Author

M. Serna

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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Biophysics· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Assay:cryo-EM· 2 Research Focus:host-pathogen & immune response· 2 Research Focus:chromatin & epigenetic regulation· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

O. Llorca· 2 shared A. Gonzalez-Corpas· 1 shared A. Lopez-Perrote· 1 shared A. Menny· 1 shared A. P. Joseph· 1 shared B. P. Morgan· 1 shared C. F. Rodriguez· 1 shared C. Garcia-Martin· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersCell Biology

O. Llorca

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

CDK1 and PLK1 cooperate to regulate BICD2, dynein activation and recruitment to the nucleus as well as centrosome separation in G2/M

N. Gallisa-Sune, P. Sanchez-Fernandez-de-Landa, F. Zimmermann, M. Serna, J. Paz, L. Regue, O. Llorca, J. Luders, J. Roig

This study identifies CDK1 and PLK1-mediated phosphorylation of BICD2 as essential for dynein activation and nuclear processes during G2/M.

bioRxiv · Nov 4, 2021Cell Biology

Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA decay factor DHX34, as evidenced by Cryo-EM

O. Llorca, A. Lopez-Perrote, N. Hug, A. Gonzalez-Corpas, C. F. Rodriguez, M. Serna, C. Garcia-Martin, J. Boskovic, R. Fernandez-Leiro, J. F. Caceres

The paper shows DHX34 interacts with RUVBL1-RUVBL2 and alters its conformation to reduce ATP hydrolysis, linking it to NMD activation.

bioRxiv · Sep 28, 2020Biophysics

CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers

A. Menny, M. Serna, C. M. Boyd, S. Gardner, A. P. Joseph, B. P. Morgan, M. Topf, N. J. Brooks, D. Bubeck

This study uses cryo-EM to show how the complement membrane attack complex interacts with lipid bilayers through distinct mechanisms involving C6/C7 and C8/C9, revealing structural insights into pore formation and membrane disruption.

bioRxiv · Aug 17, 2018Biophysics