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Journal Article

Limón, L. K., Shi, K., Dao, A., Rugloski, J., Tompkins, K. J., Aihara, H., Gordon, W. R., and Evans, R. L. (2023) The crystal structure of the human smacovirus 1 Rep domain. Acta Crystallogr F Struct Biol Commun. 79, 295-300

Everett, B. A., Litzau, L. A., Tompkins, K., Shi, K., Nelson, A., Aihara, H., Iii, R. L. Evans, and Gordon, W. R. (2019) Crystal structure of the Wheat dwarf virus Rep domain. Acta Crystallogr F Struct Biol Commun. 75, 744-749

Gordon, W. R., Vardar-Ulu, D., L'Heureux, S., Ashworth, T., Malecki, M. J., Sanchez-Irizarry, C., McArthur, D. G., Histen, G., Mitchell, J. L., Aster, J. C., and Blacklow, S. C. (2009) Effects of S1 cleavage on the structure, surface export, and signaling activity of human Notch1 and Notch2. PLoS One. 4, e6613

Anderson, M. J. M., Hayward, A. N., Smiley, A. T., Shi, K., Pawlak, M. R., Aird, E. J., Grant, E., Greenberg, L., Aihara, H., Evans, R. L., Ulens, C., and Gordon, W. R. (2024) Molecular basis of proteolytic cleavage regulation by the extracellular matrix receptor dystroglycan. Structure. 32, 1984-1996.e5

Tompkins, K. J., Houtti, M., Litzau, L. A., Aird, E. J., Everett, B. A., Nelson, A. T., Pornschloegl, L., Limón-Swanson, L. K., Evans, R. L., Evans, K., Shi, K., Aihara, H., and Gordon, W. R. (2021) Molecular underpinnings of ssDNA specificity by Rep HUH-endonucleases and implications for HUH-tag multiplexing and engineering. Nucleic Acids Res. 49, 1046-1064

Gordon, W. R., Roy, M., Vardar-Ulu, D., Garfinkel, M., Mansour, M. R., Aster, J. C., and Blacklow, S. C. (2009) Structure of the Notch1-negative regulatory region: implications for normal activation and pathogenic signaling in T-ALL. Blood. 113, 4381-90

Smiley, A. T., Tompkins, K. J., Pawlak, M. R., Krueger, A. J., Evans, R. L., Shi, K., Aihara, H., and Gordon, W. R. (2022) Watson-Crick Base-Pairing Requirements for ssDNA Recognition and Processing in Replication-Initiating HUH Endonucleases. mBio. 10.1128/mbio.02587-22

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The Northeastern Collaborative Access Team (NE-CAT) facility at the Advanced Photon Source at Argonne National Laboratory is managed by Cornell University and consists of eight member institutions:

Columbia University
Cornell University
Genentech
Harvard University
Memorial Sloan-Kettering Cancer Center
Massachusetts Institute of Technology
Rockefeller University
Yale University

Primary funding for this project comes from the National Institute of General Medical Sciences (NIGMS), a division of the National Institutes of Health (NIH). Additional financial support for NE-CAT comes from the member institutions.