Author

S. Maslen

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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Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Organism:E. coli· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

S. M. Freund· 3 shared S. H. McLaughlin· 2 shared A. Albecka· 1 shared A. Berndt· 1 shared A. Boland· 1 shared C. H. Douse· 1 shared C. W. Yu· 1 shared C. W.-H. Yu· 1 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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3 shared papersBiochemistry

S. M. Freund

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Author profile →

3 papers

Recent·Most cited

The bacterial actin-like cell division protein FtsA forms curved antiparallel double filaments upon binding of FtsN

T. Nierhaus, S. H. McLaughlin, F. Bürmann, D. Kureisaite-Ciziene, S. Maslen, M. J. Skehel, C. W. Yu, S. M. Freund, L. F. Funke, J. W. Chin, J. Löwe

This study shows that FtsA forms curved antiparallel double filaments when bound to FtsN, similar to MreB, and suggests these structures orient septal PG synthesis during bacterial division.

bioRxiv · Nov 8, 2021 · PreprintMicrobiology

Bipartite binding and partial inhibition links DEPTOR and mTOR in a mutually antagonistic embrace

R. L. Williams, M. Heimhalt, A. Berndt, J. L. Wagstaff, M. Anandapadamanaban, O. Perisic, S. Maslen, S. H. McLaughlin, C. W.-H. Yu, G. R. Masson, A. Boland, X. Ni, K. Yamashita, G. N. Murshudov, M. Skehel, S. M. Freund

This study investigates the interaction between DEPTOR and mTORC1, revealing DEPTOR as a partial inhibitor that is more effective against activated mTORC1, with mutual antagonism mediated by phosphorylation and structural interactions.

bioRxiv · Apr 28, 2021Biochemistry

Periphilin self-association underpins epigenetic silencing by the HUSH complex

D. M. Prigozhin, A. Albecka, C. H. Douse, I. A. Tchasovnikarova, R. T. Timms, L. E. Farleigh, S.-i. Oda, S. M. Freund, S. Maslen, P. J. Lehner, Y. Modis

This study identifies the physicochemical properties of Periphilin required for HUSH complex assembly and epigenetic silencing, showing its N-terminal domain drives aggregation and repressive mark deposition.

bioRxiv · Dec 18, 2019Biochemistry