Author

J. E. Molloy

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 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:development & morphogenesis· 1 Assay:DNA methylation· 1

Frequent Co-Authors

I. Kursula· 2 shared A. J. Lopez· 1 shared B. W. Hoogenboom· 1 shared D. P. Mulvihill· 1 shared G. I. Mashanov· 1 shared I. A. Gyamfi· 1 shared I. Pires· 1 shared J. Vahokoski· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 11 mutual co-author links

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2 shared papersBiochemistry

I. Kursula

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Characterization of Plasmodium falciparum myosin B in complex with the calmodulin-like domain of its light chain MLC-B

I. Pires, Y.-F. Hung, U. Bergmann, J. E. Molloy, I. Kursula

This paper characterizes Plasmodium falciparum myosin B's structure and function, showing its role in red blood cell invasion and identifying regulatory light chains that bind to it.

bioRxiv · May 28, 2022Biochemistry

Single-molecule measurements reveal that PARP1 condenses DNA by loop formation

N. A. W. Bell, P. J. Haynes, K. Brunner, T. Maia de Oliveira, M. Flocco, B. W. Hoogenboom, J. E. Molloy

This study shows PARP1 condenses undamaged DNA through loop formation using single-molecule techniques, revealing a mechanism for chromatin organization.

bioRxiv · Sep 15, 2020Biophysics

High-resolution structures of malaria parasite actomyosin and actin filaments

J. Vahokoski, L. J. Calder, A. J. Lopez, J. E. Molloy, P. B. Rosenthal, I. Kursula

This paper presents the first high-resolution structure of the malaria parasite actomyosin motor complex and reveals new atomic details of the ATPase site and conformational changes.

bioRxiv · Jul 2, 2020Biophysics

TorC2 dependent phosphorylation modulates calcium regulation of fission yeast myosin.

K. B. Baker, I. A. Gyamfi, G. I. Mashanov, J. E. Molloy, M. A. Geeves, D. P. Mulvihill

The paper investigates how TORC2-dependent phosphorylation of myosin-1 in fission yeast affects calcium regulation and cell growth during mitotic and meiotic cycles.

bioRxiv · Dec 18, 2018 · PreprintCell Biology