Publications

  1. Adelakun N.*, Parrish J.*, Chu N., “Analyzing protein posttranslational modifications using enzyme-catalyzed expressed protein ligation”. Methods in Enzymology 2023, 682:319-350.
  2. Bae H., Viennet T., Park E., Chu N., Salguero A., Eck M., Arthanari H., Cole P., “PH Domain-Mediated Autoinhibition and Oncogenic Activation of Akt”. eLife 2022, 11:e80148
  3. Butts M., Chu N., “Utilizing a Baculovirus/Insect Cell Expression System and Expressed Protein Ligation (EPL) for Protein Semisynthesis”. Current Protocols 2022
  4. Salguero A., Chen M., Balana A., Chu N., Jiang H., Palanski B., Bae H., Wright K., Nathan S., Zhu H., Gabelli S., Pratt M., Cole P., “Multifaceted Regulation of Akt by Diverse C‑Terminal Posttranslational Modifications”. ACS Chemical Biology 2021
  5. Chu N., Cole P., “Protein semisynthesis”. In: Total Chemical Protein Synthesis. Brik A, Dawson P, Liu L, editors. Weinheim, Germany: Wiley-VCH. Chapter 11, 2021.
  6. Chu N.*, Viennet T.*, Bae H., Salguero A., Boeszoermenyi A., Arthanari H., Cole P. “Structural determinants of PH domain-mediated regulation of Akt revealed by segmental labeling”. eLife 2020, 9:e59151
  7. Hsu JW., Bai M., Li K., Yang JS., Chu N., Cole P., Eck M., Li J., Hsu V. “The protein kinase Akt acts as a coat adaptor in endocytic recycling”. Nature Cell Biology 2020, 22:927-933.
  8. Cole P., Chu N., Salguero A., Bae H. “Aktivation mechanisms”. Current Opinion in Structural Biology, 2019, 59: 47-53.
  9. Miller M., Maheshwari S., Shi W., Gao Y., Chu N., Soares A., Cole P., Amzel M., Fuchs M., Jakonic J., Gabelli S. “Getting the most out of your crystals: Data collection at the new high-flux, microfocus MX beamlines at NSLS-II”. Molecules, 2019, 24: 496
  10. Chu N., Salguero A., Liu A., Chen Z., Dempsey D., Ficarro S., Alexander W., Marto J., Li Y., Amzel M., Gabelli S., Cole P. “Akt kinase activation mechanisms revealed using protein semisynthesis”. Cell, 2018, 174: 897-907.
  11. Henager S.*, Chu N.*, Chen Z., Bolduc D., Dempsey D., Hwang Y., Wells J., Cole P. “Enzyme-catalyzed expressed protein ligation”. Nature Methods, 2016, 13: 925-927.
  12. Taylor M.S., Dempsey D.R., Hwang Y., Chen Z., Chu N., Boeke J.D., Cole P.A. “Mechanistic analysis of ghrelin-O-acyltransferase using substrate analogs”. Bioorganic Chemistry, 2015, 62: 64-73.
  13. Chu N. and Cole P. “Switching immune signals on and off”. eLife 2015, 4: e07204.
  14. Chu N., Shabbir W., Bove-Fenderson E., Araman C., Lemmens-Gruber R., Harris A.D., and Becker C.F.W. A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes. Journal of Biological Chemistry, 2014, 289(43):30144-60.
  15. Tripsianes K.*, Chu N.*, Friberg A., Sattler M. and Becker C. “Studying Weak and Dynamic Interactions of Posttranslationally Modified Proteins using Expressed Protein Ligation”. ACS Chemical Biology, 2014, 9:347-352.
  16. Schwaighofer A., Kotlowski C., Araman C., Chu N., Mastrogiacomo R., Becker C., Pelosi P., Knoll W., Larisika M., Nowak C. “Honey bee Odorant Binding Protein 14: Effects on Thermal Stability upon Odorant Binding revealed by FT-IR Spectroscopy and CD Measurements”. European biophysics journal, 2014, 43:105-112.
  17. Chu N., Becker C.F. “Recombinant expression of soluble murine prion protein for C-terminal modification”. FEBS Letters, 2013, 587, 430-435.
  18. Chu N.*, Olschewski D.*, Seidel R., Winklhofer K.F., Tatzelt J., Engelhard M., Becker C.F. “Protein immobilization on liposomes and lipid-coated nanoparticles by protein trans-splicing”. Journal of Peptide Science, 2010, 16: 582–588.
  19. Chu N., BeckerF. “Semisynthesis of membrane-attached prion proteins”. Methods in Enzymology, 2009, 462: 177-193.
  20. Bergbrede, Chuky N., Schoebel S., Blankenfeldt W., Geyer M., Fuchs E., Goody R.S, Barr F. and Alexandrov K. “Biophysical analysis of the interaction of Rab6a GTPase with its effector domains”. Journal of Biological Chemistry, 2009, 284: 2628-2635.

(*: equal contributions)