Nuclear damage in mutant iPSC-derived cardiomyocytes is associated with impaired lamin localization to the nuclear envelope.

The gene encodes the nuclear envelope proteins Lamins A and C, which comprise a major part of the nuclear lamina, provide mechanical support to the nucleus, and participate in diverse intracellular signaling. mutations give rise to a collection of diseases called laminopathies, including dilated cardiomyopathy (-DCM) and muscular dystrophies. Although nuclear deformities are a hallmark of -DCM, the role of nuclear abnormalities in the pathogenesis of -DCM remains incompletely understood.

The lamin A/C Ig-fold undergoes cell density-dependent changes that alter epitope binding.

Lamins A/C are nuclear intermediate filament proteins that are involved in diverse cellular mechanical and biochemical functions. Here, we report that recognition of Lamins A/C by a commonly used antibody (JOL-2) that binds the Lamin A/C Ig-fold and other antibodies targeting similar epitopes is highly dependent on cell density, even though Lamin A/Clevels do not change. We propose that the effect is caused by partial unfolding or masking of the C'E and/or EF loops of the Ig-fold in response to cell spreading.

Exploiting dense shell/packing principles to invoke stereoselectivity in a reaction accelerated by a chiral dendrimer.

As dendrimers approach their dense shell or dense packed limit, a certain amount of conformational organization exists. Any substrate binding within the dendrimer's external layer will experience the same organizational effects. This paper describes how these effects can be exploited towards stereocontrol with respect to binding and reactivity.