General
Sarah Perrett, PhD
Professor, Institute of Biophysics, CAS

Email: sperrett [at] ibp.ac.cn
Telephone: 010-64889870
Address: Institute of Biophysics, Chinese Academy of Sciences, 
15 Datun Road, Chaoyang District, Beijing 
Postcode: 100101

Research Areas

Protein folding, post-translational modification and quality control
Molecular mechanism of prion propagation
Structure and assembly of functional amyloids
Bionanomaterials

Education

MA, PhD - University of Cambridge

Experience

   
Work Experience

1996-1997, Post-doctoral Research Associate, University of Cambridge

1997-2000, College Research Fellow, University of Cambridge

2000-2003, 1851/Royal Society Research Fellow, Institute of Biophysics, CAS

2003-present, PI, Institute of Biophysics, CAS

2015-present, Professor, University of the Chinese Academy of Science




Teaching Experience

2015-present UCAS Undergraduate Biochemistry (Protein Structure, Function & Folding; Enzymes)

2013-2015       Peking University Undergraduate Biochemistry (Seminar Class: "Classical Papers in Biochemistry")


Honors & Distinctions


2017    Fellow of the Royal Society of Chemistry (FRSC)

2015    Queen's New Years Honours List: OBE for services to UK/China relations in the scientific field

2015    CAS Young International Scientific Collaborator Prize (with Prof. T. Knowles, University of Cambridge)



Selected Publications

1.      Yao Q.Q., Wen, J.T., Perrett, S. & Wu, S.* (2022). Distinct lipid membrane-mediated pathways of Tau assembly revealed by single-molecule analysis. Nanoscale, 14, 4604-4613.

2.      Zhang, H.*, Gong, W., Wu, S. & Perrett, S.* (2022). Hsp70 in redox homeostasis. Cells 11, 829.

3.      Wen, J., Hong, L., Krainer, G., Yao, Q.Q., Knowles, T.P.J., Wu, S.* & Perrett, S.* (2021). Conformational expansion of Tau in condensates promotes irreversible aggregation. J. Am. Chem. Soc. 143, 13056-13064.

4.      Zhang, H., Gong, W., Wu, S., & Perrett, S.* (2021). Studying protein folding in health and disease using biophysical approaches. Emerg. Top. Life Sci. 5, 29-38.

5.      Yang, J., Gong, W., Wu, S., Zhang, H.* & Perrett, S.* (2021). PES inhibits human inducible Hsp70 by covalent targeting of cysteine residues in the substrate binding domain. J. Biol. Chem. 296, 100210.

6.      Yang, J., Perrett, S., Wu, S.* (2021). Single Molecule Characterization of Amyloid Oligomers. Molecules 26, 948.

7.      Yao, X., Chen, C., Wang, Y., Dong S., Liu, Y.J., Li, Y., Cui, Z., Gong, W., Perrett, S., Yao, L., Lamed, R., Bayer, E.A., Cui, Q., Feng, Y.G.* (2020). Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules. Science Advances 6, eabd7182.

8.      Yang, J., Dear, A.J., Yao, Q., Liu, Z., Dobson, C.M., Knowles, T.P.J., Wu, S.* & Perrett, S.* (2020). Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils. Nanoscale 12, 18663-18672. (On the inside cover)

9.      Yang, J., Zhang, H.*, Gong, W., Liu, Z., Wu, H., Hu, W., Chen, X., Wang, L., Wu, S., Chen, C.* & Perrett, S.* (2020). S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal α-helical lid. J. Biol. Chem. 295, 8302-8324.

10.   Dear, A.J., Michaels, T.C.T., Meisl, G., Klenerman, D., Wu, S., Perrett, S., Linse, S., Dobson, C.M., and Knowles, T.P.J.* (2020). Kinetic diversity of amyloid oligomers. PNAS 117, 12087-12094.

11.   Wu, S. Hong, L., Wang, Y., Yang, J., Yang J., Zhang, H. & Perrett, S.* (2020). A kinetic view of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function. PNAS 117, 7814-7823.

12.   Yao, Q., Hong, L., Wu, S.* & Perrett, S.* (2020). Distinct microscopic mechanisms for the accelerated aggregation of pathogenic Tau mutants revealed by kinetic analysis. PhysChemChemPhys 22, 241-7249.

13.   Yang, J., Dear, A.J., Michaels, T.C.T., Dobson, C.M., Knowles, T.P.J.*, Wu, S.* & Perrett, S.* (2018). Direct observation of oligomerization by single molecule fluorescence reveals a multi-step aggregation mechanism for the yeast prion protein Ure2. J. Am. Chem. Soc. 140, 2493-2503.

14.   Gong, W., Hu, W., Xu, L., Wu, H., Wu, S., Zhang, H., Wang, J., Jones, GW.* & Perrett, S.* (2018). The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast. J. Biol. Chem. 293, 17663-17675.

15.   Xu, L., Gong, W.*, Cusack, S.A., Wu, H., Loovers, H.M., Zhang, H., Perrett, S., & Jones G.W.* (2018). The β6/β7 region of the Hsp70 substrate-binding domain mediates heat shock response and prion propagation. Cell. Mol. Life Sci. 75, 1445-1459.

16.   Lou, F., Yang, J., Wu, S.* & Perrett, S.* (2017). A co-expression strategy to achieve labeling of individual subunits within a dimeric protein for single molecule analysis. ChemComm 53, 7971-8094. (On the Cover)

17.   Yang, W., Willemse J., Sawyer E.B., Lou F., Gong, W., Zhang, H., Gras, S.L.*, Claessen, D.* & Perrett, S.* (2017). The propensity of the bacterial rodlin protein RdlB to form amyloid fibrils determines its function in Streptomyces coelicolor. Scientific Reports 7, 42867.

18. Zhang, H., Yang, J., Si, W., Gong, W., Chen, C.* & Perrett, S.* (2016). Glutathionylation of the bacterial Hsp70 chaperone DnaK provides a link between oxidative stress and the heat shock response. J. Biol. Chem. 291, 6967-6981. (Selected for JBC “Protein Folding in the Cell” virtual issue.)

19.      Zhou, X.M., Shimanovich, U., Herling, T.W., Wu, S., Dobson, C.M., Knowles, T.P.J.* & Perrett, S.* (2015). Enzymatically-active microgels from self-assembling protein nanofibrils for microflow chemistry. ACS Nano 9, 5772-5781. (Highlighted in Asian Scientist Magazine.)

20.      Rees, J.S., Li, X.W., Perrett, S.,* Lilley, K.S.* & Jackson, A.P.* (2015). Protein neighbours and proximity proteomics. Molecular & Cellular Proteomics 14, 2848-2856. (Invited Review)