Author

D. Lane

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· 2 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

A. Chandramohan· 1 shared A. Hariharan· 1 shared A. Partridge· 1 shared A. Sadruddin· 1 shared B. Henry· 1 shared C. J. Brown· 1 shared C. S. Verma· 1 shared C. Turlan· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

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1 shared paperBiochemistry

A. Chandramohan

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Fever-like temperature bursts promote competence development via an HtrA-dependent pathway in Streptococcus pneumoniae.

M. Maziero, D. Lane, P. Polard, M. Berge

The paper shows that fever-like temperature increases induce competence in Streptococcus pneumoniae via an HtrA-dependent pathway, independent of other stress signals.

bioRxiv · Apr 15, 2023 · PreprintMicrobiology

Role of centromere sites in activation of ParB proteins for partition complex assembly

S. Audibert, N. Tanguy-le-Gac, J. Rech, C. Turlan, J.-Y. Bouet, K. Bystricky, D. Lane

The paper investigates whether ParB proteins can assemble visible partition complexes without requiring parS insertion, finding that specific parS binding is necessary for complex formation.

PLOS ONE · May 7, 2020Peer-reviewedMicrobiology

Both DNA binding domains of p53 are required for its ultra rapid recruitment to sites of UV damage

Y.-H. Wang, T. Ho, A. Hariharan, H. C. Goh, M. Sheetz, D. Lane

The paper shows p53 requires both DNA binding and C-terminal domains for ultra-rapid recruitment to UV damage sites, which is PARP-dependent and inhibited by cancer-associated mutations.

bioRxiv · Feb 9, 2020 · PreprintCell Biology

Macrocyclization of an all-D linear peptide improves target affinity and imparts cellular activity: A novel stapled α-helical peptide modality

S. Kannan, P. G. A. Aronica, S. Ng, D. Thean, Y. Frosi, S. Chee, J. Shimin, T. Y. Yuen, A. Sadruddin, H. Y. K. Kaan, A. Chandramohan, J. H. Wong, Y. S. Tan, F. J. Ferrer, P. Arumugam, , A. Partridge

This paper combines macrocyclization and D-amino acid strategies to create an all-D helical peptide with improved target affinity and cellular activity.

bioRxiv · Sep 12, 2019 · PreprintBiochemistry