Disulfide Bond Formation in the Mammalian Endoplasmic Reticulum

od Bulleid, Neil J.
Izdano 2012

Detecting peroxiredoxin hyperoxidation by one-dimensional isoelectric focusing

od Cao, Zhenbo, Bulleid, Neil J.
Izdano u Biophys Rep (2015)

Is protein disulfide isomerase a redox-dependent molecular chaperone?

od Lumb, Richard A., Bulleid, Neil J.
Izdano 2002

Peroxiredoxin IV protects cells from oxidative stress by removing H(2)O(2) produced during disulphide formation

od Tavender, Timothy J., Bulleid, Neil J.
Izdano 2010

Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway

od Robinson, Philip J., Bulleid, Neil J.
Izdano u Cells (2020)

Lack of an Efficient Endoplasmic Reticulum-localized Recycling System Protects Peroxiredoxin IV from Hyperoxidation

od Cao, Zhenbo, Subramaniam, Suraj, Bulleid, Neil J.
Izdano 2014

How Are Proteins Reduced in the Endoplasmic Reticulum?

od Ellgaard, Lars, Sevier, Carolyn S., Bulleid, Neil J.
Izdano u Trends Biochem Sci (2018)

Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen

od Tasab, Mohammed, Batten, Margaret R., Bulleid, Neil J.
Izdano 2000

The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress

od Chakravarthi, Seema, Jessop, Catherine E, Bulleid, Neil J
Izdano 2006

Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst

od Rudolf, Jana, Pringle, Marie A., Bulleid, Neil J.
Izdano 2013

Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum

od Tavender, Timothy J, Springate, Jennifer J, Bulleid, Neil J
Izdano 2010

Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases

od Shepherd, Colin, Oka, Ojore B. V., Bulleid, Neil J.
Izdano u Biochem J (2014)

Peroxiredoxin IV is an endoplasmic reticulum localised enzyme forming oligomeric complexes in human cells

od Tavender, Timothy J., Sheppard, Alyson M., Bulleid, Neil J.
Izdano u Biochem J (2008)

Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme

od Oka, Ojore B.V., Yeoh, Hui Y., Bulleid, Neil J.
Izdano u Biochem J (2015)

Protein secondary structure determines the temporal relationship between folding and disulfide formation

od Robinson, Philip J., Kanemura, Shingo, Cao, Xiaofei, Bulleid, Neil J.
Izdano u J Biol Chem (2020)

Divalent cations regulate the folding and activation status of integrins during their intracellular trafficking

od Tiwari, Shweta, Askari, Janet A., Humphries, Martin J., Bulleid, Neil J.
Izdano 2011

Real-time monitoring of redox changes in the mammalian endoplasmic reticulum

od van Lith, Marcel, Tiwari, Shweta, Pediani, John, Milligan, Graeme, Bulleid, Neil J.
Izdano 2011

Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation

od Robinson, Philip J., Pringle, Marie Anne, Woolhead, Cheryl A., Bulleid, Neil J.
Izdano u J Biol Chem (2017)

Inhibition of IRE1α-mediated XBP1 mRNA cleavage by XBP1 reveals a novel regulatory process during the unfolded protein response

od Chalmers, Fiona, van Lith, Marcel, Sweeney, Bernadette, Cain, Katharine, Bulleid, Neil J.
Izdano u Wellcome Open Res (2017)

Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1

od Chakravarthi, Seema, Jessop, Catherine E., Willer, Martin, Stirling, Colin J., Bulleid, Neil J.
Izdano 2007