The Library
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Number of items: 30.
Journal Article
Beal, Dave M., Bastow, Emma L., Staniforth, Gemma L., von der Haar, Tobias, Freedman, Robert B. and Tuite, Mick F. (2019) Quantitative analyses of the yeast oxidative protein folding pathway in vitro and in vivo. Antioxidants & Redox Signaling . doi:10.1089/ars.2018.7615 ISSN 1523-0864.
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 Römer, 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, 1865 (11 Part A). pp. 1383-1394. doi:10.1016/j.bbapap.2017.08.014 ISSN 1570-9639.
Römer, 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 ISSN 0887-3585.
Heal, Jack W., Wells, Stephen A., Blindauer, Claudia A., Freedman, R. B. and Römer, 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 ISSN 0006-3495.
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 ISSN 0167-4889.
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 ISSN 8756-7938.
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 ISSN 1932-6203.
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 ISSN 1742-464x.
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 ISSN 0264-6021.
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 ISSN 0006-2960.
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 ISSN 0006-3592.
Jiménez Roldán, J. E. (José Emilio), Freedman, R. B., Römer, 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 ISSN 1478-3967.
Heal, Jack W., Jiménez Roldán, J. E. (José Emilio), Wells, Stephen A., Freedman, R. B. and Römer, Rudolf A. (2012) Inhibition of HIV-1 protease: the rigidity perspective. Bioinformatics, Vol.28 (No.3). pp. 350-357. doi:10.1093/bioinformatics/btr683 ISSN 1367-4803.
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 ISSN 0141-0229.
Jiménez Roldán, J. E. (José Emilio), Wells, Stephen A., Freedman, R. B. and Römer, 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 ISSN 1742-6596.
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 ISSN 0006-3592.
Heal, Jack W., Wells, Stephen A., Jiménez Roldán, J. E. (José Emilio), Freedman, R. B. and Römer, 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 ISSN 1742-6596.
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 ISSN 0141-0229.
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 ISSN 0021-9258.
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 ISSN 1194-1202.
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 ISSN 0264-6021.
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 ISSN 0021-9258.
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 ISSN 0261-4189.
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 ISSN 0022-2836.
Long, V., Marland, Hilary and Freedman, R. B. Women at the dawn of British biochemistry: female contributors to the Biochemical Journal from 1906 to 1939. Biochemist, Vol.31 (No.4). pp. 50-52. ISSN 0954-982X.
Book Item
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
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
Submitted Journal Article
Heal, Jack W., Wells, Stephen A., Freedman, R. B. and Römer, 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., Römer, 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)
Dataset
Freedman, R. B., Desmond, Jasmine L., Heal, Jack W., Sanghera, Narinder, Walker, Kelly L., Wallis, A. Katrine, Wells, Stephen A. and Römer, 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]
This list was generated on Thu Mar 28 15:17:10 2024 GMT.