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The Wuthrich Laboratory

Bryan Martin


Bryan Martin, Ph.D.

Graduate Student

brmartin@scripps.edu
phone: +1 858 784 8359
fax: +1 858 784 8013


Research Interests

My research focuses on structurally characterizing splicing factors and their complexes to improve our understanding of alternative splicing dysregulation that is observed in breast, lung and prostate cancers. I am investigating RNA Binding Motif 10 (RBM10), which contains a novel, tyrosine rich globular fold that mediates protein–protein interactions to other components of the spliceosome. This OCRE domain, and the homologous sequence in RBM5, is important for regulating alternative splicing of NUMB, FAS and CASP2 pre-mRNA. I have determined the molecular architecture of the RBM10 and RBM5 OCRE domains by NMR spectroscopy and I am currently using NMR, biochemical and biophysical techniques to investigate protein–protein complexes involving OCRE domains.

 Curriculum Vitae

2012 – 2017:  Graduate Student, Laboratory of Prof. Kurt Wüthrich, The Scripps Research Institute, La Jolla, CA.
2010 – 2012:  Research Assistant, Laboratory of Prof. Juila Oxford, Boise State University, Boise, ID.
2004 – 2010:  B.S. (Chemistry, Biology), Boise State University, Boise, ID.

Publications

Serrano, P., Dutta, S.K., Proudfoot, A., Mohanty, B., Sušac, L., Martin, B., Geralt, M., Jaroszewski, L., Godzik, A., Elsliger, M., Wilson, I.A., Wüthrich, K., (2016)  FEBS J. 283, 3870–3881. NMR in structural genomics to increase structural coverage of the protein universe.

Aoto, P.C., Martin, B.T., Wright, P.E. (2016) Sci. Rep. 6, 28655. NMR Characterization of Information Flow and Allosteric Communities in the MAP Kinase p38γ.

Martin, B.T., Serrano, P., Geralt, M. and Wüthrich K. (2016) Structure 24, 1–7. Nuclear magnetic resonance structure of a novel globular domain in RBM10 containing OCRE, the octamer repeat sequence motif.

Ryan, R.E., Martin, B., Mellor, L., Jacob, R.B., Tawara, K., McDougal, O.M., Oxford, J.T., Jorcyk, C.L. (2015) Cytokine 72, 71–85. Oncostatin M binds to extracellular matrix in a bioactive conformation: implications for inflammation and metastasis.

Martin, B.T., Chingas, G.C., McDougal, O.M. (2012) J. Magn. Reson. 218, 147–152. Origin and correction of magnetic field inhomogeneity at the interface in biphasic NMR samples.

Turner, M., Eidemiller, S., Martin, B., Narver, A., Marshall, J., Zemp, L., Cornell, K.A., McIntosh, J.M., McDougal, O.M. (2009) Bioorg. Med. Chem. 17, 5894–5899. Structural basis for alpha-conotoxin potency and selectivity.