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Items: 1 to 50 of 107

1.

ERp18 regulates activation of ATF6α during unfolded protein response.

Oka OB, van Lith M, Rudolf J, Tungkum W, Pringle MA, Bulleid NJ.

EMBO J. 2019 Jun 17. pii: e100990. doi: 10.15252/embj.2018100990. [Epub ahead of print]

2.

Mix-and-Match Proteomics: Using Advanced Iodoacetyl Tandem Mass Tag Multiplexing To Investigate Cysteine Oxidation Changes with Respect to Protein Expression.

Prakash AS, Kabli AMF, Bulleid N, Burchmore R.

Anal Chem. 2018 Dec 18;90(24):14173-14180. doi: 10.1021/acs.analchem.8b02517. Epub 2018 Dec 3.

PMID:
30452864
3.

Vascular Nox (NADPH Oxidase) Compartmentalization, Protein Hyperoxidation, and Endoplasmic Reticulum Stress Response in Hypertension.

Camargo LL, Harvey AP, Rios FJ, Tsiropoulou S, Da Silva RNO, Cao Z, Graham D, McMaster C, Burchmore RJ, Hartley RC, Bulleid N, Montezano AC, Touyz RM.

Hypertension. 2018 Jul;72(1):235-246. doi: 10.1161/HYPERTENSIONAHA.118.10824. Epub 2018 May 29.

4.

Methionine sulfoxide reductase B3 requires resolving cysteine residues for full activity and can act as a stereospecific methionine oxidase.

Cao Z, Mitchell L, Hsia O, Scarpa M, Caldwell ST, Alfred AD, Gennaris A, Collet JF, Hartley RC, Bulleid NJ.

Biochem J. 2018 Feb 28;475(4):827-838. doi: 10.1042/BCJ20170929.

5.

How Are Proteins Reduced in the Endoplasmic Reticulum?

Ellgaard L, Sevier CS, Bulleid NJ.

Trends Biochem Sci. 2018 Jan;43(1):32-43. doi: 10.1016/j.tibs.2017.10.006. Epub 2017 Nov 15. Review.

6.

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

Chalmers F, van Lith M, Sweeney B, Cain K, Bulleid NJ.

Wellcome Open Res. 2017 Oct 9;2:36. doi: 10.12688/wellcomeopenres.11764.2. eCollection 2017.

7.

IgG light chain-independent secretion of heavy chain dimers: consequence for therapeutic antibody production and design.

Stoyle CL, Stephens PE, Humphreys DP, Heywood S, Cain K, Bulleid NJ.

Biochem J. 2017 Sep 7;474(18):3179-3188. doi: 10.1042/BCJ20170342.

8.

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

Robinson PJ, Pringle MA, Woolhead CA, Bulleid NJ.

J Biol Chem. 2017 Apr 28;292(17):6978-6986. doi: 10.1074/jbc.M117.780742. Epub 2017 Mar 15.

9.

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

Poet GJ, Oka OB, van Lith M, Cao Z, Robinson PJ, Pringle MA, Arnér ES, Bulleid NJ.

EMBO J. 2017 Mar 1;36(5):693-702. doi: 10.15252/embj.201695336. Epub 2017 Jan 16.

10.

The membrane topology of vitamin K epoxide reductase is conserved between human isoforms and the bacterial enzyme.

Cao Z, van Lith M, Mitchell LJ, Pringle MA, Inaba K, Bulleid NJ.

Biochem J. 2016 Apr 1;473(7):851-8. doi: 10.1042/BJ20151223. Epub 2016 Jan 15.

PMID:
26772871
11.

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

Pisoni GB, Ruddock LW, Bulleid N, Molinari M.

Mol Biol Cell. 2015 Oct 1;26(19):3390-400. doi: 10.1091/mbc.E15-05-0321. Epub 2015 Aug 5.

12.

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

Oka OB, Yeoh HY, Bulleid NJ.

Biochem J. 2015 Jul 15;469(2):279-88. doi: 10.1042/BJ20141423. Epub 2015 May 19.

13.

Detecting peroxiredoxin hyperoxidation by one-dimensional isoelectric focusing.

Cao Z, Bulleid NJ.

Biophys Rep. 2015;1:14-17. Epub 2015 Aug 21.

14.

Redox regulation in the endoplasmic reticulum.

Bulleid NJ, van Lith M.

Biochem Soc Trans. 2014 Aug;42(4):905-8. doi: 10.1042/BST20140065. Review.

PMID:
25109977
15.

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

Shepherd C, Oka OB, Bulleid NJ.

Biochem J. 2014 Jul 1;461(1):107-13. doi: 10.1042/BJ20140234.

16.

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

Martin RE, Cao Z, Bulleid NJ.

Biochem Soc Trans. 2014 Feb;42(1):42-6. doi: 10.1042/BST20130168. Review.

PMID:
24450625
17.

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

Cao Z, Subramaniam S, Bulleid NJ.

J Biol Chem. 2014 Feb 28;289(9):5490-8. doi: 10.1074/jbc.M113.529305. Epub 2014 Jan 8.

18.

Characterization of a cryogenic beam source for atoms and molecules.

Bulleid NE, Skoff SM, Hendricks RJ, Sauer BE, Hinds EA, Tarbutt MR.

Phys Chem Chem Phys. 2013 Aug 7;15(29):12299-307. doi: 10.1039/c3cp51553b. Epub 2013 Jun 17.

19.

ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor.

Oka OB, Pringle MA, Schopp IM, Braakman I, Bulleid NJ.

Mol Cell. 2013 Jun 27;50(6):793-804. doi: 10.1016/j.molcel.2013.05.014. Epub 2013 Jun 13.

20.

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

Rudolf J, Pringle MA, Bulleid NJ.

Biochem J. 2013 Sep 1;454(2):181-90. doi: 10.1042/BJ20130360.

21.

Forming disulfides in the endoplasmic reticulum.

Oka OB, Bulleid NJ.

Biochim Biophys Acta. 2013 Nov;1833(11):2425-9. doi: 10.1016/j.bbamcr.2013.02.007. Epub 2013 Feb 20. Review.

22.

Disulfide bond formation in the mammalian endoplasmic reticulum.

Bulleid NJ.

Cold Spring Harb Perspect Biol. 2012 Nov 1;4(11). pii: a013219. doi: 10.1101/cshperspect.a013219. Review.

23.

Solving the mystery of procollagen chain selectivity.

Bulleid NJ.

Nat Struct Mol Biol. 2012 Oct;19(10):977-8. doi: 10.1038/nsmb.2397.

PMID:
23037594
24.

Efficient glycosylphosphatidylinositol (GPI) modification of membrane proteins requires a C-terminal anchoring signal of marginal hydrophobicity.

Galian C, Björkholm P, Bulleid N, von Heijne G.

J Biol Chem. 2012 May 11;287(20):16399-409. doi: 10.1074/jbc.M112.350009. Epub 2012 Mar 19.

25.

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.

Cao Z, Tavender TJ, Roszak AW, Cogdell RJ, Bulleid NJ.

J Biol Chem. 2011 Dec 9;286(49):42257-66. doi: 10.1074/jbc.M111.298810. Epub 2011 Oct 12.

26.

Franck-Condon factors and radiative lifetime of the A2Π(1/2)-X2Σ+ transition of ytterbium monofluoride, YbF.

Zhuang X, Le A, Steimle TC, Bulleid NE, Smallman IJ, Hendricks RJ, Skoff SM, Hudson JJ, Sauer BE, Hinds EA, Tarbutt MR.

Phys Chem Chem Phys. 2011 Nov 14;13(42):19013-7. doi: 10.1039/c1cp21585j. Epub 2011 Aug 8.

PMID:
21822518
27.

Multiple ways to make disulfides.

Bulleid NJ, Ellgaard L.

Trends Biochem Sci. 2011 Sep;36(9):485-92. doi: 10.1016/j.tibs.2011.05.004. Epub 2011 Jul 19. Review.

PMID:
21778060
28.

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

van Lith M, Tiwari S, Pediani J, Milligan G, Bulleid NJ.

J Cell Sci. 2011 Jul 15;124(Pt 14):2349-56. doi: 10.1242/jcs.085530. Epub 2011 Jun 21.

29.

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

Tiwari S, Askari JA, Humphries MJ, Bulleid NJ.

J Cell Sci. 2011 May 15;124(Pt 10):1672-80. doi: 10.1242/jcs.084483. Epub 2011 Apr 21.

30.

Protein folding and modification in the mammalian endoplasmic reticulum.

Braakman I, Bulleid NJ.

Annu Rev Biochem. 2011;80:71-99. doi: 10.1146/annurev-biochem-062209-093836. Review.

PMID:
21495850
31.

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

Tavender TJ, Springate JJ, Bulleid NJ.

EMBO J. 2010 Dec 15;29(24):4185-97. doi: 10.1038/emboj.2010.273. Epub 2010 Nov 5.

32.

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

Chambers JE, Tavender TJ, Oka OB, Warwood S, Knight D, Bulleid NJ.

J Biol Chem. 2010 Sep 17;285(38):29200-7. doi: 10.1074/jbc.M110.156596. Epub 2010 Jul 23.

33.

Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation.

Tavender TJ, Bulleid NJ.

J Cell Sci. 2010 Aug 1;123(Pt 15):2672-9. doi: 10.1242/jcs.067843. Epub 2010 Jul 13.

34.

Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum.

Tavender TJ, Bulleid NJ.

Antioxid Redox Signal. 2010 Oct;13(8):1177-87. doi: 10.1089/ars.2010.3230. Review.

PMID:
20486761
35.

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

Jessop CE, Watkins RH, Simmons JJ, Tasab M, Bulleid NJ.

J Cell Sci. 2009 Dec 1;122(Pt 23):4287-95. doi: 10.1242/jcs.059154. Epub 2009 Nov 3.

36.
37.

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

Riemer J, Bulleid N, Herrmann JM.

Science. 2009 Jun 5;324(5932):1284-7. doi: 10.1126/science.1170653. Review.

PMID:
19498160
38.

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

Jessop CE, Tavender TJ, Watkins RH, Chambers JE, Bulleid NJ.

J Biol Chem. 2009 Jan 23;284(4):2194-202. doi: 10.1074/jbc.M808054200. Epub 2008 Dec 3.

39.

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

Baker KM, Chakravarthi S, Langton KP, Sheppard AM, Lu H, Bulleid NJ.

EMBO J. 2008 Nov 19;27(22):2988-97. doi: 10.1038/emboj.2008.230. Epub 2008 Oct 30.

40.
41.
42.

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

Wahlman J, DeMartino GN, Skach WR, Bulleid NJ, Brodsky JL, Johnson AE.

Cell. 2007 Jun 1;129(5):943-55.

43.

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

Chakravarthi S, Jessop CE, Willer M, Stirling CJ, Bulleid NJ.

Biochem J. 2007 Jun 15;404(3):403-11.

44.

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

Jessop CE, Chakravarthi S, Garbi N, Hämmerling GJ, Lovell S, Bulleid NJ.

EMBO J. 2007 Jan 10;26(1):28-40. Epub 2006 Dec 14.

45.

Differential oxidation of HLA-B2704 and HLA-B2705 in lymphoblastoid and transfected adherent cells.

Saleki K, Hartigan N, Lith Mv, Bulleid N, Benham AM.

Antioxid Redox Signal. 2006 Mar-Apr;8(3-4):292-9.

PMID:
16677075
46.

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

Chakravarthi S, Jessop CE, Bulleid NJ.

EMBO Rep. 2006 Mar;7(3):271-5. Review.

47.

Annihilation dynamics of umbilical defects in nematic liquid crystals under applied electric fields.

Dierking I, Marshall O, Wright J, Bulleid N.

Phys Rev E Stat Nonlin Soft Matter Phys. 2005 Jun;71(6 Pt 1):061709. Epub 2005 Jun 28.

PMID:
16089754
48.

Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta.

Dias-Gunasekara S, Gubbens J, van Lith M, Dunne C, Williams JA, Kataky R, Scoones D, Lapthorn A, Bulleid NJ, Benham AM.

J Biol Chem. 2005 Sep 23;280(38):33066-75. Epub 2005 Jul 12.

49.

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

O'Connor E, Eisenhaber B, Dalley J, Wang T, Missen C, Bulleid N, Bishop PN, Trump D.

Hum Mol Genet. 2005 Jul 1;14(13):1877-87. Epub 2005 May 19.

PMID:
15905181
50.

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

Jessop CE, Bulleid NJ.

J Biol Chem. 2004 Dec 31;279(53):55341-7. Epub 2004 Oct 26.

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