Dr Philip Robinson
- Research Associate (Molecular Biosciences)
telephone:
0141 330 6453
email:
Philip.Robinson@glasgow.ac.uk
Institute of MC&SB, Davidson Building, Glasgow G12 8QQ
https://orcid.org/0000-0003-2576-5010Publications
2020
Robinson, P. J. and Bulleid, N. J. (2020) Mechanisms of disulfide bond formation in nascent polypeptides entering the secretory pathway. Cells, 9(9), 1994. (doi: 10.3390/cells9091994) (PMID:32872499)
Cao, X., Lilla, S., Cao, Z., Pringle, M. A., Oka, O. B.V. , Robinson, P. J. , Szmaja, T., Van Lith, M., Zanivan, S. and Bulleid, N. (2020) The mammalian cytosolic thioredoxin reductase pathway acts via a membrane 1 protein to reduce ER-localised proteins. Journal of Cell Science, 133, jcs241976. (doi: 10.1242/jcs.241976) (PMID:32184267) (PMCID:PMC7197872)
Robinson, P. J. , Kanemura, S., Cao, X. and Bulleid, N. J. (2020) Protein secondary structure determines the temporal relationship between folding and disulfide formation. Journal of Biological Chemistry, 295(8), pp. 2438-2448. (doi: 10.1074/jbc.RA119.011983) (PMID:31953323) (PMCID:PMC7039548)
2017
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)
2013
Robinson, P.J. and Woolhead, C.A. (2013) Post-translational membrane insertion of an endogenous YidC substrate. Biochimica et Biophysica Acta: Molecular Cell Research, 1833(12), pp. 2781-2788. (doi: 10.1016/j.bbamcr.2013.07.003) (PMID:23872420)
2012
Robinson, P.J. , Findlay, J.E. and Woolhead, C.A. (2012) Compaction of a prokaryotic signal-anchor transmembrane domain begins within the ribosome tunnel and is stabilized by SRP during targeting. Journal of Molecular Biology, 423(4), pp. 600-612. (doi: 10.1016/j.jmb.2012.07.023) (PMID:22867705)
Articles
Robinson, P. J. and Bulleid, N. J. (2020) Mechanisms of disulfide bond formation in nascent polypeptides entering the secretory pathway. Cells, 9(9), 1994. (doi: 10.3390/cells9091994) (PMID:32872499)
Cao, X., Lilla, S., Cao, Z., Pringle, M. A., Oka, O. B.V. , Robinson, P. J. , Szmaja, T., Van Lith, M., Zanivan, S. and Bulleid, N. (2020) The mammalian cytosolic thioredoxin reductase pathway acts via a membrane 1 protein to reduce ER-localised proteins. Journal of Cell Science, 133, jcs241976. (doi: 10.1242/jcs.241976) (PMID:32184267) (PMCID:PMC7197872)
Robinson, P. J. , Kanemura, S., Cao, X. and Bulleid, N. J. (2020) Protein secondary structure determines the temporal relationship between folding and disulfide formation. Journal of Biological Chemistry, 295(8), pp. 2438-2448. (doi: 10.1074/jbc.RA119.011983) (PMID:31953323) (PMCID:PMC7039548)
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)
Robinson, P.J. and Woolhead, C.A. (2013) Post-translational membrane insertion of an endogenous YidC substrate. Biochimica et Biophysica Acta: Molecular Cell Research, 1833(12), pp. 2781-2788. (doi: 10.1016/j.bbamcr.2013.07.003) (PMID:23872420)
Robinson, P.J. , Findlay, J.E. and Woolhead, C.A. (2012) Compaction of a prokaryotic signal-anchor transmembrane domain begins within the ribosome tunnel and is stabilized by SRP during targeting. Journal of Molecular Biology, 423(4), pp. 600-612. (doi: 10.1016/j.jmb.2012.07.023) (PMID:22867705)
