Author

M. Balparda

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Plant Biology· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:proteomics· 3 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:development & morphogenesis· 2 Approach:experimental assay· 2 Organism:plant (other)· 2 Organism:Arabidopsis· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

V. G. Maurino· 3 shared A. R. Fernie· 2 shared S. Alseekh· 2 shared A. Bovdilova· 1 shared A. Kerim· 1 shared C. E. Alvarez· 1 shared I. C. Wuthenow· 1 shared I. Finkemeier· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersPlant Biology

V. G. Maurino

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Natural variation in Arabidopsis thaliana highlights a key role of Glyoxalase I;2 in detoxifying glucose-derived reactive carbonyl species

M. Bouzid, M. Balparda, A. Kerim, C. E. Alvarez, A. R. Fernie, S. Alseekh, V. G. Maurino

The paper identifies natural variation in Arabidopsis thaliana ecotypes for detoxifying glucose-derived reactive carbonyl species, highlighting the role of GLXI;2 in this process.

bioRxiv · Dec 20, 2023Plant Biology

Viridiplantae-specific GLXI and GLXII isoforms co-evolved and detoxify glucosone in planta

M. Balparda, J. Schmitz, M. Duemmel, I. C. Wuthenow, M. Schmidt, S. Alseekh, A. R. Fernie, M. J. Lercher, V. G. Maurino

The paper identifies two distinct glyoxalase systems in plants, showing one evolved from eukaryotes and the other acquired via horizontal gene transfer, with unique structural and functional adaptations for detoxifying reactive carbonyl species.

bioRxiv · Sep 13, 2022Plant Biology

Acetylation of conserved lysines fine-tune mitochondrial malate dehydrogenase activity in land plants

M. Balparda, M. Elsässer, M. Badia, J. Giese, A. Bovdilova, M. Hüdig, L. Reinmuth, M. Schwarzländer, I. Finkemeier, M. Schallenberg-Rüdinger, V. G. Maurino

The paper identifies lysine acetylation as a conserved regulatory mechanism in land plants, showing it fine-tunes mitochondrial malate dehydrogenase activity in a species-specific manner.

bioRxiv · Oct 30, 2020Plant Biology