Professor Nigel Hooper
Professor of Cell Biology
- Email: firstname.lastname@example.org
- Telephone: +44 (0)161 306 5765
- Alternative Telephone: +44 (0)161 306 7941 (PA: Pat Amos)
Rm 2.015 AV Hill Building
Institute of Brain, Behaviour and Mental Health
Faculty of Medical and Human Sciences
University of Manchester
Manchester M13 9PT
Director of Dementia Research
Series Editor, Essays in Biochemistry
Co-ordinator, Alzheimer's Research UK Manchester and North West Network Centre
Medical Research Council Neurosciences and Mental Health Board (2000-2004)
MRC/Department of Health Research Advisory Group for Transmissible Spongiform Encephalopathies (2001-2004)
Government's Spongiform Encephalopathy Advisory Committee (SEAC) (2004-2009)
Scientific Advisory Board of Alzheimer's Research UK (2007-2014) including latterly as Chair of the Advisory Board (2012-2014).
Editorial board (1998-2002) and deputy chairman (2002-2009) of the Biochemical Journal.
Editorial board of the Journal of Biological Chemistry (2009-2014).
Cell biology of Alzheimer’s disease and ageing
Our overall aim is to understand the basic biological processes underlying Alzheimer’s disease so as to identify opportunities for intervention, and translate research into practice that improves quality of life. Alzheimer’s disease is the commonest form of dementia affecting millions of people worldwide. Currently there is no treatment available to halt or slow the progression of the disease. Alzheimer’s is characterised by the accumulation in the brain of the extracellular amyloid-β (Aβ) peptide and of the intracellular tau protein. Aβ is derived from the larger transmembrane amyloid precursor protein (APP) through the sequential proteolytic action of the β- and γ-secretases. Understanding the molecular and cellular mechanisms that regulate APP processing and Aβ production, including the role of alternative processing pathways, is critical to our understanding of the disease. In addition, knowledge of the mechanisms by which Aβ interacts with neurons and causes neurotoxicity via post-translational modification of tau, are essential to defining the pathogenesis of AD. We are also investigating the role of other proteolytic fragments of APP, exploring the links between Aβ and the diabetes-related protein amylin, and investigating the cell-to-cell transfer of tau and other amyloidogenic proteins. We are developing stem cell models to investigate these and other processes in human neuronal systems. Other work in the group is focused on the post-translational processing of the low density lipoprotein receptor.
We use a variety of biochemical, biophysical, molecular biological and cell biological techniques on individual proteins, cells in culture (including iPSC-derived neurons), animal models and human tissues. Our research receives support from the Medical Research Council, Alzheimer’s Research UK, Alzheimer’s Society and BBSRC.
1. Determining the mechanism of action of Aβ oligomers – the role of a cell surface, lipid raft-based signalling complex containing the prion protein and how this links Aβ to tau (funded by Alzheimer’s Research UK).
2. Identifying and characterising novel regulators of APP proteolysis.
3. Identifying receptors and functions for soluble fragments of APP.
4. Unravelling the molecular and cellular mechanisms underlying the proteolytic cleavage of tau.
5. Developing neuronal and neurovascular stem cell models for Alzheimer’s disease, vascular dementia and ageing (funded by the Dr Donald Dean Fund for Dementia Research).
6. Exploring the links between Aβ and amylin.
7. Investigating the cell-to-cell transfer of tau and other amyloidogenic proteins, including the role of exosomes.
8. Characterising the proteolytic cleavage of the low density lipoprotein (LDL) receptor: a novel regulator of plasma LDL cholesterol (funded by the MRC).
9. Exploring the role of the anti-aging protein klotho.
Nigel Hooper received his Ph.D. in biochemistry at the University of Leeds in 1987. He was then awarded a Mr and Mrs John Jaffé Donation Research Fellowship from the Royal Society to work on the proteolysis and membrane anchorage of mammalian cell surface peptidases. In 1989 he was appointed as lecturer in the Department of Biochemistry at Leeds, followed by promotions to senior lecturer, reader and in 2001 to Professor of Biochemistry. He served as Director of the Institute of Molecular and Cellular Biology (2007-2011), Pro-Dean for Research (2011) and Dean (2012-2014) of the Faculty of Biological Sciences at the University of Leeds. In 2014 he was appointed to the Chair in Cell Biology in the Institute of Brain, Behaviour and Mental Health, Faculty of Medical and Human Sciences at the University of Manchester. He is currently Director of Dementia Research for the University.
His research has focused on neurodegenerative and cardiovascular diseases. He applies a range of experimental approaches (biochemical, biophysical, molecular biological and cell biological techniques on individual proteins, cells in culture, animal models and human tissues) to probe normal biology and elucidate disease processes, with a common theme of proteolytic mechanisms and protein-membrane interactions, that began with angiotensin-converting enzyme (ACE) and has led naturally into studies on Alzheimer’s and prion diseases. He was the first to show how ACE attaches to the cell membrane, and to identify the mechanism whereby it is processed (shed) into a soluble circulating form through the action of another zinc metalloprotease. This model of ectodomain shedding has become the paradigm for numerous biologically and medically-important processes, including the cleavage of the Alzheimer’s amyloid precursor protein (APP). This work also led him to identify and extensively characterise the first known human ACE homologue, ACE2, and to delineate its role in angiotensin metabolism: discoveries that have made important contributions to understanding of cardiovascular and renal pathophysiology.
His work on the membrane attachment of ACE led him to be the first to show that multiple glycosyl-phosphatidylinositol (GPI)-anchored proteins are resistant to solubilisation from the membrane by certain detergents, subsequently shown to be due to localisation within cholesterol-rich membrane rafts. This work led him to develop a productive programme of research targeting the GPI-anchored prion protein (PrP). Significantly, he identified determinants in PrP for its raft association and glypican-1 as important in its conversion into the infectious form. He also showed that PrP is involved in zinc uptake into neurons, that disease-associated mutations inhibit this metal-uptake function, that metal binding promotes the movement of PrP out of rafts prior to clathrin-mediated endocytosis, and that proteolysis contributes to its shedding from the membrane. These studies have contributed to elucidation of the normal cell biology of PrP and provided insights into how loss of function (e.g. zinc uptake) contributes to its pathogenic role in prion disease.
Through manipulating its membrane anchor his group elegantly showed that the localisation in rafts of the β-secretase, BACE1, is a key factor regulating the production of the neurotoxic amyloid-β peptide in Alzheimer’s disease. More recently he was the first to report a molecular link between PrP and Alzheimer’s disease, when he showed that PrP inhibits the β-secretase-mediated cleavage of APP and thus amyloid-β production. He have also shown that PrP must be localized in rafts in order to mediate amyloid-β binding and subsequent toxic intracellular signalling, opening up potential new avenues for therapeutic intervention in Alzheimer’s disease.
B.Sc. (Hons.) Biochemistry, University of Leeds 1984
Ph.D. Biochemistry, University of Leeds 1987
- Whitehouse, I. J., Brown, D., Baybutt, H., Diack, A. B., Kellett, K., Piccardo, P., ... Hooper, N. (2016). Ablation of prion protein in wild type human amyloid precursor protein (APP) transgenic mice does not alter the proteolysis of APP, levels of amyloid-β or pathologic phenotype. PLoS ONE. . Publication link: 93c4bde7-d002-496a-b592-7b6e5270c3be
- Xu, J., Begley, P., Church, S., Patassini, S., Mcharg, S., Kureishy, N., ... Cooper, G. (2016). Elevation of brain glucose and polyol-pathway intermediates with accompanying brain-copper deficiency in patients with Alzheimer’s disease: metabolic basis for dementia. Scientific Reports, [27524 ]. DOI:10.1038/srep27524. Publication link: f4f818a3-9643-49bf-a0eb-2932313678f8
- O'Sullivan, J., Comerford, E., Rachidi, W., Scott, M., Hooper, N. M., & McMahon, H. E. (2015). The effects of the cellular and infectious prion protein on the neuronal adaptor protein X11alpha. Biochim Biophys Acta, 1850(11), 2213-21. DOI:10.1016/j.bbagen.2015.08.010. Publication link: ac5fba54-8868-4c04-aa51-9120032de4ff
- Cruchaga, C., Karch, C. M., Jin, S. C., Benitez, B. A., Cai, Y., Guerreiro, R., ... Goate, A. M. (2014). Rare coding variants in the phospholipase D3 gene confer risk for Alzheimer's disease.Nature, 505(7484), 550-554. DOI:10.1038/nature12825. Publication link: c78d1b96-689b-4f60-8728-7b4b435ed975 | PubMed:24336208
- Hettiarachchi, N., Dallas, M., Al-Owais, M., Griffiths, H., Hooper, N., Scragg, J., ... Peers, C. (2014). Heme oxygenase-1 protects against Alzheimer's amyloid-beta(1-42)-induced toxicity via carbon monoxide production. Cell Death Dis, 5. DOI:10.1038/cddis.2014.529. Publication link: 9a5062c2-313b-4fb3-bc30-884fbb3f0365
- Lambert, D. W., Lambert, L. A., Clarke, N. E., Hooper, N. M., Porter, K. E., & Turner, A. J. (2014). Angiotensin-converting enzyme 2 is subject to post-transcriptional regulation by miR-421. Clinical Science, 127(4), 243-249. DOI:10.1042/CS20130420. Publication link: b4b81a1f-005a-40ee-bbac-7509bbacf15b
- Rushworth, J. V., Ahmed, A., Griffiths, H. H., Pollock, N. M., Hooper, N. M., & Millner, P. A. (2014). A label-free electrical impedimetric biosensor for the specific detection of Alzheimer's amyloid-beta oligomers. Biosensors and Bioelectronics, 56, 83-90. DOI:10.1016/j.bios.2013.12.036. Publication link: feecacb4-124f-487f-a688-d9e35c003ca1
- Mok, N. Y., Chadwick, J., Kellett, K. A. B., Casas-Arce, E., Hooper, N. M., Johnson, A. P., & Fishwick, C. W. G. (2013). Discovery of biphenylacetamide-derived inhibitors of BACE1 using de novo structure-based molecular design. Journal of Medicinal Chemistry, 56(5), 1843-1852. DOI:10.1021/jm301127x. Publication link: d69d3c9f-5761-4925-8a4a-93c0d678b160
- Rushworth, J. V., Griffiths, H. H., Watt, N. T., & Hooper, N. M. (2013). Prion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1. Journal of Biological Chemistry, 288(13), 8935-8951. DOI:10.1074/jbc.M112.400358. Publication link: a870302b-7704-4800-9c44-39cbce8fee6b
- Whitehouse, I. J., Miners, J. S., Glennon, E. B. C., Kehoe, P. G., Love, S., Kellett, K. A. B., & Hooper, N. M. (2013). Prion Protein Is Decreased in Alzheimer's Brain and Inversely Correlates with BACE1 Activity, Amyloid-β Levels and Braak Stage. PLoS ONE, 8(4), [e59554]. DOI:10.1371/journal.pone.0059554. Publication link: ad8dd760-0d75-4404-853e-c1ce409142e7
- Griffiths, H. H., Whitehouse, I. J., & Hooper, N. M. (2012). Regulation of amyloid-beta productiojn by the prion protein. Prion, 6, 217-222. . Publication link: ab5f1bb4-e24c-49d1-9a57-9ba59469f8f2
- Lewis, V., Whitehouse, I. J., Baybutt, H., Manson, J. C., Collins, S. J., & Hooper, N. M. (2012). Cellular prion protein expression is not regulated by the Alzheimer's amyloid precursor protein intracellular domain. PLoS ONE, 7(2), [e31754]. DOI:10.1371/journal.pone.0031754. Publication link: 7eed9b68-3e07-4f0e-b2dd-e476b805009a
- Watt, N. T., Taylor, D. R., Kerrigan, T. L., Griffiths, H. H., Rushworth, J. V., Whitehouse, I. J., & Hooper, N. M. (2012). Prion protein facilitates uptake of zinc into neuronal cells. Nature communications, 3, . DOI:http://www.nature.com/ncomms/journal/v3/n10/suppinfo/ncomms2135_S1.html. Publication link: 69e5a757-4721-472f-8176-376f605104a4
- Cilia La Corte, A. L., Carter, A. M., Rice, G. I., Duan, Q. L., Rouleau, G. A., Adam, A., ... Hooper, N. M. (2011). A functional XPNPEP2 promoter haplotype leads to reduced plasma aminopeptidase P and increased risk of ACE inhibitor-induced angioedema.Human Mutation, 32(11), 1326-1331. DOI:10.1002/humu.21579. Publication link: 1632d380-b6dd-42e2-a1e8-3f1ba49a29f2 | PubMed:21898657
- Griffiths, H. H., Whitehouse, I. J., Baybutt, H., Brown, D., Kellett, K. A. B., Jackson, C. D., ... Hooper, N. M. (2011). Prion protein interacts with BACE1 protein and differentially regulates its activity toward wild type and Swedish mutant amyloid precursor protein. Journal of Biological Chemistry, 286(38), 33489-33500. DOI:10.1074/jbc.M111.278556. Publication link: cd652ab6-a664-4bcb-90a8-c962e3d7b5ce
- Hollingworth, P., Harold, D., Sims, R., Gerrish, A., Lambert, J. C., Carrasquillo, M. M., ... Williams, J. (2011). Common variants at ABCA7, MS4A6A/MS4A4E, EPHA1, CD33 and CD2AP are associated with Alzheimer's disease. Nature Genetics, 43(5), 429-436. DOI:10.1038/ng.803. Publication link: 8bb747e7-1f8c-4dee-89c6-21cecaef55e3 | PubMed:21460840
- Hollingworth, P., Harold, D., Sims, R., Gerrish, A., Lambert, J-C., Carrasquillo, M. M., ... Williams, J. (2011). Common variants at ABCA7, MS4A6A/MS4A4E, EPHA1, CD33 and CD2AP are associated with Alzheimer's disease. Nat Genet, 43(5), 429-435. DOI:http://www.nature.com/ng/journal/v43/n5/abs/ng.803.html#supplementary-information. Publication link: 58856bef-97df-41c9-b9d1-292c11347f78
- Kellett, K. A. B., Williams, J., Vardy, E. R. L. C., Smith, D. A., & Hooper, N. M. (2011). Plasma alkaline phosphatase is elevated in Alzheimer's disease and inversely correlates with cognitive function. Int J Mol Epidemiol Genet, 2, 114-121. . Publication link: c8349713-f6bf-4638-b76b-70ce701eb5be
- Belyaev, N. D., Kellett, K. A. B., Beckett, C., Makova, N. Z., Revett, T. J., Nalivaeva, N. N., ... Turner, A. J. (2010). The transcriptionally active amyloid precursor protein (APP) intracellular domain is preferentially produced from the 695 isoform of APP in a β-secretase-dependent pathway. Journal of Biological Chemistry, 285(53), 41443-41454. DOI:10.1074/jbc.M110.141390. Publication link: 8ce537d4-17fc-4cb3-b999-0bf981207b20
- Bruns, A. F., Herbert, S. P., Odell, A. F., Jopling, H. M., Hooper, N. M., Zachary, I. C., ... Ponnambalam, S. (2010). Ligand-stimulated VEGFR2 signaling is regulated by co-ordinated trafficking and proteolysis. Traffic, 11(1), 161-174. DOI:10.1111/j.1600-0854.2009.01001.x. Publication link: 4dbcf238-c15f-4818-baa3-1362367973f2
- Whitehouse, I. J., Jackson, C. D., Turner, A. J., & Hooper, N. M. (2010). Prion protein is reduced in aging and in sporadic but not in familial Alzheimer's disease. J. Alzheimers Dis., 22, 1023-1031. . Publication link: 3c5a2dc6-aa90-4450-8ed3-27958005a24a
- Davey, K. A. B., & Hooper, N. M. (2009). Prion protein and Alzheimer's disease. Prion. . Publication link: 06ed2d28-5b4f-4f19-9401-b4135e5adeee
- Duff, C. J., Scott, M. J., Kirby, I. T., Hutchinson, S. E., Martin, S. L., & Hooper, N. M. (2009). Antibody-mediated disruption of the interaction between PCSK9 and the low-density lipoprotein receptor. Biochemical Journal, 419(3), 577-584. DOI:10.1042/BJ20082407. Publication link: 1e2b3b77-8577-46e4-966e-592a9f2008fb
- Hein, Z., Hooper, N. M., & Naim, H. Y. (2009). Association of a GPI-anchored protein with detergent-resistant membranes facilitates its trafficking through the early secretory pathway. Experimental Cell Research, 315(2), 348-356. DOI:S0014-4827(08)00458-8 [pii] 10.1016/j.yexcr.2008.10.038. Publication link: 57f3c932-d8a1-4762-86b0-0d6ebdd3ba9c
- Taylor, D. R., Parkin, E. T., Cocklin, S. L., Ault, J. R., Aschcroft, A. E., Turner, A. J., & Hooper, N. M. (2009). Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein. Journal of Biological Chemistry, 284(34), 22590-22600. DOI:M109.032599 [pii] 10.1074/jbc.M109.032599. Publication link: 92ee5398-c056-4433-902a-2326489158cd
- Walmsley, A. R., Watt, N. T., Taylor, D. R., Perera, W. S., & Hooper, N. M. (2009). alpha-cleavage of the prion protein occurs in a late compartment of the secretory pathway and is independent of lipid rafts. Mol Cell Neurosci, 40(2), 242-8. DOI:S1044-7431(08)00277-7 [pii] 10.1016/j.mcn.2008.10.012. Publication link: 2b8b1fa9-1e05-4ef7-b213-6175b9717fca
- Yi Mok, N., Chadwick, J., Kellett, K. A. B., Hooper, N. M., Johnson, A. P., & Fishwick, C. W. G. (2009). Discovery of novel non-peptide inhibitors of BACE-1 using virtual high-throughput screening. Bioorganic and Medicinal Chemistry Letters, 19(23), 6770-6774. DOI:S0960-894X(09)01371-7 [pii] 10.1016/j.bmcl.2009.09.103. Publication link: b0efda60-949b-4ae9-97d8-bf94116ea2f2
- Garner, A. E., Smith, D. A., & Hooper, N. M. (2008). Visualization of detergent solubilization of membranes: Implications for the isolation of rafts. Biophysical Journal, 94(4), 1326-1340. DOI:biophysj.107.114108 [pii] 10.1529/biophysj.107.114108. Publication link: a89687e2-5e07-4558-8ea3-94f9d99c93b4
- Griffiths, H. H., Morten, I. J., & Hooper, N. M. (2008). Emerging and potential therapies for Alzheimer's disease. Expert Opin Ther Targets, 12(6), 693-704. DOI:10.1517/14728184.108.40.2063 10.1517/14728220.127.116.113 [pii]. Publication link: 9f36a8ac-57a5-4331-8453-c01145508ef5
- Hooper, N. M., & Turner, A. J. (2008). A new take on prions: preventing Alzheimer's disease. Trends Biochem Sci, 33, 151-155. DOI:S0968-0004(08)00046-7 [pii] 10.1016/j.tibs.2008.01.004. Publication link: 3cb3c527-c97a-4347-ad48-9328a7ec45df
- La Corte, A. L. C., Carter, A. M., Turner, A. J., Grant, P. J., & Hooper, N. M. (2008). The bradykinin-degrading aminopeptidase P is increased in women taking the oral contraceptive pill. JRAAS - Journal of the Renin-Angiotensin-Aldosterone System, 9(4), 221-225. DOI:9/4/221 [pii] 10.1177/1470320308096405. Publication link: 5c30f475-2a96-4cb1-927e-ed78cdc6e243
- Lambert, D. W., Clarke, N. E., Hooper, N. M., & Turner, A. J. (2008). Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain. FEBS Letters, 582(2), 385-390. DOI:S0014-5793(07)01239-2 [pii] 10.1016/j.febslet.2007.11.085. Publication link: 51b63595-e068-4656-87ad-f92a942c4326
- Wilkinson, D. K., Turner, E. J., Parkin, E. T., Garner, A. E., Harrison, P. J., Crawford, M., ... Hooper, N. M. (2008). Membrane raft actin deficiency and altered Ca2+-induced vesiculation in stomatin-deficient overhydrated hereditary stomatocytosis. Biochimica et Biophysica Acta - Biomembranes, 1778(1), 125-132. DOI:S0005-2736(07)00355-0 [pii] 10.1016/j.bbamem.2007.09.016. Publication link: 60833429-bc59-4cd3-8825-79935cfbfda1
- Garner, A. E., Smith, D. A., & Hooper, N. M. (2007). Sphingomyelin chain length influences the distribution of GPI-anchored proteins in rafts in supported lipid bilayers. Molecular Membrane Biology, 24(3), 233-242. . Publication link: cf3e58e0-1653-482a-863f-3f2011293419
- Lambert, D. W., Hooper, N. M., & Turner, A. J. (2007). Angiotensin-converting enzyme 2 and new insights into the renin-angiotensin system. Biochem Pharmacol. . Publication link: 5cee54ad-8f49-49eb-aa1c-e1a9b7a69eba
- Parkin, E. T., Watt, N. T., Hussain, I., Eckman, E. A., Eckman, C. B., Manson, J. C., ... Hooper, N. M. (2007). Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein. PNAS, 104(26), 11062-11067. . Publication link: d243acab-11ef-4154-8e62-6e44ba30278b
- Rella, M., Elliot, J. L., Revett, T. J., Lanfear, J., Phelan, A., Jackson, R. M., ... Hooper, N. M. (2007). Identification and characterisation of the angiotensin converting enzyme-3 (ACE3) gene: A novel mammalian homologue of ACE. BMC Genomics, 8, . DOI:10.1186/1471-2164-8-194. Publication link: b26f402f-69be-43d1-b4be-16a553d1cb1b
- Say, Y. H., & Hooper, N. M. (2007). Contamination of nuclear fractions with plasma membrane lipid rafts. Proteomics, 7(7), 1059-1064. . Publication link: e70186bd-0e10-4592-a674-1a6c156d9d11
- Taylor, D. R., & Hooper, N. M. (2007). Role of lipid rafts in the processing of the pathogenic prion and Alzheimer's amyloid-beta proteins. Semin Cell Dev Biol, 18, 638-648. . Publication link: 255a76e7-96af-4f90-b441-4c30ae01b04f
- Taylor, D. R., & Hooper, N. M. (2007). The low-density lipoprotein receptor-related protein 1 (LRP1) mediates the endocytosis of the cellular prion protein. Biochemical Journal, 402(1), 17-23. . Publication link: 13e4dd56-a4ea-43a2-8f4f-6ddbf7e3bf60
- Vardy, E. R., Rice, P. J., Bowie, P. C., Holmes, J. D., Grant, P. J., & Hooper, N. M. (2007). Increased Circulating Insulin-like Growth Factor-1 in Late-onset Alzheimer's Disease. J Alzheimers Dis, 12(4), 285-90. . Publication link: 00a0d016-7392-4674-8306-11947f2bd640
- Watt, N. T., & Hooper, N. M. (2007). Prion protein and Alzheimer's disease. Future Neurology, 2, 587-590. . Publication link: d016bd1d-1b0a-4d36-9e0f-c47a5eb5ed99
- Watt, N. T., Routledge, M. N., Wild, C. P., & Hooper, N. M. (2007). Cellular prion protein protects against reactive-oxygen-species-induced DNA damage. Free Radical Biology and Medicine, 43(6), 959-967. . Publication link: de529e65-8882-4be5-b430-c37aafdb510c
- Cordy, J. M., Hooper, N. M., & Turner, A. J. (2006). The involvement of lipid rafts in Alzheimer's disease. Mol Membr Biol, 23, 111-122. . Publication link: 603d4340-3ae2-4633-9240-516168fd46dc
- Rice, G. I., Jones, A. L., Grant, P. J., Carter, A. M., Turner, A. J., & Hooper, N. M. (2006). Circulating activities of angiotensin-converting enzyme, its homolog, angiotensin-converting enzyme 2, and neprilysin in a family study. Hypertension, 48(5), 914-920. DOI:10.1161/01.HYP.0000244543.91937.79. Publication link: efa101a7-8837-472b-a413-45c6b624dcc7 | PubMed:17000927
- Taylor, D. R., & Hooper, N. M. (2006). The prion protein and lipid rafts (Review). Molecular Membrane Biology, 23(1), 89-99. . Publication link: 7013ec76-6594-4e6e-b5e1-034af9086e4c
- Thomas, D. A., Francis, P., Smith, C., Ratcliffe, S., Ede, N. J., Kay, C., ... Hooper, N. M. (2006). A broad-spectrum fluorescence-based peptide library for the rapid identification of protease substrates. Proteomics, 6(7), 2112-2120. DOI:10.1002/pmic.200500153. Publication link: 135e28c4-8c9c-45ea-841a-7f76b8a31ab8
- Vardy, E. R., Hussain, I., & Hooper, N. M. (2006). Emerging therapeutics for Alzheimer's disease. Expert Rev Neurother, 6(5), 695-704. . Publication link: 7c5797ee-ba23-4432-b462-cca205e4b7bc