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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)

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)

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)

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)

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