Professor Neil Bulleid

  • Professor in Cell Biology, Director of Research Institute (Institute of Molecular Cell & Systems Biology)

Biography

Neil obtained his first degree (BSc) in Liverpool and second degree (PhD) in Glasgow in Biochemistry. He currently holds a Chair in Cell Biology at the University of Glasgow and is the Director of the Institute of Molecular, Cell and Systems Biology. He holds a Senior Investigator Award from The Wellcome Trust with additional research grant funding from the BBSRC, MRC and the Royal Society.  He is the recipient of a Wolfson Merit Award.   He was a Royal Society Research Fellow for ten years (1990-2000) and was awarded a Chair in Biochemistry while still on this Fellowship at the University of Manchester moving to the University of Glasgow in 2009 to take up his current post.  He is on the Editorial Board of the BMC Biochemistry Journal, Antioxidants and Redox Signalling and Associate Editor for the Biochemical Journal.  He has served on the executive committee of the Biochemical Society, and on the Molecules, Genes and Cells funding panel of the Wellcome Trust, the Cell Biology panel for the Finnish Academy of Sciences and has chaired grant awarding panel of the Carnegie Trust. His past achievements include the first indication that specific enzymes and chaperones are involved in folding proteins into their three dimensional structure. His research spans many areas of molecular cell biology including disulfide formation, collagen biosynthesis, MHC Class I assembly, protein folding in the cell, lipid attachment to proteins, oxidative stress and protein degradation. He is frequently asked to present his research findings at international meetings and to contribute to graduate and undergraduate training both in the UK and abroad.  


Research interests

The ability of cells to correctly fold and assemble proteins is the final stage in protein synthesis. Protein folding requires a subset of proteins able to either catalyse folding reactions or act as molecular chaperones preventing non-productive protein aggregation. The inability of cells to carry out the folding process results in some of the most catastrophic mammalian diseases such as cystic fibrosis, Alzheimer's and CJD.

For cells and tissues to remain healthy they must be able to make proteins and the proteins they make must be able to function correctly. The cell has complex machinery for ensuring that when new proteins are made they are functional and are transported to the correct location, be it within the cell or outside. My group studies how proteins are made and delivered outside the cell and, in particular, how this delivery process breaks down during disease. The production and delivery of proteins can be summarised into two key stages: i) ensuring proteins are made correctly and adopt the correct shape, ii) transport of the proteins from the inside to the outside of the cell.
Proteins are made as a string of amino acids which coil-up or fold to adopt a characteristic shape or three-dimensional structure. Only one such shape is functional and the cell ensures that this shape is adopted by providing helper proteins or chaperones to aid this process. If cells are unable to correctly fold proteins then disease results. Our group wants to understand in detail the reasons behind the inability of cells to fold proteins and in order to do this we need to know how proteins are folded correctly and what causes them to fold incorrectly. To understand how cells fold and assemble proteins we are studying this process in mammalian cells using a combination of cell biological and biochemical techniques.

 


Grants

Grants and Awards listed are those received whilst working with the University of Glasgow.

  • How does PAP, a stress-induced metabolite, regulate gene expression?
    Biotechnology and Biological Sciences Research Council
    2019 - 2022
     
  • Potential neuroprotective effect of delta opioid receptor (DOR) via crosstalk between UPR, inflammatory response, and miRNA regulation in Parkinson's disease model
    British Council (UK)
    2019 - 2019
     
  • How does the cytosol reduce non-native disulfides formed in the endoplasmic reticulum?
    Biotechnology and Biological Sciences Research Council
    2017 - 2020
     
  • Thiol Modification and Redox Signalling
    Medical Research Council
    2016 - 2018
     
  • Protein Folding and Thiol Modification in the Mammalian Endoplasmic Reticulum
    Wellcome Trust
    2015 - 2020
     
  • Protein disulfide formation and thiol modification in the mammalian endoplasmic
    The Royal Society
    2015 - 2019
     
  • Resolution of the Structure and Function of Vitamin K Epoxide Reductase Isoforms
    The Royal Society
    2014 - 2017
     
  • Structure / Function studies of Vitamin K epoxide reductase isoforms
    Biotechnology and Biological Sciences Research Council
    2014 - 2014
     
  • Identifying the reductive pathway in the mammalian endoplasmic reticulum.
    Biotechnology and Biological Sciences Research Council
    2014 - 2017
     
  • Shedding light on oxidative stress: Identifying factors modulating the redox balance in the endoplasmic reticulum of Caenorhabditis elegans.
    Biotechnology and Biological Sciences Research Council
    2013 - 2016
     
  • Identifying factors modulating the redox balance in the endoplasmic reticulum using the model system Carnorhabditis elegans (ISSF Catalyst Fund)
    Wellcome Trust
    2011 - 2014
     
  • Transfer of protein Folding, Assembly & Secretion Expertise to Renovo.
    Innovate UK
    2011 - 2011
     
  • Disulphide formation in Plasmodium falciparum.
    The Royal Society
    2010 - 2012
     
  • High throughput screen for inhibitors of plasmiodium falciparum Ero1
    Scottish Universities Life Sciences Alliance
    2010 - 2013
     
  • Regulating the redox conditions within the mammalian endoplasmic reticulum
    Wellcome Trust
    2009 - 2015
     
  • SULSA Chair in Cell Biology
    Scottish Funding Council
    2009 - 2014
     

Teaching

  • Level 4: Cell Compartmentalisation Option
  • Level 4: Coordinator, Core skills in Molecular Cell Biology Option

Additional information

Editorial Board

  • 2008 - present: Biological Sciences Review - Editor
  • 2004 - present: BMC Biochemistry - Editorial Board
  • 2004 - present: Antioxidants and Redox Signalling - Editorial Board
  • 1998 - present: Biochemical Journal - Editorial Adviser

Grant Advisory Board

  • 2017 - present: Royal Society of Edinburgh - A4 (Cell and Molecular Biology) Sectional Committee member
  • 2012 - 2014: Wellcome Trust - Equipment Panel
  • 2012 - 2013: Finnish Academy of Sciences
  • 2010 - 2013: Biochemical Society - Member of Executive Committee
  • 2010 - 2015: BBSRC - Panel of Experts
  • 2008 - 2011: Biochemical Society - Council Member
  • 2008 - 2012: Wellcome Trust - Member of MGC Funding Panel

Invited International Presentations

  • 2015: Costa Brava, Spain - ERC meeting on thiol switches
  • 2015: Boston, MA, USA - SFR Meeting
  • 2015: Stuttgart, Germany - SFFR Meeting
  • 2014: Glasgow, UK - Plenary Lecture as ESCPB
  • 2014: Vermont, USA - FASEB meeting on Protein Folding in the Cell
  • 2013: Saxtons River, Vermont, USA - FASEB conference on "ER stress and disease"
  • 2012: Maine, USA - Gordon conference, "Redox regulation and thiol based signalling"
  • 2011: Saxtons River, Vermont, USA - FASEB meeting, "ER Stress and protein degradation"
  • 2010: Girona, Spain - EMBO meeting on Function of the Endoplasmic Reticulum
  • 2009: Vermont, USA - FASEB meeting on "Unfolded proteins to disease"
  • 2009: Glasgow, Scotland, UK - Society for Experimental Biology
  • 2008: Porto, Portugal - ESF meeting on MHC Class I
  • 2007: Ambleside, England, UK - Conference Organiser, Harden conference on protein folding in vitro and in vivo
  • 2004: Glasgow, Scotland, UK - Biochemical Society
  • 2003: Essex, England, UK - Conference Organiser, Biochemical Society meeting on Protein synthesis and quality control, University of Essex
  • 2003: Portugal - ESF meeting on Molecular chaperones
  • 2002: Hamburg, Germany - Embo course on "Protein expression purification, and crystallisation (PEPC3)", European Molecular Biology Laboratory
  • 2002: Vienna, Austria - European colloquium on "Protein folding in the ER"
  • 2001: New London, New Hampshire, USA - Collagen Gordon conference, "Maturation of procollagen in the endoplasmic reticulum"
  • 2001: Romania - Romanian Biochemical Society

Prizes, Awards and Distinctions

  • 2015: Royal Society/Wolfson Merit award
  • 2011: Royal Society of Edinburgh - Elected Fellow

Professional Learned Society

  • 2011 - present: Royal Society of Edinburgh - Fellow
  • 2008 - present: Biochemical Society - Council member

Publications

List by: Type | Date

Jump to: 2019 | 2018 | 2017 | 2016 | 2015 | 2014 | 2013 | 2012 | 2011 | 2010 | 2009 | 2008 | 2007 | 2005 | 2004 | 2003 | 2002 | 2001
Number of items: 54.

2019

Oka, O. B.V. , van Lith, M., Rudolf, J., Tungkum, W., Pringle, M.-A. and Bulleid, N. J. (2019) ERp18 regulates the activation of ATF6α during the unfolded protein response. EMBO Journal, 2019, e100990. (doi:10.15252/embj.2018100990) (PMID:31209066)

2018

Camargo, L. L. et al. (2018) Vascular Nox (NADPH oxidase) compartmentalization, protein hyperoxidation, and endoplasmic reticulum stress response in hypertension. Hypertension, 72(1), pp. 235-246. (doi:10.1161/HYPERTENSIONAHA.118.10824) (PMID:29844144)

Cao, Z., Mitchell, L., Hsia, O., Scarpa, M., Caldwell, S. T. , Alfred, A. D., Gennaris, A., Collet, J.-F., Hartley, R. C. and Bulleid, N. J. (2018) Methionine sulfoxide reductase B3 requires resolving cysteine residues for full activity and can act as a stereospecific methionine oxidase. Biochemical Journal, 475, pp. 827-838. (doi:10.1042/BCJ20170929) (PMID:29420254) (PMCID:PMC6488974)

Ellgaard, L., Sevier, C. S. and Bulleid, N. (2018) How are proteins reduced in the endoplasmic reticulum? Trends in Biochemical Sciences, 43(1), pp. 32-43. (doi:10.1016/j.tibs.2017.10.006) (PMID:29153511) (PMCID:PMC5751730)

2017

Chalmers, F., van Lith, M., Sweeney, B., Cain, K. and Bulleid, N. J. (2017) Inhibition of IRE1α-mediated XBP1 mRNA cleavage by XBP1 reveals a novel regulatory process during the unfolded protein response. Wellcome Open Research, 2, 36. (doi:10.12688/wellcomeopenres.11764.2) (PMID:29062910) (PMCID:PMC5645705)

Stoyle, C. L., Stephens, P. E., Humphreys, D. P., Heywood, S., Cain, K. and Bulleid, N. J. (2017) IgG light chain-independent secretion of heavy chain dimers: consequence for therapeutic antibody production and design. Biochemical Journal, 474(18), pp. 3179-3188. (doi:10.1042/BCJ20170342) (PMID:28784690) (PMCID:PMC5590090)

Robinson, P. J., Pringle, M. A. , Woolhead, C. A. and Bulleid, N. J. (2017) Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation. Journal of Biological Chemistry, 292(17), pp. 6978-6986. (doi:10.1074/jbc.M117.780742) (PMID:28298446) (PMCID:PMC5409466)

Poet, G. J., Oka, O. B.V. , Van Lith, M., Cao, Z., Robinson, P. J., Pringle, M. A. , Arnér, E. S.J. and Bulleid, N. (2017) Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER. EMBO Journal, 36(5), pp. 693-702. (doi:10.15252/embj.201695336) (PMID:28093500) (PMCID:PMC5331760)

2016

Cao, Z., Van Lith, M., Mitchell, L. J., Pringle, M. A. , Inaba, K. and Bulleid, N. J. (2016) The membrane topology of vitamin K epoxide reductase is conserved between human isoforms and the bacterial enzyme. Biochemical Journal, 473(7), pp. 851-858. (doi:10.1042/bj20151223) (PMID:26772871)

2015

Pisoni, G. B., Ruddock, L. W., Bulleid, N. and Molinari, M. (2015) Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides. Molecular Biology of the Cell, 26(19), pp. 3390-3400. (doi:10.1091/mbc.E15-05-0321) (PMID:26246604) (PMCID:PMC4591685)

Cao, Z. and Bulleid, N. J. (2015) Detecting peroxiredoxin hyperoxidation by one-dimensional isoelectric focusing. Biophysics Reports, 1(1), pp. 14-17. (doi:10.1007/s41048-015-0007-y) (PMID:26942215) (PMCID:PMC4762124)

Oka, O. , Yeoh, H. and Bulleid, N. (2015) Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme. Biochemical Journal, 469(2), pp. 279-288. (doi:10.1042/BJ20141423) (PMID:25989104) (PMCID:PMC4613490))

2014

Shepherd, C., Oka, O. B. V. and Bulleid, N. J. (2014) Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases. Biochemical Journal, 461(1), pp. 107-113. (doi:10.1042/BJ20140234) (PMID:24758166) (PMCID:PMC4243250)

Cao, Z., Subramaniam, S. and Bulleid, N. J. (2014) Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation. Journal of Biological Chemistry, 289(9), pp. 5490-5498. (doi:10.1074/jbc.M113.529305)

Bulleid, N. J. and van Lith, M. (2014) Redox regulation in the endoplasmic reticulum. Biochemical Society Transactions, 42(4), pp. 905-908. (doi:10.1042/BST20140065)

Martin, R. E., Cao, Z. and Bulleid, N. J. (2014) Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IV. Biochemical Society Transactions, 42(1), pp. 42-46. (doi:10.1042/BST20130168)

2013

Rudolf, J., Pringle, M. and Bulleid, N. (2013) Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst. Biochemical Journal, 2013(454), pp. 181-190. (doi:10.1042/BJ20130360)

Oka, O. B. V. , Pringle, M. A. , Schopp, I. M., Braakman, I. and Bulleid, N. J. (2013) ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor. Molecular Cell, 50(6), pp. 793-804. (doi:10.1016/j.molcel.2013.05.014)

Oka, O. B.V. and Bulleid, N. J. (2013) Forming disulfides in the endoplasmic reticulum. Biochimica et Biophysica Acta: Molecular Cell Research, 1833(11), pp. 2425-2429. (doi:10.1016/j.bbamcr.2013.02.007)

2012

Bulleid, N.J. (2012) Solving the mystery of procollagen chain selectivity. Nature Structural and Molecular Biology, 19(10), pp. 977-978. (doi:10.1038/nsmb.2397)

Bulleid, N.J. (2012) Disulfide bond formation in the mammalian endoplasmic reticulum. Cold Spring Harbor Perspectives in Biology, 4(11), a013219-a013219. (doi:10.1101/cshperspect.a013219)

Galian, C., Bjorkholm, P., Bulleid, N. and von Heijne, G. (2012) Efficient Glycosylphosphatidylinositol (GPI) modification of membrane proteins requires a C-terminal anchoring signal of marginal hydrophobicity. Journal of Biological Chemistry, 287(20), pp. 16399-16409. (doi:10.1074/jbc.M112.350009)

2011

Cao, Z., Tavender, T.J., Roszak, A.W., Cogdell, R.J. and Bulleid, N.J. (2011) 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. Journal of Biological Chemistry, 286(49), pp. 42257-42266. (doi:10.1074/jbc.M111.298810)

Van Lith, M., Tiwari, S., Pediani, J. , Milligan, G. and Bulleid, N. J. (2011) Real-time monitoring of redox changes in the mammalian endoplasmic reticulum. Journal of Cell Science, 124(14), pp. 2349-2356. (doi:10.1242/jcs.085530)

Braakman, I. and Bulleid, N.J. (2011) Protein folding and modification in the mammalian endoplasmic reticulum. Annual Review of Biochemistry, 80(1), pp. 71-99. (doi:10.1146/annurev-biochem-062209-093836)

Bulleid, N.J. and Ellgaard, L. (2011) Multiple ways to make disulfides. Trends in Biochemical Sciences, 36(9), pp. 485-492. (doi:10.1016/j.tibs.2011.05.004)

Tiwari, S., Askari, J.A., Humphries, M.J. and Bulleid, N.J. (2011) Divalent cations regulate the folding and activation status of integrins during their intracellular trafficking. Journal of Cell Science, 124(10), pp. 1672-1680. (doi:10.1242/jcs.084483)

2010

Tavender, T.J., Springate, J.J. and Bulleid, N.J. (2010) Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO Journal, 29(24), pp. 4185-4197. (doi:10.1038/emboj.2010.273)

Chambers, J.E., Tavender, T.J., Oka, O.B.V. , Warwood, S., Knight, D. and Bulleid, N.J. (2010) The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1. Journal of Biological Chemistry, 285(38), pp. 29200-29207. (doi:10.1074/jbc.M110.156596)

Gleghorn, L.J., Trump, D. and Bulleid, N.J. (2010) Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer. Biochemical Journal, 425(1), pp. 275-283. (doi:10.1042/BJ20091179)

Tavender, T.J. and Bulleid, N.J. (2010) Molecular Mechanisms Regulating Oxidative Activity of the Ero1 Family in the Endoplasmic Reticulum. Antioxidants and Redox Signaling, 13(8), pp. 1177-1187. (doi:10.1089/ars.2010.3230)

Tavender, T.J. and Bulleid, N.J. (2010) Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation. Journal of Cell Science, 123(15), pp. 2672-2679. (doi:10.1242/jcs.067843)

2009

Jessop, C.E., Watkins, R.H., Simmons, J.J., Tasab, M. and Bulleid, N.J. (2009) Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. Journal of Cell Science, 122(23), pp. 4287-4295. (doi:10.1242/jcs.059154)

Jessop, C.E., Tavender, T.J., Watkins, R.H., Chambers, J.E. and Bulleid, N.J. (2009) Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin. Journal of Biological Chemistry, 284(4), pp. 2194-2202. (doi:10.1074/jbc.M808054200)

Riemer, J., Bulleid, N.J. and Herrmann, J.M. (2009) Disulfide formation in the ER and mitochondria: two solutions to a common process. Science, 324(5932), pp. 1284-1287. (doi:10.1126/science.1170653)

2008

Baker, K.M., Chakravarthi, S., Langton, K.P., Sheppard, A.M., Lu, H. and Bulleid, N.J. (2008) Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation. EMBO Journal, 27(22), pp. 2988-2997. (doi:10.1038/emboj.2008.230)

Chambers, J.E., Jessop, C.E. and Bulleid, N.J. (2008) Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly. Journal of Biological Chemistry, 283(4), pp. 1862-1869. (doi:10.1074/jbc.M708196200)

Bulleid, N.J. (2008) How do proteins lose their shape? Biological Sciences Review, 21(1), pp. 21-25.

Tavender, T.J., Sheppard, A.M. and Bulleid, N.J. (2008) Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells. Biochemical Journal, 411(1), pp. 191-199. (doi:10.1042/BJ20071428)

2007

Wahlman, J., DeMartino, G.N., Skach, W.R., Bulleid, N.J. , Brodsky, J.L. and Johnson, A.E. (2007) Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system. Cell, 129(5), pp. 943-955. (doi:10.1016/j.cell.2007.03.046)

Jessop, C.E., Chakravarthi, S., Willer, M., Stirling, C.J. and Bulleid, N.J. (2007) Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1. Biochemical Journal, 404(3), pp. 403-411. (doi:10.1042/BJ20061510)

Jessop, C.E., Chakravarthi, S., Garbi, N., Hämmerling, G.J., Lovell, S. and Bulleid, N.J. (2007) ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO Journal, 26(1), pp. 28-40. (doi:10.1038/sj.emboj.7601505)

2005

Dias-Gunasekara, S., Gubbens, J., van Lith, M., Dunne, C., Williams, J.A.G., Kataky, R., Scoones, D., Lapthorn, A. , Bulleid, N.J. and Benham, A.M. (2005) Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1β. Journal of Biological Chemistry, 280, pp. 33066-33075. (doi:10.1074/jbc.M505023200)

O'Connor, E., Eisenhaber, B., Dalley, J., Wang, T., Missen, C., Bulleid, N.J. , Bishop, P.N. and Trump, D. (2005) Species specific membrane anchoring of nyctalopin, a small leucine-rich repeat protein. Human Molecular Genetics, 14(13), pp. 1877-1887. (doi:10.1093/hmg/ddi194)

2004

Jessop, C.E. and Bulleid, N.J. (2004) Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells. Journal of Biological Chemistry, 279(53), pp. 55341-55347. (doi:10.1074/jbc.M411409200)

Jessop, C.E., Chakravarthi, S., Watkins, R.H. and Bulleid, N.J. (2004) Oxidative protein folding in the mammalian endoplasmic reticulum. Biochemical Society Transactions, 32(5), pp. 655-658.

Chakravarthi, S. and Bulleid, N.J. (2004) Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway. Journal of Biological Chemistry, 279(38), pp. 39872-39879. (doi:10.1074/jbc.M406912200)

2003

Dalley, J.A. and Bulleid, N.J. (2003) The endoplasmic eeticulum (ER) translocon can differentiate between hydrophobic sequences allowing signals for glycosylphosphatidylinositol anchor addition to be fully translocated into the ER lumen. Journal of Biological Chemistry, 278(51), pp. 51749-51757. (doi:10.1074/jbc.M303978200)

Dalley, J.A. and Bulleid, N.J. (2003) How does the translocon differentiate between hydrophobic sequences that form part of either a GPI (glycosylphosphatidylinositol)-anchor signal or a stop transfer sequence? Biochemical Society Transactions, 31, pp. 1257-1259.

Bulleid, N.J. (2003) Quick guide: protein disulphide isomerase. Current Biology, 13(10), R380. (doi:10.1016/S0960-9822(03)00314-2)

2002

Tasab, M., Jenkinson, L. and Bulleid, N.J. (2002) Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47. Journal of Biological Chemistry, 277(38), pp. 35007-35012. (doi:10.1074/jbc.M202782200)

Lumb, R.A. and Bulleid, N.J. (2002) Is protein disulfide isomerase a redox-dependent molecular chaperone? EMBO Journal, 21(24), p. 6763. (doi:10.1093/emboj/cdf685)

2001

Bottomley, M.J., Batten, M.R., Lumb, R.A. and Bulleid, N.J. (2001) Quality control in the endoplasmic reticulum: PDI mediates the ER retention of unassembled procollagen C-propeptides. Current Biology, 11(14), pp. 1114-1118. (doi:10.1016/S0960-9822(01)00317-7)

Spurway, T.D., Dalley, J.A., High, S. and Bulleid, N.J. (2001) Early events in glycosylphosphatidylinositol anchor addition: substrate proteins associate with the transamidase subunit Gpi8p. Journal of Biological Chemistry, 276(19), pp. 15975-15982. (doi:10.1074/jbc.M010128200)

This list was generated on Tue Sep 17 14:33:27 2019 BST.
Jump to: Articles
Number of items: 54.

Articles

Oka, O. B.V. , van Lith, M., Rudolf, J., Tungkum, W., Pringle, M.-A. and Bulleid, N. J. (2019) ERp18 regulates the activation of ATF6α during the unfolded protein response. EMBO Journal, 2019, e100990. (doi:10.15252/embj.2018100990) (PMID:31209066)

Camargo, L. L. et al. (2018) Vascular Nox (NADPH oxidase) compartmentalization, protein hyperoxidation, and endoplasmic reticulum stress response in hypertension. Hypertension, 72(1), pp. 235-246. (doi:10.1161/HYPERTENSIONAHA.118.10824) (PMID:29844144)

Cao, Z., Mitchell, L., Hsia, O., Scarpa, M., Caldwell, S. T. , Alfred, A. D., Gennaris, A., Collet, J.-F., Hartley, R. C. and Bulleid, N. J. (2018) Methionine sulfoxide reductase B3 requires resolving cysteine residues for full activity and can act as a stereospecific methionine oxidase. Biochemical Journal, 475, pp. 827-838. (doi:10.1042/BCJ20170929) (PMID:29420254) (PMCID:PMC6488974)

Ellgaard, L., Sevier, C. S. and Bulleid, N. (2018) How are proteins reduced in the endoplasmic reticulum? Trends in Biochemical Sciences, 43(1), pp. 32-43. (doi:10.1016/j.tibs.2017.10.006) (PMID:29153511) (PMCID:PMC5751730)

Chalmers, F., van Lith, M., Sweeney, B., Cain, K. and Bulleid, N. J. (2017) Inhibition of IRE1α-mediated XBP1 mRNA cleavage by XBP1 reveals a novel regulatory process during the unfolded protein response. Wellcome Open Research, 2, 36. (doi:10.12688/wellcomeopenres.11764.2) (PMID:29062910) (PMCID:PMC5645705)

Stoyle, C. L., Stephens, P. E., Humphreys, D. P., Heywood, S., Cain, K. and Bulleid, N. J. (2017) IgG light chain-independent secretion of heavy chain dimers: consequence for therapeutic antibody production and design. Biochemical Journal, 474(18), pp. 3179-3188. (doi:10.1042/BCJ20170342) (PMID:28784690) (PMCID:PMC5590090)

Robinson, P. J., Pringle, M. A. , Woolhead, C. A. and Bulleid, N. J. (2017) Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation. Journal of Biological Chemistry, 292(17), pp. 6978-6986. (doi:10.1074/jbc.M117.780742) (PMID:28298446) (PMCID:PMC5409466)

Poet, G. J., Oka, O. B.V. , Van Lith, M., Cao, Z., Robinson, P. J., Pringle, M. A. , Arnér, E. S.J. and Bulleid, N. (2017) Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER. EMBO Journal, 36(5), pp. 693-702. (doi:10.15252/embj.201695336) (PMID:28093500) (PMCID:PMC5331760)

Cao, Z., Van Lith, M., Mitchell, L. J., Pringle, M. A. , Inaba, K. and Bulleid, N. J. (2016) The membrane topology of vitamin K epoxide reductase is conserved between human isoforms and the bacterial enzyme. Biochemical Journal, 473(7), pp. 851-858. (doi:10.1042/bj20151223) (PMID:26772871)

Pisoni, G. B., Ruddock, L. W., Bulleid, N. and Molinari, M. (2015) Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides. Molecular Biology of the Cell, 26(19), pp. 3390-3400. (doi:10.1091/mbc.E15-05-0321) (PMID:26246604) (PMCID:PMC4591685)

Cao, Z. and Bulleid, N. J. (2015) Detecting peroxiredoxin hyperoxidation by one-dimensional isoelectric focusing. Biophysics Reports, 1(1), pp. 14-17. (doi:10.1007/s41048-015-0007-y) (PMID:26942215) (PMCID:PMC4762124)

Oka, O. , Yeoh, H. and Bulleid, N. (2015) Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme. Biochemical Journal, 469(2), pp. 279-288. (doi:10.1042/BJ20141423) (PMID:25989104) (PMCID:PMC4613490))

Shepherd, C., Oka, O. B. V. and Bulleid, N. J. (2014) Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases. Biochemical Journal, 461(1), pp. 107-113. (doi:10.1042/BJ20140234) (PMID:24758166) (PMCID:PMC4243250)

Cao, Z., Subramaniam, S. and Bulleid, N. J. (2014) Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation. Journal of Biological Chemistry, 289(9), pp. 5490-5498. (doi:10.1074/jbc.M113.529305)

Bulleid, N. J. and van Lith, M. (2014) Redox regulation in the endoplasmic reticulum. Biochemical Society Transactions, 42(4), pp. 905-908. (doi:10.1042/BST20140065)

Martin, R. E., Cao, Z. and Bulleid, N. J. (2014) Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IV. Biochemical Society Transactions, 42(1), pp. 42-46. (doi:10.1042/BST20130168)

Rudolf, J., Pringle, M. and Bulleid, N. (2013) Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst. Biochemical Journal, 2013(454), pp. 181-190. (doi:10.1042/BJ20130360)

Oka, O. B. V. , Pringle, M. A. , Schopp, I. M., Braakman, I. and Bulleid, N. J. (2013) ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor. Molecular Cell, 50(6), pp. 793-804. (doi:10.1016/j.molcel.2013.05.014)

Oka, O. B.V. and Bulleid, N. J. (2013) Forming disulfides in the endoplasmic reticulum. Biochimica et Biophysica Acta: Molecular Cell Research, 1833(11), pp. 2425-2429. (doi:10.1016/j.bbamcr.2013.02.007)

Bulleid, N.J. (2012) Solving the mystery of procollagen chain selectivity. Nature Structural and Molecular Biology, 19(10), pp. 977-978. (doi:10.1038/nsmb.2397)

Bulleid, N.J. (2012) Disulfide bond formation in the mammalian endoplasmic reticulum. Cold Spring Harbor Perspectives in Biology, 4(11), a013219-a013219. (doi:10.1101/cshperspect.a013219)

Galian, C., Bjorkholm, P., Bulleid, N. and von Heijne, G. (2012) Efficient Glycosylphosphatidylinositol (GPI) modification of membrane proteins requires a C-terminal anchoring signal of marginal hydrophobicity. Journal of Biological Chemistry, 287(20), pp. 16399-16409. (doi:10.1074/jbc.M112.350009)

Cao, Z., Tavender, T.J., Roszak, A.W., Cogdell, R.J. and Bulleid, N.J. (2011) 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. Journal of Biological Chemistry, 286(49), pp. 42257-42266. (doi:10.1074/jbc.M111.298810)

Van Lith, M., Tiwari, S., Pediani, J. , Milligan, G. and Bulleid, N. J. (2011) Real-time monitoring of redox changes in the mammalian endoplasmic reticulum. Journal of Cell Science, 124(14), pp. 2349-2356. (doi:10.1242/jcs.085530)

Braakman, I. and Bulleid, N.J. (2011) Protein folding and modification in the mammalian endoplasmic reticulum. Annual Review of Biochemistry, 80(1), pp. 71-99. (doi:10.1146/annurev-biochem-062209-093836)

Bulleid, N.J. and Ellgaard, L. (2011) Multiple ways to make disulfides. Trends in Biochemical Sciences, 36(9), pp. 485-492. (doi:10.1016/j.tibs.2011.05.004)

Tiwari, S., Askari, J.A., Humphries, M.J. and Bulleid, N.J. (2011) Divalent cations regulate the folding and activation status of integrins during their intracellular trafficking. Journal of Cell Science, 124(10), pp. 1672-1680. (doi:10.1242/jcs.084483)

Tavender, T.J., Springate, J.J. and Bulleid, N.J. (2010) Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO Journal, 29(24), pp. 4185-4197. (doi:10.1038/emboj.2010.273)

Chambers, J.E., Tavender, T.J., Oka, O.B.V. , Warwood, S., Knight, D. and Bulleid, N.J. (2010) The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1. Journal of Biological Chemistry, 285(38), pp. 29200-29207. (doi:10.1074/jbc.M110.156596)

Gleghorn, L.J., Trump, D. and Bulleid, N.J. (2010) Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer. Biochemical Journal, 425(1), pp. 275-283. (doi:10.1042/BJ20091179)

Tavender, T.J. and Bulleid, N.J. (2010) Molecular Mechanisms Regulating Oxidative Activity of the Ero1 Family in the Endoplasmic Reticulum. Antioxidants and Redox Signaling, 13(8), pp. 1177-1187. (doi:10.1089/ars.2010.3230)

Tavender, T.J. and Bulleid, N.J. (2010) Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation. Journal of Cell Science, 123(15), pp. 2672-2679. (doi:10.1242/jcs.067843)

Jessop, C.E., Watkins, R.H., Simmons, J.J., Tasab, M. and Bulleid, N.J. (2009) Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. Journal of Cell Science, 122(23), pp. 4287-4295. (doi:10.1242/jcs.059154)

Jessop, C.E., Tavender, T.J., Watkins, R.H., Chambers, J.E. and Bulleid, N.J. (2009) Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin. Journal of Biological Chemistry, 284(4), pp. 2194-2202. (doi:10.1074/jbc.M808054200)

Riemer, J., Bulleid, N.J. and Herrmann, J.M. (2009) Disulfide formation in the ER and mitochondria: two solutions to a common process. Science, 324(5932), pp. 1284-1287. (doi:10.1126/science.1170653)

Baker, K.M., Chakravarthi, S., Langton, K.P., Sheppard, A.M., Lu, H. and Bulleid, N.J. (2008) Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation. EMBO Journal, 27(22), pp. 2988-2997. (doi:10.1038/emboj.2008.230)

Chambers, J.E., Jessop, C.E. and Bulleid, N.J. (2008) Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly. Journal of Biological Chemistry, 283(4), pp. 1862-1869. (doi:10.1074/jbc.M708196200)

Bulleid, N.J. (2008) How do proteins lose their shape? Biological Sciences Review, 21(1), pp. 21-25.

Tavender, T.J., Sheppard, A.M. and Bulleid, N.J. (2008) Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells. Biochemical Journal, 411(1), pp. 191-199. (doi:10.1042/BJ20071428)

Wahlman, J., DeMartino, G.N., Skach, W.R., Bulleid, N.J. , Brodsky, J.L. and Johnson, A.E. (2007) Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system. Cell, 129(5), pp. 943-955. (doi:10.1016/j.cell.2007.03.046)

Jessop, C.E., Chakravarthi, S., Willer, M., Stirling, C.J. and Bulleid, N.J. (2007) Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1. Biochemical Journal, 404(3), pp. 403-411. (doi:10.1042/BJ20061510)

Jessop, C.E., Chakravarthi, S., Garbi, N., Hämmerling, G.J., Lovell, S. and Bulleid, N.J. (2007) ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO Journal, 26(1), pp. 28-40. (doi:10.1038/sj.emboj.7601505)

Dias-Gunasekara, S., Gubbens, J., van Lith, M., Dunne, C., Williams, J.A.G., Kataky, R., Scoones, D., Lapthorn, A. , Bulleid, N.J. and Benham, A.M. (2005) Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1β. Journal of Biological Chemistry, 280, pp. 33066-33075. (doi:10.1074/jbc.M505023200)

O'Connor, E., Eisenhaber, B., Dalley, J., Wang, T., Missen, C., Bulleid, N.J. , Bishop, P.N. and Trump, D. (2005) Species specific membrane anchoring of nyctalopin, a small leucine-rich repeat protein. Human Molecular Genetics, 14(13), pp. 1877-1887. (doi:10.1093/hmg/ddi194)

Jessop, C.E. and Bulleid, N.J. (2004) Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells. Journal of Biological Chemistry, 279(53), pp. 55341-55347. (doi:10.1074/jbc.M411409200)

Jessop, C.E., Chakravarthi, S., Watkins, R.H. and Bulleid, N.J. (2004) Oxidative protein folding in the mammalian endoplasmic reticulum. Biochemical Society Transactions, 32(5), pp. 655-658.

Chakravarthi, S. and Bulleid, N.J. (2004) Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway. Journal of Biological Chemistry, 279(38), pp. 39872-39879. (doi:10.1074/jbc.M406912200)

Dalley, J.A. and Bulleid, N.J. (2003) The endoplasmic eeticulum (ER) translocon can differentiate between hydrophobic sequences allowing signals for glycosylphosphatidylinositol anchor addition to be fully translocated into the ER lumen. Journal of Biological Chemistry, 278(51), pp. 51749-51757. (doi:10.1074/jbc.M303978200)

Dalley, J.A. and Bulleid, N.J. (2003) How does the translocon differentiate between hydrophobic sequences that form part of either a GPI (glycosylphosphatidylinositol)-anchor signal or a stop transfer sequence? Biochemical Society Transactions, 31, pp. 1257-1259.

Bulleid, N.J. (2003) Quick guide: protein disulphide isomerase. Current Biology, 13(10), R380. (doi:10.1016/S0960-9822(03)00314-2)

Tasab, M., Jenkinson, L. and Bulleid, N.J. (2002) Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47. Journal of Biological Chemistry, 277(38), pp. 35007-35012. (doi:10.1074/jbc.M202782200)

Lumb, R.A. and Bulleid, N.J. (2002) Is protein disulfide isomerase a redox-dependent molecular chaperone? EMBO Journal, 21(24), p. 6763. (doi:10.1093/emboj/cdf685)

Bottomley, M.J., Batten, M.R., Lumb, R.A. and Bulleid, N.J. (2001) Quality control in the endoplasmic reticulum: PDI mediates the ER retention of unassembled procollagen C-propeptides. Current Biology, 11(14), pp. 1114-1118. (doi:10.1016/S0960-9822(01)00317-7)

Spurway, T.D., Dalley, J.A., High, S. and Bulleid, N.J. (2001) Early events in glycosylphosphatidylinositol anchor addition: substrate proteins associate with the transamidase subunit Gpi8p. Journal of Biological Chemistry, 276(19), pp. 15975-15982. (doi:10.1074/jbc.M010128200)

This list was generated on Tue Sep 17 14:33:27 2019 BST.