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Lloyd W Ruddock

Showing results (1-10 of 77) with videos related to

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Structure (London, England : 1993)|August 15, 2006
Gaining access to ERp57 functionLloyd W Ruddock
Antioxidants & Redox Signaling|December 31, 2011
Low-molecular-weight oxidants involved in disulfide bond formationLloyd W Ruddock
Antioxidants & Redox Signaling|May 30, 2009
Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formationFeras Hatahet, Lloyd W Ruddock
Current Pharmaceutical Design|July 16, 2009
Modulating proteostasis: peptidomimetic inhibitors and activators of protein foldingFeras Hatahet, Lloyd W Ruddock
The FEBS Journal|September 26, 2007
Substrate recognition by the protein disulfide isomerasesFeras Hatahet, Lloyd W Ruddock
EMBO Reports|January 12, 2005
The human protein disulphide isomerase family: substrate interactions and functional propertiesLars Ellgaard, Lloyd W Ruddock
Journal of Cell Science|November 1, 2006
N-glycan processing in ER quality controlLloyd W Ruddock, Maurizio Molinari
Journal of Molecular Biology|July 2, 2013
Topological plasticity of enzymes involved in disulfide bond formation allows catalysis in either the periplasm or the cytoplasmFeras Hatahet, Lloyd W Ruddock
The Journal of Biological Chemistry|February 28, 2020
Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)-protein disulfide-isomerase relay when protein folding capacity is exceededAntti Moilanen, Lloyd W Ruddock
Plos One|December 19, 2017
Complementarity determining regions and frameworks contribute to the disulfide bond independent folding of intrinsically stable scFvAnna Gąciarz, Lloyd W Ruddock
Pageof 8

Showing results (1-10 of 77) with videos related to

Sort By:
Pageof 8
Structure (London, England : 1993)|August 15, 2006
Gaining access to ERp57 functionLloyd W Ruddock
Antioxidants & Redox Signaling|December 31, 2011
Low-molecular-weight oxidants involved in disulfide bond formationLloyd W Ruddock
Antioxidants & Redox Signaling|May 30, 2009
Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formationFeras Hatahet, Lloyd W Ruddock
Current Pharmaceutical Design|July 16, 2009
Modulating proteostasis: peptidomimetic inhibitors and activators of protein foldingFeras Hatahet, Lloyd W Ruddock
The FEBS Journal|September 26, 2007
Substrate recognition by the protein disulfide isomerasesFeras Hatahet, Lloyd W Ruddock
EMBO Reports|January 12, 2005
The human protein disulphide isomerase family: substrate interactions and functional propertiesLars Ellgaard, Lloyd W Ruddock
Journal of Cell Science|November 1, 2006
N-glycan processing in ER quality controlLloyd W Ruddock, Maurizio Molinari
Journal of Molecular Biology|July 2, 2013
Topological plasticity of enzymes involved in disulfide bond formation allows catalysis in either the periplasm or the cytoplasmFeras Hatahet, Lloyd W Ruddock
The Journal of Biological Chemistry|February 28, 2020
Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)-protein disulfide-isomerase relay when protein folding capacity is exceededAntti Moilanen, Lloyd W Ruddock
Plos One|December 19, 2017
Complementarity determining regions and frameworks contribute to the disulfide bond independent folding of intrinsically stable scFvAnna Gąciarz, Lloyd W Ruddock
Pageof 8