Publications

 

Chen, Rey-Huei (September 2012) Nuclear Envelope Assembly and Disassembly During the Cell Cycle. In: eLS. John Wiley & Sons, Ltd: Chichester. DOI: 10.1002/9780470015902.a0022532 (Invited review).

Tseng, L.-C. and Chen, R.-H. 2011. Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor. Mol Biol Cell. 22, 3306-3317.

Hsieh, M.-T. and Chen, R.-H. 2011. Cdc48 and cofactors Npl4-Ufd1 are important for G1 progression during heat stress by maintaining cell wall integrity in Saccharomyces cerevisiae. PLoS One. 19, 6(4):e18988.

Chen, Y.-L. and Chen, R.-H. 2010. The AAA-ATPase Cdc48 and cofactor Shp1 promote chromosome bi-orientation by balancing Aurora B activity. J. Cell Sci. 123, 2025-2034.

Chen, R.-H. 2008. The spindle checkpoint in Xenopus laevis. Front. Biosci. 13, 2231- 2237 (Review).

Chen, R.-H. 2007. Dual inhibition of Cdc20 by the spindle checkpoint. J. Biomed. Sci. 14, 475-479 (Review).

Zhao, Y. and Chen, R.-H. 2006. Mps1 phosphorylation by MAP kinase is required for kinetochore localization of spindle-checkpoint proteins. Curr. Biol. 16, 1764-1769.

Chen, R.-H. 2004. Phosphorylation and activation of Bub1 on unattached chromosomes facilitate the spindle checkpoint. EMBO J. 23, 3113-3121.

Pan, J. and Chen, R.-H. 2004. Spindle checkpoint regulates Cdc20p stability in S. cerevisiae. Genes Dev. 18, 1439-1451.

Chung, E. and Chen, R.-H. 2003. Phosphorylation of Cdc20 is required for its inhibition by the spindle checkpoint. Nature Cell Biol. 5, 748-753.

Murphy, L.O., Smith, S., Chen, R.-H., Fingar, D.C., and Blenis J. 2002. Molecular interpretation of ERK signal duration by immediate early gene products. Nature Cell Biol. 4, 556-564.

Chen, R.-H. 2002. BubR1 is essential for kinetochore localization of other spindle checkpoint proteins and its phosphorylation requires Mad1. J. Cell Biol. 158, 487-796.

Chung, E. and Chen, R.-H. 2002. Spindle checkpoint requires Mad1-bound and Mad1-free Mad2. Mol. Biol. Cell 13, 1501-1511.

Sharp-Baker, H. and Chen, R.-H. 2001. Spindle checkpoint protein Bub1 is required for kinetochore localization of Mad1, Mad2, Bub3, and CENP-E, independently of its kinase activity. J. Cell Biol. 153, 1239-1250.

Chen, R.-H., Brady, D. M., Smith, D., Murray, A., and Hardwick, K. 1999. The spindle checkpoint of budding yeast depends on a tight complex between the Mad1 and Mad2 proteins. Mol. Biol. Cell. 10, 2607-2618.

Waters, J.C., Chen, R.-H., Murray, A.W., Gorbsky, G.J., Salmon, E.D., Nicklas, R.B. 1999. Mad2 binding by phosphorylated kinetochores links error detection and checkpoint action in mitosis. Curr. Biol.17, 649-52.

Hardwick, K.G., Li, R., Mistrot, C., Chen, R.-H., Dann, P., Rudner, A., Murray, A.W. 1999. Lesions in many different spindle components activate the spindle checkpoint in the budding yeast Saccharomyces cerevisiae. Genetics 152, 509-18.

Chen, R.-H., Shevchenko, A., Mann, M., and Murray, A. 1998. The spindle checkpoint protein Xmad1 recruits Xmad2 to unattached kinetochores. J. Cell Biol. 143, 283-295.

Gorbsky, G.J., Chen, R.-H., and Murray, A. 1998. Microinjection of anti-MAD2 protein antibody into normal mammalian cells in mitosis induces premature anaphase. J. Cell Biol. 141, 1193-1205.

Waters, J., Chen, R.-H., Murray, A., and Salmon, E.D. 1998. Mad2 monitors microtubule attachment to the kinetochore, not tension, and is necessary for mitotic arrest in response to taxol. J. Cell Biol. 141, 1181-1191.

Chen, R.-H. and Murray, A. 1997. Characterization of spindle assembly checkpoint in Xenopus egg extracts. Methods Enzymol. 283, 572-584.

Chen, R.-H., Waters, J. C., Salmon, E. D., and Murray, A. 1996. Association of spindle assembly checkpoint component XMAD2 with unattached kinetochores. Science 274, 242-246.

Chen, R.-H., Juo, P.-C., Curran, T., and Blenis, J. 1996. Phosphorylation of c-Fos at the C-terminus enhances its transforming activity. Oncogene 12(7), 1493-1502.

Chen, R.-H. 1995. RSK. in Guidebook to the small GTPases, pp165-168. eds. Zerial, M. and Huber, L. (Oxford University Press).

Papkoff, J., Chen, R.-H., Blenis, J., and Forsman, J. 1994. p42 mitogen-activated protein kinase and p90 ribosomal S6 kinase are selectively phosphorylated and activated during thrombin-induced platelet activation and aggregation. Mol. Cell. Biol. 14, 463-472.

Tsai, M., Chen, R.-H., Tam, S.-Y., Blenis, J., and Galli, S.J. 1993. Activation of MAP kinase, pp90rsk and pp70-S6 kinase in mouse mast cells by c-kit receptor tyrosine kinase or FceRI signaling. Eur. J. Immunol. 23, 3286-3291.

Chen, R.-H., Tung, R., and Blenis, J. 1993. Cytoplasmic to nuclear signal transduction by MAP kinase and RSK. Biochem. Society Transactions 21(4), 895-900. (Review)

Rivera, V.M., Misra, R.P., Miranti, C., Ginty, D.D., Chen, R.-H., Blenis, J. and Greenberg, M.E. 1993.  A growth factor-induced kinase cascade phosphorylates the serum response factor at a site that regulates its DNA binding activity. Mol. Cell. Biol. 13, 6260-6273.

Davis, I.J., Hazel, T.G., Chen, R.-H., Blenis, J., and Lau, L.F., 1993. Functional domains and phosphorylation of the orphan receptor Nur77. Mol. Endocrinol. 7, 953-964.

Chen, R.-H., Abate, C., and Blenis, J. 1993. Phosphorylation of the c-Fos transrepression domain by MAP kinase and RSK. Proc. Natl. Acad. Sci. USA 90, 10952-10956.

Chen, R.-H., Sarnecki, C. and Blenis, J. 1992. Nuclear localization and regulation of erk- and rsk-encoded protein kinases. Mol. Cell. Biol. 12, 915-927.

Chung, J., Chen, R.-H., and Blenis, J. 1991. Coordinate regulation of pp90rsk and a distinct protein-serine/threonine kinase activity that phosphorylates recombinant pp90rsk in vitro. Mol. Cell. Biol. 11, 1868-1874.

Chen, R.-H., Chung, J., and Blenis, J. 1991. Regulation of pp90rsk phosphorylation and S6 phosphotransferase activity in Swiss 3T3 cells by growth factor-, phorbol ester- and cyclic AMP-mediated signal transduction. Mol. Cell. Biol. 11, 1861-1867.

Chen, R.-H. and Blenis, J. 1990. Identification of Xenopus S6 protein kinase homologs (pp90rsk) in somatic cells: Phosphorylation and activation during initiation of cell proliferation. Mol. Cell. Biol. 10, 3204-3215.