Nature Communications (Feb 2021)
System-wide identification and prioritization of enzyme substrates by thermal analysis
- Amir Ata Saei,
- Christian M. Beusch,
- Pierre Sabatier,
- Juan Astorga Wells,
- Hassan Gharibi,
- Zhaowei Meng,
- Alexey Chernobrovkin,
- Sergey Rodin,
- Katja Näreoja,
- Ann-Gerd Thorsell,
- Tobias Karlberg,
- Qing Cheng,
- Susanna L. Lundström,
- Massimiliano Gaetani,
- Ákos Végvári,
- Elias S. J. Arnér,
- Herwig Schüler,
- Roman A. Zubarev
Affiliations
- Amir Ata Saei
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Christian M. Beusch
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Pierre Sabatier
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Juan Astorga Wells
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Hassan Gharibi
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Zhaowei Meng
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Alexey Chernobrovkin
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Sergey Rodin
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Katja Näreoja
- Department of Biosciences and Nutrition, Karolinska Institutet
- Ann-Gerd Thorsell
- Department of Biosciences and Nutrition, Karolinska Institutet
- Tobias Karlberg
- Department of Biosciences and Nutrition, Karolinska Institutet
- Qing Cheng
- Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Susanna L. Lundström
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Massimiliano Gaetani
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Ákos Végvári
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Elias S. J. Arnér
- Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Herwig Schüler
- Department of Biosciences and Nutrition, Karolinska Institutet
- Roman A. Zubarev
- Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- DOI
- https://doi.org/10.1038/s41467-021-21540-6
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 13
Abstract
The global identification of enzyme substrates is still challenging. Here, the authors develop a method based on proteome-wide thermal shift assays to discover enzyme substrates directly from cell lysates, identifying known and novel oxidoreductase, kinase and poly-(ADP-ribose) polymerase substrates.
