A non-catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway

por Freedman, Robert B
Publicado 2009

Characterization of Folding Cores in the Cyclophilin A-Cyclosporin A Complex

por Heal, Jack W., Wells, Stephen A., Blindauer, Claudia A., Freedman, Robert B., Römer, Rudolf A.
Publicado 2015

Plasticity of Human Protein Disulfide Isomerase: EVIDENCE FOR MOBILITY AROUND THE X-LINKER REGION AND ITS FUNCTIONAL SIGNIFICANCE

por Wang, Chao, Chen, Sihong, Wang, Xi, Wang, Lei, Wallis, A. Katrine, Freedman, Robert B., Wang, Chih-chen
Publicado 2010

The flexibility and dynamics of protein disulfide isomerase

por Römer, Rudolf A., Wells, Stephen A., Emilio Jimenez‐Roldan, J., Bhattacharyya, Moitrayee, Vishweshwara, Saraswathi, Freedman, Robert B.
Publicado 2016

Quantitative Analyses of the Yeast Oxidative Protein Folding Pathway In Vitro and In Vivo

por Beal, Dave M., Bastow, Emma L., Staniforth, Gemma L., von der Haar, Tobias, Freedman, Robert B., Tuite, Mick F.
Publicado 2019

High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility

por Amin, Nader T., Wallis, A. Katrine, Wells, Stephen A., Rowe, Michelle L., Williamson, Richard A., Howard, Mark J., Freedman, Robert B.
Publicado 2013

Protein Disulfide-Isomerase Interacts with a Substrate Protein at All Stages along Its Folding Pathway

por 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.
Publicado 2014

‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI)

por 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.
Publicado 2017