Joseph Matthew Rogers

Joseph Matthew Rogers

Associate Professor

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    ORCID: 0000-0002-1313-4089

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    1. Published

      Structure-activity relationship of ipglycermide binding to phosphoglycerate mutases

      Wiedmann, M., Dranchak, P. K., Aitha, M., Queme, B., Collmus, C. D., Kashipathy, M. M., Kanter, L., Lamy, L., Rogers, Joseph Matthew, Tao, D., Battaile, K. P., Rai, G., Lovell, S., Suga, H. & Inglese, J., 2021, In: The Journal of Biological Chemistry. 296, 14 p., 100628.

      Research output: Contribution to journal › Journal article › Research › peer-review

    2. Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains

      Wensley, B. G., Kwa, L. G., Shammas, S. L., Rogers, Joseph Matthew, Browning, S., Yang, Z. & Clarke, J., 30 Oct 2012, In: Proceedings of the National Academy of Sciences of the United States of America. 109, 44, p. 17795-17799 5 p.

      Research output: Contribution to journal › Journal article › Research › peer-review

    3. Protein folding: Adding a nucleus to guide helix docking reduces landscape roughness

      Wensley, B. G., Kwa, L. G., Shammas, S. L., Rogers, Joseph Matthew & Clarke, J., 26 Oct 2012, In: Journal of Molecular Biology. 423, 3, p. 273-283 11 p.

      Research output: Contribution to journal › Journal article › Research › peer-review

    4. Published

      De novo design of high-affinity binders of bioactive helical peptides

      Vázquez Torres, S., Leung, P. J. Y., Venkatesh, P., Lutz, I. D., Hink, F., Huynh, H. H., Becker, J., Yeh, A. H. W., Juergens, D., Bennett, N. R., Hoofnagle, A. N., Huang, E., MacCoss, M. J., Expòsit, M., Lee, G. R., Bera, A. K., Kang, A., De La Cruz, J., Levine, P. M., Li, X. & 10 others, Lamb, M., Gerben, S. R., Murray, A., Heine, P., Korkmaz, E. N., Nivala, J., Stewart, L., Watson, J. L., Rogers, Joseph Matthew & Baker, D., 2024, In: Nature. 626, 7998, p. 435-442

      Research output: Contribution to journal › Journal article › Research › peer-review

    5. Initiating ribosomal peptide synthesis with exotic building blocks

      Tsiamantas, C., Rogers, Joseph Matthew & Suga, H., 21 Apr 2020, In: Chemical Communications. 56, 31, p. 4265-4272 8 p.

      Research output: Contribution to journal › Review › Research › peer-review

    6. Ribosomal Incorporation of Aromatic Oligoamides as Peptide Sidechain Appendages

      Tsiamantas, C., Kwon, S., Rogers, Joseph Matthew, Douat, C., Huc, I. & Suga, H., 16 Mar 2020, In: Angewandte Chemie - International Edition. 59, 12, p. 4860-4864 5 p.

      Research output: Contribution to journal › Journal article › Research › peer-review

    7. Two immunoglobulin tandem proteins with a linking β-strand reveal unexpected differences in cooperativity and folding pathways

      Steward, A., Chen, Q., Chapman, R. I., Borgia, M. B., Rogers, Joseph Matthew, Wojtala, A., Wilmanns, M. & Clarke, J., 10 Feb 2012, In: Journal of Molecular Biology. 416, 1, p. 137-147 11 p.

      Research output: Contribution to journal › Journal article › Research › peer-review

    8. Slow, reversible, coupled folding and binding of the spectrin tetramerization domain

      Shammas, S. L., Rogers, Joseph Matthew, Hill, S. A. & Clarke, J., 21 Nov 2012, In: Biophysical Journal. 103, 10, p. 2203-2214 12 p.

      Research output: Contribution to journal › Journal article › Research › peer-review

    9. Peptide Folding and Binding Probed by Systematic Non-canonical Mutagenesis

      Rogers, Joseph Matthew, 2020, In: Frontiers in Molecular Biosciences. 7, 9 p., 100.

      Research output: Contribution to journal › Review › Research › peer-review

    10. Published

      In vivo modulation of ubiquitin chains by N -methylated non-proteinogenic cyclic peptides

      Rogers, Joseph Matthew, Nawatha, M., Lemma, B., Vamisetti, G. B., Livneh, I., Barash, U., Vlodavsky, I., Ciechanover, A., Fushman, D., Suga, H. & Brik, A., 2021, In: RSC Chemical Biology. 2, 2, p. 513-522 10 p.

      Research output: Contribution to journal › Journal article › Research › peer-review

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    ID: 238718408