scholarly journals Structural characteristics of oligomers formed by pyroglutamate-modified amyloid β peptides studied by solid-state NMR

2020 ◽  
Vol 22 (29) ◽  
pp. 16887-16895 ◽  
Author(s):  
Holger A. Scheidt ◽  
Anirban Das ◽  
Alexander Korn ◽  
Martin Krueger ◽  
Sudipta Maiti ◽  
...  

Structure of oligomers of truncated and pyroglutamate modified amyloid β variants is similar to the wild type.

2008 ◽  
Vol 380 (3) ◽  
pp. 444-450 ◽  
Author(s):  
Henrike Heise ◽  
M. Soledad Celej ◽  
Stefan Becker ◽  
Dietmar Riedel ◽  
Avishay Pelah ◽  
...  

2020 ◽  
Vol 117 (13) ◽  
pp. 7171-7175
Author(s):  
Zhiyu Sun ◽  
Yunyao Xu ◽  
Dongyu Zhang ◽  
Ann E. McDermott

Transmembrane allosteric coupling is a feature of many critical biological signaling events. Here we test whether transmembrane allosteric coupling controls the potassium binding affinity of the prototypical potassium channel KcsA in the context of C-type inactivation. Activation of KcsA is initiated by proton binding to the pH gate upon an intracellular drop in pH. Numerous studies have suggested that this proton binding also prompts a conformational switch, leading to a loss of affinity for potassium ions at the selectivity filter and therefore to channel inactivation. We tested this mechanism for inactivation using a KcsA mutant (H25R/E118A) that exhibits an open pH gate across a broad range of pH values. We present solid-state NMR measurements of this open mutant at neutral pH to probe the affinity for potassium at the selectivity filter. The potassium binding affinity in the selectivity filter of this mutant, 81 mM, is about four orders of magnitude weaker than that of wild-type KcsA at neutral pH and is comparable to the value for wild-type KcsA at low pH (pH ≈ 3.5). This result strongly supports our assertion that the open pH gate allosterically affects the potassium binding affinity of the selectivity filter. In this mutant, the protonation state of a glutamate residue (E120) in the pH sensor is sensitive to potassium binding, suggesting that this mutant also has flexibility in the activation gate and is subject to transmembrane allostery.


2016 ◽  
Vol 10 (2) ◽  
pp. 269-276 ◽  
Author(s):  
Francesco Ravotti ◽  
Marielle Aulikki Wälti ◽  
Peter Güntert ◽  
Roland Riek ◽  
Anja Böckmann ◽  
...  

2012 ◽  
Vol 287 (27) ◽  
pp. 22822-22826 ◽  
Author(s):  
Holger A. Scheidt ◽  
Isabel Morgado ◽  
Daniel Huster

2002 ◽  
Vol 4 (22) ◽  
pp. 5524-5530 ◽  
Author(s):  
Fredrick Lindström ◽  
Marcus Bokvist ◽  
Tobias Sparrman ◽  
Gerhard Gröbner

RSC Advances ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 4310-4321 ◽  
Author(s):  
Krishna Kishor Dey ◽  
Shovanlal Gayen ◽  
Manasi Ghosh

Structural characteristics of clocortolone pivalate are unique in the topical corticosteroid field having high penetration power through the stratum corneum of skin as well as low corticosteroid-related adverse effects.


2015 ◽  
Vol 137 (20) ◽  
pp. 6480-6483 ◽  
Author(s):  
Sudhakar Parthasarathy ◽  
Masafumi Inoue ◽  
Yiling Xiao ◽  
Yoshitaka Matsumura ◽  
Yo-ichi Nabeshima ◽  
...  

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