Biomedical Sciences Research Complex (BSRC)
The Biomedical Sciences Research Complex (BSRC) is an interdisciplinary research centre involving the Schools of Biology, Chemistry, Medicine and Physics and Astronomy. Research at the centre focuses on infection and immunity, chemical biology, DNA repair and enzymology, and is underpinned by world-class facilities for structural biology, proteomics and synthetic chemistry.
For more information please visit the Biomedical Sciences Research Complex (BSRC) home page.
This material is presented to ensure timely dissemination of scholarly and technical work. Copyright and all rights therein are retained by authors or by other copyright holders. All persons copying this information are expected to adhere to the terms and constraints invoked by each author's copyright. In most cases, these works may not be reposted without the explicit permission of the copyright holder.
Collections in this community
(2016-08-01) - Journal itemMonoamine oxidases (MAO) influence the monoamine levels in brain by virtue of their role in neurotransmitter breakdown. MAO B is the predominant form in glial cells and in platelets. MAO B structure, function and kinetics ...
Fatty acid-mediated inhibition of metal binding to the multi-metal site on serum albumin : implications for cardiovascular disease (2016) - Journal articleHuman serum albumin (HSA) is the major protein in blood plasma and is responsible for circulatory transport of a range of small molecules including fatty acids, metal ions and drugs. We previously identified the major ...
(2017-01-24) - Journal item
Recombinant vacuolar iron transporter family homologue PfVIT from human malaria-causing Plasmodium falciparum is a Fe2+/H+ exchanger (2017-02-15) - Journal articleVacuolar iron transporters (VITs) are a poorly understood family of integral membrane proteins that can function in iron homeostasis via sequestration of labile Fe2+ into vacuolar compartments. Here we report on the ...
(2016-02-15) - Journal articleThe substrate scope of fluorinase enzyme mediated transhalogenation reactions is extended. Substrate tolerance allows a peptide cargo to be tethered to a 5'-chloro-5'-deoxynucleoside substrate for transhalogenation by the ...