Publications

Found 33 results
Filters: Author is Grant, Robert A  [Clear All Filters]
2020
Wang, B., Grant, R. A., and Laub, M. T. (2020) ppGpp Coordinates Nucleotide and Amino-Acid Synthesis in E. coli During Starvation.. Mol Cell. 10.1016/j.molcel.2020.08.005
Lite, T. - L. V., Grant, R. A., Nocedal, I., Littlehale, M. L., Guo, M. S., and Laub, M. T. (2020) Uncovering the basis of protein-protein interaction specificity with a combinatorially complete library. Elife. 10.7554/eLife.60924
2021
Hymel, D., Tsuji, K., Grant, R. A., Chingle, R. M., Kunciw, D. L., Yaffe, M. B., and Burke, T. R. (2021) Design and synthesis of a new orthogonally protected glutamic acid analog and its use in the preparation of high affinity polo-like kinase 1 polo-box domain - binding peptide macrocycles. Org Biomol Chem. 19, 7843-7854
Hwang, T., Parker, S. S., Hill, S. M., Ilunga, M. W., Grant, R. A., Mouneimne, G., and Keating, A. E. (2021) A distributed residue network permits conformational binding specificity in a conserved family of actin remodelers. Elife. 10.7554/eLife.70601
Baytshtok, V., Fei, X., Shih, T. - T., Grant, R. A., Santos, J. C., Baker, T. A., and Sauer, R. T. (2021) Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Cell Rep. 34, 108639
2022
Hwang, T., Parker, S. S., Hill, S. M., Grant, R. A., Ilunga, M. W., Sivaraman, V., Mouneimne, G., and Keating, A. E. (2022) Native proline-rich motifs exploit sequence context to target actin-remodeling Ena/VASP protein ENAH. Elife. 10.7554/eLife.70680
2023
Aguilar, F., Yu, S., Grant, R. A., Swanson, S., Ghose, D., Su, B. G., Sarosiek, K. A., and Keating, A. E. (2023) Peptides from human BNIP5 and PXT1 and non-native binders of pro-apoptotic BAK can directly activate or inhibit BAK-mediated membrane permeabilization. Structure. 31, 265-281.e7
2024
Yoon, J., Zhang, Y. Meng, Her, C., Grant, R. A., Ponomarenko, A. I., Ackermann, B. E., Hui, T., Lin, Y. - S., Debelouchina, G. T., and Shoulders, M. D. (2024) The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure. Sci Adv. 10, eadl6144

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