Immunocytochemical staining of endogenous nuclear proteins with the HIS-1 anti-poly-histidine monoclonal antibody: a potential source of error in His-tagged protein detection

Next generation e-learning platform: virtual laboratory simulations
Smith, C.L. and Markiv, A. 2016. Next generation e-learning platform: virtual laboratory simulations. Heads of Biological Sciences, Royal Society of Biology, Spring 2016. University of Leicester 04 - 05 May 2016

The effects of catalase and kisspeptin overexpression on amyloid peptide toxicity
Chilumuri, A. 2014. The effects of catalase and kisspeptin overexpression on amyloid peptide toxicity. PhD thesis University of Westminster School of Life Sciences https://doi.org/10.34737/8yq40

Polymorphism of amyloid fibrils and their complexes with catalase
Milton, N.G.N. and Harris, J.R. 2014. Polymorphism of amyloid fibrils and their complexes with catalase. in: Uversky, V.N. and Lyubchenko, Y.L. (ed.) Bio-nanoimaging: protein misfolding and aggregation Boston Academic Press. pp. 255-262

The neuroprotective role of catalase overexpression in SH-SY5Y cells against beta-amyloid and H2O2 toxicity
Chilumuri, A., Odell, M. and Milton, N.G.N. 2013. The neuroprotective role of catalase overexpression in SH-SY5Y cells against beta-amyloid and H2O2 toxicity. Alzheimer's & Dementia. 9 (4), p. P361.

Sulforaphane alters cerebral leukocyte endothelial cell interactions post global ischaemia reperfusion
Gillespie, S., Milton, N.G.N., Ashioti, M. and Gavins, F.N.E. 2013. Sulforaphane alters cerebral leukocyte endothelial cell interactions post global ischaemia reperfusion. FASEB Journal. 27, p. 687.18.

Kissorphin peptides for use in the treatment of Alzheimer's disease, Creutzfeldt-Jakob disease or diabetes mellitus
Milton, N.G.N. 2013. Kissorphin peptides for use in the treatment of Alzheimer's disease, Creutzfeldt-Jakob disease or diabetes mellitus.

Benzothiazole aniline-tetra(ethylene glycol) and 3-amino-1,2,4-triazole inhibit neuroprotection against amyloid peptides by catalase overexpression in vitro
Chilumuri, A., Odell, M. and Milton, N.G.N. 2013. Benzothiazole aniline-tetra(ethylene glycol) and 3-amino-1,2,4-triazole inhibit neuroprotection against amyloid peptides by catalase overexpression in vitro. ACS chemical neuroscience. 4 (11), pp. 1501-1512. https://doi.org/10.1021/cn400146a

The role of neurotransmitters in protection against amyloid-β toxicity by KiSS-1 overexpression in SH-SY5Y neurons
Chilumuri, A. and Milton, N.G.N. 2013. The role of neurotransmitters in protection against amyloid-β toxicity by KiSS-1 overexpression in SH-SY5Y neurons. ISRN Neuroscience. 2013 253210. https://doi.org/10.1155/2013/253210

Immunolocalization of kisspeptin associated with amyloid-β deposits in the pons of an Alzheimer’s disease patient
Chilumuri, A., Ashioti, M., Nercessian, A.N. and Milton, N.G.N. 2013. Immunolocalization of kisspeptin associated with amyloid-β deposits in the pons of an Alzheimer’s disease patient. Journal of Neurodegenerative Diseases. 2013 879710. https://doi.org/10.1155/2013/879710

Neuroprotective efficacy of the endogenous neuropeptide Urocortin in a oxygen-glucose deprivation model of transient cerebral ischaemia with reperfusion
Ashioti, M., Getting, S.J., Locke, I.C. and Milton, N.G.N. 2013. Neuroprotective efficacy of the endogenous neuropeptide Urocortin in a oxygen-glucose deprivation model of transient cerebral ischaemia with reperfusion. British Neuroscience Association 22nd Biennial Meeting. London 7th-10th April 2013

Fibril formation and toxicity of the non-amyloidogenic rat amylin peptide
Milton, N.G.N. and Harris, J.R. 2013. Fibril formation and toxicity of the non-amyloidogenic rat amylin peptide. Micron. 44, pp. 246-253. https://doi.org/10.1016/j.micron.2012.07.001

Identification of metastasis-associated glycoproteins in colorectal cancer
Peiris, D., Markiv, A., Curley, G.P. and Dwek, M. 2012. Identification of metastasis-associated glycoproteins in colorectal cancer. European Journal of Cancer. 48 (5), pp. S39-S40. https://doi.org/10.1016/S0959-8049(12)70863-8

Ribosome display of combinatorial antibody libraries derived from mice immunised with heat-killed Xylella fastidiosa and the selection of MopB-specific single-chain antibodies
Azizi, A., Arora, A., Markiv, A., Lampe, D.J., Miller, T. and Kang, A.S. 2012. Ribosome display of combinatorial antibody libraries derived from mice immunised with heat-killed Xylella fastidiosa and the selection of MopB-specific single-chain antibodies. Applied and Environmental Microbiology. 78 (8), pp. 2638-2647. https://doi.org/10.1128/AEM.07807-11

Kisspeptin prevention of Amyloid-β Peptide neurotoxicity in vitro
Milton, N.G.N., Chilumuri, A., Rocha-Ferreira, E., Nercessian, A.N. and Ashioti, M. 2012. Kisspeptin prevention of Amyloid-β Peptide neurotoxicity in vitro. ACS chemical neuroscience. 3 (9), pp. 706-719. https://doi.org/10.1021/cn300045d

Kissorphin, a hexapeptide derivative of Kisspeptin, acts via Neuropeptide FF receptors to inhibit cyclic adenosine monophosphate release but has no Gonadotrophin-Releasing-Hormone releasing activity
Milton, N.G.N. 2012. Kissorphin, a hexapeptide derivative of Kisspeptin, acts via Neuropeptide FF receptors to inhibit cyclic adenosine monophosphate release but has no Gonadotrophin-Releasing-Hormone releasing activity. Endocrine Abstracts. 28, p. OC2.3.

In vitro activities of Kissorphin, a novel hexapeptide KiSS-1 derivative, in neuronal cells
Milton, N.G.N. 2012. In vitro activities of Kissorphin, a novel hexapeptide KiSS-1 derivative, in neuronal cells. Journal of Amino Acids. 2012 691463. https://doi.org/10.1155/2012/691463

Introduction and technical survey: protein aggregation and fibrillogenesis
Harris, J.R. and Milton, N.G.N. 2012. Introduction and technical survey: protein aggregation and fibrillogenesis. Subcellular Biochemistry. 65, pp. 3-25. https://doi.org/10.1007/978-94-007-5416-4_1

A novel approach to determining the affinity of protein-carbohydrate interactions employing adherent cancer cells grown on a biosensor surface
Peiris, D., Markiv, A., Curley, G.P. and Dwek, M. 2012. A novel approach to determining the affinity of protein-carbohydrate interactions employing adherent cancer cells grown on a biosensor surface. Biosensors and Bioelectronics. 35 (1), pp. 160-166. https://doi.org/10.1016/j.bios.2012.02.037

Beyond the genome and proteome: targeting protein modifications in cancer
Markiv, A., Rambaruth, N.D.S. and Dwek, M. 2012. Beyond the genome and proteome: targeting protein modifications in cancer. Current Opinions in Pharmacology.. 12 (4), pp. 408-413. https://doi.org/10.1016/j.coph.2012.04.003

A physiological approach to assess the affinity of lectin carbohydrate interactions using cancer cells immobilised on a biosensor surface
Peiris, D., Markiv, A. and Dwek, M. 2011. A physiological approach to assess the affinity of lectin carbohydrate interactions using cancer cells immobilised on a biosensor surface. Glycobiology. 21 (11), p. 1523. https://doi.org/10.1093/glycob/cwr126

Identification, cloning and characterization of two N-acetylgalactosamine binding lectins from the albumen gland of Helix pomatia
Markiv, A., Peiris, D., Curley, G.P., Odell, M. and Dwek, M. 2011. Identification, cloning and characterization of two N-acetylgalactosamine binding lectins from the albumen gland of Helix pomatia. Journal of Biological Chemistry. 286 (23), pp. 20260-20266. https://doi.org/10.1074/jbc.M110.184515

Module based antibody engineering: a novel synthetic REDantibody
Markiv, A., Anani, B., Durvasula, R.V. and Kang, A.S. 2011. Module based antibody engineering: a novel synthetic REDantibody. Journal of Immunological Methods. 364 (1-2), pp. 40-49. https://doi.org/10.1016/j.jim.2010.10.009

Kissorphin Peptides used in the treatment of Alzheimer’s Disease, Creutzfeldt Jakob Disease or Diabetes Mellitus P.
Milton, N.G.N. 2011. Kissorphin Peptides used in the treatment of Alzheimer’s Disease, Creutzfeldt Jakob Disease or Diabetes Mellitus P.

Kissorphin Peptides used in the treatment of Alzheimer’s Disease, Creutzfeldt Jakob Disease or Diabetes Mellitus P.
Milton, N.G.N. 2011. Kissorphin Peptides used in the treatment of Alzheimer’s Disease, Creutzfeldt Jakob Disease or Diabetes Mellitus P.

Fluorescent fusion polypeptides and methods of use
Markiv, A., Durvasula, R.V. and Kang, A.S. 2011. Fluorescent fusion polypeptides and methods of use.

Expression of recombinant multi-coloured fluorescent antibodies in gor -/trxB - E. coli cytoplasm
Markiv, A., Beatson, R., Burchell, J., Durvasula, R.V. and Kang, A.S. 2011. Expression of recombinant multi-coloured fluorescent antibodies in gor -/trxB - E. coli cytoplasm. BMC Biotechnology. 11 (117), p. 1. https://doi.org/10.1186/1472-6750-11-117

Human islet amyloid polypeptide fibril binding to catalase: a transmission electron microscopy and microplate study
Milton, N.G.N. and Harris, J.R. 2010. Human islet amyloid polypeptide fibril binding to catalase: a transmission electron microscopy and microplate study. ScientificWorldJournal. 10, pp. 879-893. https://doi.org/10.1100/tsw.2010.73

Cholesterol in Alzheimer's disease and other amyloidogenic disorders
Harris, J.R. and Milton, N.G.N. 2010. Cholesterol in Alzheimer's disease and other amyloidogenic disorders. Subcellular Biochemistry. 51, pp. 47-75. https://doi.org/10.1007/978-90-481-8622-8_2

Polymorphism of amyloid-ß fibrils and its effects on human erythrocyte catalase binding
Milton, N.G.N. and Harris, J.R. 2009. Polymorphism of amyloid-ß fibrils and its effects on human erythrocyte catalase binding. Micron. 40 (8), pp. 800-810. https://doi.org/10.1016/j.micron.2009.07.006

Cancer prognostication using a recombinant form of the lectin from Helix pomatia agglutinin
Dwek, M., Markiv, A. and Odell, M. 2009. Cancer prognostication using a recombinant form of the lectin from Helix pomatia agglutinin. Glycobiology. 19 (11), p. 1318. https://doi.org/10.1093/glycob/cwp135

Microbial biosynthesis of PHAs and its applications
Roy, I., Philip, S.E., Francis, L., Rai, R., Valappil, S.P., Markiv, A., Keshavarz, T., Misra, S.K., Decheng, M. and Boccaccini, A.R. 2008. Microbial biosynthesis of PHAs and its applications. COST Action 868: Biotechnical Functionalisation of Renewable Polymeric Materials: 2008 Annual Workshop (combined Working Group and Management Committee meeting). Varna, Bulgaria 18 -19 Sep 2008

Microbial PHA biosynthesis and its applications
Roy, I., Philip, S.E., Francis, L., Rai, R., Valappil, S.P., Markiv, A., Keshavarz, T., Misra, S.K., Decheng, M. and Boccaccini, A.R. 2008. Microbial PHA biosynthesis and its applications. 11th International Symposium on Biodegradable Polyesters. Massey University in Auckland, New Zealand 23 - 26 Nov 2008

Homocysteine inhibits hydrogen peroxide breakdown by catalase
Milton, N.G.N. 2008. Homocysteine inhibits hydrogen peroxide breakdown by catalase. Open Enzyme Inhibition Journal. 1, pp. 34-41. https://doi.org/10.2174/1874940200801010034

The three-dimensional structure of codakine and related marine C-type lectins
Gourdine, J.P., Markiv, A. and Smith-Ravin, J. 2007. The three-dimensional structure of codakine and related marine C-type lectins. Fish & Shellfish Immunology. 23 (4), pp. 831-839. https://doi.org/10.1016/j.fsi.2007.03.009

Interactions between amyloid-ß and enzymes
Milton, N.G.N. 2006. Interactions between amyloid-ß and enzymes. in: Harris, J.R., Graham, J. and Rickwood, D. (ed.) Cell biology protocols Chichester Wiley. pp. 359-363

Anti-sense peptides
Milton, N.G.N. 2006. Anti-sense peptides. in: Harris, J.R., Graham, J. and Rickwood, D. (ed.) Cell biology protocols Chichester Wiley. pp. 353-358

Amyloid-ß phosphorylation
Milton, N.G.N. 2006. Amyloid-ß phosphorylation. in: Harris, J.R., Graham, J. and Rickwood, D. (ed.) Cell biology protocols Chichester Wiley. pp. 364-368

Phosphorylated Amyloid-ß 1-43 protein and its use in the treatment of Alzheimer's disease
Milton, N.G.N. 2005. Phosphorylated Amyloid-ß 1-43 protein and its use in the treatment of Alzheimer's disease.

Phosphorylated amyloid-ß: the toxic intermediate in Alzheimer's disease neurodegeneration
Milton, N.G.N. 2005. Phosphorylated amyloid-ß: the toxic intermediate in Alzheimer's disease neurodegeneration. Subcellular Biochemistry. 38, pp. 381-402.

Peptides for use in the treatment of Alzheimer's disease
Milton, N.G.N. 2004. Peptides for use in the treatment of Alzheimer's disease.

Role of hydrogen peroxide in the aetiology of Alzheimer's disease: implications for treatment
Milton, N.G.N. 2004. Role of hydrogen peroxide in the aetiology of Alzheimer's disease: implications for treatment. Drugs & Aging. 21 (2), pp. 81-100.

Peptides for use in the treatment of Alzheimer's disease
Milton, N.G.N. 2003. Peptides for use in the treatment of Alzheimer's disease.

Anandamide and noladin ether prevent neurotoxicity of the human amyloid-ß peptide
Milton, N.G.N. 2002. Anandamide and noladin ether prevent neurotoxicity of the human amyloid-ß peptide. Neuroscience Letters. 332 (2), pp. 127-130. https://doi.org/10.1016/S0304-3940(02)00936-9

The amyloid-β peptide binds to cyclin B1 and increases human cyclin-dependent kinase-1 activity
Milton, N.G.N. 2002. The amyloid-β peptide binds to cyclin B1 and increases human cyclin-dependent kinase-1 activity. Neuroscience Letters. 322 (2), pp. 131-133. https://doi.org/10.1016/S0304-3940(02)00081-2

Lipoprotein (a) does not participate in the early acute phase response to training or extreme physical activity and is unlikely to enhance any associated immediate cardiovascular risk
Byrne, D.J., Jagroop, I.A., Montgomery, H., Thomas, M., Mikhailidis, D.P., Milton, N.G.N. and Winder, A.F. 2002. Lipoprotein (a) does not participate in the early acute phase response to training or extreme physical activity and is unlikely to enhance any associated immediate cardiovascular risk. Journal of Clinical Pathology. 55 (4), pp. 280-285.

Peptides for use in the treatment of Alzheimer's disease
Milton, N.G.N. 2002. Peptides for use in the treatment of Alzheimer's disease.

Phosphorylation of amyloid-ß at the serine 26 residue by human cdc2 kinase
Milton, N.G.N. 2001. Phosphorylation of amyloid-ß at the serine 26 residue by human cdc2 kinase. NeuroReport. 12 (17), pp. 3839-3844.

Inhibition of catalase activity with 3-amino-triazole enhances the cytotoxicity of the Alzheimer’s amyloid-ß peptide
Milton, N.G.N. 2001. Inhibition of catalase activity with 3-amino-triazole enhances the cytotoxicity of the Alzheimer’s amyloid-ß peptide. NeuroToxicology. 72 (6), pp. 767-774. https://doi.org/10.1016/S0161-813X(01)00064-X

Identification of amyloid-ß binding sites using an antisense peptide approach
Milton, N.G.N., Mayor, N.P. and Rawlinson, J. 2001. Identification of amyloid-ß binding sites using an antisense peptide approach. NeuroReport. 12 (11), pp. 2561-2566.