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Cover Feature: Super‐resolution Imaging of Amyloid Structures over Extended Times by Using Transient Binding of Single Thioflavin T Molecules (ChemBioChem 18/2018)
Author(s) -
Spehar Kevin,
Ding Tianben,
Sun Yuanzi,
Kedia Niraja,
Lu Jin,
Nahass George R.,
Lew Matthew D.,
Bieschke Jan
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800489
Subject(s) - thioflavin , amyloid (mycology) , amyloid fibril , fibril , biophysics , chemistry , fluorescence , cover (algebra) , resolution (logic) , feature (linguistics) , amyloid disease , amyloid β , crystallography , biochemistry , biology , physics , computer science , alzheimer's disease , pathology , optics , medicine , artificial intelligence , inorganic chemistry , mechanical engineering , linguistics , philosophy , disease , engineering
The cover feature picture shows an amyloid fibril being imaged by using transient amyloid binding super‐resolution microscopy. As thioflavin T molecules spontaneously bind to amyloid structures, they emit flashes of fluorescence, and these blinking events can be used to visualize native amyloid fibrils at nanoscale resolution for several days. More information can be found in the communication by M. D. Lew, J. Bieschke et al. on page 1944 in Issue 18, 2018 (DOI: 10.1002/cbic.201800352).