Staff profile

I graduated from St. Catherine's College, Oxford University, with first class honours in Biochemistry and was awarded a Wellcome-funded PhD in transplantation immunology with Prof. John Fabre at the Institute of Child Health, University College, London. I received a Marie-Curie EU postdoctoral fellowship to study the biochemistry of antigen presentation with Prof. Jacques Neefjes at the Netherlands Cancer Institute in Amsterdam and then joined Prof. Ineke Braakman's laboratory at Utrecht University, Netherlands, to research mechanisms of protein quality control in the endoplasmic reticulum (ER).

I am the Postgraduate Director for Biosciences at Durham with responsibility for postgraduate training provision in the Department. I am the Durham academic lead for the MRC-funded "Discovery Medicine North Across the Lifecourse" (DiMeN-XL) DLA training partnership, the training lead for the BBSRC-funded "North-East England Doctoral Landscape" (NEEDL) DLA postgraduate programme, and I am on the management board of the BBSRC-funded "Bioconvergence for Sustainable Consumer Innovations" (BiSCI) industrial DLA postgraduate programme.

In my research at Durham University, I lead a group that investigates proteostasis and the quality control of proteins in the secretory pathway, including proteins involved in antigen presentation and oxidative protein folding in various cells and tissues. My laboratory is interested in how these fundamentally important biological pathways underpin human health. For example, we discovered a novel member of the Protein Disulfide Isomerase (PDI) family called PDILT that is required for sperm:egg binding (in collaboration with Osaka University, Japan). This work has increased our understanding of unexplained male infertility and has been covered extensively by the media.

Our work on immune molecules (the Major Histocompatibility Complex, MHC) seeks to discover how these proteins are loaded with their peptide cargo and how oxidative protein folding and ER chaperones contribute to their quality control. This research has applications in understanding infection and also neoantigen presentation for the design of cancer vaccines. In current work, we are seeking to unravel the trafficking of MHC-neoantigen complexes in melanoma.

Other studies in my laboratory have revealed links between the ER quality control machinery and gastrointestinal disease (in collaboration with James Cook University Hospital, Middlesbrough). We have been harnessing new high-resolution bioimaging and quantitative proteomics technologies (SWATH) to explore the biology of proteostasis and stress responses in the skin (in collaboration with P&G and our Bioimaging lead), including extracellular matrix proteins such as collagen, and pigment trafficking proteins in melanocytes.

I have established and delivered undergraduate teaching provision on a range of courses at Durham. Currently, I lead the Level 2 “Immune Systems” module and I am course contributor for the Level 3 “Biology of Disease” module. I have been appointed as an external examiner for various undergraduate degree courses and postgraduate programmes.

I am on the editorial board of the journal "Antioxidants and Redox Signaling" and I serve on the Biochemical Society Conferences and Training Panel. I am the Durham representative for Immunology North East and I am a member of the following learned societies: Royal Society of Biology, Biochemical Society, British Society for Immunology, Society for Experimental Biology.

My research has been funded by the BBSRC, MRC, Wellcome Trust, Arthritis Research UK, Leverhulme Trust, Royal Society, European Union, JGWP Foundation, IBM, P&G and FAPESP (Brazil) and the support of these organisations is gratefully acknowledged.

A selection of our peer-reviewed research publications can be found below.

• cell biology and biochemistry
• immune system
• oxidative folding of proteins in the Endoplasmic Reticulum

Chapter in book

• Protein secretion and the endoplasmic reticulum
  
  Benham, A. (2012). Protein secretion and the endoplasmic reticulum. In J. Hershey, N. Sonenberg, & M. Mathews (Eds.), Protein Synthesis and Translational Control (pp. 147-162). Cold Spring Harbor Press. https://doi.org/10.1101/cshperspect.a012872

Journal Article

• New imaging tools reveal live cellular collagen secretion, fibril dynamics and network organisation
  
  Kent, O., Casey, E. R., Brown, M., Bell, S., Ehrman, M. C., Flagler, M. J., Määttä, A., Benham, A. M., & Hawkins, T. J. (2025). New imaging tools reveal live cellular collagen secretion, fibril dynamics and network organisation. Scientific Reports, 15, Article 13764. https://doi.org/10.1038/s41598-025-96280-4
• Epididymal mRNA expression profiles for the protein disulfide isomerase gene family: Modulation by development and androgens.
  
  Fernandes, S. G., Ferreira, L. G. A., Benham, A. M., & Avellar, M. C. W. (2024). Epididymal mRNA expression profiles for the protein disulfide isomerase gene family: Modulation by development and androgens. Andrology. Advance online publication. https://doi.org/10.1111/andr.13700
• Para-Hydroxycinnamic Acid Mitigates Senescence and Inflammaging in Human Skin Models
  
  Tan, C. Y. R., Morenc, M., Setiawan, M., Lim, Z. Z. Y., Soon, A. L., Bierman, J. C., Vires, L., Laughlin, T., DeAngelis, Y. M., Rovito, H., Jarrold, B. B., Nguyen, T. Q. N., Lim, J. S. Y., Kent, O., Määttä, A., Benham, A. M., Hawkins, T. J., Lee, X. E., Ehrman, M. C., … Bellanger, S. (2024). Para-Hydroxycinnamic Acid Mitigates Senescence and Inflammaging in Human Skin Models. International Journal of Molecular Sciences, 25(15), Article 8153. https://doi.org/10.3390/ijms25158153
• Inhibition of PDIs Downregulates Core LINC Complex Proteins, Promoting the Invasiveness of MDA-MB-231 Breast Cancer Cells in Confined Spaces In Vitro
  
  Young, N., Gui, Z., Mustafa, S., Papa, K., Jessop, E., Ruddell, E., Bevington, L., Quinlan, R. A., Benham, A. M., Goldberg, M. W., Obara, B., & Karakesisoglou, I. (2024). Inhibition of PDIs Downregulates Core LINC Complex Proteins, Promoting the Invasiveness of MDA-MB-231 Breast Cancer Cells in Confined Spaces In Vitro. Cells, 13(11), Article 906. https://doi.org/10.3390/cells13110906
• A Potential Role of Keratinocyte-Derived Bilirubin in Human Skin Yellowness and Its Amelioration by Sucrose Laurate/Dilaurate
  
  Fang, B., Card, P. D., Chen, J., Li, L., Laughlin, T., Jarrold, B., Zhao, W., Benham, A. M., Määttä, A. T., Hawkins, T. J., & Hakozaki, T. (2022). A Potential Role of Keratinocyte-Derived Bilirubin in Human Skin Yellowness and Its Amelioration by Sucrose Laurate/Dilaurate. International Journal of Molecular Sciences, 23(11), Article 5884. https://doi.org/10.3390/ijms23115884
• Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro
  
  Hunter-Featherstone, E., Young, N., Chamberlain, K., Cubillas, P., Hulette, B., Wei, X., Tiesman, J. P., Bascom, C. C., Benham, A. M., Goldberg, M. W., Saretzki, G., & Karakesisoglou, I. (2021). Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro. Cells, 10(5). https://doi.org/10.3390/cells10051177
• Elucidation of the AGR2 interactome in esophageal adenocarcinoma cells identifies a redox sensitive chaperone hub for the quality control of MUC-5AC
  
  Worfolk, J., Bell, S., Simpson, L., Carne, N., Francis, S., Engelbertsen, V., Brown, A., Walker, J., Viswanath, Y., & Benham, A. (2019). Elucidation of the AGR2 interactome in esophageal adenocarcinoma cells identifies a redox sensitive chaperone hub for the quality control of MUC-5AC. Antioxidants and Redox Signaling, 31(15), 1117-1132. https://doi.org/10.1089/ars.2018.7647
• Reductive stress selectively disrupts collagen homeostasis and modifies growth factor-independent signalling through the MAPK/Akt pathway in human dermal fibroblasts
  
  Carne, N., Brown, A., Bell, S., Maatta, A., Flagler, M., & Benham, A. (2019). Reductive stress selectively disrupts collagen homeostasis and modifies growth factor-independent signalling through the MAPK/Akt pathway in human dermal fibroblasts. Molecular and Cellular Proteomics, 18(6), 1123-1137. https://doi.org/10.1074/mcp.ra118.001140
• Endoplasmic Reticulum redox pathways: in sickness and in health
  
  Benham, A. M. (2019). Endoplasmic Reticulum redox pathways: in sickness and in health. FEBS Journal, 286(2), 311--321. https://doi.org/10.1111/febs.14618
• GnRH immunization alters the expression and distribution of protein disulfide isomerases in the epididymis
  
  Schorr-Lenz, A., Alves, J., Hence, N., Seidel, P., Benham, A., & Bustamante-Filho, I. (2016). GnRH immunization alters the expression and distribution of protein disulfide isomerases in the epididymis. Andrology, 4(5), 957-963. https://doi.org/10.1111/andr.12205
• Calreticulin is required for development of the cumulus oocyte complex and female fertility
  
  Tokuhiro, K., Satouh, Y., Nozawa, K., Isotani, A., Fujihara, Y., Hirashima, Y., Matsumura, H., Takumi, K., Miyano, T., Okabe, M., Benham, A., & Ikawa, M. (2015). Calreticulin is required for development of the cumulus oocyte complex and female fertility. Scientific Reports, 5. https://doi.org/10.1038/srep14254
• Platinum(II) Complexes of N^C^N‑Coordinating 1,3-Bis(2-pyridyl)benzene Ligands: Thiolate Coligands Lead to Strong Red Luminescence from Charge-Transfer States
  
  Tarran, W., Freeman, G., Murphy, L., Benham, A., Kataky, R., & Williams, J. (2014). Platinum(II) Complexes of N^C^N‑Coordinating 1,3-Bis(2-pyridyl)benzene Ligands: Thiolate Coligands Lead to Strong Red Luminescence from Charge-Transfer States. Inorganic Chemistry, 53(11), 5738-5749. https://doi.org/10.1021/ic500555w
• Expression of the Endoplasmic Reticulum Oxidoreductase Ero1α in gastro-intestinal cancer reveals a link between homocysteine and oxidative protein folding.
  
  Battle, D., Dias-Gunasekara, S., Watson, G., Mohamed Ahmed, E., Saysell, C., Altaf, N., Sanusi, A., Munipalle, P., Scoones, D., Walker, J., Viswanath, Y., & Benham, A. (2013). Expression of the Endoplasmic Reticulum Oxidoreductase Ero1α in gastro-intestinal cancer reveals a link between homocysteine and oxidative protein folding. Antioxidants and Redox Signaling, 19(1), 24-45. https://doi.org/10.1089/ars.2012.4651
• Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
  
  Benham, A., van Lith, M., Sitia, R., & Braakman, I. (2013). Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum. Philosophical Transactions of the Royal Society B: Biological Sciences, 368(1617), Article 20110403. https://doi.org/10.1098/rstb.2011.0403
• Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility
  
  Tokuhiro, K., Ikawa, M., Benham, A., & Okabe, M. (2012). Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility. Proceedings of the National Academy of Sciences, 109(10), 3850-3855. https://doi.org/10.1073/pnas.1117963109
• The protein disulfide isomerase family: key players in health and disease.
  
  Benham, A. (2012). The protein disulfide isomerase family: key players in health and disease. Antioxidants and Redox Signaling, 16(8), 781-789. https://doi.org/10.1089/ars.2011.4439
• Conserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation
  
  Pekovic, V., Gibbs-Seymour, I., Markiewicz, E., Alzoghaibi, F., Benham, A., Edwards, R., Wehnert, M., von Zlignicki, T., & Hutchison, C. (2011). Conserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation. Aging Cell, 10(6), 1067-1079. https://doi.org/10.1111/j.1474-9726.2011.00750.x
• Calsperin is a testis-specific chaperone required for sperm fertility
  
  Ikawa, M., Tokuhiro, K., Yamaguchi, R., Benham, A., Tamura, T., Wada, I., Satouh, Y., Inoue, N., & Okabe, M. (2011). Calsperin is a testis-specific chaperone required for sperm fertility. Journal of Biological Chemistry, 286(7), 5639-5646. https://doi.org/10.1074/jbc.m110.140152
• Fertilization: a sperm's journey to and interaction with the oocyte.
  
  Ikawa, M., Inoue, N., Benham, A., & Okabe, M. (2010). Fertilization: a sperm’s journey to and interaction with the oocyte. Journal of Clinical Investigation, 120(4), 984-994. https://doi.org/10.1172/jci41585
• HLA-DP, HLA-DQ and HLA-DR have different requirements for invariant chain and HLA-DM
  
  van Lith, M., McEwen-Smith, R., & Benham, A. (2010). HLA-DP, HLA-DQ and HLA-DR have different requirements for invariant chain and HLA-DM. Journal of Biological Chemistry, 285(52), 40800-40808. https://doi.org/10.1074/jbc.m110.148155
• Protein folding and disulfide bond formation in the eukaryotic cell.
  
  Benham, A. (2009). Protein folding and disulfide bond formation in the eukaryotic cell. FEBS Journal, 276(23), 6905-11. https://doi.org/10.1111/j.1742-4658.2009.07409.x
• A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells
  
  van Lith, M., Karala, A., Bown, D., Gatehouse, J., Ruddock, L., Saunders, P., & Benham, A. (2007). A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells. Molecular Biology of the Cell, 18(8), 2795-2804. https://doi.org/10.1091/mbc.e07-02-0147
• Activation of the unfolded protein response and alternative splicing of ATF6α in HLA-B27 positive lymphocytes
  
  Lemin, A., Saleki, K., van Lith, M., & Benham, A. (2007). Activation of the unfolded protein response and alternative splicing of ATF6α in HLA-B27 positive lymphocytes. FEBS Letters, 581(9), 1819-1824. https://doi.org/10.1016/j.febslet.2007.03.069
• An introduction to thiol redox proteins in the endoplasmic reticulum and a review of current electrochemical methods of detection of thiols
  
  Kruusma, J., Benham, A. M., Gareth Williams, J. A., & Kataky, R. (2006). An introduction to thiol redox proteins in the endoplasmic reticulum and a review of current electrochemical methods of detection of thiols. Analyst, 131(4), 459-473. https://doi.org/10.1039/b515874e
• The DM and DM chain cooperate in the oxidation and folding of HLA-DM1
  
  van Lith, M., & Benham, A. (2006). The DM and DM chain cooperate in the oxidation and folding of HLA-DM1. Journal of Immunology, 177(8), 5430-5439.
• Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1b
  
  Dias-Gunasekara, S., van Lith, M., Williams, J., Kataky, R., & Benham, A. (2006). Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1b. Journal of Biological Chemistry, 281(35), 25018-25025. https://doi.org/10.1074/jbc.m602354200
• Differential oxidation of HLA-B2704 and HLA-B2705 in lymphoblastoid and transfected adherent cell lines
  
  Saleki, K., Hartigan, N., van Lith, M., Bulleid, N., & Benham, A. (2006). Differential oxidation of HLA-B2704 and HLA-B2705 in lymphoblastoid and transfected adherent cell lines. Antioxidants and Redox Signaling, 8(3-4), 292-299. https://doi.org/10.1089/ars.2006.8.292
• Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb
  
  Dias-Gunasekara, S., Gubbens, J., van Lith, M., Dunne, C., Williams, J., Kataky, R., Scoones, D., Lapthorn, A., Bulleid, N., & Benham, A. (2005). Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb. Journal of Biological Chemistry, 280(38), 33066-33075. https://doi.org/10.1074/jbc.m505023200
• PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum
  
  van Lith, M., Hartigan, N., Hatch, J., & Benham, A. (2005). PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum. Journal of Biological Chemistry, 280(2), 1376-1383. https://doi.org/10.1074/jbc.m408651200
• Cloning and initial characterization of the Arabidopsis thaliana Endoplasmic Reticulum Oxidoreductins
  
  Dixon, D., van Lith, M., Edwards, R., & Benham, A. (2003). Cloning and initial characterization of the Arabidopsis thaliana Endoplasmic Reticulum Oxidoreductins. Antioxidants and Redox Signaling, 5(4), 389-396. https://doi.org/10.1089/152308603768295122
• Manipulation of oxidative protein folding and PDI redox state in mammalian cells.
  
  Mezghrani, A., Fassio, A., Benham, A., Simmen, T., Braakman, I., & Sitia, R. (2001). Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO Journal, 20(22), 6288-6296. https://doi.org/10.1093/emboj/20.22.6288
• The CXXCXXC motif determines the folding, structure and stability of human Ero1-La.
  
  Benham, A., Cabibbo, A., Fassio, A., Bulleid, N., Sitia, R., & Braakman, I. (2000). The CXXCXXC motif determines the folding, structure and stability of human Ero1-La. EMBO Journal, 19(17), 4493-4502. https://doi.org/10.1093/emboj/19.17.4493
• Allelic differences in the relationship between proteasome activity and MHC class I peptide loading.
  
  Benham, A., Grommé, M., & Neefjes, J. (1998). Allelic differences in the relationship between proteasome activity and MHC class I peptide loading. Journal of Immunology, 161(1), 83-89.
• Synthesis and assembly of MHC-peptide complexes.
  
  Benham, A., Tulp, A., & Neefjes, J. (1995). Synthesis and assembly of MHC-peptide complexes. Immunology Today., 16(7), 359-362. https://doi.org/10.1016/0167-5699%2895%2980157-x

Working Paper

• New imaging tools reveal live cellular collagen secretion, fibril dynamics and network organisation
  
  Kent, O., Casey, E. R., Brown, M., Bell, S., Ehrman, M., Flagler, M., Määttä, A., Benham, A. M., & Hawkins, T. J. (2024). New imaging tools reveal live cellular collagen secretion, fibril dynamics and network organisation. BioRxiv. https://doi.org/10.1101/2024.08.15.608104