Disulfide Bond Formation in the Mammalian Endoplasmic Reticulum

Por Bulleid, Neil J.
Publicado em 2012

Detecting peroxiredoxin hyperoxidation by one-dimensional isoelectric focusing

Por Cao, Zhenbo, Bulleid, Neil J.
Publicado no Biophys Rep (2015)

Is protein disulfide isomerase a redox-dependent molecular chaperone?

Por Lumb, Richard A., Bulleid, Neil J.
Publicado em 2002

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

Por Tavender, Timothy J., Bulleid, Neil J.
Publicado em 2010

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

Por Robinson, Philip J., Bulleid, Neil J.
Publicado no Cells (2020)

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

Por Cao, Zhenbo, Subramaniam, Suraj, Bulleid, Neil J.
Publicado em 2014

How Are Proteins Reduced in the Endoplasmic Reticulum?

Por Ellgaard, Lars, Sevier, Carolyn S., Bulleid, Neil J.
Publicado no Trends Biochem Sci (2018)

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

Por Tasab, Mohammed, Batten, Margaret R., Bulleid, Neil J.
Publicado em 2000

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

Por Chakravarthi, Seema, Jessop, Catherine E, Bulleid, Neil J
Publicado em 2006

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

Por Rudolf, Jana, Pringle, Marie A., Bulleid, Neil J.
Publicado em 2013

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

Por Tavender, Timothy J, Springate, Jennifer J, Bulleid, Neil J
Publicado em 2010

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

Por Shepherd, Colin, Oka, Ojore B. V., Bulleid, Neil J.
Publicado no Biochem J (2014)

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

Por Tavender, Timothy J., Sheppard, Alyson M., Bulleid, Neil J.
Publicado no Biochem J (2008)

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

Por Oka, Ojore B.V., Yeoh, Hui Y., Bulleid, Neil J.
Publicado no Biochem J (2015)

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

Por Robinson, Philip J., Kanemura, Shingo, Cao, Xiaofei, Bulleid, Neil J.
Publicado no J Biol Chem (2020)

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

Por Tiwari, Shweta, Askari, Janet A., Humphries, Martin J., Bulleid, Neil J.
Publicado em 2011

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

Por van Lith, Marcel, Tiwari, Shweta, Pediani, John, Milligan, Graeme, Bulleid, Neil J.
Publicado em 2011

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

Por Robinson, Philip J., Pringle, Marie Anne, Woolhead, Cheryl A., Bulleid, Neil J.
Publicado no J Biol Chem (2017)

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

Por Chalmers, Fiona, van Lith, Marcel, Sweeney, Bernadette, Cain, Katharine, Bulleid, Neil J.
Publicado no Wellcome Open Res (2017)

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

Por Chakravarthi, Seema, Jessop, Catherine E., Willer, Martin, Stirling, Colin J., Bulleid, Neil J.
Publicado em 2007