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

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

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)

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

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

Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins

Por Jessop, Catherine E., Watkins, Rachel H., Simmons, Jennifer J., Tasab, Mohammed, Bulleid, Neil J.
Publicado em 2009

Crystal Structure of Reduced and of Oxidized Peroxiredoxin IV Enzyme Reveals a Stable Oxidized Decamer and a Non-disulfide-bonded Intermediate in the Catalytic Cycle

Por Cao, Zhenbo, Tavender, Timothy J., Roszak, Aleksander W., Cogdell, Richard J., Bulleid, Neil J.
Publicado em 2011

ERp57 is essential for efficient folding of glycoproteins sharing common structural domains

Por Jessop, Catherine E, Chakravarthi, Seema, Garbi, Natalio, Hämmerling, Günter J, Lovell, Simon, Bulleid, Neil J
Publicado em 2007

Substrate Specificity of the Oxidoreductase ERp57 Is Determined Primarily by Its Interaction with Calnexin and Calreticulin

Por Jessop, Catherine E., Tavender, Timothy J., Watkins, Rachel H., Chambers, Joseph E., Bulleid, Neil J.
Publicado em 2009

Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation

Por Baker, Karl M, Chakravarthi, Seema, Langton, Kevin P, Sheppard, Alyson M, Lu, Hui, Bulleid, Neil J
Publicado em 2008