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Methods (San Diego, Calif.)|December 15, 2010
Studying the effects of chaperones on amyloid fibril formationHong Zhang, Li-Qiong Xu, Sarah PerrettThe Journal of Biological Chemistry|September 17, 2004
The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar formsMing Bai, Jun-Mei Zhou, Sarah PerrettThe Biochemical Journal|September 10, 2008
Characterization of the activity and folding of the glutathione transferase from Escherichia coli and the roles of residues Cys(10) and His(106)Xin-Yu Wang, Zai-Rong Zhang, Sarah PerrettBiochemical Society Transactions|July 3, 2025
Single-molecule study of the dynamics of the molecular chaperone Hsp70 during the functional cycleHuimin Hu, Ming Yang, Sarah Perrett, et al.Emerging Topics in Life Sciences|March 4, 2021
Studying protein folding in health and disease using biophysical approachesHong Zhang, Weibin Gong, Si Wu, et al.The Journal of Biological Chemistry|January 1, 2014
Retinoblastoma-binding protein 1 has an interdigitated double Tudor domain with DNA binding activityWeibin Gong, Jinfeng Wang, Sarah Perrett, et al.Biochemical Society Transactions|September 23, 2011
The yeast prion protein Ure2: insights into the mechanism of amyloid formationLi-Jun Chen, Elizabeth B Sawyer, Sarah PerrettThe Journal of Biological Chemistry|January 6, 2005
Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refoldingChuan-Peng Liu, Sarah Perrett, Jun-Mei ZhouChemical Communications (Cambridge, England)|June 27, 2017
A co-expression strategy to achieve labeling of individual subunits within a dimeric protein for single molecule analysisFei Lou, Jie Yang, Si Wu, et al.Pageof 9