Showing results (21-30 of 88) with videos related to
Sort By:
Pageof 9
Chemical 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.Nanoscale|March 9, 2022
Distinct lipid membrane-mediated pathways of Tau assembly revealed by single-molecule analysisQiong-Qiong Yao, Jitao Wen, Sarah Perrett, et al.The Biochemical Journal|November 25, 2010
Flexibility of the Ure2 prion domain is important for amyloid fibril formationYong Yu, Hai-Yan Wang, Ming Bai, et al.Physical Chemistry Chemical Physics : PCCP|March 25, 2020
Distinct microscopic mechanisms for the accelerated aggregation of pathogenic Tau mutants revealed by kinetic analysisQiong-Qiong Yao, Liu Hong, Si Wu, et al.Protein Science : a Publication of the Protein Society|October 19, 2023
Interaction between huntingtin exon 1 and HEAT repeat structure probed by chimeric model proteinsHong Zhang, Si Wu, Laura S Itzhaki, et al.Biochimie|October 13, 2006
Characterisation of the fibrinogenolytic properties of the buccal gland secretion from Lampetra japonicaRong Xiao, Qing-Wei Li, Sarah Perrett, et al.Biomolecular NMR Assignments|February 16, 2015
Resonance assignments for the substrate binding domain of Hsp70 chaperone Ssa1 from Saccharomyces cerevisiaeWanhui Hu, Huiwen Wu, Hong Zhang, et al.Journal of Structural Biology|March 23, 2011
The fibrils of Ure2p homologs from Saccharomyces cerevisiae and Saccharoymyces paradoxus have similar cross-β structure in both dried and hydrated formsYi-Qian Wang, Marie Bongiovanni, Sally L Gras, et al.Biochemical Society Transactions|July 24, 2012
Exploiting amyloid: how and why bacteria use cross-β fibrilsElizabeth B Sawyer, Dennis Claessen, Sally L Gras, et al.Bioorganic & Medicinal Chemistry Letters|January 20, 2022
PES derivative PESA is a potent tool to globally profile cellular targets of PESJie Yang, Zhenyan Liu, Sarah Perrett, et al.Pageof 9