List of works - Neil J. Bulleid

A cautionary note when using pepsin as a probe for the formation of a collagen triple helix

scientific article

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

scientific article

Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER.

scientific article published on 16 January 2017

Disulfide bond formation in the mammalian endoplasmic reticulum

scientific article

Disulfide formation in the ER and mitochondria: two solutions to a common process.

scientific article published on June 2009

Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides

scientific article

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

scientific article

ERp18 regulates activation of ATF6α during unfolded protein response

scientific article published on 17 June 2019

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

scientific article

Effects of metyrapone and norharmane on microsomal mono-oxygenase and epoxide hydrolase activities

scientific article published on 01 May 1984

Expression of an engineered form of recombinant procollagen in mouse milk

scientific article published on 01 April 1999

Folding and assembly of type X collagen mutants that cause metaphyseal chondrodysplasia-type schmid. Evidence for co-assembly of the mutant and wild-type chains and binding to molecular chaperones.

scientific article

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

scientific article

Folding of human intestinal lactase-phlorizin hydrolase

scientific article published on 01 August 1995

Forming disulfides in the endoplasmic reticulum.

scientific article published on 20 February 2013

Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells

scientific article published on 26 October 2004

Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway

scientific article published on 14 July 2004

Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen

scientific article published on March 1997

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

scientific article published on July 2014

Induction of microsomal epoxide hydrolase by nitrosamines in rat liver. Effect on messenger ribonucleic acids

scientific article published on January 1988

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

scientific article published on 9 October 2017

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

scientific article

Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion

scientific article published on 01 March 1995

Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase

scientific article published on 01 May 1999

Is protein disulfide isomerase a redox-dependent molecular chaperone?

scientific article

Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation.

scientific article published on 08 January 2014

Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.

scientific article published on 30 October 2008

Methionine Sulfoxide Reductase B3 Requires Resolving Cysteine Residues for full Activity and can act as a Stereospecific Methionine Oxidase.

scientific article

Multiple ways to make disulfides

scientific article published on 19 July 2011

Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells.

scientific article published on April 2008

Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain.

scientific article

Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen

scientific journal article

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

scientific article

Protein folding and modification in the mammalian endoplasmic reticulum.

scientific article published on January 2011

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

scientific article published on 17 January 2020

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

scientific article published on September 2013

Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system.

scientific article published on June 2007

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

scientific article

Redox regulation in the endoplasmic reticulum.

scientific article

Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IV.

scientific article published on February 2014

Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47.

scientific article

Solving the mystery of procollagen chain selectivity

scientific article published on 01 October 2012

Species specific membrane anchoring of nyctalopin, a small leucine-rich repeat protein

scientific article published on 19 May 2005

Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin.

scientific article

The endoplasmic reticulum (ER) translocon can differentiate between hydrophobic sequences allowing signals for glycosylphosphatidylinositol anchor addition to be fully translocated into the ER lumen

scientific article published on 06 October 2003

The mammalian cytosolic thioredoxin reductase pathway acts via a membrane protein to reduce ER-localised proteins

scientific article published on 17 March 2020

The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α.

scientific article

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

scientific article

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

scientific article

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

scientific article

List of works by Neil J. Bulleid

A cautionary note when using pepsin as a probe for the formation of a collagen triple helix

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

Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER.

Disulfide bond formation in the mammalian endoplasmic reticulum

Disulfide formation in the ER and mitochondria: two solutions to a common process.

Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

ERp18 regulates activation of ATF6α during unfolded protein response

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

Effects of metyrapone and norharmane on microsomal mono-oxygenase and epoxide hydrolase activities

Expression of an engineered form of recombinant procollagen in mouse milk

Folding and assembly of type X collagen mutants that cause metaphyseal chondrodysplasia-type schmid. Evidence for co-assembly of the mutant and wild-type chains and binding to molecular chaperones.

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

Folding of human intestinal lactase-phlorizin hydrolase

Forming disulfides in the endoplasmic reticulum.

Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells

Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway

Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen

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

Induction of microsomal epoxide hydrolase by nitrosamines in rat liver. Effect on messenger ribonucleic acids

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

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

Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion

Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase

Is protein disulfide isomerase a redox-dependent molecular chaperone?

Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation.

Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.

Methionine Sulfoxide Reductase B3 Requires Resolving Cysteine Residues for full Activity and can act as a Stereospecific Methionine Oxidase.

Multiple ways to make disulfides

Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells.

Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain.

Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen

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

Protein folding and modification in the mammalian endoplasmic reticulum.

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

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

Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system.

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

Redox regulation in the endoplasmic reticulum.

Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IV.

Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47.

Solving the mystery of procollagen chain selectivity

Species specific membrane anchoring of nyctalopin, a small leucine-rich repeat protein

Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin.

The endoplasmic reticulum (ER) translocon can differentiate between hydrophobic sequences allowing signals for glycosylphosphatidylinositol anchor addition to be fully translocated into the ER lumen

The mammalian cytosolic thioredoxin reductase pathway acts via a membrane protein to reduce ER-localised proteins

The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α.

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

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

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.