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Dr. Rita P.-Y.  Chen
Associate Research Fellow
Room 504, Institute of Biological Chemistry, Academia Sinica
128, Academia Road Sec. 2, Nankang, Taipei 115, Taiwan
TEL: +886-2-27855696 ext. 5040
FAX: +886-2-2788-9759
Rita P.-Y. Chen's Website

My research interest is regarding protein folding and misfolding behaviors in order to answer how proteins can fold into its native structure and how certain proteins can misfold and cause disease. Studies about protein folding are mainly the development of new methodologies to explore the folding process in order to unravel the intrinsic folding properties. Studies about protein misfolding are focus on two diseases: prion disease and Alzheimer’s disease. We are interested in studying the mechanism of amyloid fibril formation, factors influencing molecular assembly, designing inhibitor for amyloid formation, and species barrier in prion disease.

1993,09 - 1998,04 Ph. D, Department of Biochemistry, University of Cambridge, UK
1989,09 - 1991,06 M. Sc., Institute of Biochemical Sciences, National Taiwan University
1985,10 - 1989,06 B. S., Department of Agricultural Chemistry, National Taiwan University

2010,05 - present Associate Research Fellow, Institute of Biological Chemistry, Academia Sinica
2003,04 - 2010,05 Assistant Research Fellow, Institute of Biological Chemistry, Academia Sinica
1999,06 - 2003,03 postdoctor, Institute of Chemistry, Academia Sinica
1992,08 - 1993,07 Research Assistant, Institute of Biological Chemistry, Academia Sinica

    Publications List
An intranasally delivered peptide drug ameliorates cognitive decline in Alzheimer transgenic mice.
Cheng YS, Chen ZT, Liao TY, Lin C, Shen HC, Wang YH, Chang CW, Liu RS, Chen RP, Tu PH EMBO molecular medicine (2017)
Revealing structural changes of prion protein during conversion from alpha-helical monomer to beta-oligomers by means of ESR and nanochannel encapsulation.
Yang, C., Lo, W. L., Kuo, Y. H., Sang, J. C., Lee, C. Y., Chiang, Y. W. & Chen, R. P. ACS Chem Biol (2015)
Thioflavin T and its photo-irradiative derivatives: Exploring their spectroscopic properties in the absence and presence of amyloid fibrils.
Hsu, J. C., Chen, H. L., Snoeberger, R. C., Luh, F. Y., Lim, T. S., Hsu, C. & Chen, R. P. J Phys Chem B (2013)
Observation of protein folding/unfolding dynamics of ubiquitin trapped in agarose gel by single-molecule FRET.
Yang, L. L., Kao, M. W., Chen, H. L., Lim, T. S., Fann, W. & Chen, R. P. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS (2012)
Slow spontaneous α-to-β structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein.
Sang, J. C., Lee, C. Y., Luh, F. Y., Huang, Y. W., Chiang, Y. W. & Chen, R. P. Prion (2012)
Leu-138 in the bovine prion peptide fibrils is involved in the seeding discrimination related to codon-129 M/V polymorphism in the prion peptide seeding experiment.
Liao TY, Lee LY, Chen RP FEBS journal (2011)
A highly sensitive peptide substrate for detecting two Abeta-degrading enzymes: Neprilysin and insulin-degrading enzyme.
Chen PT, Liao TY, Hu CJ, Wu ST, Wang SS, Chen RP Journal of neuroscience methods (2010)
A new amyloid-like beta-aggregate with amyloid characteristics, except fibril morphology.
Chang ES, Liao TY, Lim TS, Fann W, Chen RP JOURNAL OF MOLECULAR BIOLOGY (2009)
Quantifying the Sequence-Dependent Species Barrier between Hamster and Mouse Prions.
Measuring the refolding of beta-sheets with different turn sequences on a nanosecond time scale.
Chen, R.P., Huang, J.J., Chen, H.L., Jan, H., Velusamy, M., Lee, C.T., Fann, W.S., Larsen, R.W., and Chan, S.I. Proc. Natl. Acad. Sci. USA (2004)

Updated 2017.03.08

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