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A Potential Role of Keratinocyte-Derived Bilirubin in Human Skin Yellowness and Its Amelioration by Sucrose Laurate/Dilaurate (2022)
Journal Article
Fang, B., Card, P. D., Chen, J., Li, L., Laughlin, T., Jarrold, B., …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

Sallow and/or dull skin appearance is greatly attributable to the yellow components of skin tone. Bilirubin is a yellow chromophore known to be made in the liver and/or spleen and is transported throughout the body via the blood stream. Recent public... Read More about A Potential Role of Keratinocyte-Derived Bilirubin in Human Skin Yellowness and Its Amelioration by Sucrose Laurate/Dilaurate.

Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro (2021)
Journal Article
Hunter-Featherstone, E., Young, N., Chamberlain, K., Cubillas, P., Hulette, B., Wei, X., …Karakesisoglou, I. (2021). Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro. Cells, 10(5), https://doi.org/10.3390/cells10051177

Mechanotransduction is defined as the ability of cells to sense mechanical stimuli from their surroundings and translate them into biochemical signals. Epidermal keratinocytes respond to mechanical cues by altering their proliferation, migration, and... Read More about Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro.

Elucidation of the AGR2 interactome in esophageal adenocarcinoma cells identifies a redox sensitive chaperone hub for the quality control of MUC-5AC (2019)
Journal Article
Worfolk, J., Bell, S., Simpson, L., Carne, N., Francis, S., Engelbertsen, V., …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

Aims: AGR2 is a tissue-restricted member of the protein disulfide isomerase family that has attracted interest because it is highly expressed in a number of cancers, including gastroesophageal adenocarcinoma. The behavior of AGR2 was analyzed under o... Read More about Elucidation of the AGR2 interactome in esophageal adenocarcinoma cells identifies a redox sensitive chaperone hub for the quality control of MUC-5AC.

Reductive stress selectively disrupts collagen homeostasis and modifies growth factor-independent signalling through the MAPK/Akt pathway in human dermal fibroblasts (2019)
Journal Article
Carne, N., Bell, S., Brown, A., 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

Redox stress is a well-known contributor to ageing and diseases in skin. Reductants such as dithiothreitol (DTT) can trigger a stress response by disrupting disulfide bonds. However, the quantitative response of the cellular proteome to reductants ha... Read More about Reductive stress selectively disrupts collagen homeostasis and modifies growth factor-independent signalling through the MAPK/Akt pathway in human dermal fibroblasts.

Endoplasmic Reticulum redox pathways: in sickness and in health (2018)
Journal Article
Benham, A. M. (2019). Endoplasmic Reticulum redox pathways: in sickness and in health. The FEBS Journal, 286(2), 311--321. https://doi.org/10.1111/febs.14618

The Endoplasmic Reticulum (ER) is the major site for secretory protein production in eukaryotic cells and like an efficient factory, it has the capacity to expand or contract its output depending on the demand for its services. A primary function of... Read More about Endoplasmic Reticulum redox pathways: in sickness and in health.

GnRH immunization alters the expression and distribution of protein disulfide isomerases in the epididymis (2016)
Journal Article
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

Hypogonadism is defined as the inadequate gonadal production of testosterone. Low serum testosterone leads to infertility by impairing spermatogenesis and reducing sperm count, however, the impact of hypogonadism in epididymal sperm maturation is poo... Read More about GnRH immunization alters the expression and distribution of protein disulfide isomerases in the epididymis.

Calreticulin is required for development of the cumulus oocyte complex and female fertility (2015)
Journal Article
Tokuhiro, K., Satouh, Y., Nozawa, K., Isotani, A., Fujihara, Y., Hirashima, Y., …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

Calnexin (CANX) and calreticulin (CALR) chaperones mediate nascent glycoprotein folding in the endoplasmic reticulum. Here we report that these chaperones have distinct roles in male and female fertility. Canx null mice are growth retarded but fertil... Read More about Calreticulin is required for development of the cumulus oocyte complex and female fertility.

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 (2014)
Journal Article
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

A new family of platinum(II) complexes of the form PtLnSR have been prepared, where Ln represents a cyclometalating, NCN-bound tridentate ligand and SR is a monodentate thiolate ligand. The complexes fall into two groups, those of PtL1SR where HL1 =... Read More about 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.

Expression of the Endoplasmic Reticulum Oxidoreductase Ero1α in gastro-intestinal cancer reveals a link between homocysteine and oxidative protein folding. (2013)
Journal Article
Battle, D., Dias-Gunasekara, S., Watson, G., Mohamed Ahmed, E., Saysell, C., Altaf, N., …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 (2013)
Journal Article
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

The protein folding machinery of the endoplasmic reticulum (ER) ensures that proteins entering the eukaryotic secretory pathway acquire appropriate post-translational modifications and reach a stably folded state. An important component of this prote... Read More about Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum.

Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility (2012)
Journal Article
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

A disintegrin and metalloproteinase 3 (ADAM3) is a sperm membrane protein critical for both sperm migration from the uterus into the oviduct and sperm primary binding to the zona pellucida (ZP). Here we show that the testis-specific protein disulfide... Read More about Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility.

Conserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation (2011)
Journal Article
Pekovic, V., Gibbs-Seymour, I., Markiewicz, E., Alzoghaibi, F., Benham, A., Edwards, R., …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

Pre-lamin A and progerin have been implicated in normal aging, and the pathogenesis of age-related degenerative diseases is termed ‘laminopathies’. Here, we show that mature lamin A has an essential role in cellular fitness and that oxidative damage... Read More about Conserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation.

Fertilization: a sperm's journey to and interaction with the oocyte. (2010)
Journal Article
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

Mammalian fertilization comprises sperm migration through the female reproductive tract, biochemical and morphological changes to sperm, and sperm-egg interaction in the oviduct. Recent gene knockout approaches in mice have revealed that many factors... Read More about Fertilization: a sperm's journey to and interaction with the oocyte..

Protein folding and disulfide bond formation in the eukaryotic cell. (2009)
Journal Article
Benham, A. (2009). Protein folding and disulfide bond formation in the eukaryotic cell. The FEBS Journal, 276(23), 6905-11. https://doi.org/10.1111/j.1742-4658.2009.07409.x

The endoplasmic reticulum (ER) plays a critical role as a compartment for protein folding in eukaryotic cells. Defects in protein folding contribute to a growing list of diseases, and advances in our understanding of the molecular details of protein... Read More about Protein folding and disulfide bond formation in the eukaryotic cell..

A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells (2007)
Journal Article
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

Glycoprotein folding is mediated by lectin-like chaperones and protein disulfide isomerases (PDIs) in the endoplasmic reticulum (ER). Calnexin and the PDI homologue ERp57 work together to help fold nascent polypeptides with glycans located toward the... Read More about A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells.

Activation of the unfolded protein response and alternative splicing of ATF6α in HLA-B27 positive lymphocytes (2007)
Journal Article
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

Misfolding of major histocompatibility complex (MHC) class I molecules has been implicated in the rheumatic autoimmune disease ankylosing spondylitis (AS), and has been linked to the unfolded protein response (UPR) in rodent AS models. XBP1 and ATF6α... Read More about Activation of the unfolded protein response and alternative splicing of ATF6α in HLA-B27 positive lymphocytes.

The DM and DM chain cooperate in the oxidation and folding of HLA-DM1 (2006)
Journal Article
van Lith, M., & Benham, A. (2006). The DM and DM chain cooperate in the oxidation and folding of HLA-DM1. The Journal of Immunology, 177(8), 5430-5439

HLA-DM (DM) is a heterodimeric MHC molecule that catalyzes the peptide loading of classical MHC class II molecules in the endosomal/lysosomal compartments of APCs. Although the function of DM is well-established, little is known about how DM and -cha... Read More about The DM and DM chain cooperate in the oxidation and folding of HLA-DM1.

Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1b (2006)
Journal Article
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

Disulfide bond catalysis is an essential component of protein biogenesis in the secretory pathway, from yeast through to man. In the endoplasmic reticulum (ER), protein-disulfide isomerase (PDI) catalyzes the oxidation and isomerization of disulfide... Read More about Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1b.

Differential oxidation of HLA-B2704 and HLA-B2705 in lymphoblastoid and transfected adherent cell lines (2006)
Journal Article
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

MHC class I molecules are predominantly involved in the presentation of antigens from viral proteins to CD8+ T cells of the immune system. However, MHC proteins can also be linked to autoimmune diseases, and the HLA-B27 allele is expressed by 95% of... Read More about Differential oxidation of HLA-B2704 and HLA-B2705 in lymphoblastoid and transfected adherent cell lines.

Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb (2005)
Journal Article
Dias-Gunasekara, S., Gubbens, J., van Lith, M., Dunne, C., Williams, J., Kataky, R., …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

Endoplasmic reticulum oxidoreductases (Eros) are essential for the formation of disulfide bonds. Understanding disulfide bond catalysis in mammals is important because of the involvement of protein misfolding in conditions such as diabetes, arthritis... Read More about Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb.

PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum (2005)
Journal Article
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

Protein disulfide isomerase (PDI) is the archetypal enzyme involved in the formation and reshuffling of disulfide bonds in the endoplasmic reticulum (ER). PDI achieves its redox function through two highly conserved thioredoxin domains, and PDI can a... Read More about PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.

Cloning and initial characterization of the Arabidopsis thaliana Endoplasmic Reticulum Oxidoreductins (2003)
Journal Article
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

The oxidation and isomerization of disulfide bonds is necessary for the growth of all organisms. In yeast, the oxidative folding of secretory pathway proteins is catalyzed by protein disulfide isomerase (PDI), which requires Ero1p (endoplasmic reticu... Read More about Cloning and initial characterization of the Arabidopsis thaliana Endoplasmic Reticulum Oxidoreductins.

Manipulation of oxidative protein folding and PDI redox state in mammalian cells. (2001)
Journal Article
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. The EMBO Journal, 20(22), 6288-6296. https://doi.org/10.1093/emboj/20.22.6288

In the endoplasmic reticulum (ER), disulfide bonds are simultaneously formed in nascent proteins and removed from incorrectly folded or assembled molecules. In this compartment, the redox state must be, therefore, precisely regulated. Here we show th... Read More about Manipulation of oxidative protein folding and PDI redox state in mammalian cells..

The CXXCXXC motif determines the folding, structure and stability of human Ero1-La. (2000)
Journal Article
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. The EMBO Journal, 19(17), 4493-4502. https://doi.org/10.1093/emboj/19.17.4493

The presence of correctly formed disulfide bonds is crucial to the structure and function of proteins that are synthesized in the endoplasmic reticulum (ER). Disulfide bond formation occurs in the ER owing to the presence of several specialized catal... Read More about The CXXCXXC motif determines the folding, structure and stability of human Ero1-La..

Allelic differences in the relationship between proteasome activity and MHC class I peptide loading. (1998)
Journal Article
Benham, A., Grommé, M., & Neefjes, J. (1998). Allelic differences in the relationship between proteasome activity and MHC class I peptide loading. The Journal of Immunology, 161(1), 83-89

MHC class I molecules are cell surface glycoproteins that play a pivotal role in the response to intracellular pathogens. The loading of MHC class I molecules with antigenic substrates takes place in the endoplasmic reticulum. This requires a functio... Read More about Allelic differences in the relationship between proteasome activity and MHC class I peptide loading..