NECAT Beamline

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 seven member institutions:

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

    NIGMS at a Glance.

    Supported by:

    National Institutes of Health
    National Institute of General Medical Sciences

    Publications from the Eiger Detector

     

    Babault, N., Allali-Hassani, A., Li, F., Fan, J., Yue, A., Ju, K., Liu, F., Vedadi, M., Liu, J., and Jin, J. (2018) Discovery of Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (Nnmt), J Med Chem 61, 1541-1551.
    https://www.ncbi.nlm.nih.gov/pubmed/29320176

    Coleman, J. A., and Gouaux, E. (2018) Structural Basis for Recognition of Diverse Antidepressants by the Human Serotonin Transporter, Nat Struct Mol Biol.
    https://www.ncbi.nlm.nih.gov/pubmed/29379174

    Dawson, T. K., Dziedzic, P., Robertson, M. J., Cisneros, J. A., Krimmer, S. G., Newton, A. S., Tirado-Rives, J., and Jorgensen, W. L. (2017) Adding a Hydrogen Bond May Not Help: Naphthyridinone Vs Quinoline Inhibitors of Macrophage Migration Inhibitory Factor, ACS Med Chem Lett 8, 1287-1291.
    https://www.ncbi.nlm.nih.gov/pubmed/29259749

    Goodman, M. C., Xu, S., Rouzer, C. A., Banerjee, S., Ghebreselasie, K., Migliore, M., Piomelli, D., and Marnett, L. J. (2018) Dual Cyclooxygenase-Fatty Acid Amide Hydrolase Inhibitor Exploits Novel Binding Interactions in the Cyclooxygenase Active Site, J Biol Chem.
    https://www.ncbi.nlm.nih.gov/pubmed/29326169

    Ha, B. H., and Boggon, T. J. (2017) The Crystal Structure of Pseudokinase Peak1 (Sugen Kinase 269) Reveals an Unusual Catalytic Cleft and a Novel Mode of Kinase Fold Dimerization, J Biol Chem.
    https://www.ncbi.nlm.nih.gov/pubmed/29212708

    Lam, K. H., Qi, R., Liu, S., Kroh, A., Yao, G., Perry, K., Rummel, A., and Jin, R. (2017) The Hypothetical Protein P47 of Clostridium Botulinum E1 Strain Beluga Has a Structural Topology Similar to Bactericidal/Permeability-Increasing Protein, Toxicon.
    https://www.ncbi.nlm.nih.gov/pubmed/29042313

    May, J. M., Owens, T. W., Mandler, M. D., Simpson, B. W., Lazarus, M. B., Sherman, D. J., Davis, R. M., Okuda, S., Massefski, W., Ruiz, N., and Kahne, D. (2017) The Antibiotic Novobiocin Binds and Activates the Atpase That Powers Lipopolysaccharide Transport, J Am Chem Soc 139, 17221-17224.
    https://www.ncbi.nlm.nih.gov/pubmed/29135241

    Rezaei Araghi, R., Bird, G. H., Ryan, J. A., Jenson, J. M., Godes, M., Pritz, J. R., Grant, R. A., Letai, A., Walensky, L. D., and Keating, A. E. (2018) Iterative Optimization Yields Mcl-1-Targeting Stapled Peptides with Selective Cytotoxicity to Mcl-1-Dependent Cancer Cells, Proc Natl Acad Sci U S A 115, E886-E895.
    https://www.ncbi.nlm.nih.gov/pubmed/29339518

    Schaefer, K., Owens, T. W., Kahne, D., and Walker, S. (2018) Substrate Preferences Establish the Order of Cell Wall Assembly in Staphylococcus Aureus, J Am Chem Soc 140, 2442-2445.
    https://www.ncbi.nlm.nih.gov/pubmed/29402087

    Xiong, Y., Li, F., Babault, N., Wu, H., Dong, A., Zeng, H., Chen, X., Arrowsmith, C. H., Brown, P. J., Liu, J., Vedadi, M., and Jin, J. (2017) Structure-Activity Relationship Studies of G9a-Like Protein (Glp) Inhibitors, Bioorg Med Chem 25, 4414-4423.
    https://www.ncbi.nlm.nih.gov/pubmed/28662962

    Yoo, J., Mashalidis, E. H., Kuk, A. C. Y., Yamamoto, K., Kaeser, B., Ichikawa, S., and Lee, S. Y. (2018) Glcnac-1-P-Transferase-Tunicamycin Complex Structure Reveals Basis for Inhibition of N-Glycosylation, Nat Struct Mol Biol.
    https://www.ncbi.nlm.nih.gov/pubmed/29459785