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- Publications
- Influence
Differential plasma protein binding to metal oxide nanoparticles.
- Z. Deng, Gysell M. Mortimer, Tara Schiller, Anthony W. Musumeci, D. Martin, R. Minchin
- Chemistry, Medicine
- Nanotechnology
- 11 November 2009
Nanoparticles rapidly interact with the proteins present in biological fluids, such as blood. The proteins that are adsorbed onto the surface potentially dictate the biokinetics of the nanomaterials… Expand
Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation.
- Z. Deng, Mingtao Liang, M. Monteiro, I. Toth, R. Minchin
- Chemistry, Medicine
- Nature nanotechnology
- 2011
The chemical composition, size, shape and surface characteristics of nanoparticles affect the way proteins bind to these particles, and this in turn influences the way in which nanoparticles interact… Expand
Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli.
- C. Cruickshank, R. Minchin, A. L. Le Dain, B. Martinac
- Chemistry, Medicine
- Biophysical journal
- 1 October 1997
The open channel diameter of Escherichia coli recombinant large-conductance mechanosensitive ion channels (MscL) was estimated using the model of Hille (Hille, B. 1968. Pharmacological modifications… Expand
N-and O-acetylation of aromatic and heterocyclic amine carcinogens by human monomorphic and polymorphic acetyltransferases expressed in COS-1 cells.
- R. Minchin, P. Reeves, +4 authors F. Kadlubar
- Chemistry, Medicine
- Biochemical and biophysical research…
- 30 June 1992
Human monomorphic and polymorphic arylamine acetyltransferases (EC 2.3.1.5) were expressed in monkey kidney COS-1 cells and used to study the N- and O-acetylation of a number of carcinogenic amines… Expand
Proteasomal Degradation of N-Acetyltransferase 1 Is Prevented by Acetylation of the Active Site Cysteine
- N. Butcher, A. Arulpragasam, R. Minchin
- Biology, Medicine
- Journal of Biological Chemistry
- 21 May 2004
Many drugs and chemicals found in the environment are either detoxified by N-acetyltransferase 1 (NAT1, EC 2.3.1.5) and eliminated from the body or bioactivated to metabolites that have the potential… Expand
Cross-linking studies and membrane localization and assembly of radiolabelled large mechanosensitive ion channel (MscL) of Escherichia coli.
- C. Häse, R. Minchin, A. Kloda, B. Martinac
- Biology, Medicine
- Biochemical and biophysical research…
- 27 March 1997
The gene encoding the large conductance mechanosensitive ion channel (MscL) of Escherichia coli and several deletion mutants of mscL were cloned under the control of the T7 RNA polymerase promoter.… Expand
Metabolism of drugs and other xenobiotics in the gut lumen and wall.
- K. Ilett, L. B. Tee, P. Reeves, R. Minchin
- Biology, Medicine
- Pharmacology & therapeutics
- 1990
Metabolism in the gut lumen and wall can decrease the bioavailability and the pharmacological effects of a wide variety of drugs. Bacterial flora in the gut, the environmental pH and oxidative or… Expand
Role of intratumoural heterogeneity in cancer drug resistance: molecular and clinical perspectives
- N. A. Saunders, F. Simpson, +5 authors A. Guminski
- Biology, Medicine
- EMBO molecular medicine
- 25 June 2012
Drug resistance continues to be a major barrier to the delivery of curative therapies in cancer. Historically, drug resistance has been associated with over‐expression of drug transporters, changes… Expand
Genomic organization of human arylamine N-acetyltransferase Type I reveals alternative promoters that generate different 5'-UTR splice variants with altered translational activities.
- N. Butcher, A. Arulpragasam, H. L. Goh, T. Davey, R. Minchin
- Biology, Medicine
- The Biochemical journal
- 1 April 2005
In humans, a polymorphic gene encodes the drug-metabolizing enzyme NAT1 (arylamine N-acetyltransferase Type 1), which is widely expressed throughout the body. While the protein-coding region of NAT1… Expand
Acetylation of p-aminobenzoylglutamate, a folic acid catabolite, by recombinant human arylamine N-acetyltransferase and U937 cells.
- R. Minchin
- Chemistry, Medicine
- The Biochemical journal
- 1 April 1995
N-acetyl-p-aminobenzoylglutamate is a major urinary metabolite of folic acid. It is formed by acetylation of p-aminobenzoylglutamate following cleavage of the C9-N10 bond of folic acid. Using… Expand