Search Results - "FREEDMAN, Robert B"

Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway by Irvine, Alistair G, Wallis, A Katrine, Sanghera, Narinder, Rowe, Michelle L, Ruddock, Lloyd W, Howard, Mark J, Williamson, Richard A, Blindauer, Claudia A, Freedman, Robert B

“…In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to…”
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Efficient export of prefolded, disulfide-bonded recombinant proteins to the periplasm by the Tat pathway in Escherichia coli CyDisCo strains by Matos, Cristina F. R. O., Robinson, Colin, Alanen, Heli I., Prus, Piotr, Uchida, Yuko, Ruddock, Lloyd W., Freedman, Robert B., Keshavarz-Moore, Eli

“…Numerous high‐value therapeutic proteins are produced in Escherichia coli and exported to the periplasm, as this approach simplifies downstream processing and…”
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High-yield export of a native heterologous protein to the periplasm by the tat translocation pathway in Escherichia coli by Matos, Cristina F.R.O., Branston, Steven D., Albiniak, Anna, Dhanoya, Arjun, Freedman, Robert B., Keshavarz-Moore, Eli, Robinson, Colin

“…Numerous high‐value recombinant proteins that are produced in bacteria are exported to the periplasm as this approach offers relatively easy downstream…”
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Mapping of the ligand-binding site on the b' domain of human PDI: interaction with peptide ligands and the x-linker region by Byrne, Lee J, Sidhu, Ateesh, Wallis, A Katrine, Ruddock, Lloyd W, Freedman, Robert B, Howard, Mark J, Williamson, Richard A

“…PDI (protein disulfide-isomerase) catalyses the formation of native disulfide bonds of secretory proteins in the endoplasmic reticulum. PDI consists of four…”
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Alternative Conformations of the x Region of Human Protein Disulphide-Isomerase Modulate Exposure of the Substrate Binding b’ Domain by Nguyen, Van Dat, Wallis, Katrine, Howard, Mark J., Haapalainen, Antti M., Salo, Kirsi E.H., Saaranen, Mirva J., Sidhu, Ateesh, Wierenga, Rik K., Freedman, Robert B., Ruddock, Lloyd W., Williamson, Richard A.

“…Protein disulphide isomerase (PDI) is a key multi-domain protein folding catalyst in the endoplasmic reticulum. The b’ domain of PDI is essential for the…”
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High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility by Amin, Nader T, Wallis, A Katrine, Wells, Stephen A, Rowe, Michelle L, Williamson, Richard A, Howard, Mark J, Freedman, Robert B

“…ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted…”
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A Major Fraction of Endoplasmic Reticulum-located Glutathione Is Present as Mixed Disulfides with Protein by Bass, Rosemary, Ruddock, Lloyd W., Klappa, Peter, Freedman, Robert B.

“…The tripeptide glutathione is the most abundant thiol/disulfide component of the eukaryotic cell and is known to be present in the endoplasmic reticulum lumen…”
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The mechanism of inactivation of glucose oxidase from Penicillium amagasakiense under ambient storage conditions by Caves, Michael S., Derham, Barry K., Jezek, Jan, Freedman, Robert B.

“…Glucose oxidase (GOx) from Penicillium amagasakiense has a higher specific activity than the more commonly studied Aspergillus niger enzyme, and may therefore…”
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Characterization of Folding Cores in the Cyclophilin A-Cyclosporin A Complex by Heal, Jack W., Wells, Stephen A., Blindauer, Claudia A., Freedman, Robert B., Römer, Rudolf A.

“…Determining the folding core of a protein yields information about its folding process and dynamics. The experimental procedures for identifying the amino…”
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Protein disulfide isomerases exploit synergy between catalytic and specific binding domains by Freedman, Robert B., Klappa, Peter, Ruddock, Lloyd W.

“…Protein disulfide isomerases (PDIs) catalyse the formation of native disulfide bonds in protein folding pathways. The key steps involve disulfide formation and…”
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Molecular Characterization of the Principal Substrate Binding Site of the Ubiquitous Folding Catalyst Protein Disulfide Isomerase by Pirneskoski, Annamari, Klappa, Peter, Lobell, Mario, Williamson, Richard A., Byrne, Lee, Alanen, Heli I., Salo, Kirsi E.H., Kivirikko, Kari I., Freedman, Robert B., Ruddock, Lloyd W.

“…Disulfide bond formation in the endoplasmic reticulum of eukaryotes is catalyzed by the ubiquitously expressed enzyme protein disulfide isomerase (PDI). The…”
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Investigation of the impact of Tat export pathway enhancement on E. coli culture, protein production and early stage recovery by Branston, Steven D., Matos, Cristina F.R.O., Freedman, Robert B., Robinson, Colin, Keshavarz-Moore, Eli

“…The twin arginine translocation (Tat) pathway occurs naturally in E. coli and has the distinct ability to translocate folded proteins across the inner membrane…”
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Catalytic Activity and Chaperone Function of Human Protein-disulfide Isomerase Are Required for the Efficient Refolding of Proinsulin by Winter, Jeannette, Klappa, Peter, Freedman, Robert B., Lilie, Hauke, Rudolph, Rainer

“…Protein-disulfide isomerase (PDI) catalyzes the formation, rearrangement, and breakage of disulfide bonds and is capable of binding peptides and unfolded…”
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The ligand‐binding b′ domain of human protein disulphide‐isomerase mediates homodimerization by Wallis, Anne Katrine, Sidhu, Ateesh, Byrne, Lee J., Howard, Mark J., Ruddock, Lloyd W., Williamson, Richard A., Freedman, Robert B.

“…Purified preparations of the recombinant b′x domain fragment of human protein‐disulphide isomerase (PDI), which are homogeneous by mass spectrometry and sodium…”
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Reconstitution of Human Ero1-Lα/Protein-Disulfide Isomerase Oxidative Folding Pathway in Vitro: POSITION-DEPENDENT DIFFERENCES IN ROLE BETWEEN THE a AND a' DOMAINS OF PROTEIN-DISULFIDE ISOMERASE by Wang, Lei, Li, Sheng-jian, Sidhu, Ateesh, Zhu, Li, Liang, Yi, Freedman, Robert B, Wang, Chih-chen

“…Protein-disulfide isomerase (PDI), a critical enzyme responsible for oxidative protein folding in the eukaryotic endoplasmic reticulum, is composed of four…”
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‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI) by Freedman, Robert B., Desmond, Jasmine L., Byrne, Lee J., Heal, Jack W., Howard, Mark J., Sanghera, Narinder, Walker, Kelly L., Wallis, A. Katrine, Wells, Stephen A., Williamson, Richard A., Römer, Rudolf A.

“…Protein disulfide isomerase (PDI) has diverse functions in the endoplasmic reticulum as catalyst of redox transfer, disulfide isomerization and oxidative…”
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Quantitative Analyses of the Yeast Oxidative Protein Folding Pathway In Vitro and In Vivo by Beal, Dave M, Bastow, Emma L, Staniforth, Gemma L, von der Haar, Tobias, Freedman, Robert B, Tuite, Mick F

“…Efficient oxidative protein folding (OPF) in the endoplasmic reticulum (ER) is a key requirement of the eukaryotic secretory pathway. In particular, protein…”
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Enzyme hyperactivity in AOT water-in-oil microemulsions is induced by 'lone' sodium counterions in the water-pool by Oldfield, Christopher, Freedman, Robert B, Robinson, Brian H

“…Water-in-oil microemulsions are thermodynamically stable single-phase dispersions of water and surfactant within a continuous oil phase. The classical ternary…”
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Plasticity of Human Protein Disulfide Isomerase: EVIDENCE FOR MOBILITY AROUND THE X-LINKER REGION AND ITS FUNCTIONAL SIGNIFICANCE by Wang, Chao, Chen, Sihong, Wang, Xi, Wang, Lei, Wallis, A. Katrine, Freedman, Robert B, Wang, Chih-chen

“…Protein disulfide isomerase (PDI), which consists of multiple domains arranged as abb'xa'c, is a key enzyme responsible for oxidative folding in the…”
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Thermal Inactivation of Uricase (Urate Oxidase): Mechanism and Effects of Additives by Caves, Michael S, Derham, Barry K, Jezek, Jan, Freedman, Robert B

“…Uricase (Urc) is an oxidoreductase enzyme of both general and commercial interest, the former because of its lack of a cofactor and the latter because of its…”
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