Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.

@article{Rajagopal2015StructureOT,
  title={Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.},
  author={Ponni Rajagopal and Ying Liu and Lei Shi and Amanda F. Clouser and Rachel E. Klevit},
  journal={Journal of biomolecular NMR},
  year={2015},
  volume={63 2},
  pages={223-8}
}
Cells subject to various stresses such as ischemia, oxidation, and heat shock are at risk of accumulating unfolded or misfolded proteins that can aggregate and negatively affect cellular function. Chaperones are expressed at high levels under stress conditions to (1) maintain proteins in soluble states and (2) help proteins regain their native fold. Small Heat Shock Proteins (sHSPs) are ATP-independent chaperones that perform the former function and HSP90 or HSP70 are ATP-dependent chaperones… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-10 of 19 references

Effect of disulfide crosslinking on thermal transitions and chaperone - like activity of human small heat shock protein HspB 1

  • AS Chalova, MV Sudnitsyna
  • Cell Stress Chaperones
  • 2014

Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1. Cell Stress Chaperones

  • AS Chalova, MV Sudnitsyna
  • 2014

Crystal structure of R120G disease mutant of human alphaB-crystallin domain dimer shows closure of a groove

  • AR Clark, CE Naylor
  • J Mol Biol
  • 2011

Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings

  • NG Sgourakis, OF Lange
  • J Am Chem Soc
  • 2011

The polydispersity of alphaBcrystallin is rationalized by an interconverting polyhedral architecture

  • AJ Baldwin, H Lioe
  • 2011

Three-dimensional structure of alpha-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6

  • EV Baranova, SD Weeks
  • J Mol Biol
  • 2011

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