Publication for Pdia3 and Pdia6
| Species | Symbol | Function* | Entrez Gene ID* | Other ID | Gene coexpression |
CoexViewer |
|---|---|---|---|---|---|---|
| mmu | Pdia3 | protein disulfide isomerase associated 3 | 14827 | [link] | ||
| mmu | Pdia6 | protein disulfide isomerase associated 6 | 71853 |
| 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. | |
| 0.92 | PDIA3, PDIA4 and PDIA6) was not dramatically changed. | |
| 22719900 | 0.98 | PDIA3 (ERP57), PDIA5, PDIA6 (TXNDC7), PDIA10 (ERP44/TXNDC4) and PDIA11 (TXNDC1) were up-regulated in caput and/or cauda tissue samples of the double mutant animals compared to WT. |
| 0.97 | PDIA3 (ERP57), PDIA5, PDIA6 (TXNDC7), PDIA10 (TXNDC4/ERP44) a PDI-chaperone protein which was shown to be involved in the control of oxidative protein folding and PDIA11 (TCXNDC1), were found significantly up-regulated in the epididymis of the double mutant animals. | |
| 22860010 | 0.98 | 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.). |
| 24046357 | 0.98 | PDIA3, PDIA4, PDIA6, Grp94 (Hsp90b1) and calreticulin. |
| 24843047 | 0.98 | Pdi and Pdia6 transcript levels were significantly increased (Supplementary Fig S5C-E). |
| 26321202 | 0.98 | PDIA3, PDIA6) in the Type I SMA MNs (Figure 2F), suggesting the activation of the UPR pathway in these MNs. |
| 27138799 | 0.98 | Pdia3, Pdia4, Pdia6, Sec61g and Herpud1), in particular to the ER-associated degradation pathway. |
| 29382365 | 0.98 | ERp57, calnexin/calreticulin, and PDIA6, and assists in folding of Igmu heavy chain. |
| 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). |
| 29283886 | 0.97 | Pdia3 and Pdia6), which exist in the ER lumen and provide a disulfide bond, was changed significantly. |
| 0.97 | PDIA3, and PDIA6) were reduced, with the reduction in Pdia3 the most pronounced (Figure 4A-C). | |
| 0.97 | PDIA6 have a known role in the folding of glycoproteins that may have an important impact on ER stress, but the ablation of the PDIA3 protein did not affect the expression of PDI or PDIA6 (Figure 5C). | |
| 0.84 | PDIA6, we wondered whether PDIA3 could also bind to IRE1alpha. | |
| 31260448 | 0.97 | PDIA3 and PDIA6. |
| 0.97 | Pdia3, Pdia4, Pdia6 and Xbp1 gene expression. | |
| 0.91 | Pdia3 and Pdia6 are upregulated both in EDM5 and in AD, and Cryab, Dnaja4 and Hsph1 are downregulated in both conditions whilst ERAD components are not affected. | |
| 21093319 | 0.97 | ERp57 and PDIA6 (CaBP1) as Mzb1-associated proteins (Figure 3B and Table S2). |
| 26151086 | 0.97 | PDIA3 and PDIA6) and selenoprotein 15 (SEP15) were up-regulated in insulin resistant islets. |
| 27097807 | 0.97 | PDI (PDIA3 and PDIA6) was shown to be a marker for aggressiveness in primary ductal breast cancer. |
| 29262583 | 0.97 | PDI, PDIA6, ERp57, ERp72 are strongly expressed in all xenografts. |
| 32232194 | 0.97 | Pdia3, Pdia6, and Pdia4) are found associated with secreted milk fat globules. |
| 23956175 | 0.96 | Pdia3/Erp57, Pdia4/Erp72 and Pdia6/P5, while PDI was shown to be up-regulated by western blotting. |
| 0.69 | 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 | Pdia3, and Pdia6 were previously detected in proteomic studies enriching 14-3-3 proteins to identify novel binding partners. |
| 0.94 | Pdia3, Pdia4, Pdia6, Sel1l, and Eef2), within the context of the larger network of compared proteins obtained by LC-MS/MS. | |
| 31184304 | 0.95 | Pdia6 or Pdia3 mRNAs (Figure 1B). |
| 30397214 | 0.71 | PDI A3 and PDI A6 (Table 2). |
| 24508390 | 0.67 | 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). |
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