Publication for Pdia3 and Hspa5

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Pdia3	protein disulfide isomerase associated 3	14827			[link]
mmu	Hspa5	heat shock protein 5	14828

Pubmed ID	Priority	Text
19023445	0.99	Bip, PDIA1, PDIA3, PDIA4 and PDIA6 proteins.
	0.98	Bip, PDIA1 and PDIA3.
	0.98	Bip, PDIA1, PDIA3, PDIA4 and PDIA6 proteins, in response to Thapsigargin, a pharmacological ER-stress agent.
	0.98	Bip, PDIA1 and PDIA3.
	0.98	Bip, PDIA1 and PDIA3 were detected in eIF2B-mutated oligodendroglial-derived cells (Fig. 4) in contrast to eIF2B-mutated fibroblasts (Mintz et al., submitted for publication).
	0.96	Bip, PDIA1 and PDIA3 were high to begin within sh2B5+2B5(R195H) cells, it further increased compared to DDR1 cells under mild ER stress (2.65+-0.06, 2.2+-0.03 and 1.7+-0.08 fold up-regulation at 24 h; 2.1+-0.16 and 2.0+-0.01 fold up-regulation at 12 h for Bip and PDIA1, respectively) (Fig. 5).
	0.94	Bip and PDIA3 were significantly above basal levels as compared to DDR1 control cells (2.0+-0.09 and 1.54+-0.06 fold up-regulation, respectively).
	0.91	Bip (also known as glucose related protein 78, GRP78) and four members of the protein disulfide isomerase family (PDIA1, PDIA3, PDIA4 and PDIA6) was not dramatically changed.
28437467	0.99	Bip, calnexin and PDI.
	0.98	BiP, calnexin and protein disulphide isomerase (PDI) as mutant uromodulin interactors (Fig 2C), suggesting the involvement of these chaperones in uromodulin folding.
	0.98	PDI and BiP, suggesting that uromodulin enters the calnexin cycle to be properly folded.
	0.89	PDI and BiP with mutant uromodulin relative to wild type one.
19732428	0.98	ER chaperone proteins, GRP78/BiP and ERp72.
	0.98	ER chaperone/folding enzymes ERp72 and GRP78/BiP occurred early after ablation of PERK function suggesting that changes in ER secretory functions may give rise to the other defects including reduced insulin gene expression, secretion, and cell proliferation.
	0.98	ER and is controlled by the binding of the ER chaperone proteins, GRP78/BiP and GRP94, and calcium.
	0.98	GRP/78 mRNA expression is the first hint of ER dysfunction, and is followed by increased levels of these proteins and the oxidized isoform of ERp72 and ERp57.
	0.98	ER luminal domain via binding of GRP78/BiP complexed with calcium.
	0.98	ER, which occurs after the elevation of two key chaperone proteins GRP78/BiP and ERp72.
	0.97	GRP78/BiP and ERp72 are the earliest changes observed after ablation of Perk, we suggest that ER dysfunctions give rise to defects in proinsulin trafficking, insulin secretion, and cell proliferation.
	0.94	ER chaperones ERp72 and GRP78/BiP by treating AdDNPerk-832/13 beta cells with cyclohexamide, a potent inhibitor of protein synthesis.
	0.90	ER chaperone genes ERp72 and GRP78/BiP were substantially induced while most other ER chaperones (ERp58, ERp57, Ero1beta, and Ero1L) and ERAD associated (Psma5, Sec61a, Sec63, and Der1) genes were not significantly elevated (Figure 6).
	0.53	GRP78/BiP in AdDNPerk-832/13 beta cells (Figure 5B) and did not reduce or delay the appearance of Impacted-ER beta cells (data not shown) thus arguing against this hypothesis.
29765493	0.98	glucose-regulated protein 78 (GRP78, also known as BiP), and 94 (GRP94), calnexin, and thiol-disulfide oxidoreductase:protein disulphide isomerase (PDI), which belongs to the TRX superfamily.
	0.98	GRP78, PDI, and CHOP are increased in skeletal muscle tissues of old animals as compared to younger animals.
	0.98	GRP78 (13.7%, p > 0.05) and PDI (9.4%, p > 0.05) proteins were observed to occur upon long-term exercise in T.A. muscle of OE mice (Figure 3).
	0.97	GRP78 and PDI proteins after long-term exercise in T.A. muscle of OE mice.
	0.94	GRP78 chaperone, PDI, and CHOP proteins (Figure 3).
	0.93	GRP78, PDI, and CHOP in gastrocnemius muscle of 24-month-old mice in comparison with 6-month-old mice.
	0.89	GRP78 and PDI, were not significantly influenced in skeletal muscles by long-term exercise.
	0.87	GRP78, PDI, and CHOP in T.A. and soleus muscles of mice.
	0.79	GRP78, PDI, and CHOP.
19816510	0.98	GRP78 depleted PCs activate UPR including induction of GRP94, PDI, CHOP and GADD34, feedback suppression of eIF2alpha phosphorylation and apoptotic cell death.
	0.98	GRP78 and GRP94 and folding enzymes such as PDI to alleviate protein misfolding.
	0.98	GRP78 deficiency, ER chaperone GRP94 and folding enzyme PDI are upregulated, consistent with previous reports in Grp78 heterozygous mouse embryo fibroblasts and in established cell lines where GRP78 was knockdown by siRNA.
	0.98	GRP78 result in dramatic decrease in the cytosolic protein substrates for ubiquitination, the same cells show robust levels of GRP94, PDI, calnexin, GADD34, CHOP, eIF2alpha, calbindin, neurofilament and beta-actin.
	0.97	PDI, GADD34, phosphorylated eIF2alpha and eIF2alpha immunostaining indicates that GRP78 depletion significantly upregulates GRP94, PDI, and GADD34 and suppresses eIF2alpha phosphorylation without affecting eIF2alpha level in PCs of F/-; pc-Cre mice compared with their F/- littermates.
29207602	0.98	ERp57 (Figure 5G) protein levels were up regulated whereas BiP (Figure 5H) and Grp94 (Figure 5I) UPR proteins were reduced in TRPV1 KO compared with WT thymocytes.
	0.97	BiP, Grp94 and ERp57 chaperone protein expression.
	0.97	BiP, Grp94 and ERp57 protein expression (Figure 4A, 4B).
	0.96	BiP and Grp94 UPR proteins and increase of ERp57 levels.
	0.91	BiP, Grp94 and ERp57 chaperones, in thymocytes treated for different times (1, 2 and 4h) with CPS.
20520781	0.98	GRP78, CNX and CRT but not PDI were upregulated in Grp94-/- ESCs.
	0.96	GRP78 in the Grp78+/- cells led to a 1.7- and 2-fold increase in the basal level of GRP94 and PDI respectively, but with no change in calnexin (CNX) and calreticulin (CRT) levels.
	0.96	Grp78 and Grp94 mice show no obvious abnormal phenotype, cells with partial GRP78 knockdown upregulate GRP94 and PDI; however no such compensation is observed for partial GRP94 deficiency.
	0.94	GRP78, a partner protein of GRP94 in the GRP78/GRP94 chaperone system, and also of the CNX/CRT chaperone system, but apparently not the thiol oxidoreductases such as PDI.
21093319	0.98	ERp57 and forming a substrate-specific complex with the BiP and Grp94 chaperones.
	0.98	BiP multichaperone complex and ERp57 in the absence of the calreticulin and calnexin chaperones.
	0.97	ERp57, and BiP were efficiently coimmunoprecipitated with anti-Mzb1 in the absence of Ca2+ and less efficiently in the presence of 2.5 mM Ca2+, suggesting that these proteins associate with Mzb1 in a calcium-dependent manner (Figures 3C and 3D).
	0.95	BiP, as well as the protein disulfide isomerases ERp57 and PDIA6 (CaBP1) as Mzb1-associated proteins (Figure 3B and Table S2).
21559407	0.98	Grp78/BiP, Grp58/Erp57 and Grp94, and activated caspase-12, a protein involved in ER stress-induced apoptosis.
	0.97	Grp78/BiP and Grp58/Erp57, were induced in sporadic and variant CJD, and in bovine spongiform encephalopathy, and their up-regulation correlated with disease progression in prion-infected mice.
	0.96	Grp78/BiP and Grp58/Erp57 are not induced in the brain and primary neurons from mutant PrP mice.
	0.75	Grp78/BiP, Grp58/Erp57 and CHOP/GADD153 in the brains of Tg(PG14) and Tg(CJD) mice at different stages of their neurological illness.
24364984	0.98	GRP78, GRP94 and ERp57.
	0.98	GRP78 (Bip), ATF650kDa, a PDI-ERp57 and CHOP.
	0.93	GRP78 (Bip), GRP94, and ERp57.
	0.62	GRP78 in HDM challenged mice treated with Si-ERp57 + ATF6alpha as compared to Si-scr.
16696860	0.98	BiP, CHOP, Calreticulin and grp58, are known to be specifically associated with ER stress.
	0.97	BiP (grp78), CHOP (Gadd153), calreticulin, and grp58 in cultured microglia, and BiP and CHOP in microglia enriched fractions from infected mouse brains, indicated that FrCasE infection did not induce these ER stress genes either in vitro or in vivo.
	0.81	BiP, CHOP, calreticulin or Grp58 was observed in FrCasE-infected microglial cultures when compared with mock or Fr57E-infected cells.
19851784	0.98	BiP, Grp98 and PDI, and are targeted for degradation (Schroder).
	0.97	BiP, CRT, PDI, ERp72 and Grp94 were localised to the electron-dense material in the dilated ER (Hecht et al.).
	0.91	PDI), Grp94, ERp72 and BiP (Grp78; Hecht et al.; Vranka et al.).
21670312	0.98	PDI and BiP (Fig. 3A).
	0.97	BiP, gp96 and PDI are induced by thapsigargin treatment, which depletes ER calcium, but not by tunicamycin treatment, which inhibits protein glycosylation.
	0.97	BiP, PDI and gp96 may in part involve calcium-dependent processes.
23370284	0.98	Grp58, Grp78, and Grp94 proteins, which are expressed in the endoplasmic reticulum (ER) and are involved in primary folding of nascent proteins translated in the ER.
	0.94	Grp58 associated with 22L and 139A strains while Grp78 and Grp94 were selectively upregulated in ME7 and 87V infected mice and in APPPS1-21 mice.
	0.85	Grp78, and Grp94 levels but not Grp58 level.
24046357	0.98	BiP (Hspa5), Hsp47, PDIA1, PDIA3, PDIA4, PDIA6, Grp94 (Hsp90b1) and calreticulin.
	0.97	BiP, ERp57 (PDIA3), calreticulin (CRT) and calnexin (CNX) transcripts were normal in the chondrocytes of Col2-Tgrdw mice.
	0.97	BiP (~twofold, P<0.0001), PDI (~threefold, P<0.01) and ERp72 (PDIA4; ~twofold, P<0.001), but normal levels of ERp57 (PDIA3) in Col2-Tgrdw mice (Fig. 4A,B); increased levels of GRP94 in Col2-Tgrdw chondrocytes was confirmed by MS (Fig. 4C).
30430766	0.98	PDI, GRP78, XBP1 and thrombospondin protects cardiomyocytes from ER stress as well as improving cardiac function (Kitakaze and Tsukamoto 2010; Toldo et al. 2011; Wang et al. 2017).
	0.82	GRP78, PDI, and CHOP) and pro- (Bax, Caspase 3) and antiapoptotic (Bcl2), prooxidant (eNOS, Nox4, Gp91-phox) and antioxidant (Nrf2, MsrA) signaling pathways, in relation to calcium-handling proteins in AS-overexpressing female mice.
	0.77	GRP78, PDI, CHOP)
31607947	0.98	ER chaperones GRP 94, calnexin, GRP78, calreticulin, and ERp72 was enhanced in the pathological muscle area.
	0.98	ER stress, and found involvement of ATF4, XBP-1, GRP78, eIF2alpha, PERK, CHOP, IRE1alpha, ATF6, and ATF3 in acutely damaged TA muscles of B6 mice on day 4 or 7 post injury, compared to healthy muscles (Figure 1A).
	0.97	ER stress and UPR activation, we further performed qPCR and verified that the expression levels of XBP-1S, ATF4, eIF2alpha, ATF6, CHOP, GRP78, and GRP94 were elevated in the damaged muscles on day 4 and 7 but were decreased on day 10 and 14 post injury (Figure 1B).
22961085	0.98	BiP, calnexin, eIF2ak3, eIF2as1, and PDIA3 (Fig. 4A-E).
	0.97	BiP, calnexin, eIF2ak3, eIF2as1, and PDIA3 to the levels in the nondiabetic WT group (Fig. 4A-E).
23750325	0.98	GRP78 belongs to the large ER chaperone network along with other molecular chaperones including GRP94, PDI, ERp72, GRP170/ORP150, CaBP1 (calcium binding protein), cyclophilin B and SDF2-L1, which processes unfolded protein substrates.
	0.98	BiP, PDI, calnexin and GRP94, through oxidative "wear" during the aging process.
28431525	0.98	GRP58, HSPA5 and HSP70 has been reported.
	0.96	HSPA5, PDIA3, ATP5A1, GAPDH and beta-actin) are annotated as "myelin sheath" associated proteins.
32029702	0.98	GRP78 and PDI, in these cells.
	0.97	GRP78 and PDI upregulation specifically in the neck region of Manf-deficient OHCs.
21503947	0.98	GRP78 in UPR, the loss of GRP78 activated the three branches of UPR as indicated by increased phosphorylation of IRE1alpha, PERK, eIF2, JNK and serine of IRS, altered expression of GRP94, ORP15, PDI, CHOP, ATF4, Trib3, Gadd34, FoxO, IL-6Ralpha, C1q, TNFR1, and hepcidin 2 involved in UPR or ER stress response.
24915520	0.98	BIP, and ERp72 levels were significantly elevated in Perk+/- beta-cells, while ERp57 mRNA was reduced (Fig 7A).
30978945	0.98	GRP78 and heat shock protein glucose-regulated protein (GP96, also known as GRP94), and this led to a modest increase in the protein expression of ATF4 and endoplasmic reticulum resident protein 57.
28933220	0.97	HSPA5, GNG11, CALR, and PDIA3 are significantly upregulated and HGF, H2-L, NFKBIA, CCL17, and IL12RB1 are significantly downregulated at subacute phase.
	0.88	HSPA5, CALR, and PDIA3; downregulation: H2-L) were activated by RNA-seq (Table 3; Fig. 3).
	0.75	HSPA5, CALR, and PDIA3) and 1 downregulated gene (H2-L) in antigen processing and presentation.
21799787	0.97	ERp57 and GRP78 were expressed in the spermatocytes with the decreased expression of ERp57 and increased expression of GRP78 in the ICSI testis.
	0.92	ERp57 decreased and that of GRP78 and Omi increased in ICSI testes when compared to the control group.
27535430	0.97	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).
22110961	0.97	ERp57 and Derl3 in the liver GRP78 knockouts, leading to aggravated lipid accumulation in the liver.
22623366	0.97	ERp57, total GRP78, KDEL-positive GRP94, and ORP150 in the liver of LPS-challenged GSNOR-/- mice were reversed by further genetic deletion of iNOS (Fig. 5D).
23123197	0.97	GRP78, GRP75, and endoplasmic reticulum (ER) protein (ERp)72 (Figure 4A).
24022788	0.97	Grp78, heat-shock proteins, valosin-containing protein, PDIA3, calnexin) are linked with the UPP in myositic skeletal muscle.
28439080	0.97	Pdi (C,D) and Grp78/BiP (E,F) in wild-type (C,E) and Tg-ERG (D,F) mouse prostates show elevated expression.
29565997	0.97	HSPA5, PDIA3, CALR, GANAB and HYOU1 suggesting its functional link with protein folding and response to stress.
30400605	0.97	GRP78, CHOP, and XBP1-downstream target genes, ER degradation enhancing alpha-mannosidase-like protein (EDEM) and protein-disulfide isomerase-associated 3 (Pdia3) (Figure 7A-E).
30713523	0.97	PDI, ERC1, FXYD2, KCIP-1, histone H4, GRP78 (p < 0.01), ACO2, and PRDX2 (p < 0.001) (Figure 6D).
30713500	0.96	GRP78 (p < 0.05) and HSP47 (p < 0.01) were increased (Figures 2C,D), suggesting partial induction of UPR by 2-week sACVR2B-Fc administration, while other UPR indicators were unchanged (PERK, PDI, and IRE1alpha) (Figures 2E-G).
25309899	0.94	ERP57 knockdown inhibited caspase-3 activation and further protected against hyperoxia-induced apoptosis, while ERP57 overexpression exacerbated hyperoxia- or tunicamycin-induced apoptosis and augmented caspase-3 activation, while reducing GRP78 induction.
30647818	0.94	BiP, GRP94, ERp57, or UDP-glucose-glycoprotein glucosyltransferase results in embryonic lethality.
28428745	0.92	GRP78, and DJ-1 were significantly lower in early ALS than in late ALS, and therefore can be considered phenotypic biomarkers (Figures 2A-C,E), while ERp57 did not change (Figure 2D).
24918436	0.89	BiP, PDI A3, IRE, XBP1, and ATF6 were unchanged following uridine treatment ( Figure 2A, B ).
20428984	0.85	BiP, Grp94, calnexin, ERp72, calreticulin and ERp57 were unchanged in treated mice compared to untreated mice (Table 2).
	0.64	PDI, BiP or Grp94, and this disparity in the chaperone protein profile between the in vitro and in vivo studies is most likely due to differences in the recognition and processing of full-length mutant matrilin-3 (this study) compared to the mutant A-domain alone (Cotterill et al.).
26764098	0.78	BiP and PDI), or the cytosolic protein GAPDH.