Publication for Calr and Pdia3

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Calr	calreticulin	12317			[link]
mmu	Pdia3	protein disulfide isomerase associated 3	14827

Pubmed ID	Priority	Text
21263072	0.99	ERp57 binding sites of calreticulin are important for its recruitment into the PLC and for the assembly-promoting functions of calreticulin.
	0.98	calreticulin and ERp57 to the PLC are co-dependent and also dependent upon the ERp57 binding site and the glycan of the assembly factor tapasin.
	0.98	ERp57 and the endoplasmic reticulum (ER) chaperones calreticulin and calnexin.
	0.98	calreticulin recruitment was slightly impacted in cells expressing tapasin(N233Q) (note the slightly higher level of tapasin present in the context of this mutant), and essentially undetectable in cells expressing tapasin(CANQ) (Figure 2A, CRT blot, lanes 1-8) indicated that tapasin's glycan and tapasin-associated ERp57 represented the major modes of calreticulin recruitment to the PLC.
	0.98	calreticulin recruitment to the PLC was abrogated by mutations of the glycosylation and ERp57 binding sites of tapasin.
	0.98	ERp57-dependent interactions contribute to calreticulin recruitment to the PLCs of murine fibroblasts.
	0.98	Calreticulin bound to tapasin's glycan could transiently initiate ERp57 recruitment via a calreticulin P-domain-ERp57 interaction.
	0.98	calreticulin may equilibrate between conformational states in which its recruitment to the PLC is stabilized by tapasin's glycan and tapasin-associated ERp57 (Figure 7A 7B).
	0.98	calreticulin could stabilize the recruitment of both ERp57 and MHC class I molecules via cooperative binding interactions.
	0.98	ERp57 recruitment by transient interaction of ERp57 with the tip of calreticulin's P-domain, thus bringing ERp57 into proximity to tapasin(C95).
	0.97	calreticulin and partner oxidoreductase ERp57 are important in MHC class I assembly, but the sequence of assembly events and specific interactions involved remain incompletely understood.
	0.97	ERp57 or tapasin-calreticulin complexes were not required.
	0.97	calreticulin also interact with their partner ER oxidoreductase ERp57 via an elongated beta-stranded hairpin structure called the P-domain.
	0.97	calreticulin and ERp57 are able to interact independently of other PLC components, P domain-dependent binding between calreticulin and ERp57 could serve as a point for the recruitment of calreticulin into the PLC, in addition to a glycan within the PLC (MHC class I and/or tapasin).
	0.97	ERp57 and tapasin's glycan are the relevant sites that mediate calreticulin recruitment.
	0.97	calreticulin and ERp57 under conditions of heavy chain deficiency, and enhanced recruitment of heavy chains into the PLC of 721.221 cells does not result in a parallel increase in the recruitment of beta2m, calreticulin or ERp57 (Figure 5).
	0.97	ERp57- and/or calreticulin-dependent recruitment of beta2m into the PLC can stabilize weaker binding between heavy chains and tapasin, and serve as a point of contact for stable heavy chain recruitment to the PLC.
	0.97	ERp57 or calreticulin (Figure 6A and 6B).
	0.97	calreticulin and ERp57, that could impact the generation of optimally-assembled heterodimers.
	0.97	calreticulin and ERp57 to the PLC are shown to be co-dependent and also dependent upon tapasin(C95) and tapasin's glycan.
	0.96	ERp57 and C95 of tapasin may induce a conformational change within the complex depicted in Figure 7A, that disengages calreticulin from tapasin's glycan, re-positioning calreticulin for binding to tapasin-conjugated ERp57, via a P domain-based interaction (Figure 7B).
	0.96	calreticulin and ERp57 recruitment, non-classical heavy chains are estimated to be present at low levels (<= 1%) in 721.221 cells compared to classical MHC class I heavy chain.
	0.94	calreticulin recruitment to the PLC (Figure 3), or calreticulin-deficiency itself, also impacted the recruitment efficiencies of ERp57 into the PLC (data not shown).
	0.93	calreticulin structure and the tapasin-ERp57 complex structure) suggest that a calreticulin bound to tapasin's glycan cannot simultaneously contact the ERp57 molecule present within the same tapasin-ERp57 conjugate (Wijeyesakare and Raghavan, unpublished observations).
	0.91	calreticulin from tapasin's glycan, and link calreticulin to the PLC via P domain-mediated interactions with tapasin(C95)-associated ERp57.
	0.90	calreticulin or ERp57 were detectable (Figure 6F), again indicating an absence of coupling of beta2m binding to TAP, tapasin or calreticulin to the beta2m-heavy chain interaction.
	0.90	ERp57 heterodimers provide a valuable starting point for the construction of model for a mature PLC, whether calreticulin in fact interacts with the MHC class I glycan within the PLC as suggested remains to be established, as well as the nature of interactions between tapasin-ERp57, beta2m and calreticulin.
	0.88	calreticulin and ERp57 suggested the possibility that the latter interactions were independent of heavy chain recruitment.
	0.85	calreticulin and ERp57 were co-immunoprecipitated with TAP1 (Figure 5A).
	0.81	calreticulin and ERp57 into the PLC (Figure 5A, lanes 3-4 compared to lanes 5-6 of beta2m, tapasin, calreticulin and ERp57 blots).
	0.80	ERp57, beta2m and calreticulin (Figures 7C and 7D).
23717280	0.99	ERp57 binds to nascent proteins at N-glycosylation sites in association with another ER chaperone, calreticulin.
	0.97	ERp57 and calreticulin.
	0.96	ERp57 and calreticulin, which keep it in solution.
21670312	0.98	calreticulin, gp96, PDI and BiP (Fig. 3A).
	0.98	calreticulin proteins were induced on the cell surface in response to thapsigargin treatment at levels that correlated with their total expression in the lysates, rather than with their abilities to interact with ERp57 (Fig. 3E).
	0.98	calreticulin, 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	calreticulin and secretion of calreticulin, BiP, gp96 and PDI are induced by thapsigargin treatment, which depletes ER calcium, but not by tunicamycin treatment, which inhibits protein glycosylation.
	0.97	calreticulin surface expression is independent of ERp57 co-translocation
	0.97	calreticulin-ERp57 complexes to the cell surface.
	0.97	calreticulin-ERp57 co-translocation mechanism.
	0.97	calreticulin expression is independent of calreticulin-ERp57 binding
	0.96	calreticulin surface expression is independent of calreticulin-ERp57 binding (Fig. 3E).
	0.96	calreticulin, ER retention of BiP, PDI and gp96 may in part involve calcium-dependent processes.
	0.95	calreticulin release from the ER is distinct from that suggested for anthracyclin-induced calreticulin surface expression, where the specific co-translocation of calreticulin-ERp57 complexes was indicated.
	0.94	calreticulin release from the ER is distinct from that described for anthracyclin-induced surface calreticulin expression, where co-translocation with ERp57 is suggested.
	0.94	calreticulin and ERp57 interact via the P-domain of calreticulin, and amino acid W244 within the P-domain of calreticulin is important for binding to ERp57.
	0.94	calreticulin does not require association with ERp57 to be expressed on the cell surface in response to ER calcium depletion.
	0.55	PDI (Fig. 3B) and induced similar elevations of surface calreticulin expression (data not shown).
23298205	0.98	ERp57 mutated in the b' domain showed that the ability of ERp57 to bind CRT is essential for MHC-I recruitment to the PLC and normal MHC-I peptide loading.
	0.98	CRT-dependent interactions with the MHC-I glycan and ERp57 that mediate MHC-I binding to the PLC, there is also a direct interaction between MHC-I and tapasin.
	0.97	CRT and ERp57 in the PLC.
	0.96	ERp57-negative cells, as well as CRT-negative cells, also have reduced numbers of MHC-I molecules on the cell surface.
	0.95	CRT/CNX/ERp57 quality control cycle, enzymatic removal of mannose residues from the N-linked glycan will render it unsusceptible to re-glucosylation by UGT1.
	0.86	ERp57 conjugates, and up to two CRT molecules and MHCI-beta2m dimers can be recruited (Figure 3).
	0.82	CRT nor tapasin-associated ERp57 were needed for peptide binding when the MHC-I heavy chain and tapasin were artificially coupled by the addition of leucine zippers to their C-termini.
30647818	0.98	ERp57 is dependent on interactions with calnexin and calreticulin, which mediate the recognition and binding of N-glycosylated substrates.
	0.98	calreticulin were induced and the stimulation with thapsigargin, an ER stress inducer, increased the ERp57 expression in chondrocytes 2.8-fold.
	0.98	ERp57 and the calnexin/calreticulin cycle appears to be particularly active during ER stress in osteoarthritic cartilage cells.
	0.97	calreticulin in addition bind the PDI ERp57, assisting in folding by disulfide exchange reactions.
	0.96	ERp57, that is, as a part of the calnexin/calreticulin cycle, mainly engaged in folding of glycoproteins with unstructured disulfide-rich domains.
	0.94	calreticulin, BiP, GRP94, ERp57, or UDP-glucose-glycoprotein glucosyltransferase results in embryonic lethality.
	0.71	calreticulin-calnexin ERp57 cycle over other protein folding mechanisms might also play a role in this context.
21093319	0.98	ERp57 forms a complex with calnexin and calreticulin, whereby these lectin chaperones mediate substrate recognition.
	0.98	ERp57, exists in a complex with calreticulin and calnexin whereby these lectin chaperones mediate a broad substrate recognition.
	0.98	ERp57 in the absence of the calreticulin and calnexin chaperones.
	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.
	0.94	ERp57 acts in concert with tapasin, independently of its partners calreticulin and calnexin.
	0.76	ERp57, we detected abundant amounts of calnexin and calreticulin in lysates from siMzb1-knockdown cells, but not in lysates from control-knockdown and Mzb1*-rescue cells.
28938588	0.98	CRT production by siERp57 or siCXCR1 (Figure 4F) indicated that multiple interactions of at least two different proteins, including CXCR1 and ERp57, are required for CRT translocation in Mtb-infected macrophages.
	0.98	CRT with ERp57 and the subsequent translocation of both proteins to the macrophage plasma membrane.
	0.96	CRT levels, without any change in those of CXCR1 or ERp57 (Figure 5B).
	0.96	CRT was shown to be dependent on interaction of the protein with ERp57.
	0.95	ERp57, which binds to CRT in the ER and co-translocates with the protein to the plasma membrane, was not affected in cells exposed to heat-killed Mtb, whereas the levels of CRT, GRP78, and CHOP were reduced.
	0.93	ERp57 is important for the cell-surface translocation of CRT, and CXCR1 is associated with the exposure of CRT on the surface of stressed and dying cells, we evaluated the effect of ERp57 knockdown on CXCR1 production during Mtb-induced CRT synthesis.
18567819	0.98	CRT and PDI and revealed upregulation of CNX (~1.8-fold), a membrane bound chaperone and phospho-JNK-1 ~2.0-fold, a downstream effector protein of the UPR.
	0.98	CRT, CNX, and PDI, a foldase that catalyzed disulfide bond formation.
	0.98	CRT, CNX, and PDI were all upregulated in fat of obese compared with nonobese volunteers (Figs. 1-3), indicating activation of UPR and suggesting presence of ER stress.
	0.97	CRT, a protein chaperone, increased from undetectable to 1,019 +- 236 arbitrary units; PDI, a protein foldase, increased approximately threefold; and glutathione-S-transferase P, an antioxidant protein belonging to a UPR-regulated pathway, increased ~1.8-fold (Fig. 1; Table 2).
	0.96	calreticulin, protein disulfide-isomerase A3, and glutathione-S-transferase P. Western blotting revealed upregulation of several other UPR stress-related proteins, including calnexin, a membrane-bound chaperone, and phospho c-jun NH2-terminal kinase (JNK)-1, a downstream effector protein of ER stress.
25688334	0.98	calreticulin and ERp57 was accompanied by phosphorylation of PERK and its substrate eIF2alpha.
	0.98	calreticulin/ERp57 translocation in mitoxantrone treated CT26 cells ore MEFs, as cells depleted for caspase-8 lost their ability to translocate calreticulin/ERp57.
	0.96	calreticulin that was unable to bind ERp57, had equal amounts of cell surface calreticulin compared to wildtype MEFs during thapsigargin treatment.
	0.94	calreticulin/ERp57 exposure.
	0.58	calreticulin/ERp57 exposure, whereas it did not affect the sensitivity toward anthracyclin induced cell death.
23509727	0.98	Calreticulin (CRT) is a 46 kDa Ca2+-binding protein prevalently located in ER lumen, where it acts in proper folding of proteins, by interacting with ER-resident disulfide isomerase ERp57 and calnexin (CNX), and in Ca2+ homeostasis/signaling regulation.
	0.97	CRT translocation on plasma membrane occurs in a SNARE-dependent exocytosis, based on a "CRT/Erp57 cotranslocation module".
	0.95	CRT with ERp57, that has been described in immunogenic apoptosis, is probably not a universal phenomenon strictly necessary for the immunogenic outcome in cancer therapies.
	0.95	ERp57-independent CRT exposure upon phox-ER stress.
25184039	0.98	ER and the important role of calnexin/calreticulin in glycoprotein folding, perturbation of calcium homeostasis, as produced by the calcium pump inhibitor thapsigargin, would be predicted to adversely affect the folding of numerous glycoproteins and hence the induction of the UPR.
	0.97	ER is a calcium-rich environment, whereas the cytosol is not: consequently, calcium-binding chaperones, such as calnexin and calreticulin participate in folding reactions in the ER.
	0.97	calreticulin, assisted by oxidoreductases, such as ERp57 to enable additional attempts at reaching a fully native fold.
	0.58	ER-lumenal proteins, the calnexin/calreticulin cycle employs an ER-resident glucosidase and (uridine 5'-diphospho-glucose-4-epimerase) [UDP]-glucose glycoprotein glucosyltransferase.
27337472	0.98	CRT (or the related chaperone calnexin) also cooperates with ERp57 via a glycan-independent, noncovalent interaction to facilitate their correct folding and disulfide bond formation.
	0.98	ERp57 with tapasin in the PLC provides a secondary anchor via CRT to cooperatively maintain the association of newly synthesized MHC-I with the PLC in an adaptation of the normal glycoprotein folding cycle.
	0.97	CRT interactions with a monoglucosylated N-linked glycan on the heavy chain and ERp57 disulfide linked to tapasin in the PLC.
	0.94	CRT, ERp57, and UGT-1 are all required for optimal MHC-I peptide loading.
16696860	0.98	Calreticulin and grp58, are known to be specifically associated with ER stress.
	0.97	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.
	0.80	calreticulin or Grp58 was observed in FrCasE-infected microglial cultures when compared with mock or Fr57E-infected cells.
23762310	0.98	calreticulin and ERp57, and liberation of HMBG1 and ATP.
	0.98	calreticulin (CRT) and the endoplasmic reticulum chaperone ERp57 translocation at the cell surface.
	0.98	CRT and ERp57 onto tumor cell plasma membrane in three mouse cancer models (Figure 1b).
24327935	0.98	calreticulin and ERp57 on the cell surface, the activation of autophagy and the secretion of ATP.
	0.98	calreticulin (CRT) and ERp57 on the cell surface, the activation of autophagy and ATP secretion.
	0.97	calreticulin and ERp57 exposure on the cell surface, autophagy and ATP release, in vitro.
26361352	0.98	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	calreticulin (CRT) cycle, ERp57 is predicted to participate in the folding of numerous cysteine-rich glycoproteins.
	0.97	ERp57 may have a relevant activity in sustaining glial proteostasis as a central component of the CNX-CRT cycle.
27073369	0.98	ERp57 catalyzes the formation, disruption and isomerization of disulfide bonds of glycoproteins mediated by a cooperative interaction with the endoplasmic reticulum (ER) chaperones calnexin and calreticulin (Turano et al., 2002) (Figure 1A, B).
	0.98	ERp57 mediated in part the folding of synaptic proteins, like SV2, as a component of the calnexin and calreticulin cycle.
	0.96	ERp57 altered the physical association with calnexin and calreticulin (Woehlbier et al., 2016).
18443227	0.98	calreticulin (CRT), and ERp57.
	0.98	CRT, and ERp57 proteins.
20428984	0.98	PDI can also interact with the lectin chaperones calreticulin and calnexin, which were also increased in mutant chondrocytes.
	0.82	calreticulin and ERp57 were unchanged in treated mice compared to untreated mice (Table 2).
24046357	0.98	PDIA3, PDIA4, PDIA6, Grp94 (Hsp90b1) and calreticulin.
	0.97	ERp57 (PDIA3), calreticulin (CRT) and calnexin (CNX) transcripts were normal in the chondrocytes of Col2-Tgrdw mice.
25514597	0.98	Erp57, an ER-resident thiol disulfide oxidoreductase that forms a complex with CRT, was recently reported to modulate STAT3 signaling.
	0.97	Erp57 and dependent on the formation of Erp57-CRT complexes, Tg-induced ER stress might induce Erp57 malfunction by disassociating it with CRT.
30149659	0.98	calreticulin (CRT) complexes with a lumenal protein of the ER (ERp57) during transport from the ER and docks onto CD91/low-density lipoprotein receptor related protein 1 (LRP1).
	0.98	CRT/ERp57 signals through CD91 and scavenger receptor class A (SR-A) as well as scavenger receptor expressed by endothelial cell-I (SREC-I) on innate immune cells, promoting phagocytosis and nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kB) pathway activation.
31046837	0.98	calreticulin (CRT), calnexin (CLNX), and ER protein 57 (ERp57).
	0.97	CRT and CLNX can regulate SERCA directly or possibly indirectly by recruiting other enzymes, such as ERp57.
31210425	0.98	CRT/ERp57 provides an 'eat me' signal that promotes phagocytosis of the cell by DCs; similarly, extracellularly secreted adenosine triphosphate is regarded as a 'find me' signal, which triggers P2X7 receptors on DCs and is responsible for the activation of the NALP3-ASC-inflammasome and the secretion of IL-1beta.
	0.95	calreticulin (CRT, a 46 kDa Ca2+-binding protein), from the perinuclear ER to the cellular periphery and similarly relocalize ERp57.22 Once the CRT/ERp57 complex is exposed on the cell surface, it provides an 'eat me' signal to promote phagocytosis by DCs.15, 23 Moreover, the exposure of CRT on the surface of cancer cells succumbing to ICD also induces tumour antigen presentation and tumour-specific CTL responses.15
16492806	0.98	CRT association with SERCA reduced pump activity through the recruitment of the ER oxidoreductase ERp57 and oxidation of critical ER facing thiol groups of SERCA.
18851953	0.98	GRP58, retained in endoplasmic reticulum, specifically interacts with glycoproteins such as calnexin and calreticulin, playing an important role as a molecular chaperone during glycoprotein biosynthesis and folding.
19147124	0.98	Calreticulin as a lectin helps glycosylated proteins interact with PDI A3 .
19365408	0.98	calreticulin (CRT) and the disulfide isomerase ERp57 on their cell surface.
19889996	0.98	Erp57 is a PDI homolog that shares enzymatic functions with PDI, but unlike PDI, forms direct interactions with the ER lectins calnexin and calreticulin.
20348926	0.98	Pdia3 and Calr (encoding calreticulin) was considerably upregulated in the WT liver, whereas this chaperone response was totally blunted in the ob/ob mice (Fig. 4d-g).
23437120	0.98	PDI and ERp57, was increased in CRT-TG hearts (Fig. 3A,B).
24677236	0.98	ERp57 interacts with ER lectins calnexin and calreticulin, and has been implicated in glycoprotein folding .
24946135	0.98	Pdia3, also known as ERp60, ERp57, Grp58, and 1,25-MARRS) located in caveolae, which are 50-100 nm lipid rafts highly enriched with cholesterol and glycosphingolipids.
25140116	0.98	CRT and CNX (calnexin) interact with the ERp57 to promote disulfide bond isomerization in bound unfolded glycoproteins.
25309899	0.98	ERP57-calreticulin interactions are necessary for calreticulin membrane translocation.
26035385	0.98	PDIA3 exhibits a major role as molecular chaperone involved in the quality control process for newly synthesized glycoproteins in the endoplasmic reticulum (ER), interacting with calnexin or calreticulin.
26388295	0.98	CALR may cooperate with PDIA3 (ERP57) to regulate the quality control of GDF9/BMP15.
27036911	0.98	ERp57, calreticulin facilitates the folding of nascent client proteins such as major histocompatibility complex (MHC) class I molecules (reviewed in).
29470977	0.98	ER protein of 57 kDa (ERp57), an integral component of the calnexin/calreticulin system and an oxidoreductase in the ER, catalyzes disulfide bond formation between ERp57 and substrates.
30604742	0.98	Protein disulfide isomerase family A member 3 (Pdia3) encodes an ER protein, which interacts with calreticulin and calnexin to promote formation of disulfide bonds during protein folding.
31607947	0.98	ER chaperones GRP 94, calnexin, GRP78, calreticulin, and ERp72 was enhanced in the pathological muscle area.
32206098	0.98	calreticulin (CRT), ERP57, HMGB1, ATP, and heat shock proteins from dying cells.
27581066	0.97	Pdi, Calr, Sdf2l1 and Manf (Fig. 3g).
	0.97	Pdi, Calr, Sdf2l1 and Manf (Fig. 8a and summarized data in b through e).
	0.97	Pdi, Calr, Sdf2l1 and Manf), yet leaved the contractile protein levels unchanged.
	0.97	Pdi, Calr, Sdf2l1 and Manf.
	0.94	Calr, Manf, Sdf2l1 and Pdi increased as did ER size, whereas contractile markers were reduced.
	0.91	Calr, Manf, Sdf2l1 and Pdi and caused ER expansion, but the contractile markers were inert.
	0.90	Pdi, Calr, Manf and Sdf2l1 in KO compared to WT bladders (Fig. 9c and summarized data in panels d through g).
	0.74	Pdi, Calr and Manf was not affected (panel c and summarized data in (e) through (g)).
19798432	0.97	Pdia3 and calreticulin reside at the cell surface of neuroblastoma cells
	0.96	Pdia3, P4hb and calreticulin was enriched in streptavidin eluate fractions derived from in vivo biotinylated cells compared to the corresponding samples derived from mock-treated control cells.
	0.96	Pdia3- and calreticulin-specific signals present in eluate fractions from biotinylated (lanes 6 and 8) versus non-biotinylated samples (lanes 5 and 7) is consistent with the conclusion that a subset of these proteins resided at the cell surface during the biotinylation step.
	0.68	Pdia3, P4hb and calreticulin are also present at the cell surface in mouse neuroblastoma cells, a cell surface biotinylation experiment was undertaken.
	0.66	calreticulin, Calr; endoplasmin, Hsp90b1), (ii) isomerases which facilitate disulfide or proline cis-trans rearrangements (protein disulfide isomerase associated 3, Pdia3; protein disulfide isomerase associated 4, Pdia4; prolyl 4-hydroxylase beta polypeptide, P4hb; peptidylprolyl isomerase B, Ppib), or (iii) proteins involved in the trafficking between ER and Golgi compartments (transmembrane emp24 transport domain containing 9, Tmed9; and transmembrane emp24-like trafficking protein 10, Tmed10).
	0.61	Pdia3, P4hb and calreticulin that may share these characteristics.
	0.51	Pdia3 (also known as ERp57) was represented with strong sequence coverage (61%) and its identification was further corroborated by similarly strong identifications for calnexin and calreticulin, known interactors of this PDI.
19687800	0.97	ERp57 normally also interacts with another component of the peptide-loading complex, calreticulin.
	0.97	calreticulin was discovered to interact with ERp57 in the presence of wild type or C95S tapasin, but not in the absence of tapasin.
	0.95	ERp57 and immunoblotting with anti-calreticulin antibody revealed that free calreticulin association with ERp57 was unchanged by the presence of mouse tapasin C95S, relative to the presence of wild type mouse tapasin (Figure 2B).
	0.74	Calreticulin associated with ERp57 in the presence of either wild type or C95S mouse tapasin
	0.69	ERp57, and both wild type and C95S tapasin were found to bind only non-covalently with calreticulin.
	0.57	calreticulin, ERp57, Bap 29/31, and protein disulfide isomerase.
25372053	0.97	CALR and PDI interact in distinct Ca2+ concentrations.
	0.97	CALR to bind PDI and inhibit its activity.
	0.96	PDI and CALR.
	0.93	CALR and PDI.
24983750	0.97	PDIA3 and CALR act together in the major histocompatibility complex class I assembly pathway.
	0.85	protein disulfide isomerase associated 3 (PDIA3) and Calreticulin (CALR).
	0.84	Protein disulfide isomerase associated 3 (PDIA3) and Calreticulin (CALR) were also upregulated after selenate treatment in our study.
28933220	0.97	CALR, and PDIA3 are significantly upregulated and HGF, H2-L, NFKBIA, CCL17, and IL12RB1 are significantly downregulated at subacute phase.
	0.90	CALR, and PDIA3; downregulation: H2-L) were activated by RNA-seq (Table 3; Fig. 3).
	0.74	CALR, and PDIA3) and 1 downregulated gene (H2-L) in antigen processing and presentation.
19851784	0.97	CRT, PDI, ERp72 and Grp94 were localised to the electron-dense material in the dilated ER (Hecht et al.).
	0.91	calreticulin (CRT), protein disulphide isomerise (PDI), Grp94, ERp72 and BiP (Grp78; Hecht et al.; Vranka et al.).
20410492	0.97	calreticulin has been proposed to have a role in stabilizing empty MHC molecules by directly interacting with ERp57 and glycan residues of the MHC heavy chain).
	0.96	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.
22138314	0.97	ERp57 dimer has a higher affinity for empty MHC class I molecules than tapasin alone because it possesses two binding sites: tapasin binds directly to MHC class I molecules while ERp57 interacts with calreticulin bound to the mono-glucosylated N-linked glycan of recruited MHC class I molecules.
	0.97	ERp57 and calreticulin; tapasin links the peptide loading complex to the peptide transporter TAP (not shown).
28487627	0.97	calreticulin, and PDIA3 (a protein foldase that catalyzes the formation and correct isomerization of disulfide bonds and interacts with both calnexin and calreticulin), are the core components of the ER protein quality control system (Hebert and Molinari,).
	0.97	PDIA3, calreticulin, and calnexin, may influence the function and integrity of the BBB.
18751977	0.97	calreticulin, and ERp57) and beta2 microglobulin (beta2m).
22169163	0.97	calreticulin and ERp57 to associate with Kd correlated with the binding of tapasin to Kd, consistent with the cooperative nature of peptide-loading complex protein interactions.
23395171	0.97	ER protein 57 (also known as 1,25-MARRS, ERp57, ERp60, GRP58, or Pdia3), calreticulin, sarcalumenin, histidine-rich Ca2+-binding protein (HRC), and calumenin, associate with and regulate SERCA2b stability and activity, but the mechanisms are not completely understood.
27656684	0.97	PDI, Sec61-alpha, calreticulin, and GP96, were specifically associated with purified microsomes (Fig. 5B).
29565997	0.97	PDIA3, CALR, GANAB and HYOU1 suggesting its functional link with protein folding and response to stress.
25050214	0.96	CRT and ERp57 on the cell surface, others (e.g., lanatoside C) resemble hypericin-based photodynamic therapy, which causes ICD independently of the translocation of ERp57 on the outer leaflet of the plasma membrane (Fig. 2E).
	0.96	CRT or ERp57 (Fig. 2E), suggesting that the signaling cascades elicited by these putative ICD inducers involve multiple manifestations of the ER stress response that cannot easily be linked to each other.
	0.60	CRT-GFP and ERp57-GFP was not always comparable.
20193000	0.96	Calreticulin is envisioned as protecting the empty peptide-binding groove from reduction by oxidoreductases in the ER (e.g. free ERp57 or PDI), which might target it for degradation prior to optimal peptide loading.
20520781	0.95	PDI respectively, but with no change in calnexin (CNX) and calreticulin (CRT) levels.
25405762	0.94	protein disulfide isomerase A3 (PDIA3), also referred to as 1alpha,25(OH)2D3-membrane associated rapid response steroid binding protein (1,25-MARRS), GRP58, ERp60, ERp58 and ERp57.
23089196	0.89	calreticulin, the thiol oxidoreductase ERp57, and tapasin.
29542339	0.87	ERp57 interacts with lectin chaperones calnexin and calreticulin, whereas PDI does not.
29122814	0.84	Calr at HIEL was different from the Calr in the EC monolayer, we used proximity ligation assay; the protein ERp57 is a widely recognized binding partner of ER-localized Calr.