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Professor Adam Benham's Outputs (33)

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..