2017

Freedman, R. 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. and Roemer, Rudolf A. (2017) ‘Something in the way she moves’ : the functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI). Biochimica et Biophysica Acta - Proteins and Proteomics . doi:10.1016/j.bbapap.2017.08.014 (In Press)

Freedman, R. B., Desmond, Jasmine L., Heal, Jack W., Sanghera, Narinder, Walker, Kelly L., Wallis, A. Katrine, Wells, Stephen A. and Roemer, Rudolf A. (2017) Data for 'Something in the way she moves': the functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI). [Dataset]

2016

Roemer, Rudolf A., Wells, Stephen A., Jiménez Roldán, J. E. (José Emilio), Bhattacharyya, Moitrayee, Vishweshwara, Saraswathi and Freedman, R. B. (2016) The flexibility and dynamics of protein disulphide-isomerase. Proteins : Structure, Function, and Bioinformatics, 84 (12). pp. 1776-1785. doi:10.1002/prot.25159

2015

Heal, Jack W., Wells, Stephen A., Blindauer, Claudia A., Freedman, R. B. and Roemer, Rudolf A. (2015) Characterization of folding cores in the cyclophilin A-cyclosporin A complex. Biophysical Journal, Volume 108 (Number 7). pp. 1739-1746. doi:10.1016/j.bpj.2015.02.017

Alanen, Heli I., Walker, Kelly L., Lourdes Velez Suberbie, M., Matos, Cristina F.R.O., Bönisch, Sarah, Freedman, Robert B., Keshavarz-Moore, Eli, Ruddock, Lloyd W. and Robinson, Colin (2015) Efficient export of human growth hormone, interferon α2b and antibody fragments to the periplasm by the Escherichia coli Tat pathway in the absence of prior disulfide bond formation. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Volume 1853 (Number 3). pp. 756-763. doi:10.1016/j.bbamcr.2014.12.027

2014

Heal, Jack W., Wells, Stephen A., Freedman, R. B. and Roemer, Rudolf A. (2014) Characterising the folding core of the cyclophilin A — cyclosporin A complex II : improving folding core predictions by including mobility. Biophysical Journal . (Submitted)

Heal, Jack W., Roemer, Rudolf A., Blindauer, Claudia A. and Freedman, R. B. (2014) Characterising the folding core of the cyclophilin A — cyclosporin A complex I : hydrogen exchange data and rigidity analysis. Biophysical Journal . (Submitted)

Matos, Cristina F. R. O., Robinson, Colin, Alanen, Heli I., Prus, Piotr, Uchida, Yuko, Ruddock, Lloyd W., Freedman, Robert B. and Keshavarz-Moore, Eli (2014) Efficient export of prefolded, disulfide-bonded recombinant proteins to the periplasm by the Tat pathway in Escherichia coli CyDisCo strains. Biotechnology Progress , Volume 30 (Number 2). pp. 281-290. doi:10.1002/btpr.1858

Irvine, Alistair, Wallis, A. Katrine, Sanghera, Narinder, Rowe, Michelle L., Ruddock, Lloyd W., Howard, Mark J., Williamson, Richard A., Blindauer, Claudia A. and Freedman, R. B. (2014) Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway. PLoS One, Volume 9 (Number 1). Article number e82511. doi:10.1371/journal.pone.0082511

2013

Albiniak, A. M., Matos, Cristina F. R. O., Branston, Steven D., Freedman, R. B., Keshavarz-Moore, Eli and Robinson, Colin (2013) High-level secretion of a recombinant protein to the culture medium with a Bacillus subtilistwin-arginine translocation system in Escherichia coli. FEBS Journal, Volume 280 (Issue 16). pp. 3810-3821. doi:10.1111/febs.12376

Amin, Nader T., Wallis, A. Katrine, Wells, Stephen A., Rowe, Michelle L., Williamson, Richard A., Howard, Mark J. and Freedman, R. B. (2013) High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility. Biochemical Journal, Volume 450 (Number 2). pp. 321-332. doi:10.1042/BJ20121635

Caves, Michael S., Derham, Barry K., Jezek, Jan and Freedman, R. B. (2013) Thermal inactivation of uricase (urate oxidase) : mechanism and effects of additives. Biochemistry, Volume 52 (Number 3). pp. 497-507. doi:10.1021/bi301334w

Wallis, A. Katrine and Freedman, R. B. (2013) Assisting oxidative protein folding : how do protein disulphide-isomerases couple conformational and chemical processes in protein folding? In: Topics in Current Chemistry. Springer, pp. 1-34. ISBN 978-3-642-34551-7

2012

Matos, Cristina F. R. O., Branston, Steven D., Albiniak, A. M., Dhanoya, Arjun, Freedman, R. B., Keshavarz-Moore, Eli and Robinson, Colin (2012) High-yield export of a native heterologous protein to the periplasm by the tat translocation pathway in Escherichia coli. Biotechnology and Bioengineering, Vol.109 (No.10). pp. 2533-2542. doi:10.1002/bit.24535

Jiménez Roldán, J. E. (José Emilio), Freedman, R. B., Roemer, Rudolf A. and Wells, Stephen A. (2012) Rapid simulation of protein motion : merging flexibility, rigidity and normal mode analyses. Physical Biology, Vol.9 (No.1). 016008. doi:10.1088/1478-3975/9/1/016008

Heal, Jack W., Jiménez Roldán, J. E. (José Emilio), Wells, Stephen A., Freedman, R. B. and Roemer, Rudolf A. (2012) Inhibition of HIV-1 protease: the rigidity perspective. Bioinformatics, Vol.28 (No.3). pp. 350-357. doi:10.1093/bioinformatics/btr683

2011

Caves, Michael S., Derham, Barry K., Jezek, Jan and Freedman, R. B. (2011) Corrigendum to “The mechanism of inactivation of glucose oxidase from Penicillium amagasakiense under ambient storage conditions” [Enzyme Microb. Technol. 49 (2011) 79–87]. Enzyme and Microbial Technology, Vol.49 (No.4). p. 427. doi:10.1016/j.enzmictec.2011.07.001

Jiménez Roldán, J. E. (José Emilio), Wells, Stephen A., Freedman, R. B. and Roemer, Rudolf A. (2011) Integration of FIRST, FRODA and NMM in a coarse grained method to study Protein Disulphide Isomerase conformational change. Journal of Physics: Conference Series, Vol.286 (No.1). Article No. 012002. doi:10.1088/1742-6596/286/1/012002

Branston, Steven D., Matos, Cristina F. R. O., Freedman, R. B., Robinson, Colin and Keshavarz-Moore, Eli (2011) Investigation of the impact of Tat export pathway enhancement on E. coli culture, protein production and early stage recovery. Biotechnology and Bioengineering, Vol.109 (No.4). pp. 983-991. doi:10.1002/bit.24384

Heal, Jack W., Wells, Stephen A., Jiménez Roldán, J. E. (José Emilio), Freedman, R. B. and Roemer, Rudolf A. (2011) Rigidity analysis of HIV-1 protease. Journal of Physics: Conference Series, Vol.286 (No.1). article no. 012006. doi:10.1088/1742-6596/286/1/012006

Caves, Michael S., Derham, Barry K., Jezek, Jan and Freedman, R. B. (2011) The mechanism of inactivation of glucose oxidase from Penicillium amagasakiense under ambient storage conditions. Enzyme and Microbial Technology, Vol.49 (No.1). pp. 79-87. doi:10.1016/j.enzmictec.2011.03.004

2010

Wang, Chao, Chen, Sihong, Wang, Xi, Wang, Lei, Wallis, A. Katrine, Freedman, R. B. and Wang, Chih-chen (2010) Plasticity of human protein disulfide isomerase : evidence for mobility around the x-linker region and its functional significance. Journal of Biological Chemistry, Vol.285 (No.35). pp. 26788-26797. doi:10.1074/jbc.M110.107839

2009

Wallis, A. Katrine, Sidhu, Ateesh, Byrne, Lee J., Howard, Mark J., Ruddock, Lloyd W., Williamson, Richard A. and Freedman, R. B. (2009) The ligand-binding b' domain of human protein disulphide-isomerase mediates homodimerization. Protein Science, Vol.18 (No.12). pp. 2569-2577. doi:10.1002/pro.270

Byrne, Lee J., Sidhu, Ateesh, Wallis, A. Katrine, Ruddock, Lloyd W., Freedman, R. B., Howard, Mark J. and Williamson, Richard A. (2009) Mapping of the ligand-binding site on the b ' domain of human PDI: interaction with peptide ligands and the x-linker region. Biochemical Journal, Vol.423 (No.2). pp. 209-217. doi:10.1042/BJ20090565

Wang, Lei, Li, Sheng-jian, Sidhu, Ateesh, Zhu, Li, Liang, Yi, Freedman, R. B. and Wang, Chih-chen (2009) Reconstitution of human Ero1-L alpha/protein-disulfide isomerase oxidative folding pathway in vitro: position-dependent differences in role between the a and a' domains of protein-disulfide isomerase. Journal of Biological Chemistry, Vol.284 (No.1). pp. 199-206. doi:10.1074/jbc.M806645200

Freedman, R. B. (2009) Eukaryotic Protein Disulfide-isomerases and their Potential in the Production of Disulfide-bonded Protein Products: What We Need to Know but Do Not! In: Oxidative Folding of Peptides and Proteins. RSC Biomolecular Sciences (Chapter 1.7). Cambridge, UK: Royal Society of Chemistry, pp. 121-157. ISBN 978-1-84755-926-5

Freedman, R. B. (2009) A non-catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway. EMBO Journal, Vol.28 . pp. 169-170. doi:10.1038/emboj.2008.293

2008

Dat Nguyen, Van, Wallis, A. Katrine, Howard, Mark J., Haapalainen, Antti M., Salo, Kirsi E. H., Saaranen, Mirva J. , Sidhu, Ateesh, Wierenga, Rik K., Freedman, R. B., Ruddock, Lloyd W. and Williamson, Richard A. (2008) Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b’ domain. Journal of Molecular Biology, Vol.383 (No.5). pp. 1144-1155. doi:10.1016/j.jmb.2008.08.085