1. Fung, H.Y., Fu, S.C. and Chook, Y.M. Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals. (2017) eLife;6:e23961.
  2. Hing, Z.A., Fung, H.Y., Ranganathan, P., Mitchell, S., El-Gamal, D., Woyach, J.A., Williams, K., Goettl, V.M., Smith, J., Yu, X., Meng, X., Sun, Q., Cağatay, T., Lehman, A.M., Lucas, D.M., Baloglu, E., Shacham, S., Kauffman, M.G., Byrd, J.C., Chook, Y.M., Garzon, R. and Lapalombella, R. Next-generation XPO1 inhibitor shows improved efficacy and in vivo tolerability in hematological malignancies. (2016) Leukemia, 30(12):2364-2372.
  3. Soniat, M. and Chook, Y.M. Karyopherin-β2 recognition of a PY-NLS variant that lacks the proline-tyrosine Motif. (2016) Structure, 24(10):1802-1809.
  4. Soniat, M., Cağatay, T. and Chook, Y.M. Recognition elements in the histone H3 and H4 tails for seven different importins. (2016) J Biol Chem, 291(40):21171-21183.
  5. Volpon, L., Culjkovic-Kraljacic, B., Osborne, M.J., Ramteke, A., Sun, Q., Niesman, A., Chook, Y.M. and Borden K.L. Importin 8 mediates m7G cap-sensitive nuclear import of the eukaryotic translation initiation factor eIF4E. (2016) Proc Natl Acad Sci U S A, 113(19):5263-8.
  6. Fung, H.Y., Fu, S.C., Brautigam, C.A. and Chook, Y.M. Structural determinants of nuclear export signal orientation in binding to exportin CRM1. (2015) eLife;4:e10034.
  7. Soniat, M. and Chook, Y.M. Nuclear localization signals for four distinct karyopherin-β nuclear import systems. (2015) Biochemical Journal, 468(3):353-362.
  8. Haines, J.D., Herbin, O., Moy, G.A., Vidaurre, O.G., Adula, K., Sun, Q., Fung, H.Y.J., Albrecht, S., Alexandropoulos, K., McCauley, D., Chook, Y.M., Kuhlmann, T., Kidd, G.J., Shacham, S. and Casaccia, P. Nuclear export inhibitors avert progression in preclinical models of inflammatory demyelination. (2015) Nat. Neuroscience, 18(4):511-520.
  9. Xu, D., Marquis, K., Pei, J., Fu, S.C., Cağatay, T., Grishin, N.V. and Chook, Y.M. LocNES: a computational tool for locating classical NESs in CRM1 cargo proteins. (2015) Bioinformatics, 31(9):1357-1367.
  10. Fung, H. Y. J. and Chook, Y. M. Atomic basis of CRM1-cargo recognition, release and inhibition. (2014) Seminars in Cancer Biology, 27:52-61.
  11. Bernis, C., Swift-Taylor, B., Nord, M., Carmona, S., Chook, Y.M., Forbes, D.J. Transportin Acts to Regulate Mitotic Assembly Events by Target Binding rather than Ran Sequestration. (2014) Mol Biol Cell. 25(7):992-1009.
  12. Soniat, M., Sampathkumar, P., Collett, G., Gizzi, A.S., Banu, R.N., Bhosle, R.C., Chamala, S., Chowdhury, S., Fiser, A., Glenn, A.S., Hammonds J., Hillerich, B., Khafizov, K., Love, J.D., Matikainen, B., Seidel, R.D., Toro, R., Rajesh Kumar, P., Bonanno J.B., Chook, Y.M., Almo, S.C. Crystal structure of human Karyopherin β2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2. (2013) J Struct Funct Genomics, 14(2):31-5.
  13. Sun, Q, Carrasco, Y.P., Hu, Y., Guo, X., Mirzaei, H., Macmillan, J., Chook, Y.M. Nuclear export inhibition through covalent conjugation and hydrolysis of Leptomycin B by CRM1. (2013) Proc. Natl. Acad. Sci. USA, 10(4):1303-8.
  14. Etchin, J. Sun, Q., Kentsis A., Farmer A., Zhang Z.C., Sanda T., Mansour M.R., Barcelo C., McCauley D., Kauffman M., Shacham S., Christie A.L., Kung A.L., Rodig S.J., Chook Y.M., and Look A.T. Antileukemic activity of nuclear export inhibitors that spare normal hematopoietic cells. (2013) Leukemia, 27(1):66-74.
  15. Lapalombella, R., Sun, Q., Williams, K., Tangeman, L., Jha, S., Zhong, Y., Goettl, V., Mahoney, E., Berglund, C., Gupta, S., Farmer, A., Mani, R., Johnson, A.J., Lucas, D., Mo, X., Daelemans, D., Sandanayaka, V., Shechter, S., McCauley, D., Shacham, S., Kauffman, M., Chook, Y.M., Byrd, J.C. Selective inhibitors of nuclear export (SINE) show that CRM1/XPO1 is a target in chronic lymphocytic leukemia. (2012) Blood, 120(23):4621-34.
  16. Xu, D., Grishin N.V. and Chook, Y.M. NESdb: a database of NES-containing CRM1 cargoes. (2012) Mol. Biol. Cell, 23(18):3673-6.
  17. Xu, D., Farmer, A. , Collet G., Grishin N.V. and Chook, Y.M. Sequence and structural analyses of nuclear export signals in the NESdb database. (2012) Mol. Biol. Cell, 23(18):3677-93.
  18. Zhang Z.C. and Chook Y.M. Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS). (2012) Proc. Natl. Acad. Sci. USA, 109(30):12017-21
  19. Chook, Y. M. and Süel, K. E. Nuclear import by karyopherin-βs: Recognition and inhibition. (2011) Biochim Biophys Acta. 1813(9):1593-606.
  20. Zhang Z.C., Satterly N., Fontoura B.M., and Chook Y.M. Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1. (2011) Mol. Biol. Cell, 22(23):4657-68.


  1. Xu, D., Farmer, A. and Chook, Y.M. Recognition of nuclear targeting signals by Karyopherin-β proteins. (2010) Curr Opin Struct Biol. 20(6):782-90.
  2. Süel, K. E. and Chook, Y. M. Kap104p imports the PY-NLS-containing transcription factor Tfg2p into the nucleus. (2009) J. Biol. Chem. 284(23):15416-24.
  3. Dong, X., Biswas, A. and Chook, Y. M. (2009) Structural basis for assembly and disassembly of the CRM1 nuclear export complex. Nat. Struc. & Mol. Biol., 16(5):558-560.
  4. Dong, X., Biswas, A., Süel, K. E, Jackson, L. K., Martinez, R., Gu, H. and Chook, Y. M. Structural basis for leucine-rich nuclear export signal recognition by CRM1. (2009) Nature, 458: 1136-1141.
  5. Zhang, Z. C. and Chook, Y. M. Structural Analysis of Karyopherin-mediated nucleocytoplasmic transport. (2008) Nuclear Transport, edited by Ralph Kehlenbach, Landes Bioscience.
  6. Süel, K. E., Gu, H. and Chook, Y. M. Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals. (2008) PLoS Biology, 6(6):e137.
  7. Cansizoglu, A. E. and Chook, Y. M. Conformational heterogeneity of Karyopherinβ2 is segmental. (2007) Structure, 15(11):1431-1441.
  8. Cansizoglu, A. E., Lee, B. J., Zhang, Z. C., Fontoura, B. M. A. and Chook, Y. M. Structure-based design of a pathway-specific nuclear import inhibitor. (2007) Nat. Struc. & Mol. Biol., 14(5):452-454.
  9. Süel, K. E., Cansizoglu, A. E. and Chook, Y. M. Atomic resolution structures in nuclear transport. (2006) Methods, 39(4):342-5.
  10. Lee, B. J., Cansizoglu, A. E., Süel, K. E., Louis, T. H., Zhang, Z. and Chook, Y. M. Rules for nuclear localization sequence recognition by Karyopherinβ2. (2006) Cell, 126:543-558.
  11. Faria, A.M.C, Levay, A., Kamphorst, A. O., Rosa, M. L. P., Nussenzveig, D. R., Balkan, W., Chook, Y. M., Wang, Y., Levy, D. E., and Fontoura, B.M.A. The nucleoporin Nup96 is required for proper expression of interferon-regulated proteins and functions. (2006) Immunity, 24(3):295-304.
  12. Wang W., Yang X., Kawai T., de Silanes I.L., Mazan-Mamczarz K., Chen P , Chook Y.M., Quensel C., Kohler M. and Gorospe M. AMP-activated protein kinase-regulated phosphorylation and acetylation of importin alpha1: involvement in the nuclear import of RNA-binding protein HuR. (2004) J. Biol Chem. 2004 279(46):48376-88.
  13. Chook, Y.M., Jung, A., Rosen, M.K. and Blobel, G. Uncoupling Ran binding and substrate dissociation in the Karyopherin b2 nuclear import pathway. (2002) Biochemistry 41, 6955-6966.
  14. Chook, Y.M. and Blobel, G. Karyopherins and nuclear import. (2001) Current Opinions in Structural Biology 11(6):703-715.
  15. Chook, Y.M., Cingolani, G., Conti, E., Stewart, M., Vetter, I., Wittinghofer, A. Pictures in cell biology. Structures of nuclear-transport components. (1999) Trends Cell Biol. 9(8), 310-311.
  16. Chook, Y.M. and Blobel, G. Structure of the nuclear transport complex karyopherin-β2-Ran•GppNHp. (1999) Nature 399, 230-237.

Earlier Publications

  1. Chook, Y.M., Lipscomb, W.N. and Ke, H. Detection and Use of Pseudo Translation in Determination of Protein Structures. (1998) Acta Cryst. D54, 822-827.
  2. Lipscomb, W.N., Chook, Y.M. and Ke, H. Chorismate Mutase, essentially a template enzyme. (1997) Chapter 17, 235-244. Biological NMR Spectroscopy. John L. Markley, Stanley Opella (editors) and Richard Ernst. Oxford University Press.
  3. Kubiseski, T.J., Chook, Y.M., Parris, W.E., Rozakis-Adcock, M. and Pawson, T. High Affinity Binding of the Pleckstrin Homology Domain of mSos1 to Phosphatidylinositol (4,5) Bisphosphate. (1997) J. Biol. Chem. 272 (3), 1799-1804.
  4. Chook, Y.M., Gish, G.D., Kay, C.Y., Pai, E.F. and Pawson, T. The Grb2-mSos1 Complex Binds Phosphopeptides with Higher Affinity than Grb2. (1996) J. Biol. Chem. 271(48), 30472-30478.
  5. Chook, Y.M., Ke, H., Gray, J.V. and Lipscomb, W.N. The monofunctional chorismate mutase from Bacillus subtilis: Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications on the mechanism of enzymatic reaction. (1994) J. Mol. Biol. 240(5), 476-500.
  6. Chook, Y.M., Ke, H. and Lipscomb, W.N. Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog. (1993) Proc. Natl. Acad. Sci. USA, 90, 8600-8603.
  7. Stevens, R.C., Chook, Y.M., Cho, C.Y., Lipscomb, W.N. and Kantrowitz, E.R. Escherichia coli aspartate carbamoyltransferase: The probing of crystal structure analysis via site-specific mutagenesis. (1991) Protein Engineering 4(4), 391-408.
  8. Chey, J., Choe, H.S., Chook, Y.M., Jensen, E., Seida, P.R. and Francl, M.M. p-Complexes of alkenes to trivalent aluminum. (1990) Organometallics, 9(9), 2430-2436.