Publication for Pdia4 and Pdia3

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Pdia4	protein disulfide isomerase associated 4	12304			[link]
mmu	Pdia3	protein disulfide isomerase associated 3	14827

Pubmed ID	Priority	Text
19023445	0.99	PDIA3, PDIA4 and PDIA6 proteins.
	0.98	PDIA3, PDIA4 and PDIA6 proteins, in response to Thapsigargin, a pharmacological ER-stress agent.
	0.91	PDIA3, PDIA4 and PDIA6) was not dramatically changed.
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	ERp72 was elevated (Figure 8B) and became localized to large balloon-like structures in Impacted-ER cells (Figure 4B).
	0.98	ERp72 protein, AdDNPerk-832/13 beta cells exhibited an increase in the oxidized isoforms of ERp72 and ERp57 (Figure 8C) that were first seen at 24 hours post transduction and increased significantly by 36 hours.
	0.98	ERp72 and 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	ERp72, PDI, and ERp57, mediate their oxidative protein folding functions by forming transient mixed disulfides with ER client proteins such as proinsulin.
	0.98	ER, which occurs after the elevation of two key chaperone proteins GRP78/BiP and ERp72.
	0.97	ERp72, a family member of the protein disulfide isomerases (PDI), is localized in the ER and plays a major role in quality control and folding.
	0.97	ERp72 assists proper protein folding whereas PDI facilitates unfolding of misfolded proteins in preparation for proteosomal degradation.
	0.97	ERp72 accumulates in a sub compartment of the ER and its oxidized isoform is substantially increased.
	0.97	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.
	0.95	ERp72 and ERp57 suggests that redox state of the ER is abnormal or that the oxidation and reduction of protein disulfides is imbalanced.
	0.94	ER chaperones ERp72 and GRP78/BiP by treating AdDNPerk-832/13 beta cells with cyclohexamide, a potent inhibitor of protein synthesis.
	0.94	ERp72 and ERp57 in 832/13 cells infected with AdDNPerk compared to cells infected with AdLacZ.
	0.93	ERp72 localization seen in IHC images (Figure 4B) to TEM images of Impacted-ER beta cells suggest that these structures correspond to one of two types of distended ER most similar to Russell bodies.
	0.92	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).
	0.92	PDI family of ER folding enzymes including ERp72 and ERp57 is known to vary according to changes in the oxidative and functional states of the ER.
	0.87	ERp72 is upregulated in cells infected with AdDNPerk and the increase in ERp72 staining appeared earlier than the Impacted-ER phenotype (upper panel, right arrow).
	0.81	ERp72 and ERp57 were also increased suggesting an imbalance in the redox state of the ER.
	0.72	ERp72 in AdDNPerk-832/13 cells was also seen by immunohistochemistry earlier than the appearance of the Impacted-ER cells (Figure 4A).
	0.56	ERp72 and 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.
29994898	0.98	ERp57, ERp5 and ERp72 have roles in fibrin deposition in vivo.
	0.97	ERp57, ERp5, and ERp72 were shown to mediate platelet accumulation and fibrin generation in vivo.
	0.97	ERp57, ERp5 and ERp72 have roles in ATP release from dense granules and P-selectin expression from alpha-granules of platelets, raising the possibility of targets in platelet secretion pathways.
	0.97	ERp57 and ERp72 are present on the resting platelet surface, and the levels increase following platelet activation.
	0.96	ERp57 and ERp72 bind poorly to thrombin-activated or Mn2+-treated platelets lacking the alphaIIbbeta3 integrin suggesting these enzymes also interact with this integrin.
	0.95	ERp57 or ERp72 from platelets results in an ~50-70% decrease in platelet aggregation.
	0.95	ERp72, PDI or ERp57-null platelets was only recovered by the PDI that was missing, implying that each enzyme has a different role in activation of alphaIIbbeta3.
	0.95	ERp57, ERp5, and ERp72 with alphaIIbbeta3 is unknown, a single PDI molecule could interact with multiple molecules of alphaIIbbeta3.
	0.91	ERp57, ERp5, AND ERp72 ARE REQUIRED FOR PLATELET FUNCTION AND COAGULATION
	0.90	ERp72 are similar to ERp57, surface charge differences allow the b' domain of ERp57, but not ERp72, to bind calnexin.
	0.90	ERp72 and ERp57 have roles in GPVI-stimulated Ca2+-mobilization in platelets, while PDI and ERp5 do not.
	0.85	ERp57, ERp5 and ERp72 interact with substrates by different mechanisms.
	0.84	ERp57, and ERp72 have distinct roles in platelet aggregation
	0.83	ERp57, and the a and a' active site of ERp72 support thrombosis.
	0.58	ERp57, ERp5 and ERp72 with the alphaIIbbeta3 fibrinogen receptor
29052936	0.98	ERp72 into mice resulted in delayed thrombus formation, suggesting that ERp72, like ERp5, PDI and ERp57, is crucial for normal platelet function.
	0.98	ERp72 knockout mouse was published that corroborates our findings that ERp72 is important for platelet activation and granule secretion and revealed that similar to ERp57 and PDI, ERp72 is able to form a functional association with, and modulate changes in, the thiol content of integrin alphaIIbbeta3.
	0.93	ERp72 and ERp5 inhibition 10 but not by ERp57 inhibition or PDI deficiency 14, 30.
	0.89	ERp72 confirmed previous findings that some assays of platelet function are sensitive to differential regulation by thiol isomerases, for example ERp72 and ERp57 blockade inhibits GPVI-stimulated Ca2+ flux 14 but ERp5 and PDI ablation does not 10, 30.
	0.85	ERp72, an abundant thiol isomerase, comprises 645 amino acid residues with three catalytically active thioredoxin-like domains similar to those found in ERp5, ERp57 and PDI 1, and sequence analysis reveals that ERp72 is most similar to ERp57 with 40% overall sequence identity.
	0.85	ERp72, ERp57 or PDI was only rescued through supplementation with the respective enzyme that was absent.
22355653	0.98	ERP72, PDI, and PDIA3, which are members of protein disulfide isomerase (PDI) family that play role in oxidative protein folding.
	0.97	ERP72, PDI, and PDIA3 is dependent on CBF activity in hepatocytes in vivo.
	0.96	ERP72, PDI and PDIA3, with a progressive reduction from 2 to 4 weeks.
24046357	0.98	ERp72, but also protein disulfide-isomerase (PDI) and ERp57].
	0.98	PDIA3, PDIA4, PDIA6, Grp94 (Hsp90b1) and calreticulin.
	0.97	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).
19081072	0.98	Erp72, Erp57, p58IPK, Grp94), as well as genes involved in ERAD (Derl3, Edem1), was attenuated in Atf6alpha-null livers (Figure 2B).
21384408	0.98	ERp72, PDI, was shifted towards the oxidized form and ER stress-responsive transcription factor ATF6 was activated by APAP administration at sub-lethal doses.
21935428	0.98	Erp57, Erp72, and Ero1lb, and components of the ERAD pathway such as Derl3 and Syvn1 (Table S6).
22275310	0.98	ERp72, Ero1alpha, and PDI, ERAD components Herpud1 and Wfs1, and the antioxidative stress response nuclear factor-erythroid 2-related factor 2 (Nrf2).
23274897	0.98	p58, Erp72, Fkbp11, and Grp94; Fig. 3A) and deleterious (Atf3, Chop, and Trib3; Fig. 3C) UPR genes.
23750325	0.98	PDI, ERp72, GRP170/ORP150, CaBP1 (calcium binding protein), cyclophilin B and SDF2-L1, which processes unfolded protein substrates.
24151436	0.98	ERp57, ERp72, PDI and P5) have been found on the equatorial segment of murine spermatozoa with roles in protein refolding which might trigger sperm-oocyte fusion.
24915520	0.98	ERp72 levels were significantly elevated in Perk+/- beta-cells, while ERp57 mRNA was reduced (Fig 7A).
26190652	0.98	ERp57 and ERp72.
27138799	0.98	Pdia3, Pdia4, Pdia6, Sec61g and Herpud1), in particular to the ER-associated degradation pathway.
28718225	0.98	PDI, ERp72, GRP94) in Snell dwarf fibroblasts compared to control fibroblasts, various pro-apoptotic markers (e.g. CHOP, caspase-12 levels, caspase-3 activity, c-JUN phosphorylation) were all significantly increased in Snell dwarf fibroblasts following ER stress (Sadighi Akha et al. 2011).
29515832	0.98	PDI, ERp57, ERp5 and ERp72, have been found to be essential for thrombosis in mice, and proteins involved in thrombosis, such as thrombospondin-1, vitronectin, plasminogen and tissue factor, are known to be regulated by allosteric disulfides.
31004027	0.98	Pdia3, Pdia4, Pdia6, several Hsp, as well as Sel1l and Syvn1 which have been shown to regulate an ER-associated protein degradation (ERAD) pathway (Figure 6F and Online Supplementary Table S1).
31527703	0.98	Pdia3, Pdia4 and Txndc5) are involved in the protein processing in endoplasmic reticulum (ER) pathway (KEGG identifier mmu04141, odds-ratio = 6.7, P-value = 0.002, Fisher's Exact test, see Fig. 6C), enlightening the molecular basis of the changes in ER architecture that take place during the transition from oocyte to embryo and that are concomitant to the increase in protein synthesis and folding after EGA.
32232194	0.98	Pdia3, Pdia6, and Pdia4) are found associated with secreted milk fat globules.
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.).
22623366	0.97	ERp72, ERp5, PDI, 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).
	0.97	ERp57, ERp72, and ERp5 was downregulated by iNOS-derived S-nitrosylation in liver of GSNOR-/- mice, and that ERp72 and ERp5 were readily S-nitrosylated.
23874395	0.97	ERp72 in SOD1G86R mice, which may represent compensatory mechanism due to ERp57 down regulation as previously suggested.
	0.81	ERp57 (also known as Grp58), PDI, and ERp72.
31260448	0.97	Pdia3, Pdia4, Pdia6 and Xbp1 gene expression.
	0.96	Pdia3, Pdia4, Trib3 and Xbp1 (S1 Table).
23040069	0.97	Erp57 and Erp72, which are not regulated by XBP1s, was unchanged (Figure 6A and Figure S5A).
26361352	0.97	PDI family members, PDIA1 and ERp72 in dissected midbrain regions, and observed a significant increase in Non-Tg animals injected with 6-OHDA (Fig 2A).
26700264	0.97	PDIA3, PDIA4 and TXND5, with substantially increased levels of SSG modifications after exposure to CoO ENPs.
28379196	0.97	ER Protein (ERP) 57 and ERP72.
28487627	0.97	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.
29262583	0.97	PDI, PDIA6, ERp57, ERp72 are strongly expressed in all xenografts.
29542339	0.96	ERp57, ERp5 and ERp72 also play a role in initiation of thrombus formation but their specific extracellular substrates are unknown.
	0.96	ERp57 did not rescue aggregation defect in ERp72-null platelets, supporting a distinct role of ERp72 in platelet function.
	0.95	ERp57, ERp5 and ERp72 have already been implicated in thrombus formation, the full repertoire of thiol isomerases that participate in thrombosis remains to be identified.
	0.93	ERp57, ERp5 and ERp72 are implicated in thrombus formation.
	0.62	ERp72-knockout mice that do not express ERp72 in platelets, but retain normal levels of PDI, ERp57 and ERp5.
23956175	0.96	Pdia3/Erp57, Pdia4/Erp72 and Pdia6/P5, while PDI was shown to be up-regulated by western blotting.
	0.66	ERp57 (PDIA3), PDI (PDIA1), P5 (PDIA6), ERp18 (PDIA6), ERp72 (PDIA4) and ERp46 (PDIA15) all formed higher order mixed disulphides, whereas the repsective wild-type proteins did not.
24677236	0.96	PDI, ERp5, ERp57, ERp44, ERp29, ERp72 and TMX3 are stored and released from platelets (Figure 1).
	0.78	PDI among thiol isomerases and failed to inhibit ERp57, ERp5, ERp72, or thioredoxin reductase , they are highly hydprophobic and have alternative targets.
29930975	0.94	Pdia3, Pdia4, Pdia6, Sel1l, and Eef2), within the context of the larger network of compared proteins obtained by LC-MS/MS.
26246604	0.92	PDI system is also highlighted by the hardly detectable phenotypes in cell lines derived from knockout mice where surrogate PDIs can functionally replace PDIs that have been deleted (e.g., ERp72 efficiently replaces ERp57 in assisting maturation of model glycoproteins, and other examples have been reported.
25518935	0.88	ERp57 and ERp72 (Figure 1A and Supplemental Figure S1A) in both Hepa1-6 and McA cells.
30647818	0.88	PDI or ERp72, could not efficiently compensate for the loss of ERp57.
20428984	0.87	ERp72, calreticulin and ERp57 were unchanged in treated mice compared to untreated mice (Table 2).
23245351	0.87	Pdia3 knockdown revealed partial functional restoration by the PDIA4 protein, although, to date, no Pdia4 knockout mouse has been generated.
25594042	0.86	ERp57 is an ER resident thiol disulfide oxidoreductase while Erp72 is a disulfide isomerase.
24024666	0.76	ERp72 (pdia4), has also shown the chaperon and disulfide isomerase activities in nascent protein folding through forming native disulfide bond, and active site motif of the enzyme is similar to ERp57 (C X X C).
21080494	0.71	ERp72, ERp57, ERp44, ERp29, and ERp46).
20813146	0.70	ERp57 and ERp72).
25973683	0.65	PDIA3 (ERp57), PDIA4 (ERp70), ERp44 and FKBP7, and the N-linked glycosylation factor SDF2L1.
25693198	0.62	PDI and ERp72 (PDIA4) expression which is not mirrored in ColIITgcog mice (data not shown).
18172663	0.59	ERp72, ERp57, ERp44, ERp29, and ERp46).