Browse the search results

Photoswitchable ceramides containing an azobenzene photoswitch behave as light-controllable substrates for both sphingomyelin synthase and glucosylceramide synthase.

Hypervariable regions of mtDNA contribute to transcriptional regulation by serving as sites for TFAM binding and looping.

Mechanically stimulating mitochondria causes them to divide via the recruitment of the mitochondrial fission machinery to the mechanically strained site, showing that intracellular organelles can be mechanoresponsive.

Adhesion force measurements reveal that proper N-glycosylation of flagellar membrane proteins is crucial for adhering C. reinhardtii cells onto surfaces.

Atomic force microscopy based single-molecule force spectroscopy of smooth muscle myosin light chain kinase strongly indicates the existence of a mechanically triggerable activation pathway analogous to its well-established biochemical regulation pathway via calcium-loaded calmodulin.

A single-molecule approach is able to discriminate the redundant binding conformations of cellulosomal dockerin based on differences in their mechanical properties.

High-speed atomic force microscopy reveals that the open state of the divalent ion channel CorA is highly dynamic and defined by the fast exchange between conformations.

A new approach using combination of electron microscopy (EM) and high-speed atomic force microscopy (HS-AFM) clearly demonstrates dynamics of dynamin-amphiphysin complexes during membrane constriction and fission suggesting a novel 'clusterase' model of the dynamin-mediated membrane fission.

Compressive force spectroscopy of single molecules reveals that intra-protein forces underlie the long-distance coordination of structural changes within a cytotoxin during pore formation.

Laboratory-based methods are presented that produce filamentous tau aggregates with the same structures as those observed in neurodegenerative disease.