Browse the search results

A key molecule that connects leukemogenic proteins to aberrant HOX gene regulation turned out to be a nuclear export factor, CRM1.

A major cytoplasmic chaperone, Ssa2p, acts as a nuclear import carrier for tRNAs upon nutrient starvation in Saccharomyces cerevisiae.

Protocols that greatly simplify the use of nanobodies in fluorescence imaging and affinity purification have been developed.

Structure and simulations reveal SARS-CoV-2 NSP10 is more resistant to genetic variations than other SARS-CoV-2 NSPs and that the presence of mutations conserves structural and dynamic changes in NSP10.

Traumatic injury leads to functional defects in nucleocytoplasmic transport and TDP-43 pathology in multiple model systems.

Nuclear pores assemble asymmetrically, by an inside-out evagination of the inner nuclear membrane that grows in diameter and depth until it fuses with the flat outer nuclear membrane.

The nuclear pore complex is transiently proteolyzed during cell differentiation and the nuclear proteome experience dramatic change.

The Ran GTPase plays a role in defining the physical properties of the nuclear pore complex transport channel by remodeling the binding interactions of importin-β with the nucleoporin Nup153 at the nuclear face of the pore.

Polarized fluorescence microscopy of individual nuclear pores in vivo reveals conformational changes in select domains of proteins of the inner ring.