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Internally quenched peptides for the study of lysostaphin: An antimicrobial protease that kills Staphylococcus aureus (2006)
Journal Article

Lysostaphin (EC. 3.4.24.75) is a protein secreted by Staphylococcus simulans biovar staphylolyticus and has been shown to be active against methicillin resistant S. aureus (MRSA). The design and synthesis of three internally quenched substrates for l... Read More about Internally quenched peptides for the study of lysostaphin: An antimicrobial protease that kills Staphylococcus aureus.

The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA (2006)
Journal Article
Zhang, W., Allen, S., Roberts, C. J., & Soultanas, P. (2006). The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA. Journal of Bacteriology, 188(15), https://doi.org/10.1128/JB.00339-06

The essential Bacillus subtilis DnaD and DnaB proteins have been implicated in the initiation of DNA replication. Recently, DNA remodeling activities associated with both proteins were discovered that could provide a link between global or local nucl... Read More about The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.

A Porous Framework Polymer Based on a Zinc(II) 4,4‘-Bipyridine-2,6,2‘,6‘-tetracarboxylate:  Synthesis, Structure, and “Zeolite-Like” Behaviors (2006)
Journal Article

The robust metal-organic framework compound {[Zn2(L)] ·4H2O}∞ I has been synthesized by hydrothermal reaction of ZnCl2 and 4,4′-bipyridine-2,6, 2′,6′-tetracarboxylic acid (H4L). Compound I crystallizes in a chiral space group, P42212, with the chiral... Read More about A Porous Framework Polymer Based on a Zinc(II) 4,4‘-Bipyridine-2,6,2‘,6‘-tetracarboxylate:  Synthesis, Structure, and “Zeolite-Like” Behaviors.

Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis (2006)
Journal Article
Ioannou, C., Schaeffer, P. M., Dixon, N. E., & Soultanas, P. (2006). Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis. Nucleic Acids Research, 34(18), https://doi.org/10.1093/nar/gkl690

The Bacillus subtilis DnaI, DnaB and DnaD proteins load the replicative ring helicase DnaC onto DNA during priming of DNA replication. Here we show that DnaI consists of a C-terminal domain (Cd) with ATPase and DNA-binding activities and an N-termina... Read More about Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis.