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Article

Biogenesis of secretory immunoglobulin M requires intermediate non‐native disulfide bonds and engagement of the protein disulfide isomerase ERp44

27 Dec 2021

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Identifiers

PMID: 34957576
DOI: 10.15252/embj.2021108518

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Research trail→

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Biogenesis of secretory immunoglobulin M requires intermediate non‐native disulfide bonds and engagement of the protein disulfide isomerase ERp44PMID 34957576Read ↗

Membrane immunoglobulins are stabilized by interchain disulfide bonds occurring within the extracellular membrane-proximal domain.Semantic proximity Read ↗

Cysteines in CH1 underlie retention of unassembled Ig heavy chains.Semantic proximity Read ↗

The synthesis, assembly, and secretion of immunoglobulin: a biochemical and genetic approach.Semantic proximity Read ↗

Understanding the biosynthesis of human IgM SAM-6 through a combinatorial expression of mutant subunits that affect product assembly and secretion.Semantic proximity Read ↗

Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway.Semantic proximity Read ↗

Intracellular antigen processing by ERAP2: Molecular mechanism and roles in health and diseaseSemantic proximity Read ↗

The special unfolded protein response in plasma cellsSemantic proximity Read ↗

Assembly of IgM. Role of disulfide bonding and noncovalent interactions.Semantic proximity Read ↗

Manipulation of oxidative protein folding and PDI redox state in mammalian cells.Semantic proximity Read ↗

Nonnative interactions between cysteines direct productive assembly of P22 tailspike protein.Semantic proximity Read ↗

The structure and dynamics of secretory component and its interactions with polymeric immunoglobulinsSemantic proximity Read ↗

Transport of meprin subunits through the secretory pathway: role of the transmembrane and cytoplasmic domains and oligomerization.Semantic proximity Read ↗

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