ArticleFEBS open bio2020
IbpB-bound substrate release in living cells as revealed by unnatural amino acid-mediated photo-crosslinking.
Article in FEBS open bio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Membrane translocation process revealed by in situ structures of type II secretion system secretins.Nature communications · 2023Article
- Genetically encoded crosslinkers to address protein-protein interactions.Protein science : a publication of the Protein Society · 2023Review
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Authors and funding
2 authors.
Funding
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Abstract
Small heat shock proteins (sHSPs) are known to bind non-native substrates and prevent irreversible aggregation in an ATP-independent manner. However, the dynamic interaction between sHSPs and their substrates in vivo is less studied. Here, by utilizing a genetically incorporated crosslinker, we characterized the interaction between sHSP IbpB and its endogenous substrates in living cells. Through photo-crosslinking analysis of five Bpa variants of IbpB, we found that the substrate binding of IbpB in living cells is reversible upon short-time exposure at 50 °C. Our data provide in vivo evidence that IbpB engages in dynamic substrate release under nonstress conditions and suggest that photo-crosslinking may be a suitable method for investigating dynamic interaction between molecular chaperones and their substrates in living cells.
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