Inhibition of immunoglobin folding and secretion by dominant negative BiP ATPase mutants

Inhibition of immunoglobin folding and secretion by dominant negative BiP ATPase mutants

Hendershot et al examine how the BiP protein interacts with immunoglobin light chain during its folding. The results indicate that light chains undergo both BiP-dependent and BiP-independent folding steps, demonstrating that both ATP binding and hydrolysis activities of BiP are essential for the com...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1996-05, Vol.93 (11), p.5269
Hauptverfasser: Hendershot, Linda, Wei, Jueyang, Gaut, James, Melnick, Jeffrey
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Sprache:eng
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Biochemistry
Proteins
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container_issue 11
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container_title Proceedings of the National Academy of Sciences - PNAS
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creator Hendershot, Linda
Wei, Jueyang
Gaut, James
Melnick, Jeffrey
description Hendershot et al examine how the BiP protein interacts with immunoglobin light chain during its folding. The results indicate that light chains undergo both BiP-dependent and BiP-independent folding steps, demonstrating that both ATP binding and hydrolysis activities of BiP are essential for the completion of light chain folding in vivo.
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1091-6490
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source Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry
subjects Biochemistry
Proteins
title Inhibition of immunoglobin folding and secretion by dominant negative BiP ATPase mutants
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