Search Results - "Lloyd W. Ruddock"
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Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation
Published in Antioxidants & redox signaling (01-11-2009)“…Disulfide bond formation is probably involved in the biogenesis of approximately one third of human proteins. A central player in this essential process is…”
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Design of an alternate antibody fragment format that can be produced in the cytoplasm of Escherichia coli
Published in Scientific reports (30-08-2023)“…With increased accessibility and tissue penetration, smaller antibody formats such as antibody fragments (Fab) and single chain variable fragments (scFv) show…”
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Efficient Production of Fc Fusion Proteins in the Cytoplasm of Escherichia coli : Dissecting and Mitigating Redox Heterogeneity
Published in International journal of molecular sciences (25-11-2022)“…Cost-effective production of therapeutic proteins in microbial hosts is an indispensable tool towards accessible healthcare. Many of these heterologously…”
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N-glycan processing in ER quality control
Published in Journal of cell science (01-11-2006)“…Glycosylation of asparagine residues in Asn-x-Ser/Thr motifs is a common covalent modification of proteins in the lumen of the endoplasmic reticulum (ER). By…”
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The human protein disulphide isomerase family: substrate interactions and functional properties
Published in EMBO reports (01-01-2005)“…The process of disulphide bond formation in the endoplasmic reticulum of eukaryotic cells was one of the first mechanisms of catalysed protein folding to be…”
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Biophysical and structural studies of fibulin-2
Published in Scientific reports (02-07-2024)“…Fibulin-2 is a multidomain, disulfide-rich, homodimeric protein which belongs to a broader extracellular matrix family. It plays an important role in the…”
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Complementarity determining regions and frameworks contribute to the disulfide bond independent folding of intrinsically stable scFv
Published in PloS one (18-12-2017)“…CyDisCo is a system facilitating disulfide bond formation in recombinant proteins in the cytoplasm of Escherichia coli. Previously we screened for soluble…”
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Production of neutralizing antibody fragment variants in the cytoplasm of E. coli for rapid screening: SARS-CoV-2 a case study
Published in Scientific reports (16-03-2023)“…Global health challenges such as the coronavirus pandemic warrant the urgent need for a system that allows efficient production of diagnostic and therapeutic…”
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The crystal structure of human microsomal triglyceride transfer protein
Published in Proceedings of the National Academy of Sciences - PNAS (27-08-2019)“…Microsomal triglyceride transfer protein (MTP) plays an essential role in lipid metabolism, especially in the biogenesis of very low-density lipoproteins and…”
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Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease
Published in Scientific reports (30-04-2018)“…Coronary artery disease is the most common cause of death globally and is linked to a number of risk factors including serum low density lipoprotein, high…”
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Substrate recognition by the protein disulfide isomerases
Published in The FEBS journal (01-10-2007)“…Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the…”
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Structural analysis of human NHLRC2, mutations of which are associated with FINCA disease
Published in PloS one (23-08-2018)“…NHLRC2 (NHL repeat-containing protein 2) is an essential protein. Mutations of NHLRC2, including Asp148Tyr, have been recently associated with a novel FINCA…”
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High-resolution Crystal Structure of Human pERp1, A Saposin-like Protein Involved in IgA, IgM and Integrin Maturation in the Endoplasmic Reticulum
Published in Journal of molecular biology (05-03-2021)“…[Display omitted] •The CNPY family are specialized protein folding factors in the ER.•Here we present the high-resolution crystal structure of human pERp1.•The…”
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Systematic screening of soluble expression of antibody fragments in the cytoplasm of E. coli
Published in Microbial cell factories (25-01-2016)“…Disulfide bonds are the most common structural, post-translational modification found in proteins. Antibodies contain up to 25 disulfide bonds depending on…”
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Efficient soluble expression of disulfide bonded proteins in the cytoplasm of Escherichia coli in fed-batch fermentations on chemically defined minimal media
Published in Microbial cell factories (15-06-2017)“…The production of recombinant proteins containing disulfide bonds in Escherichia coli is challenging. In most cases the protein of interest needs to be either…”
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Low-molecular-weight oxidants involved in disulfide bond formation
Published in Antioxidants & redox signaling (15-05-2012)“…The biogenesis of most secreted and outer membrane proteins involves the formation of structure stabilizing disulfide bonds. Hence knowledge of the mechanisms…”
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Reexamination of the Role of Interplay between Glutathione and Protein Disulfide Isomerase
Published in Journal of molecular biology (03-06-2011)“…Protein disulfide isomerase (PDI) has an essential role in the process of disulfide bond formation, where it catalyzes disulfide bond formation, reduction, and…”
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Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides
Published in Molecular biology of the cell (01-10-2015)“…The endoplasmic reticulum (ER) is the site of maturation for secretory and membrane proteins in eukaryotic cells. The lumen of the mammalian ER contains >20…”
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Production of Extracellular Matrix Proteins in the Cytoplasm of E. coli : Making Giants in Tiny Factories
Published in International journal of molecular sciences (21-01-2020)“…is the most widely used protein production host in academia and a major host for industrial protein production. However, recombinant production of eukaryotic…”
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Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli
Published in Microbial cell factories (07-01-2011)“…Disulfide bonds are one of the most common post-translational modifications found in proteins. The production of proteins that contain native disulfide bonds…”
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