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A Phaseolin Domain Involved Directly in Trimer Assembly Is a Determinant for Binding by the Chaperone BiP

The binding protein (BiP; a member of the heat-shock 70 family) is a major chaperone of the endoplasmic reticulum (ER). Interactions with BiP are believed to inhibit unproductive aggregation of newly synthesized secretory proteins during folding and assembly. In vitro, BiP has a preference for pepti...

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Dettagli Bibliografici
Pubblicato in:Plant Cell
Autori principali: Foresti, Ombretta, Frigerio, Lorenzo, Holkeri, Heidi, de Virgilio, Maddalena, Vavassori, Stefano, Vitale, Alessandro
Natura: Artigo
Lingua:Inglês
Pubblicazione: Oxford University Press 2003
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Accesso online:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC197309/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/14508011/
https://ncbi.nlm.nih.govhttps://doi.org/10.1105/tpc.013052
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