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Neil J Bulleid

Showing results (21-30 of 54) with videos related to

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Trends in Biochemical Sciences|November 21, 2017
How Are Proteins Reduced in the Endoplasmic Reticulum?Lars Ellgaard, Carolyn S Sevier, Neil J Bulleid
Biochemical Society Transactions|January 24, 2014
Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IVRachel E Martin, Zhenbo Cao, Neil J Bulleid
The Biochemical Journal|October 24, 2009
Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamerLindsay J Gleghorn, Dorothy Trump, Neil J Bulleid
The Biochemical Journal|May 30, 2013
Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalystJana Rudolf, Marie A Pringle, Neil J Bulleid
The 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 Bulleid
The Biochemical Journal|April 25, 2014
Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerasesColin Shepherd, Ojore B V Oka, Neil J Bulleid
The 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 Bulleid
The 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 Bulleid
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 Bulleid
The 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.
Pageof 6

Showing results (21-30 of 54) with videos related to

Sort By:
Pageof 6
Trends in Biochemical Sciences|November 21, 2017
How Are Proteins Reduced in the Endoplasmic Reticulum?Lars Ellgaard, Carolyn S Sevier, Neil J Bulleid
Biochemical Society Transactions|January 24, 2014
Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IVRachel E Martin, Zhenbo Cao, Neil J Bulleid
The Biochemical Journal|October 24, 2009
Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamerLindsay J Gleghorn, Dorothy Trump, Neil J Bulleid
The Biochemical Journal|May 30, 2013
Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalystJana Rudolf, Marie A Pringle, Neil J Bulleid
The 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 Bulleid
The Biochemical Journal|April 25, 2014
Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerasesColin Shepherd, Ojore B V Oka, Neil J Bulleid
The 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 Bulleid
The 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 Bulleid
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 Bulleid
The 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.
Pageof 6