BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress

@article{Crofts1998BiPAC,
  title={BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress},
  author={Crofts and Leborgne-Castel and Pesca and Vitale and Denecke},
  journal={The Plant cell},
  year={1998},
  volume={10 5},
  pages={813-24}
}
BiP is found in association with calreticulin, both in the presence and absence of endoplasmic reticulum stress. Although the BiP-calreticulin complex can be disrupted by ATP, several properties suggest that the calreticulin associated with BiP is neither unfolded nor partially or improperly folded. (1) The complex is stable in vivo and does not dissociate during 8 hr of chase. (2) When present in the complex, calreticulin masks epitopes at the C terminus of BiP that are not masked when BiP is… CONTINUE READING
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In - vitro characterization of the lectin properties of purified recombinant calnexin and calreticulin

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