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ProteomicsIntramembrane client recognition potentiates the chaperone functions of calnexin
One-third of the human proteome is comprised of membrane proteins, which are particularly vulnerable to misfolding and often require folding assistance by molecular chaperones. Calnexin (CNX), which engages client proteins via its sugar-binding lectin domain, is one of the most abundant ER chaperone...
ORGANISM(S): Homo sapiens (Human) 
2022-11-09 | PXD031140 | Pride
Membrane proteins Protein quality control Molecular chaperones Calnexin 
ProteomicsThe EMC acts as a chaperone to labile transmembrane domains
Structure formation of membrane proteins is error-prone and thus requires chaperones that oversee this essential process in cell biology. The ER membrane protein complex (EMC) is well-defined as a transmembrane domain (TMD) integrase. In this study, we characterize an additional chaperone function o...
ORGANISM(S): Homo sapiens (Human) 
2025-08-25 | PXD059792 | Pride
Membrane proteins Endoplasmic reticulum Chaperone Protein folding 
ProteomicsA comprehensive set of ER PDI family members supports the biogenesis of pro-inflammatory interleukin 12 family cytokines
Cytokines of the interleukin 12 (IL-12) family are assembled combinatorially from shared alpha and beta subunits. A common theme is that human IL-12 family alpha subunits remain incompletely structured in isolation until they pair with a designate beta subunit. Accordingly, chaperones need to suppor...
ORGANISM(S): Homo sapiens (Human) 
2022-11-28 | PXD036463 | Pride
Interleukin Chaperone Protein disulfide isomerase Protein folding Genetic code expansion 
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