Bing K. Jap

TL;DR: In this article, crystal structures of the 11-subunit bc1 complex from bovine heart reveal full views of this bifunctional enzyme, and the "Rieske" iron-sulfur protein subunit shows significant conformational changes in different crystal forms.

TL;DR: The analysis of the AQP1 pore indicates that the transport of protons through this channel is highly energetically unfavourable, and residues of the constriction region, in particular histidine 182, which is conserved among all known water-specific channels, are critical in establishing water specificity.

TL;DR: The purification of the native gamma-secretase complexes from HeLa cell membranes and the identification of an additional gamma- secretase complex subunit, CD147, a transmembrane glycoprotein with two Ig-like domains are reported, indicating that the presence of the CD147 subunit within the gamma-Secretase complex down-modulates the production of Abeta-peptides.

TL;DR: It is proposed that APP may serve as a cellular cholesterol sensor that is linked to mechanisms for suppressing cellular cholesterol uptake, and may be critical for the trafficking of these proteins to cholesterol-rich membrane domains, which leads to cleavage by beta- and gamma-secretase and resulting amyloid-beta production.

TL;DR: The structure of PhoE porin provides a clue as to how deletions of segments of polypeptide, which are found in certain mutants, can result in an actual increase in the channel size.