Dr Dirk Wildeboer


NameDr Dirk Wildeboer
Job titleSL-Bioscience & Biomedical Science
Research institute
Primary appointmentNatural Sciences
Email addressd.wildeboer@mdx.ac.uk
ORCIDhttps://orcid.org/0000-0003-1298-7511
Contact categoryResearcher

Research outputs

Wastewater monitoring for detection of public health markers during the COVID-19 pandemic: Near-source monitoring of schools in England over an academic year

Hassard, F., Vu, M., Rahimzadeh, S., Castro-Gutierrez, V., Stanton, I., Burczynska, B., Wildeboer, D., Baio, G., Brown, M., Garelick, H., Hofman, J., Kasprzyk-Hordern, B., Majeed, A., Priest, S., Denise, H., Khalifa, M., Bassano, I., Wade, M., Grimsley, J., Lundy, L., Singer, A. and Di Cesare, M. 2023. Wastewater monitoring for detection of public health markers during the COVID-19 pandemic: Near-source monitoring of schools in England over an academic year. PLoS ONE. 18 (5). https://doi.org/10.1371/journal.pone.0286259

Monitoring occurrence of SARS-CoV-2 in school populations: A wastewater-based approach

Castro-Gutierrez, V., Hassard, F., Vu, M., Leitao, R., Burczynska, B., Wildeboer, D., Stanton, I., Rahimzadeh, S., Baio, G., Garelick, H., Hofman, J., Kasprzyk-Hordern, B., Kwiatkowska, R., Majeed, A., Priest, S., Grimsley, J., Lundy, L., Singer, A. and Di Cesare, M. 2022. Monitoring occurrence of SARS-CoV-2 in school populations: A wastewater-based approach. PLoS ONE. 17 (6). https://doi.org/10.1371/journal.pone.0270168

Characterization of the complete mitochondrial genome of Diplostomum baeri

Landeryou, T., Ropiquet, A., Kett, S., Wildeboer, D. and Lawton, S. 2020. Characterization of the complete mitochondrial genome of Diplostomum baeri. Parasitology International. 79. https://doi.org/10.1016/j.parint.2020.102166

Competition of As and other Group 15 elements for surface binding sites of an extremophilic Acidomyces acidophilus isolated from a historical tin mining site

Chan, W., Wildeboer, D., Garelick, H. and Purchase, D. 2018. Competition of As and other Group 15 elements for surface binding sites of an extremophilic Acidomyces acidophilus isolated from a historical tin mining site. Extremophiles. 22 (5), pp. 795-809. https://doi.org/10.1007/s00792-018-1039-2

Metal water-sediment interactions and impacts on an urban ecosystem

Lundy, L., Alves, L., Revitt, D. and Wildeboer, D. 2017. Metal water-sediment interactions and impacts on an urban ecosystem. 14th IWA/IAHR International Conference on Urban Drainage. Prague, Czech Republic 10 - 15 Sep 2017 pp. 148-156

Environmental waters and E. coli as a marker, including pathogenic and resistant strains

Price, R. and Wildeboer, D. 2017. Environmental waters and E. coli as a marker, including pathogenic and resistant strains. in: Samie, A. (ed.) Escherichia coli - Recent Advances on Physiology, Pathogenesis and Biotechnological Applications InTech.

Metal water-sediment interactions and impacts on an urban ecosystem

Lundy, L., Alves, L., Revitt, D. and Wildeboer, D. 2017. Metal water-sediment interactions and impacts on an urban ecosystem. International Journal of Environmental Research and Public Health. 14 (7), pp. 1-12. https://doi.org/10.3390/ijerph14070722

Mycoremediation of heavy metal/metalloid-contaminated soil: current understanding and future prospects

Chan, W., Wildeboer, D., Garelick, H. and Purchase, D. 2016. Mycoremediation of heavy metal/metalloid-contaminated soil: current understanding and future prospects. in: Purchase, D. (ed.) Fungal Applications in Sustainable Environmental Biotechnology Cham, Switzerland Springer International Publishing. pp. 249-272

A proteomic study on the responses to arsenate stress by an acidophilic fungal strain Acidomyces acidophilus WKC1

Chan, W., Wildeboer, D., Garelick, H. and Purchase, D. 2016. A proteomic study on the responses to arsenate stress by an acidophilic fungal strain Acidomyces acidophilus WKC1. Biotechnology World Convention. Sao Paulo, Brazil 15 - 17 Aug 2016 OMICS International. pp. 35-35 https://doi.org/10.4172/2155-952X.C1.058

Methods of analysis for bacterial contamination in environmental waters

Price, R. and Wildeboer, D. 2015. Methods of analysis for bacterial contamination in environmental waters. in: McCoy, G. (ed.) Coliforms: occurrence, detection methods and environmental impact Nova Science Publishers.

Investigating arsenic resistance in fungi from tin-mining soil and the possible interaction between arsenic and tin/antimony

Chan, W., Wildeboer, D., Garelick, H. and Purchase, D. 2014. Investigating arsenic resistance in fungi from tin-mining soil and the possible interaction between arsenic and tin/antimony. 10th International Mycological Congress. Bangkok, Thailand 03 - 08 Aug 2014

Escherichia coli contamination of the river Thames in different seasons and weather conditions

Amirat, L., Wildeboer, D., Abuknesha, R. and Price, R. 2012. Escherichia coli contamination of the river Thames in different seasons and weather conditions. Water and Environment Journal. 26 (4), pp. 482-489. https://doi.org/10.1111/j.1747-6593.2012.00308.x

Specific protease activity indicates the degree of Pseudomonas aeruginosa infection in chronic infected wounds

Wildeboer, D., Hill, K., Jeganathan, F., Williams, D., Riddell, A., Price, P., Thomas, D., Stephens, P., Abuknesha, R. and Price, R. 2012. Specific protease activity indicates the degree of Pseudomonas aeruginosa infection in chronic infected wounds. European Journal of Clinical Microbiology & Infectious Diseases. 31 (9), pp. 2183-2189. https://doi.org/10.1007/s10096-012-1553-6

ADAM8/MS2/CD156a: a metalloprotease-disintegrin involved in immune responses

Bartsch, J., Naus, S., Rittger, A., Schlomann, U. and Wildeboer, D. 2005. ADAM8/MS2/CD156a: a metalloprotease-disintegrin involved in immune responses. in: Hooper, N. and Lendeckel, U. (ed.) The ADAM family of Proteases Dordrecht, Netherlands Springer.

Tumor Necrosis Factor-α (TNF-α) regulates shedding of TNF-α receptor 1 by the metalloprotease-disintegrin ADAM8: evidence for a protease-regulated feedback loop in neuroprotection

Bartsch, J., Wildeboer, D., Koller, G., Naus, S., Rittger, A., Moss, M., Minai, Y. and Jockusch, H. 2010. Tumor Necrosis Factor-α (TNF-α) regulates shedding of TNF-α receptor 1 by the metalloprotease-disintegrin ADAM8: evidence for a protease-regulated feedback loop in neuroprotection. Journal of Neuroscience. 30 (36), pp. 12210-12218. https://doi.org/10.1523/JNEUROSCI.1520-10.2010

Detection of proteases using an immunochemical method with haptenylated–gelatin as a solid-phase substrate

Abuknesha, R., Jeganathan, F., DeGroot, R., Wildeboer, D. and Price, R. 2010. Detection of proteases using an immunochemical method with haptenylated–gelatin as a solid-phase substrate. Analytical and Bioanalytical Chemistry. 396 (7), pp. 2547-2558. https://doi.org/10.1007/s00216-010-3540-z

Optimisation of the detection of bacterial proteases using adsorbed immunoglobulins as universal substrates

Abuknesha, R., Jeganathan, F., Wildeboer, D. and Price, R. 2010. Optimisation of the detection of bacterial proteases using adsorbed immunoglobulins as universal substrates. Talanta. 81 (4-5), pp. 1237-1244. https://doi.org/10.1016/j.talanta.2010.02.015

Rapid detection of Escherichia coli in water using a hand-held fluorescence detector

Wildeboer, D., Amirat, L., Price, R. and Abuknesha, R. 2010. Rapid detection of Escherichia coli in water using a hand-held fluorescence detector. Water Research. 44 (8), pp. 2621-2628. https://doi.org/10.1016/j.watres.2010.01.020

Use of antibody–hapten complexes attached to optical sensor surfaces as a substrate for proteases: real-time biosensing of protease activity

Wildeboer, D., Jiang, P., Price, R., Yu, S., Jeganathan, F. and Abuknesha, R. 2010. Use of antibody–hapten complexes attached to optical sensor surfaces as a substrate for proteases: real-time biosensing of protease activity. Talanta. 81 (1-2), pp. 68-75. https://doi.org/10.1016/j.talanta.2009.11.036

Characterization of bacterial proteases with a panel of fluorescent peptide substrates

Wildeboer, D., Jeganathan, F., Price, R. and Abuknesha, R. 2009. Characterization of bacterial proteases with a panel of fluorescent peptide substrates. Analytical Biochemistry. 384 (2), pp. 321-328. https://doi.org/10.1016/j.ab.2008.10.004

Screening of herbal constituents for aromatase inhibitory activity

Paoletta, S., Steventon, G., Wildeboer, D., Ehrman, T., Hylands, P. and Barlow, D. 2008. Screening of herbal constituents for aromatase inhibitory activity. Bioorganic & Medicinal Chemistry. 16 (18), pp. 8466-8470. https://doi.org/10.1016/j.bmc.2008.08.034

The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events

Moss, M., Bomar, M., Liu, Q., Sage, H., Dempsey, P., Lenhart, P., Gillispie, P., Stoeck, A., Wildeboer, D., Bartsch, J., Palmisano, R. and Zhou, P. 2007. The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events. Journal of Biological Chemistry. 282 (49), pp. 35712-35721. https://doi.org/10.1074/jbc.M703231200

Metalloproteinase disintegrins ADAM8 and ADAM19 are highly regulated in human primary brain tumors and their expression levels and activities are associated with invasiveness.

Wildeboer, D., Naus, S., Sang, Q., Bartsch, J. and Pagenstecher, A. 2006. Metalloproteinase disintegrins ADAM8 and ADAM19 are highly regulated in human primary brain tumors and their expression levels and activities are associated with invasiveness. Journal of Neuropathology and Experimental Neurology. 65 (5), pp. 516-527.

Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8.

Naus, S., Reipschläger, S., Wildeboer, D., Lichtenthaler, S., Mitterreiter, S., Guan, Z., Moss, M. and Bartsch, J. 2006. Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8. Biological Chemistry. 387 (3), pp. 337-346. https://doi.org/10.1515/BC.2006.045

Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death

Naus, S., Richter, M., Wildeboer, D., Moss, M., Schachner, M. and Bartsch, J. 2004. Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. Journal of Biological Chemistry. 279 (16), pp. 16083-16090. https://doi.org/10.1074/jbc.M400560200

The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion

Schlomann, U., Wildeboer, D., Webster, A., Antropova, O., Zeuschner, D., Knight, C., Docherty, A., Lambert, M., Skelton, L., Jockusch, H. and Bartsch, J. 2002. The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion. Journal of Biological Chemistry. 277 (50), pp. 48210-48219. https://doi.org/10.1074/jbc.M203355200
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