Publication for Pdia3 and Hsp90b1

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Pdia3	protein disulfide isomerase associated 3	14827			[link]
mmu	Hsp90b1	heat shock protein 90, beta (Grp94), member 1	22027

Pubmed ID	Priority	Text
21093319	0.98	Grp94, Mzb1 augmented the function of the oxidoreductase ERp57 in favoring the expression of integrins in their activated conformation.
	0.98	ERp57 and forming a substrate-specific complex with the BiP and Grp94 chaperones.
	0.98	Grp94, a protein with high-affinity binding sites for Ca2+, and ERp57 interact with their client proteins at high Ca2+ concentrations.
	0.98	Grp94-BiP multichaperone complex and ERp57 in the absence of the calreticulin and calnexin chaperones.
	0.97	Grp94, 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).
	0.97	ERp57 and Mzb1, but not that of Grp94 and Mzb1, suggesting that the association of Mzb1 and ERp57 involves disulfide bonds (Figure 3F).
	0.97	ERp57 and Grp94.
	0.97	ERp57 and Grp94 regulate ER Ca2+ homeostasis.
	0.97	Grp94 and ERp57 to SERCA2b, which was also identified in our proteomic analysis.
	0.96	Grp94 and BiP, as well as the protein disulfide isomerases ERp57 and PDIA6 (CaBP1) as Mzb1-associated proteins (Figure 3B and Table S2).
	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.
	0.85	ERp57 and Grp94.
	0.83	ERp57 and Grp94 in vivo, one might expect some overlap of phenotypes observed in B cells with altered Mzb1, ERp57, or Grp94 expression.
19816510	0.98	GRP94, PDI, CHOP and GADD34, feedback suppression of eIF2alpha phosphorylation and apoptotic cell death.
	0.98	GRP94 and folding enzymes such as PDI to alleviate protein misfolding.
	0.98	GRP94 and PDI were upregulated in almost all PCs of 3 week old F/-; pc-Cre mice (Figure 4a).
	0.98	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	GRP94, PDI, calnexin, GADD34, CHOP, eIF2alpha, calbindin, neurofilament and beta-actin.
	0.97	GRP94, 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.
	0.91	GRP94, PDI, GADD34 and CHOP, and readily detectable level of other cellular proteins including calbindin, eIF2alpha, and beta-actin (Figures 2a, 4 and data not shown), cystolic ubiquitin staining was nearly undetectable in the PCs of F/-; pc-Cre mice by 3 week (Figure 5a).
21670312	0.98	gp96, PDI and BiP (Fig. 3A).
	0.98	PDI and gp96 may in part involve calcium-dependent processes.
	0.98	PDI and gp96 into the apical follicular lumen of cog/cog mice thyroids compared to their wild type counterparts, correlating with significant enhancement in total chaperone levels in the cog/cog thyroid lysates (Jeffery, Kellogg, Arvan and Raghavan, unpublished observations).
	0.97	gp96 and PDI are induced by thapsigargin treatment, which depletes ER calcium, but not by tunicamycin treatment, which inhibits protein glycosylation.
	0.96	PDI and gp96 was detectable for several hours following thapsigargin removal from target cells, although at significantly reduced levels compared to those detected during drug treatment (Fig. S2A, CM1 compared to CM2).
	0.58	gp96 and PDI (Fig. 3B) and induced similar elevations of surface calreticulin expression (data not shown).
20520781	0.98	PDI were upregulated in Grp94-/- ESCs.
	0.96	GRP94 and PDI respectively, but with no change in calnexin (CNX) and calreticulin (CRT) levels.
	0.95	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	GRP94 by increasing 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.
	0.61	PDI, the increase, if any, was minor; and may even slightly decrease upon 16 hr of Tg treatment in the Grp94 null cells (Figure 6A, B).
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	Grp94 and ERp57 chaperone protein expression.
	0.97	Grp94 and ERp57 protein expression (Figure 4A, 4B).
	0.96	Grp94 UPR proteins and increase of ERp57 levels.
	0.92	Grp94 and ERp57 chaperones, in thymocytes treated for different times (1, 2 and 4h) with CPS.
21503947	0.98	GRP94, ORP150, all isoforms of PDI, catalase, GSTmu1 and GSTpi1, UCCR, cytochrome b-5, glyoxylase 1, MUPs; ADRP, FPP and L-FABP (Table S3), confirming the constitutive UPR and impaired energy metabolism at protein levels in LGKO.
	0.98	GRP94, PDI, IRE, p-eIF2alpha, ADRP, L-FABP1 and MUP1, and slight activations of NFkappaB and CREBH in the LGKO liver (Figure 2A).
	0.98	GRP94, ORP15, PDI, CHOP, ATF4, Trib3, Gadd34, FoxO, IL-6Ralpha, C1q, TNFR1, and hepcidin 2 involved in UPR or ER stress response.
	0.88	GRP94, ORP15, PDI, p58IPK, ERdj5 and calreticulin; ubiquitin and protein degradation factors including Usp 4 and 18, Herp1, Ube3b, EDEM2 and derlin3 (derl3); transcription factors regulating apoptosis including Nupr1, CHOP, Trib3, Gadd45 and FoxO; some NFkappaB targeted genes including IL-6 receptor alpha, C1q (TNF related protein 1) and TNFR1 were among the genes with increased expression whereas Biklk and the CREBH targeted gene hepcidin 2 were decreased in LGKO (Table S2).
24364984	0.98	GRP94 and ERp57.
	0.98	GRP94, GRP78 (Bip), ATF650kDa, a PDI-ERp57 and CHOP.
	0.97	GRP94 was not altered following HDM challenge and treatment with Si-ERp57 + ATF6alpha relative to Si-scr HDM groups (Figure 3B and Additional file 1: Figure S2), demonstrating that not all ER stress responders were altered by knockdown of ERp57 and ATF6alpha.
	0.94	GRP94, and ERp57.
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.
	0.95	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	Grp94 levels but not Grp58 level.
24046357	0.98	PDIA3, PDIA4, PDIA6, Grp94 (Hsp90b1) and calreticulin.
	0.97	GRP94, BiP, ERp57 (PDIA3), calreticulin (CRT) and calnexin (CNX) transcripts were normal in the chondrocytes of Col2-Tgrdw mice.
	0.96	ERp57 (PDIA3) in Col2-Tgrdw mice (Fig. 4A,B); increased levels of GRP94 in Col2-Tgrdw chondrocytes was confirmed by MS (Fig. 4C).
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.
21209925	0.98	Grp94, Grp78/BiP and Grp58/ERp57 levels revealed a stronger ER stress response in N2a-RML cells over time when compared to non-infected cells, manifested by a marked increase in the expression of these three ER stress-responsive chaperones (Figure 1F).
	0.98	Grp58, Grp78 and Grp94 (Figure 3A), indicating the occurrence of ER stress.
23750325	0.98	GRP94, PDI, ERp72, GRP170/ORP150, CaBP1 (calcium binding protein), cyclophilin B and SDF2-L1, which processes unfolded protein substrates.
	0.98	PDI, calnexin and GRP94, through oxidative "wear" during the aging process.
29114203	0.98	endoplasmin (Hsp90b1) and protein disulfide-isomerase A3 (Pdia3) decreased in both wild-type and Col6a1-/- mice (Figure 3).
	0.96	Hsp90b1, Pdia3 and tripartite motif-containing protein 72 (Trim72) were decreased.
19081072	0.98	Erp57, p58IPK, Grp94), as well as genes involved in ERAD (Derl3, Edem1), was attenuated in Atf6alpha-null livers (Figure 2B).
19732428	0.98	ER and is controlled by the binding of the ER chaperone proteins, GRP78/BiP and GRP94, and calcium.
20223290	0.98	GRP94 and PDI, are induced.
21559407	0.98	Grp58/Erp57 and Grp94, and activated caspase-12, a protein involved in ER stress-induced apoptosis.
21935428	0.98	Grp94, foldases such as Erp57, Erp72, and Ero1lb, and components of the ERAD pathway such as Derl3 and Syvn1 (Table S6).
23702335	0.98	Grp94, Gadd34, Pdi, Atf4, and Chop in Nrf1+/- livers compared to wild type controls after treatment with bortezomib (Fig. 4C).
24024552	0.98	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.
25321471	0.98	Grp94 and Pdia3, which help in relieving ER stress, and the genes Chop and Gadd34, which mediate pro-apoptosis signal of ER stress, were significantly increased in Arl6ip5Delta2/Delta2 POBs compared with Arl6ip5+/+ (Figure 5b).
29382365	0.98	GRP94, ERp57, calnexin/calreticulin, and PDIA6, and assists in folding of Igmu heavy chain.
29765493	0.98	GRP94), calnexin, and thiol-disulfide oxidoreductase:protein disulphide isomerase (PDI), which belongs to the TRX superfamily.
19851784	0.97	PDI, ERp72 and Grp94 were localised to the electron-dense material in the dilated ER (Hecht et al.).
	0.92	PDI), Grp94, ERp72 and BiP (Grp78; Hecht et al.; Vranka et al.).
	0.55	PDI, Grp78/Bip and Grp94 (Cotterill et al.).
20410492	0.97	gp96 and calreticulin in loading MHC I molecules with peptides is the ability to co-immunoprecipitate either chaperone with MHC I. The recent investigation of the dynamic interactions between ERp57 and tapasin has shed light on their role in the PLC at a molecular and structural level.
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).
26435004	0.97	ERp57 as well as other ER stress markers such as GRP94, cleaved 50 kD fragment of ATF6 (ATF650) and CHOP in HDM challenged mice as compared to those challenged with PBS (Fig 1 B).
26779479	0.97	ERp57, Grp94, and BiP (Hetz et al.,).
28487627	0.97	GRP94, ERdj3, cyclophilin B, PDI, PDIA4, SDF2, and additional members of the PDI family proteins form large protein folding complexes that interact with misfolded and unfolded proteins (Hebert and Molinari,; Halperin et al.,) to assist in their proper processing.
30978945	0.97	GP96, also known as GRP94), and this led to a modest increase in the protein expression of ATF4 and endoplasmic reticulum resident protein 57.
31260448	0.97	Grp94, Hyou1, Manf (Armet), Pdia3, Pdia4, Trib3 and Xbp1 (S1 Table).
31607947	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).
30647818	0.95	GRP94, ERp57, or UDP-glucose-glycoprotein glucosyltransferase results in embryonic lethality.
19666463	0.93	GRP94, and PDI mRNA levels were 1.3 +- 0.1-, 1.4 +- 0.1-, and 1.3 +- 0.1-fold higher, respectively, in Arg-61 apoE astrocytes than WT; p < 0.05) (Fig. 3, A-C).
21853118	0.91	PDI, GRP94, EDEM1, unspliced XBP-1, spliced XBP-1 or CHOP, all involved in the 3 branches of the UPR.
20428984	0.87	Grp94, calnexin, ERp72, calreticulin and ERp57 were unchanged in treated mice compared to untreated mice (Table 2).
	0.60	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.).
22934019	0.84	GRP94), the lectins, calnexin and calreticulin, and the thiol-disulfide oxidoreductases, protein disulfide isomerase (PDI) and ERp57.
25973683	0.78	glucose-regulated protein 94 (GRP94; HSP90B1), calreticulin (CALR), GRP110 (HYOU1), ERdj3 (DNAJB11) and ERdj6 (DNAJC3), the ER foldases PDIA3 (ERp57), PDIA4 (ERp70), ERp44 and FKBP7, and the N-linked glycosylation factor SDF2L1.
22536506	0.62	Grp94, calnexin, PDI, and others.