Publication for Canx and Pdia3

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Canx	calnexin	12330			[link]
mmu	Pdia3	protein disulfide isomerase associated 3	14827

Pubmed ID	Priority	Text
28437467	0.99	calnexin and PDI.
	0.98	calnexin and protein disulphide isomerase (PDI) as mutant uromodulin interactors (Fig 2C), suggesting the involvement of these chaperones in uromodulin folding.
	0.98	calnexin, PDI and BiP, suggesting that uromodulin enters the calnexin cycle to be properly folded.
19650649	0.98	CNX forms a functional complex with the ER resident oxidoreductase, ERp57, leading to formation and isomerization of disulfide bonds.
	0.98	CNX and ERp57 in the neuronal cells.
	0.97	ERp57 and CNX in brain neurons further links Sep15 to the folding processes involving these chaperones.
	0.93	ERp57 and CNX, key proteins involved in quality control in the ER, had very similar expression profiles.
	0.84	CNX and ERp57 were present in cerebellum similar to Sep15, although their expression pattern was not uniform.
	0.58	CNX and oxidoreductase ERp57, which are the major components of the quality control mechanism in the ER, were evaluated across 159 different brain regions.
21093319	0.98	ERp57 forms a complex with calnexin and calreticulin, whereby these lectin chaperones mediate substrate recognition.
	0.98	ERp57, exists in a complex with calreticulin and calnexin whereby these lectin chaperones mediate a broad substrate recognition.
	0.98	ERp57 in the absence of the calreticulin and calnexin chaperones.
	0.95	ERp57-associated chaperones by Mzb1 is supported by the coimmunoprecipitation of calnexin and calreticulin with ERp57 antibody in Mzb1-knockdown cells, whereas Grp94 is preferentially coimmunoprecipitated in control and Mzb1*-rescue cells.
	0.93	ERp57 acts in concert with tapasin, independently of its partners calreticulin and calnexin.
	0.81	ERp57, we detected abundant amounts of calnexin and calreticulin in lysates from siMzb1-knockdown cells, but not in lysates from control-knockdown and Mzb1*-rescue cells.
30647818	0.98	ERp57 is dependent on interactions with calnexin and calreticulin, which mediate the recognition and binding of N-glycosylated substrates.
	0.98	calnexin and calreticulin were induced and the stimulation with thapsigargin, an ER stress inducer, increased the ERp57 expression in chondrocytes 2.8-fold.
	0.98	ERp57 and the calnexin/calreticulin cycle appears to be particularly active during ER stress in osteoarthritic cartilage cells.
	0.96	calnexin and calreticulin in addition bind the PDI ERp57, assisting in folding by disulfide exchange reactions.
	0.96	ERp57, that is, as a part of the calnexin/calreticulin cycle, mainly engaged in folding of glycoproteins with unstructured disulfide-rich domains.
	0.73	calnexin ERp57 cycle over other protein folding mechanisms might also play a role in this context.
18567819	0.98	PDI and revealed upregulation of CNX (~1.8-fold), a membrane bound chaperone and phospho-JNK-1 ~2.0-fold, a downstream effector protein of the UPR.
	0.98	CNX, and PDI, a foldase that catalyzed disulfide bond formation.
	0.98	CNX, and PDI were all upregulated in fat of obese compared with nonobese volunteers (Figs. 1-3), indicating activation of UPR and suggesting presence of ER stress.
	0.97	protein disulfide-isomerase A3, and glutathione-S-transferase P. Western blotting revealed upregulation of several other UPR stress-related proteins, including calnexin, a membrane-bound chaperone, and phospho c-jun NH2-terminal kinase (JNK)-1, a downstream effector protein of ER stress.
25184039	0.98	ER and the important role of calnexin/calreticulin in glycoprotein folding, perturbation of calcium homeostasis, as produced by the calcium pump inhibitor thapsigargin, would be predicted to adversely affect the folding of numerous glycoproteins and hence the induction of the UPR.
	0.97	ER is a calcium-rich environment, whereas the cytosol is not: consequently, calcium-binding chaperones, such as calnexin and calreticulin participate in folding reactions in the ER.
	0.97	calnexin/calreticulin, assisted by oxidoreductases, such as ERp57 to enable additional attempts at reaching a fully native fold.
	0.94	ER-lumenal proteins, the calnexin/calreticulin cycle employs an ER-resident glucosidase and (uridine 5'-diphospho-glucose-4-epimerase) [UDP]-glucose glycoprotein glucosyltransferase.
26361352	0.98	ERp57 binding partner, CNX, interacts and assists the folding of peripheral myelin proteins, contributing to peripheral neuropathies in mouse models.
	0.97	ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle.
	0.97	calnexin (CNX) and calreticulin (CRT) cycle, ERp57 is predicted to participate in the folding of numerous cysteine-rich glycoproteins.
	0.97	ERp57 may have a relevant activity in sustaining glial proteostasis as a central component of the CNX-CRT cycle.
18270596	0.98	PDI, Grp78, Grp94 and calnexin was seen in rtTA RNF5 DTg but not control mice (Fig. 5A), suggesting that ER stress occurs in the muscles of RNF5 overexpressing animals.
	0.98	PDI, GRP78, GRP94 and calnexin in the muscle of the RNF5-overexpressing animals and the delay in GRP94 and calnexin induction in RNF5 KO.
	0.81	calnexin was slightly delayed whereas expression of PDI was elevated in RNF5 KO.
20520781	0.98	CNX and CRT but not PDI were upregulated in Grp94-/- ESCs.
	0.96	PDI respectively, but with no change in calnexin (CNX) and calreticulin (CRT) levels.
	0.95	CNX/CRT chaperone system, but apparently not the thiol oxidoreductases such as PDI.
27073369	0.98	ERp57 catalyzes the formation, disruption and isomerization of disulfide bonds of glycoproteins mediated by a cooperative interaction with the endoplasmic reticulum (ER) chaperones calnexin and calreticulin (Turano et al., 2002) (Figure 1A, B).
	0.98	ERp57 mediated in part the folding of synaptic proteins, like SV2, as a component of the calnexin and calreticulin cycle.
	0.96	ERp57 altered the physical association with calnexin and calreticulin (Woehlbier et al., 2016).
19139267	0.98	PDI, and calnexin were all increased in Certgt/gt embryonic extract.
	0.98	calnexin, PDI, and ATF4 were increased in the Certgt/gt cells (Fig. 4 B).
20428984	0.98	PDI can also interact with the lectin chaperones calreticulin and calnexin, which were also increased in mutant chondrocytes.
	0.83	calnexin, ERp72, calreticulin and ERp57 were unchanged in treated mice compared to untreated mice (Table 2).
22706078	0.98	calnexin, calreticulin, and ERp57, further supporting the concept that platelets process antigen and regulate MHCI expression.
	0.96	calnexin, calreticulin, and ERp57.
22961085	0.98	calnexin, eIF2ak3, eIF2as1, and PDIA3 (Fig. 4A-E).
	0.97	calnexin, eIF2ak3, eIF2as1, and PDIA3 to the levels in the nondiabetic WT group (Fig. 4A-E).
23791840	0.98	calnexin, (3) eIF2alphak3, (4) eIF2alphas1, and (5) PDIA3 (Figure 4).
	0.98	calnexin, eIF2alphas1, eIF2alphak3, and PDIA3 are all significantly increased in WT embryos of the diabetic group and that SOD1 overexpression abrogates the expression of these ER chaperone genes.
24022788	0.98	protein disulfide isomerase A3 (PDIA3), eukaryotic elongation factor 1A2, calnexin, and heat-shock proteins (HspB1, Hsp7C), was observed in HT mouse muscle (Supplementary Table 1, http://onlinelibrary.wiley.com/doi/10.1002/art.38180/abstract).
	0.97	PDIA3, calnexin) are linked with the UPP in myositic skeletal muscle.
27337472	0.98	calnexin) also cooperates with ERp57 via a glycan-independent, noncovalent interaction to facilitate their correct folding and disulfide bond formation.
	0.97	calnexin (CNX) and, after binding beta2m, are recruited to the PLC by simultaneous noncovalent CRT interactions with a monoglucosylated N-linked glycan on the heavy chain and ERp57 disulfide linked to tapasin in the PLC.
29056908	0.98	calnexin, calreticulin, PDI, and ERp57) (Figure 3D).
	0.95	calnexin, calreticulin, PDI, as well as ERp57, was found in EGFRI-treated F3II and D122 cells when compared with untreated cells.
31046837	0.98	calnexin (CLNX), and ER protein 57 (ERp57).
	0.97	CLNX can regulate SERCA directly or possibly indirectly by recruiting other enzymes, such as ERp57.
18851953	0.98	GRP58, retained in endoplasmic reticulum, specifically interacts with glycoproteins such as calnexin and calreticulin, playing an important role as a molecular chaperone during glycoprotein biosynthesis and folding.
19816510	0.98	PDI, calnexin, GADD34, CHOP, eIF2alpha, calbindin, neurofilament and beta-actin.
19889996	0.98	Erp57 is a PDI homolog that shares enzymatic functions with PDI, but unlike PDI, forms direct interactions with the ER lectins calnexin and calreticulin.
23509727	0.98	ERp57 and calnexin (CNX), and in Ca2+ homeostasis/signaling regulation.
24024552	0.98	calnexin, calreticulin, gp96, thiol-disulphide oxidoreductase, protein disulphide isomerase (PDI) and ERp57, within the ER act in concert to guide protein maturation through trafficking, folding, assembling and sorting, and preventing the export of improperly folded protein from the ER.
25140116	0.98	CNX (calnexin) interact with the ERp57 to promote disulfide bond isomerization in bound unfolded glycoproteins.
26035385	0.98	PDIA3 exhibits a major role as molecular chaperone involved in the quality control process for newly synthesized glycoproteins in the endoplasmic reticulum (ER), interacting with calnexin or calreticulin.
26190652	0.98	calnexin (CNX) and calretculin (CRT), which function in complex with ERp57 and ERp72.
26700264	0.98	PDI, heat shock protein 90 (HSP90) and calnexin (Table S6), confirm that CoO ENP treatment triggers the PERK-dependent ER stress pathway.
28101003	0.98	CNX, ERp57, an ER-resident disulfide isomerase, has been implicated in the folding of the disulfide-bond-containing protein P0, but not in the folding of MOG, suggesting that different ERQC factors are involved in the maturation and post-translational modification of different myelin proteins (Jung et al.,; Jung and Michalak,).
29765493	0.98	calnexin, and thiol-disulfide oxidoreductase:protein disulphide isomerase (PDI), which belongs to the TRX superfamily.
31607947	0.98	ER chaperones GRP 94, calnexin, GRP78, calreticulin, and ERp72 was enhanced in the pathological muscle area.
21263072	0.97	ERp57 and the endoplasmic reticulum (ER) chaperones calreticulin and calnexin.
	0.97	Calnexin and calreticulin also interact with their partner ER oxidoreductase ERp57 via an elongated beta-stranded hairpin structure called the P-domain.
	0.92	calnexin's structure as a model for calreticulin structure and the tapasin-ERp57 complex structure) suggest that a calreticulin bound to tapasin's glycan cannot simultaneously contact the ERp57 molecule present within the same tapasin-ERp57 conjugate (Wijeyesakare and Raghavan, unpublished observations).
27535430	0.97	calnexin, GRP78, and PDIA3, which were also identified by LC-MS/MS:the presence of Sec22b in MFGMs but not in CLDs supports a strong interaction between the ER and CLDs and the possibility that the ER contributes to the formation of the MFGM, as Sec22b is an ER-resident transmembrane SNARE.
	0.92	PdiA3, GRP78), ER membrane (calnexin, Stx18), Golgi (GM130), or cytosol (beta-actin), and 3) the CLD fraction was significantly enriched for PLIN2, a specific marker of CLDs (Figure 2D, CLDs).
28487627	0.97	Calnexin, calreticulin, and PDIA3 (a protein foldase that catalyzes the formation and correct isomerization of disulfide bonds and interacts with both calnexin and calreticulin), are the core components of the ER protein quality control system (Hebert and Molinari,).
	0.97	PDIA3, calreticulin, and calnexin, may influence the function and integrity of the BBB.
29468369	0.97	calnexin (p< 0.05), Chop (p<0.001) and Pdi (p= 0.06), compared with retinas of vehicle-injected animals (Fig. 1b).
	0.97	Pdi (p<001), Chop (p< 0.05) and calnexin (p= 0.09) (Fig. 5a).
29542339	0.97	ERp57 likely includes glycoproteins that enter the calnexin cycle.
	0.85	ERp57 interacts with lectin chaperones calnexin and calreticulin, whereas PDI does not.
31260448	0.97	Canx, Dnajc3, Grp94, Hyou1, Manf (Armet), Pdia3, Pdia4, Trib3 and Xbp1 (S1 Table).
	0.97	Canx, Creld2, Derl3, Dnajc3, Hyou1, Manf, Pdia3, Pdia4, Pdia6 and Xbp1 gene expression.
18751977	0.97	calnexin, calreticulin, and ERp57) and beta2 microglobulin (beta2m).
24046357	0.97	ERp57 (PDIA3), calreticulin (CRT) and calnexin (CNX) transcripts were normal in the chondrocytes of Col2-Tgrdw mice.
25534658	0.96	ERp57 is a paradigm for those cellular proteins that are strictly dependent on CNX, CRT and ERp57 and whose incapacity to attain the functional conformation causes the embryonic or the early mortality in the corresponding knockout mice.
23298205	0.95	CNX/ERp57 quality control cycle, enzymatic removal of mannose residues from the N-linked glycan will render it unsusceptible to re-glucosylation by UGT1.
23789114	0.94	PDI and calnexin (Fig. 7A).
26676362	0.93	calnexin, calreticulin, ERp57 or UGGT1, the deletion of these factors in mice causes severe phenotypes.
28225807	0.88	endoplasmic reticulum protein 57 (ERP57) and calnexin (CANX) were not detectable in circulating EVs, but were detected in whole liver lysates, regardless of APAP treatment (Figure F in S1 File).
25419710	0.83	calnexin and PDI are equally distributed between MAM and bulk ER, while sigma1 receptor is found preferentially at the MAM.
29994898	0.82	ERp57, surface charge differences allow the b' domain of ERp57, but not ERp72, to bind calnexin.
26619807	0.80	calnexin (top panels in Supplemental Figure 1) and the ER membrane enzyme PDI (middle panels in Supplemental Figure 1) are not found in RIDNs.
18172663	0.60	calnexin, calreticulin), peptidylprolyl isomerases, thiol disulphide oxidoreductases (PDI, P5 (CaBP1), ERp72, ERp57, ERp44, ERp29, and ERp46).
29160038	0.58	Canx and the role of D348 in Canx, which when mutated abrogated interactions between Canx and PDIA9, PDIA3 and cyclophilin B (CypB).