Plasticity and transient binding are key ingredients of the periplasmic chaperone network
Sign Up to like & getrecommendations! Published in 2019 at "Protein Science"
DOI: 10.1002/pro.3641
Abstract: SurA, Skp, FkpA, and DegP constitute a chaperone network that ensures biogenesis of outer membrane proteins (OMPs) in Gram‐negative bacteria. Both Skp and FkpA are holdases that prevent the self‐aggregation of unfolded OMPs, whereas SurA… read more here.
Keywords: network; skp fkpa; chaperone network; plasticity transient ... See more keywords
The Hsp70 chaperone network
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DOI: 10.1038/s41580-019-0133-3
Abstract: The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a large variety of cellular protein folding and remodelling processes. They function virtually at all stages of the life of proteins from… read more here.
Keywords: protein; network; hsp70 chaperone; biology ... See more keywords
The Small Ones Matter—sHsps in the Bacterial Chaperone Network
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DOI: 10.3389/fmolb.2021.666893
Abstract: Small heat shock proteins (sHsps) are an evolutionarily conserved class of ATP-independent chaperones that form the first line of defence during proteotoxic stress. sHsps are defined not only by their relatively low molecular weight, but… read more here.
Keywords: matter shsps; small ones; ones matter; chaperone network ... See more keywords