Biochemical and spectroscopic studies of human melanotransferrin (MTf): electron-paramagnetic resonance evidence for a difference between the iron-binding site of MTf and other transferrins

Hydrophobically modified chitosan nanoliposomes for intestinal drug delivery
Zariwala, M., Bendre, H., Markiv, A., Farnaud, S., Renshaw, D., Taylor, K.M.G. and Somavarapu, S. 2018. Hydrophobically modified chitosan nanoliposomes for intestinal drug delivery. International Journal of Nanomedicine. 13, pp. 5837-5848. https://doi.org/10.2147/IJN.S166901

A novel in vitro model of simulated twice a day iron supplementation for assessment of iron uptake and cellular damage
Apostolova, P., Blesia, C., Tossou, C., Renshaw, D., Farnaud, S., Evans, R. and Zariwala, M. 2017. A novel in vitro model of simulated twice a day iron supplementation for assessment of iron uptake and cellular damage. 7th Meeting of the International Bioiron Society. Los Angeles 07 - 11 May 2017 https://doi.org/10.1002/ajh.24812

HFE mRNA expression is responsive to intracellular and extracellular iron loading: short communication
Mehta, K., Farnaud, S. and Patel, V.B. 2017. HFE mRNA expression is responsive to intracellular and extracellular iron loading: short communication. Molecular Biology Reports. 44 (5), pp. 399-403. https://doi.org/10.1007/s11033-017-4123-2

Comparative study of the bioavailability of different iron supplements to bacteria
Renshaw, D., Zariwala, M. and Farnaud, S. 2016. Comparative study of the bioavailability of different iron supplements to bacteria. European Iron Club. Innsbruck, Austria 07 - 10 Apr 2016

Fabrication and characterisation of novel protein-polysaccharide biopolymer based nanoparticles for iron delivery
Al-Obaidi, H., Patel, N., Ghafarzada, R., Malik, R., Musa, S., Chandramohan, S., Apostolova, P., Farnaud, S., Renshaw, D. and Zariwala, M. 2016. Fabrication and characterisation of novel protein-polysaccharide biopolymer based nanoparticles for iron delivery. European Iron Club. Innsbruck, Austria 07 - 10 Apr 2016

Beef protein isolate: a novel bio-matrix for formulating ferrous iron for nutritional applications
Zariwala, M., Farnaud, S., Renshaw, D. and Somavarapu, S. 2016. Beef protein isolate: a novel bio-matrix for formulating ferrous iron for nutritional applications. European Iron Club Meeting. Innsbruck, Austria 07 - 10 Apr 2016

Novel potato protein-polysaccharide nano-formulations for oral nutrient delivery
Zariwala, M., Somavarapu, S., Evans, R.W., Farnaud, S. and Renshaw, D. 2016. Novel potato protein-polysaccharide nano-formulations for oral nutrient delivery. Vitafoods. Geneva, Switzerland 30 - 30 May 2016

Characterization of hepcidin response to holotransferrin in novel recombinant TfR1 HepG2 cells
Mehta, K., Busbridge, Mark, Renshaw, D., Evans, R.W., Farnaud, S. and Patel, V. 2016. Characterization of hepcidin response to holotransferrin in novel recombinant TfR1 HepG2 cells. Blood Cells, Molecules, and Diseases. 61, pp. 37-45. https://doi.org/10.1016/j.bcmd.2016.06.008

Comparative study of bioavailability of different iron supplements to bacteria
Dagos, D., Selvam, P., Kelly, P., Evans, R., Zariwala, M., Renshaw, D. and Farnaud, S. 2015. Comparative study of bioavailability of different iron supplements to bacteria. 6th Meeting of the International Bioiron Society. Hangzhou, China 06 - 10 Sep 2015 Wiley. https://doi.org/10.1002/ajh.24277

A preliminary study of the link between iron increase in dopaminergic cells and Parkinson's disease
Mehta, K., Ahmed, B., Zariwala, M., Evans, R. and Farnaud, S. 2015. A preliminary study of the link between iron increase in dopaminergic cells and Parkinson's disease. 6th Meeting of the International Bioiron Society. Hangzhou, China 06 - 10 Sep 2015 Wiley. https://doi.org/10.1002/ajh.24277

What could insulin teach us about hepcidin? A comparative study between the iron hormone hepcidin and insulin
Mehta, K., Zariwala, M., Renshaw, D. and Farnaud, S. 2015. What could insulin teach us about hepcidin? A comparative study between the iron hormone hepcidin and insulin. 6th Meeting of the International Bioiron Society. Hangzhou, China 06 - 10 Sep 2015 Wiley. https://doi.org/10.1002/ajh.24277

Novel beta-casein nanocarriers for oral iron delivery
Zariwala, M., Somavarapu, S., Evans, R., Farnaud, S. and Renshaw, D. 2015. Novel beta-casein nanocarriers for oral iron delivery. 6th Meeting of the International Bioiron Society. Hangzhou, China 06 - 10 Sep 2015 Wiley. https://doi.org/10.1002/ajh.24277

Platform delivery technologies for nutraceutical applications
Zariwala, M., Somavarapu, S., Evans, R.W., Farnaud, S. and Renshaw, D. 2015. Platform delivery technologies for nutraceutical applications. Vitafoods . Geneva, Switzerland 05 - 07 May 2015

Novel whey protein isolate nanocarriers for oral micronutrient delivery
Farnaud, S., Renshaw, D., Somavarapu, S. and Zariwala, M. 2015. Novel whey protein isolate nanocarriers for oral micronutrient delivery. 9th NIZO Dairy Conference Milk Protein Functionality . Papendal, Netherlands 30 Sep - 02 Oct 2015

A human cell model of Parkinson’s disease confirms iron accumulation in dopaminergic neurons following 6-OHDOPA treatment
Zariwala, M. and Farnaud, S. 2014. A human cell model of Parkinson’s disease confirms iron accumulation in dopaminergic neurons following 6-OHDOPA treatment. European Iron Club Annual Meeting 2014. Verona, Italy 11 - 14 Sep 2014

Fabrication and characterization of novel hydrophobically modified chitosan nanoliposomes for oral iron delivery
Zariwala, M., Bendre, H., Markiv, A., Farnaud, S., Somavarapu, S. and Renshaw, D. 2014. Fabrication and characterization of novel hydrophobically modified chitosan nanoliposomes for oral iron delivery. European Iron Club Annual Meeting 2014. Verona, Italy 11 - 14 Sep 2014

Ascorbyl palmitate/DSPE-PEG nanocarriers for oral iron delivery: Preparation, characterisation and in vitro evaluation
Zariwala, M.G., Farnaud, S., Merchant, Z., Somavarapu, S. and Renshaw, D. 2014. Ascorbyl palmitate/DSPE-PEG nanocarriers for oral iron delivery: Preparation, characterisation and in vitro evaluation. Colloids and Surfaces B: Biointerfaces. 115 (3), pp. 86-92. https://doi.org/10.1016/j.colsurfb.2013.11.028

A novel approach to oral iron delivery using ferrous sulphate loaded solid lipid nanoparticles
Gulrez Zariwala, M., Elsaid, N., Jackson, T.L., Corral López, F., Farnaud, S., Somavarapu, S. and Renshaw, D. 2013. A novel approach to oral iron delivery using ferrous sulphate loaded solid lipid nanoparticles. International Journal of Pharmaceutics. 456 (2), pp. 400-407. https://doi.org/10.1016/j.ijpharm.2013.08.070

Preparation and Characterisation of Solid Lipid Particles for Oral Iron Delivery
Zariwala, M., Farnaud, S., Somavarapu, S. and Renshaw, D. 2013. Preparation and Characterisation of Solid Lipid Particles for Oral Iron Delivery. Fifth Congress of the International BioIron Society (IBIS), Biennial World Meeting. University College London 14 - 18 Apr 2013 Wiley. https://doi.org/10.1002/ajh.23453

Hepcidin transcription and peptide secretion are governed by different regulatory mechanisms
Mehta, K., Patel, V., Busbridge, M., Renshaw, D., Zariwala, M., Evans, R. and Farnaud, S. 2013. Hepcidin transcription and peptide secretion are governed by different regulatory mechanisms. Fifth Congress of the International BioIron Society (IBIS), Biennial World Meeting. University College London 14 - 18 Apr 2013 Wiley. https://doi.org/10.1002/ajh.23453

Hepcidin transcription and peptide secretion are governed by different regulatory mechanisms
Mehta, K., Patel, V., Busbridge Mark, Renshaw, D., Zariwala, M.G., Evans, R. and Farnaud, S. 2013. Hepcidin transcription and peptide secretion are governed by different regulatory mechanisms. American Journal of Hematology. 88, p. E55.

The transfer of iron between ceruloplasmin and transferrins
White, K.N., Conesa, C., Sánchez, L., Amini, M., Farnaud, S., Lorvoralaka, C. and Evans, R.W. 2012. The transfer of iron between ceruloplasmin and transferrins. Biochimica et Biophysica Acta: general subjects. 1820 (3), pp. 411-416. https://doi.org/10.1016/j.bbagen.2011.10.006

Increased transferrin-bound iron uptake in HepG2 cells is followed by an increase in expression of the iron hormone hepcidin pre-and post-translationally
Mehta, K., Patel, V., Busbridge Mark, Renshaw, D., Zariwala, M., Evans, R. and Farnaud, S. 2012. Increased transferrin-bound iron uptake in HepG2 cells is followed by an increase in expression of the iron hormone hepcidin pre-and post-translationally. European Iron Club Annual Meeting 2012. Rennes, France 29 - 31 Aug 2012

Comparison of iron absorption from iron supplement preparations using an in vitro Caco-2 model
Zariwala, M., Farnaud, S. and Renshaw, D. 2012. Comparison of iron absorption from iron supplement preparations using an in vitro Caco-2 model. European Iron Club Annual Meeting 2012. Rennes, France 29 - 31 Aug 2012

Transferrin receptor 2 is crucial for iron sensing in human hepatocytes
Rapisarda, C., Puppi, J., Hughes, R.D., Dhawan, A., Farnaud, S., Evans, R.W. and Sharp, P.A. 2010. Transferrin receptor 2 is crucial for iron sensing in human hepatocytes. American Journal of Physiology: Gastrointestinal and liver physiology. 299 (3), pp. G778-G783. https://doi.org/10.​1152/​ajpgi.​00157.​2010

Saliva: physiology and diagnostic potential in health and disease
Farnaud, S., Kosti, O., Getting, S.J. and Renshaw, D. 2010. Saliva: physiology and diagnostic potential in health and disease. ScientificWorldJournal. 10, pp. 434-456. https://doi.org/10.1100/tsw.2010.38

Opinion: Microdosing: safer clinical trials
Langley, G. and Farnaud, S. 2010. Opinion: Microdosing: safer clinical trials. Bioanalysis. 2 (3), pp. 393-395.

The Dr Hadwen Trust for humane research: 39 years of replacement science
Farnaud, S. 2009. The Dr Hadwen Trust for humane research: 39 years of replacement science. Alternatives to Laboratory Animals. 37 (S2), pp. 39-43.

The evolution of the three Rs
Farnaud, S. 2009. The evolution of the three Rs. Alternatives to Laboratory Animals. 37 (3), pp. 249-254.

Identification of an iron-hepcidin complex
Farnaud, S., Rapisarda, C., Bui, T.T.T., Drake, A.F., Cammack, R. and Evans, R.W. 2008. Identification of an iron-hepcidin complex. Biochemical Journal. 413 (3), pp. 553-557. https://doi.org/10.1042/BJ20080406

Isolation of lactoferrin from milk of different species: calorimetric and antimicrobial studies
Conesa, C., Sánchez, L., Rota, C., Pérez, M.D., Calvo, M., Farnaud, S. and Evans, R.W. 2008. Isolation of lactoferrin from milk of different species: calorimetric and antimicrobial studies. Comparative Biochemistry and Physiology. Part B: Biochemistry & Molecular Biology. 150 (1), pp. 131-139. https://doi.org/10.1016/j.cbpb.2008.02.005

The interaction of arginine- and tryptophan-rich cyclic hexapeptides with Escherichia coli membranes
Junkes, C., Wessolowski, A., Farnaud, S., Evans, R.W., Good, L., Bienert, M. and Dathe, M. 2008. The interaction of arginine- and tryptophan-rich cyclic hexapeptides with Escherichia coli membranes. Journal of Peptide Science. 14 (4), pp. 535-543. https://doi.org/10.1002/psc.940

Characterisation of recombinant unglycosylated human serum transferrin purified from Saccharomyces cerevisiae
Sargent, P.J., Farnaud, S., Cammack, R., Zoller, H.M.P. and Evans, R.W. 2006. Characterisation of recombinant unglycosylated human serum transferrin purified from Saccharomyces cerevisiae. BioMetals. 19 (5), pp. 513-519. https://doi.org/10.1007/s10534-005-5532-6

Modelling of a metal-containing hepcidin
Farnaud, S., Patel, A. and Evans, R.W. 2006. Modelling of a metal-containing hepcidin. BioMetals. 19 (5), pp. 527-533. https://doi.org/10.1007/s10534-005-5883-z

An overview of molecular aspects of iron metabolism
Syed, B.A., Sargent, P.J., Farnaud, S. and Evans, R.W. 2006. An overview of molecular aspects of iron metabolism. Hemoglobin. 30 (1), pp. 69-80. https://doi.org/10.1080/03630260500455318

Towards a tree-induction approach to antimicrobial activity analysis of cationic peptides
Farnaud, S., Wang, Z., Dybowski, R., Odell, E.W. and Evans, R.W. 2006. Towards a tree-induction approach to antimicrobial activity analysis of cationic peptides. Biochemistry and Cell Biology. 84 (3), p. 394. https://doi.org/10.1139/O06-900

Structure/function overview of proteins involved in iron storage and transport
Sargent, P.J., Farnaud, S. and Evans, R.W. 2005. Structure/function overview of proteins involved in iron storage and transport. Current Medicinal Chemistry. 12 (23), pp. 2683-2693. https://doi.org/10.2174/092986705774462969

Lactoferrin: the conductor of the immunological system?
Farnaud, S. and Evans, R.W. 2005. Lactoferrin: the conductor of the immunological system? in: Veskler, B.A. (ed.) New research on immunology New York Nova Science Publishers.

Variation in antimicrobial activity of lactoferricin-derived peptides explained by structure modelling
Farnaud, S., Patel, A., Odell, E.W. and Evans, R.W. 2004. Variation in antimicrobial activity of lactoferricin-derived peptides explained by structure modelling. FEMS Microbiology Letters. 238 (1), pp. 221-226. https://doi.org/10.1111/j.1574-6968.2004.tb09759.x

The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane β-barrel
Oke, M., Sarra, R., Ghirlando, R., Farnaud, S., Gorringe, A.R., Evans, R.W. and Buchanan, S.K. 2004. The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane β-barrel. FEBS Letters. 564 (3), pp. 294-300. https://doi.org/10.1016/S0014-5793(04)00196-6

Interactions of lactoferricin-derived peptides with LPS and antimicrobial activity
Farnaud, S., Spiller, C., Moriarty, L.C., Patel, A., Gant, V., Odell, E.W. and Evans, R.W. 2004. Interactions of lactoferricin-derived peptides with LPS and antimicrobial activity. FEMS Microbiology Letters. 233 (2/29), pp. 193-199. https://doi.org/10.1111/j.1574-6968.2004.tb09482.x

Lactoferrin: a multifunctional protein with antimicrobial properties
Farnaud, S. and Evans, R.W. 2003. Lactoferrin: a multifunctional protein with antimicrobial properties. Molecular Immunology. 40 (7), pp. 395-405. https://doi.org/10.1016/S0161-5890(03)00152-4

Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity
Novo, C., Farnaud, S., Tata, R., Clemente, A. and Brown, P.R. 2002. Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity. Biochemical Journal. 365 (3), pp. 731-738. https://doi.org/10.1042/BJ20011714

Evidence that cysteine-166 is the active-site nucleophile of Pseudomonas aeruginosa amidase: crystallization and preliminary X-ray diffraction analysis of the enzyme
Farnaud, S., Tata, R., Sohi, M.K., Wan, T., Brown, P.R. and Sutton, B.J. 1999. Evidence that cysteine-166 is the active-site nucleophile of Pseudomonas aeruginosa amidase: crystallization and preliminary X-ray diffraction analysis of the enzyme. Biochemical Journal. 340 (3), pp. 711-714.

Aluminium speciation: NMR studies of blood plasma, transferrin and citrate complexes
Bell, J.D., Evans, R.W., Kiang, W., Kubal, G., Radulovic, S., Sadler, P.J. and Williams, G. 1991. Aluminium speciation: NMR studies of blood plasma, transferrin and citrate complexes. Journal of Inorganic Biochemistry. 43 (2-3), p. 488. https://doi.org/10.1016/0162-0134(91)84467-N

Nuclear magnetic resonance and circular dichroism spectroscopic studies of copper complexation in blood plasma
Bligh, S.W.A., Drake, A.F. and Sadler, P.J. 1990. Nuclear magnetic resonance and circular dichroism spectroscopic studies of copper complexation in blood plasma. Biochemical Society Transactions. 18, pp. 999-1000. https://doi.org/10.1042/bst0180999

Ultraviolet and magnetic-circular-diochroic spectroscopic studies of Gd(III) complexed with diethylenetriaminepentaacetic acid
Bligh, S.W.A., Drake, A.F. and Sadler, P.J. 1989. Ultraviolet and magnetic-circular-diochroic spectroscopic studies of Gd(III) complexed with diethylenetriaminepentaacetic acid. European Journal of Biochemistry. 181 (1), pp. 223-224. https://doi.org/10.1111/j.1432-1033.1989.tb14714.x