Sentence examples for nuclear chaperones from inspiring English sources

Nuclear trafficking of these proteins requires liberation from membrane attachment and import by nuclear chaperones, and results in binding to chromatin and altered gene transcription.

The interactome reveals that Hc Hsp60 engages nuclear chaperones, small chaperones and Hsp90 families.

Proteins that mediate these reactions, generally termed molecular (or nuclear) chaperones, have been identified biochemically.

Nucleophosmin 1 (NPM1), also named nucleolar phosphoprotein B23, belongs to the NucleoPhosMin/NucleoPlasMin family of nuclear chaperones.

It has also been shown that PLSCR1 when not palmitoylated is avidly imported into the nucleus by the importin-α β nuclear chaperones, where it functions as a DNA-binding protein with transcriptional activity (Ben-Efraim et al., 2004).

Studies suggest that the related proteins nucleoplasmin and nucleophosmin (also called B23, NO38 or numatrin) are nuclear chaperones that mediate the assembly of nucleosomes and ribosomes, respectively, and that these activities are accomplished through the binding of basic proteins via their acidic domains.

Our data support the contention that oxidative stress results in cellular uptake and accumulation of full-length crystallin in the cytosol and nucleus, where it could act as a nuclear chaperone.

For example, the MESD chaperone (contig 01700) specifically assists in the folding of β-propeller/EGF molecules within low density lipoprotein receptors (LDLRs) and the nuclear chaperone Asf1 (contig 05542) facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.

NPM2 and NPM3 are nuclear chaperone proteins.

This protein is conserved thoughout eukaryotes and plays the role of a nuclear chaperone in most organisms.

The striking similarities in amino acid sequence and domain structure between NPM3 and its chaperone relatives, nucleophosmin and nucleoplasmin, together with abundant expression levels and nuclear localization, strongly suggests that NPM3 shares fundamental nuclear chaperone functions with these proteins.