Author

W. Margolin

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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Microbiology· 3 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:E. coli· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:cell type annotation· 2 Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:development & morphogenesis· 1

Frequent Co-Authors

G. Rivas· 2 shared A. Bhambhani· 1 shared A. Burt· 1 shared A. Desfosses· 1 shared A. Marconi· 1 shared A. Parks· 1 shared B. Monterroso· 1 shared C. Alfonso· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersBiochemistry

G. Rivas

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

A fluorescent reporter for FtsA is functional as the sole FtsA in Escherichia coli and has hypermorphic properties

T. A. Cameron, W. Margolin

The paper develops a fluorescent FtsA fusion that functions as the sole FtsA in E. coli, enabling live-cell monitoring of FtsA dynamics during division.

bioRxiv · Oct 31, 2022 · PreprintMicrobiology

Bacteriophage SP01 Gene Product 56 (gp56) Inhibits Bacillus subtilis Cell Division by Interacting with DivIC/FtsL to Prevent Pbp2B/FtsW Recruitment

A. Bhambhani, I. Iadicicco, J. Lee, S. Ahmed, M. Belfatto, D. Held, A. Marconi, A. Parks, C. Stewart, W. Margolin, P. A. Levin, D. P. Haeusser

This paper identifies gp56, a bacteriophage protein, as an inhibitor of Bacillus subtilis cell division by blocking recruitment of late division proteins through interaction with DivIC/FtsL.

Journal of Bacteriology · Dec 18, 2020Peer-reviewedMicrobiology

Assembly of bacterial cell division protein FtsZ into dynamic biomolecular condensates

M. A. Robles-Ramos, S. Zorrilla, C. Alfonso, W. Margolin, G. Rivas, B. Monterroso

This study shows FtsZ can form dynamic biomolecular condensates independently of SlmA, suggesting a broader role for phase separation in bacterial cell division.

bioRxiv · Aug 27, 2020Biochemistry

Complete structure of the core signalling unit of the E. coli chemosensory array in an optimised minicell strain

A. Burt, C. K. Cassidy, P. Ames, M. Bacia-Verloop, M. Baulard, K. Huard, Z. Luthey-Schulten, A. Desfosses, P. J. Stansfeld, W. Margolin, J. S. Parkinson, I. Gutsche

The paper presents a 3D map of the E. coli chemosensory core signalling unit using cryo-ET and subtomogram averaging, combined with molecular dynamics simulations to create an atomistic model.

bioRxiv · Aug 5, 2019Cell Biology

Escherichia coli ZipA organizes FtsZ polymers into dynamic ring-like protofilament structures

W. Margolin, M. Krupka, M. Sobrinos-Sanguino, M. Jimenez, G. Rivas

This paper shows ZipA does not reduce FtsZ dynamics by bundling but instead allows dynamic FtsZ vortices at low surface densities on lipid membranes.

bioRxiv · May 14, 2018Microbiology