approach:experimental assay· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:deep learning· 1 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

A. A. Saei· 3 shared A. Vegvari· 3 shared M. Gaetani· 3 shared H. Gharibi· 2 shared H. Lyu· 2 shared R. A. Zubarev· 2 shared Z. Meng· 2 shared A. Chernobrovkin· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiochemistry

A. A. Saei

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Author profile →

3 papers

Recent·Most cited

Gel-Assisted Proteome Position Integral Shift (GAPPIS) Assay Returns Molecular Weight to Shotgun Proteomics and Identifies Novel Caspase 3 Substrates

Z. Meng, A. A. Saei, X. Zhang, H. Lyu, H. Gharibi, S. L. Lundstrom, A. Vegvari, M. Gaetani, R. A. Zubarev

The paper introduces GAPPIS, a method to recover molecular weight information from shotgun proteomics, identifying novel caspase 3 substrates in apoptotic cells.

bioRxiv · Feb 14, 2024 · PreprintBiochemistry

Mapping the GALNT1 substrate landscape with versatile proteomics tools

A. A. Saei, S. L. Lundstrom, H. Lyu, H. Gharibi, W. Lu, P. Fang, X. Zhang, Z. Meng, J. Wang, M. Gaetani, A. Vegvari, S. P. Gygi, R. A. Zubarev

This study identifies hundreds of novel GALNT1 substrates using proteomics tools, revealing preferences for Thr residues and Pro at positions +3 and +4, and implicating GALNT1 in diverse biological pathways.

bioRxiv · Aug 24, 2022 · PreprintBiochemistry

System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA)

A. A. Saei, C. Beusch, P. Sabatier, J. Astorga Wells, A. Chernobrovkin, S. Rodin, K. Nareoja, A.-G. Thorsell, T. Karlberg, Q. Cheng, S. L. Lundstrom, M. Gaetani, A. Vegvari, E. S. J. Arner, H. Schuler, R. Zubarev

SIESTA identifies and prioritizes enzyme substrates by detecting thermal stability changes caused by post-translational modifications, demonstrating effectiveness across multiple enzyme systems.

bioRxiv · Jan 21, 2020Biochemistry