Frauke Gräter

TL;DR: A model has been constructed that integrates all quantitative data and includes structural models of abundant proteins and, with the exception of the V-ATPase, contains numerous copies of proteins essential for membrane traffic and neurotransmitter uptake.

TL;DR: It is shown that mechanical strain activates ATP binding before unfolding of the structural titin domains, and that TK can thus act as a biological force sensor and identify the steps in which the autoinhibition of TK is mechanically relieved at low forces, leading to binding of the cosubstrate ATP and priming the enzyme for subsequent autophosphorylation and substrate turnover.

TL;DR: The molecular photoswitching mechanism of asFP595, a green fluorescent protein (GFP)-like protein that can be transferred from a nonfluorescent "off" to a fluorescent "on" state and back again, is clarified by green and blue light, respectively.

TL;DR: The results indicate that substrate conformational changes may be important in the regulation of Trx activity under conditions of oxidative stress and mechanical injury, such as those experienced in cardiovascular disease, and support the view that the Trx active site regulates the geometry of the participating sulphur atoms with sub-ångström precision to achieve efficient catalysis.

TL;DR: This work shows that a rapidly fluctuating FG-Nup populates an ensemble of conformations that are prone to bind NTRs with near diffusion-limited on rates, and proposes that these exceptional physical characteristics enable a rapid and specific transport mechanism in the physiological context, supported by single molecule in-cell assays on intact NPCs.