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The Biochemical Journal|May 30, 2013
Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalystJana Rudolf, Marie A Pringle, Neil J BulleidThe FEBS Journal|December 20, 2011
Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradationFranziska Kriegenburg, Lars Ellgaard, Rasmus Hartmann-PetersenThe EMBO Journal|November 9, 2010
Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulumTimothy J Tavender, Jennifer J Springate, Neil J BulleidThe Biochemical Journal|April 25, 2014
Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerasesColin Shepherd, Ojore B V Oka, Neil J BulleidThe Journal of Biological Chemistry|November 28, 2007
Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assemblyJoseph E Chambers, Catherine E Jessop, Neil J BulleidThe Biochemical Journal|December 7, 2007
Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cellsTimothy J Tavender, Alyson M Sheppard, Neil J BulleidTraffic (Copenhagen, Denmark)|March 8, 2016
Co- and Post-Translational Protein Folding in the ERLars Ellgaard, Nicholas McCaul, Anna Chatsisvili, et al.The Biochemical Journal|May 20, 2015
Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzymeOjore B V Oka, Hui Y Yeoh, Neil J BulleidThe Journal of Biological Chemistry|January 19, 2020
Protein secondary structure determines the temporal relationship between folding and disulfide formationPhilip J Robinson, Shingo Kanemura, Xiaofei Cao, et al.Biochemistry|January 5, 2018
Disrupted Hydrogen-Bond Network and Impaired ATPase Activity in an Hsc70 Cysteine MutantJohn P O'Donnell, Heather M Marsh, Holger Sondermann, et al.Pageof 13