Author

L. K. M. Blomgren

University of ZurichORCID 0000-0003-3833-0227Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:cell-cell communication· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

Céline Bürer· 2 shared D. Sean FroeseiD· 2 shared Arnaud BasléiD· 1 shared Linda R. Buchler· 1 shared Melanie Huber· 1 shared Sabrina R. MackinnoniD· 1 shared Thomas J. McCorvieiD· 1 shared V. R. T. ZanotelliiD· 1 shared

Activity by Year

2023-2024 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 26 mutual co-author links

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2 shared papersBiochemistry

Céline Bürer

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2 papers

Recent·Most cited

BiochemistryBiochimiePeer-reviewedNov 19, 2024

Evidence for Interaction of 5,10-Methylenetetrahydrofolate Reductase (MTHFR) with Methylenetetrahydrofolate Dehydrogenase (MTHFD1) and General Control Nonderepressible 1 (GCN1)

Linda R. Buchler, L. K. M. Blomgren, Céline Bürer…·D. Sean Froese

The paper shows that MTHFR phosphorylation depends on methionine levels and identifies MTHFR interactions with MTHFD1 and GCN1.

2 citations

humanproteomics

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BiochemistrybioRxivAug 2, 2023

Dynamic inter-domain transformations mediate the allosteric regulation of human 5, 10-methylenetetrahydrofolate reductase

Linnea K. M. Blomgren, Melanie Huber, Sabrina R. Mackinnon…·Thomas J. McCorvie

The paper determines cryo-EM structures of human MTHFR bound to SAM and SAH, revealing how inter-domain transformations mediate allosteric regulation by altering active site accessibility.

DOI 10.1038/s41467-024-47174-y

𝕏 PostBluesky