Publication for Pdia3 and P4hb

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Pdia3	protein disulfide isomerase associated 3	14827			[link]
mmu	P4hb	prolyl 4-hydroxylase, beta polypeptide	18453

Pubmed ID	Priority	Text
19023445	0.99	PDIA1, PDIA3, PDIA4 and PDIA6 proteins.
	0.98	PDIA1 and PDIA3.
	0.98	PDIA1, PDIA3, PDIA4 and PDIA6 proteins, in response to Thapsigargin, a pharmacological ER-stress agent.
	0.98	PDIA1 and PDIA3.
	0.98	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	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).
	0.90	protein disulfide isomerase family (PDIA1, PDIA3, PDIA4 and PDIA6) was not dramatically changed.
29542339	0.98	PDI and ERp57, a subpopulation of ERp5 is transported to the cell membrane and extracellularly, where it carries out its extracellular functions, including thrombus formation.
	0.98	PDI and ERp57, ERp5 is secreted from platelets upon cell activation, and inhibition of ERp5 activity using anti-ERp5 antibody prevents platelet aggregation and fibrinogen binding to the activated platelets in vitro.
	0.98	PDI and ERp57 in the ER are unique, with the latter having propensity to modify disulfide bonds in glycoproteins.
	0.97	PDI, ERp57, ERp5 and ERp72 are implicated in thrombus formation.
	0.96	PDI, extra-ER sites of ERp57 storage are not known, although it is found in the membrane fraction of the endothelial cells in addition to the ER.
	0.96	PDI, 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.
	0.95	PDI or ERp57 did not rescue aggregation defect in ERp72-null platelets, supporting a distinct role of ERp72 in platelet function.
	0.95	ERp57 antibodies further impair platelet aggregation, ATP release and IIbbeta3 activation in PDI-null mouse platelets.
	0.94	ERp57 is primarily located in the ER and like PDI contains the ER retention sequence, KDEL.
	0.91	ERp57 and PDI accounting for different substrate specificities.
	0.90	PDIA3, ERp57 shares a common domain structure with PDI.
	0.83	ERp57 interacts with lectin chaperones calnexin and calreticulin, whereas PDI does not.
	0.82	PDI, the extracellular substrates of ERp57 in plasma or those released from activated platelets have not been identified although preliminary studies indicate that ERp57 targets the components of the lectin pathway of complement activation (Eriksson and Furie, 2018) Vitronectin is not a substrate of ERp57.
	0.71	PDI, ERp57 and ERp5.
	0.59	ERp57fl/flPF4Cre-positive mice that do not express ERp57 in their platelets have normal fibrin generation, similar to the results obtained for PDI.
29994898	0.98	PDI, 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.
	0.98	PDI, ERp57, ERp5 and ERp72 have roles in fibrin deposition in vivo.
	0.98	PDI and ERp57 are found in the dense tubular system (DTS) of platelets and are released on the surface of activated platelets in an actin-dependent process.
	0.97	PDI, ERp5, ERp57 and ERp72 are present on the resting platelet surface, and the levels increase following platelet activation.
	0.95	PDI, ERp57, ERp5, AND ERp72 ARE REQUIRED FOR PLATELET FUNCTION AND COAGULATION
	0.94	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.
	0.94	PDI, ERp57, ERp5, and ERp72 with alphaIIbbeta3 is unknown, a single PDI molecule could interact with multiple molecules of alphaIIbbeta3.
	0.88	PDI, ERp57, ERp5 and ERp72 interact with substrates by different mechanisms.
	0.88	ERp57 have roles in GPVI-stimulated Ca2+-mobilization in platelets, while PDI and ERp5 do not.
	0.86	PDI, ERp57, and ERp72 have distinct roles in platelet aggregation
	0.83	PDI and ERp57, and the a and a' active site of ERp72 support thrombosis.
	0.68	PDI, ERp57, and ERp72 contain a flexible x-linker domain.
	0.52	PDI, ERp57, ERp5 and ERp72 with the alphaIIbbeta3 fibrinogen receptor
31956274	0.98	PDIA1 and PDIA3 have recently been identified as two activators of alphaVbeta3 integrin through isomerization of disulfide bonds in integrin beta3 subunits.
	0.98	PDIA1 or PDIA3 at the cell surface causes beta3 integrin inactivation and then impairs the cellular capacities for migration, adhesion, and fusion, which are all basic cell behaviors involved in myogenesis during muscle regeneration.
	0.98	PDIA1 and PDIA3 were expressed in undifferentiated myoblasts and that PDIA3 expression was correlated with the levels of the myogenic marker proteins myogenin and MyHC, which increased gradually during C2C12 myoblast differentiation.
	0.97	PDI family members (PDIs) are localized within the endoplasmic reticulum (ER); however, some PDI family members can escape from the ER and be secreted into the ECM or translocate to the cell surface, such as PDIA1 and PDIA3.
	0.97	PDI isoform PDIA3 plays a major role in mediating myogenesis, whereas the PDI isoform PDIA1 plays little or no role in this process.
	0.92	PDIA1 and PDIA3 plays a role in myogenesis is unknown.
	0.87	PDI family, further study of the mechanism underlying the effects of other PDIs (such as PDIA1 and PDIA2) on myogenesis is warranted.
	0.83	PDI participated in the regulation of skeletal muscle regeneration, we first measured the mRNA and protein levels of PDIA1 and PDIA3 in regenerated adult mouse skeletal muscle in the CTX injury model.
26361352	0.98	ERp57, and its closest homologue PDIA1, are also upregulated in the spinal cord from sporadic ALS cases.
	0.98	ERp57 and PDIA1 are among the strongest induced proteins in symptomatic animals.
	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	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).
	0.92	PDIA1 and ERp57 in models of Huntington's disease and AD.
	0.85	PDIA1 and ERp57 were also identified as possible biomarkers to monitor disease progression in blood samples from ALS cases.
	0.59	ERp57 and PDIA1 in ALS cases.
27073369	0.98	PDIA1 and ERp57 in promoting neurite outgrowth and connectivity, an activity fully loss when the ALS-linked mutants were expressed (Woehlbier et al., 2016).
	0.97	ERp57 and PDIA1 in PMDs (reviewed in Andreu et al., 2012).
	0.96	ERp57 and PDIA1 is detected in PMDs.
	0.96	PDIA1 modified its enzymatic activity, whereas mutations in ERp57 altered the physical association with calnexin and calreticulin (Woehlbier et al., 2016).
	0.94	ERp57 and its closest homologue PDI (also known as PDIA1) to diseases affecting the central nervous system, including amyotrophic lateral sclerosis (ALS), Parkinson's disease (PD), Alzheimer's disease (AD), among others (Andreu et al., 2012).
	0.91	ERp57 and PDIA1 as risk factors to develop ALS (Gonzalez-Perez et al., 2015).
	0.88	ERp57 and protein disulfide isomerase (PDI) in neurodegeneration.
26435004	0.98	PDI, ERp57, mediates misfolded protein-induced apoptosis by oligomerization of pro-apoptotic Bak through the formation of inter-molecular disulfide (-S-S-) bridges and the permeabilization of mitochondria.
	0.98	ERp57 is a protein disulfide isomerase that specifically facilitates disulfide (-S-S-) bond formation on glycoproteins being processed and secreted by the ER.
	0.98	protein disulfide isomerase-ERp57 modulates allergen induced inflammation, AHR and airways fibrosis in the lung.
	0.97	PDI-AGR2, and not ERp57.
	0.92	Protein Disulfide Isomerase-ERp57 regulates allergen-induced airways inflammation, fibrosis and hyperresponsiveness
21111739	0.98	PDI and ERp57.
	0.97	PDI and ERp57 were increased by 40% in ethanol-fed wild-type mice compared to controls (Figs. 6C-6D).
	0.90	PDI and ERp57 were reduced in the absence of sXBP1 upregulation (Xbp1+/- mice).
21419848	0.98	ERp57 is a thiol oxidoreductase of the protein disulfide isomerase family that acts as a molecular chaperone.
	0.97	PDI (ERp57) was increased in mutant Purkinje cells compared to control cells.
	0.77	ERp57, a protein disulfide isomerase (PDI) in Purkinje cells of 1 month Tsc2f/f;Cre mice (D) compared to control (C).
22355653	0.98	PDI, and PDIA3, which are members of protein disulfide isomerase (PDI) family that play role in oxidative protein folding.
	0.97	PDI, and PDIA3 is dependent on CBF activity in hepatocytes in vivo.
	0.88	protein disulfide isomerase (PDI) family genes, ERP72, PDI and PDIA3, with a progressive reduction from 2 to 4 weeks.
24046357	0.98	protein disulfide-isomerase (PDI) and ERp57].
	0.98	PDIA1, PDIA3, PDIA4, PDIA6, Grp94 (Hsp90b1) and calreticulin.
	0.97	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).
24677236	0.98	Protein disulfide isomerase, ERp5 and ERp57, among perhaps other thiol isomerases, are important for the initiation of thrombus formation.
	0.97	Protein disulfide isomerase (PDI) has long been identified as a critical functional component of the biosynthetic pathway in the synthesis of proteins.
	0.85	Protein disulfide isomerase as an antithrombotic target is being explored using isoquercetin and quercetin 3-rutinoside, inhibitors of PDI identified by high throughput screening.
23874395	0.98	ERp57 and PDI was completed inhibited in ATF4-/-/SOD1G86R animals when compared to control SOD1G86R mice (Figure 3A, B).
	0.75	PDI-family members in the spinal cord of mutant SOD1 transgenic mice, including ERp57 (also known as Grp58), PDI, and ERp72.
24324498	0.98	PDIA1 and ERp57 (also known as Grp58 or PDIA3) as major up-regulated proteins was the first study suggesting a possible participation of PDIs in ALS.
	0.96	PDIA1 and ERp57 may actually have a pro-apoptotic activity in models of Alzheimer and Huntington's disease.
24364984	0.98	PDI, ERp57, mediates misfolded protein-induced apoptosis by oligomerization of Bak through the formation of inter-molecular disulfide (-S-S-) bridges and the permeabilization of mitochondria.
	0.98	PDI-ERp57 and CHOP.
28439080	0.98	P4hb/Pdi in Tg-ERG mouse prostates, a significant correlation of P4HB/PDI up-regulation was observed in ERG positive human prostate tumors (Fig. 4G).
	0.97	P4hb/Pdi (C,D) and Grp78/BiP (E,F) in wild-type (C,E) and Tg-ERG (D,F) mouse prostates show elevated expression.
18851953	0.98	GRP58), a 58-kDa protein with significant homology to protein disulfide isomerase has two thioredoxin-like domains and is suspected to function as thiol-dependent oxidoreductase.
20569467	0.98	ERp59 and ERp61 are normally in the endoplasmic reticulum, their detection in conditioned medium may suggest suggest that the early embryo's membrane may be actively remodeled by vesicular fusion.
21093319	0.98	protein disulfide isomerase (PDI) and ERp57 (PDIA3), allows for the efficient folding of glycoproteins by catalyzing the formation and isomerization of intra- and intermolecular disulfide bonds.
22860010	0.98	Pdia1, Pdia3 and Pdia6, Table 1), and heat shock proteins (Hspd1, Hspa2, Hspa9, Table 1), which are modulated in other models of cellular stress (e.g.).
26839892	0.98	PDI and GRP58, which may lead to increased unfolded protein load in mesangial cells and induction of proteasomal degradation processes.
28167899	0.98	PDIA1 and PDIA3 (also known as ERp57) are up-regulated in spinal cords of SOD1G93A mice, from pre-symptomatic to end stages of disease, and in tissues (spinal cord and peripheral blood mononuclear cells) from sALS patient (Atkin et al.,; Nardo et al.,).
30735910	0.98	PDIA1 is found at high levels in the secretory granules of eosinophils, and we have previously shown siRNA knockdown or ablation of Pdia3 in lung epithelial cells decreases various cytokine levels, and alters oxidative folding of Eotaxin, EGF and Periostin in mice.
18949096	0.97	ERp57 and PDI were during embryonic development, while these proteins are barely detectable in adult tissues.
	0.97	Erp57 and PDI is higher in embryonic hearts than adult hearts.
	0.86	PDI and ERp57 Expression During Heart Development
	0.76	ERp57 and PDI during mouse heart develop-ment.
	0.52	PDI and ERp57 during mouse embryo development, we performed Western blot analyses of PDI and ERp57 in mouse embryonic and adult heart tissues.
25156521	0.97	PDI contributes to fibrin deposition in vivo and endothelial cells also secrete ERp57 that may be involved in fibrin deposition.
	0.96	PDI and ERp57 have distinct roles in coagulation.
	0.95	ERp57fl/fl mice (Fig. 2A, B, D) implies that PDI cannot compensate for the loss of ERp57.
	0.94	PDI catalyzes similar reactions as ERp57 and may directly modulate tissue factor activity raising the possibility that ERp57 also affects tissue factor activity.
	0.83	PDI and ERp57 in coagulation.
28109037	0.97	ERp57, the closest homologue of PDI in platelets, are important for platelet function and thrombosis.
	0.97	PDI, the C-terminal active site of ERp57 supports platelet aggregation, and platelet accumulation and fibrin generation in vivo.
	0.82	ERp57, ERp5 and thioredoxin, and to inhibit both active sites of PDI.
19889996	0.97	Erp57 is a PDI homolog that shares enzymatic functions with PDI, but unlike PDI, forms direct interactions with the ER lectins calnexin and calreticulin.
	0.91	PDI-related protein Erp57 (Suppl.
22623366	0.97	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	PDI, 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.
20193000	0.97	ERp57 or PDI), which might target it for degradation prior to optimal peptide loading.
21629710	0.97	protein disulfide isomerase (PDI) family: disulfide-isomerase A3 (Pdia3).
22443930	0.97	PDI and ERp57) depends on the ER Ca2+ concentration.
23592792	0.97	ERp57 (protein-disulfide isomerase A3) and SPARC (secreted protein acidic and rich in cysteine), are classically secreted proteins and have a predicted signal peptide.
24118938	0.97	PDI and ERp57 with blocking antibodies affects not only thrombosis but also hemostasis in mice, the function of platelet PDI is probably limited to the propagation step of thrombus formation, whereas PDI released from other intravascular cells could be important for the initiation of thrombogenesis and hemostasis (Fig. 2).
25309899	0.97	PDI family member Erp57 (PDIA3; GRP58) correlates with the accumulation of misfolded prion protein.
25913742	0.97	PDI family members known as PDIA1 (also referred to as PDI or P4HB) and ERp57 (also referred to as PDIA3 or Grp58), a finding that was confirmed in spinal cord tissue and cerebrospinal fluid of sALS patients.
26725377	0.97	PDI, ERp57, and ERp5 have been implicated in thrombus formation.
26854753	0.97	PDI, ERp5, or ERp57 blocks thrombus formation in mouse models, indicating distinct and essential roles for each of them.
28218242	0.97	ERp57 produce a fingerprint of mixed disulfide complexes distinct from PDI, suggesting unique sets of substrates (Fig. 2c).
29160038	0.97	PDIA1 (PDI) and PDIA3 (ERp57) are protective against neurodegenerative diseases related to protein misfolding, including ALS, which is a rapidly progressing disorder affecting motor neurons in the brain, brainstem and spinal cord, resulting in paralysis and death usually 2-5 years post-diagnosis.
31260448	0.97	PDIA1, PDIA3 and PDIA6.
23956175	0.96	Pdia3/Erp57, Pdia4/Erp72 and Pdia6/P5, while PDI was shown to be up-regulated by western blotting.
	0.68	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.
29930975	0.96	Pdia1, Pdia3, and Pdia6 were previously detected in proteomic studies enriching 14-3-3 proteins to identify novel binding partners.
	0.94	P4hb, Pdia3, Pdia4, Pdia6, Sel1l, and Eef2), within the context of the larger network of compared proteins obtained by LC-MS/MS.
26986548	0.96	PDI, ERp5 or ERp57.
19147124	0.95	PDI A1 and PDI A3 would be likely to affect perforin, consistent with our observations that granule fractions containing PDI A3 and purified PDI A1 have CxRP2 activity.
	0.91	PDI A1 and PDI A3 bind proteins through two domains, the a and b'.
	0.72	PDI A3 is predicted to have disulfide oxidase and reductase activities similar to protein disulfide isomerase (PDI).
21079601	0.95	protein disulfide isomerase (PDIA1 and PDIA3) as specific targets of 16F16A which we then confirmed by competitive binding assays, labelling purified PDI, and a Western blot of affinity purified target proteins (Fig. 3b-d, Supplementary Tables 1, 2, and 3).
26282323	0.94	PDIA1 (PDI) and PDIA3 (ERp57) have been reported, as well as intronic variants of PDIA1 as a genetic risk factor for ALS, which warrants further attention to the involvement of this key protein in oxidative folding in the pathogenesis of ALS.
31184304	0.93	Pdia1 mRNA in isolated islets from the ss cell-specific Pdia1-knock out mice (Pdia1 fl/fl;CreERT herein, KO, but genotypes are defined in the figures) with no effects on Insulin 2, Pdia6 or Pdia3 mRNAs (Figure 1B).
22934019	0.73	protein disulfide isomerase (PDI) and ERp57.
30207066	0.56	ERp57 inhibited platelet aggregation in a manner similar to SNO-PDI (Fig. 7D-F).
24508390	0.55	PDIA1 (P4HB), which is 2.5X more abundant than PDIA6 in 3T3 cells, or PDIA3, which has a known role in folding of glycoproteins, had no effect on UPR responsiveness (Fig. 1F-G and Fig. 3 below).