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Increased tumour protein levels of calnexin may be of prognostic significance in colorectal cancer, and calnexin may represent a potential target for future therapies.
FUNDC1 (show FUNDC1 Proteins) integrates mitochondrial fission and mitophagy at the interface of the endoplasmic reticulum-mitochondrial contact site by working in concert with DRP1 (show CRMP1 Proteins) and calnexin under hypoxic conditions in mammalian cells.
Results of further analyses by using a CNX mutant imply that ERp29 (show ERP29 Proteins) and ERp57 (show PDIA3 Proteins) recognize the same domain of CNX, whereas the mode of interaction with CNX might be somewhat different between them.
Inhibit interaction between HIV-1 Nef and Calnexin to reverse HIV-induced lipid accumulation and prevent atherosclerosis.
Endogenous NOX4 (show NOX4 Proteins) forms macromolecular complexes with calnexin, which are needed for the proper maturation, processing, and function of NOX4 (show NOX4 Proteins) in the endoplasmic reticulum.
To study principles underlying dynamics and regulation of palmitoylation, the ER chaperone calnexin, which requires dual palmitoylation for function, was investigated.
These observations point at a previously unrecognized contribution of calnexin to the retention of NMT1 (show NMT1 Proteins) at the ER membrane.
Charcot-Marie-Tooth disease-related PMP22 (show PMP22 Proteins) is trapped in the endoplasmic reticulum by calnexin-dependent retention and Rer1 (show RER1 Proteins)-mediated early Golgi retrieval systems and partly degraded by the Hrd1 (show SYVN1 Proteins)-mediated endoplasmic reticulum-associated degradation system.
Data indicate that protein tyrosine phosphatase 1B (PTP1B (show PTPN1 Proteins)) association with calnexin is ubiquitin conjugating enzyme 9 (UBC9 (show UBE2I Proteins))-dependent.
H-ERG (show KCNH2 Proteins) trafficking was impaired by H2O2 after 48 h treatment, accompanied by reciprocal changes of expression between miR-17-5p seed miRNAs and several chaperones (Hsp70 (show HSP70 Proteins), Hsc70 (show HSPA8 Proteins), CANX, and Golga20)
CNX has a specific role in cardiomyocyte viability and Ca(2 (show CA2 Proteins)+) cycling through its effects on endoplasmic reticulum stress, apoptosis and Ca(2 (show CA2 Proteins)+) channel expression.
Calnexin discriminates between different conformational states of GlyT2 displaying a lectin-independent chaperone activity.
calnexin and ERp57 (show PDIA3 Proteins), but not calreticulin (show CALR Proteins), play an important role in the biology of peripheral myelin proteins PMP22 (show PMP22 Proteins) and P0, and, consequently, these chaperones may contribute to the pathogenesis of peripheral neuropathies
Enhanced clathrin-dependent endocytosis in the absence of calnexin may contribute to the neurological phenotype of calnexin-deficient mice
Data show that the E351 mutation led to slightly enhanced ERp57 (show PDIA3 Proteins) binding to calnexin, whereas W428 greatly enhanced binding of ERp57 (show PDIA3 Proteins) to calnexin.
Suggest that Adam7 (show ADAM7 Proteins) functions in fertilization through the formation of a complex with heat shock protein 5 (show HSPA5 Proteins), calnexin and Itm2b (show ITM2B Proteins) during capacitation in sperm.
endoplasmic reticulum stress has effects on group VIA phospholipase A2 (show YWHAZ Proteins) in beta cells that include tyrosine phosphorylation and increased association with calnexin
Calnexin deficiency leads to dysmyelination
Data give novel evidence that CyCAP (show LGALS3BP Proteins) regulates the post-translational modification of tissue transglutaminase (show TGM2 Proteins) through its colocalization with calnexin in endoplasmic reticulum.
Association with mutant peripheral myelin protein-22 (show PMP22 Proteins) ex vivo: a basis for "gain-of-function" ER diseases.
Results suggest that calnexin is essential for neuromast formation during lateral line development.
This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. It may also play a central role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Alternatively spliced transcript variants encoding the same protein have been described.
major histocompatibility complex class I antigen-binding protein p88
, hypothetical protein