Sentence examples for regulate the folding from inspiring English sources

It will be of particular interest to further investigate how these factors regulate the folding of chromatin fiber, which is essential for understanding the structural principles of chromatin dynamics and its correlation with gene regulation.

Inside cells, proteins called chaperones regulate the folding of other proteins and help to prevent aggregate formation.

Heat shock proteins are molecular chaperones that regulate the folding, localization, accumulation, and degradation of protein molecules in both plant and animal species [ 9].

Hsps are molecular chaperones that regulate the folding, localization, accumulation, and degradation of protein molecules in both plant and animal species [ 10].

Alternatively, as Agrs belong to the superfamily of protein disulfide isomerases (PDI), which modulate folding of other proteins (Hatahet and Ruddock, 2009; Persson et al., 2005), they might regulate the folding of some extracellular proteins in the intercellular space.

The members of 70 kDa HSP family (HSP70) are molecular chaperones able to regulate the folding, transport, and assembly of proteins into complexes [ 9], not only under stress conditions such as heat, but also under normal physiological conditions.

The GR itself forms a heterocomplex with several other proteins, including the chaperone heat-shock protein 90 (hsp90) as well as the co-chaperone FKBP5, which regulates the folding and trafficking of the GR [8], [9].

This finding is not too surprising as it is thought that the products of these genes are primarily responsible for bringing protein clients to chaperone activities [93]; and one might expect significant diversity in regulating the folding of both unique and ubiquitous protein clients across the many diverse cell populations of the brain.

HSP70 and HSP90 are molecular chaperone which regulates the folding of proteins and recognizes misfolded polypeptides.

Because IGF signaling is known to suppress the folding defects associated with other non-membrane-localized substrates (Hsu et al., 2003; Morley and Morimoto, 2004), these data suggest that the genetic mechanisms regulating the folding and stability of the PGP-3ΔF508 PGP-3ΔF508rotein are distinct fromembraneregulating the folding of proteinsly described cytosolic substrares in C. elegans.

NCT00687934 Heat shock protein 90 (Hsp90) belongs to a class of molecular chaperone proteins that helps modulate cellular responses to environmental stress, and regulates the folding, stability, and function of many so-called "client" proteins, such as RAF, KIT, EGFR, HER2, PDGFRα and VEGFR2[ 1].