Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
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Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.5711834
ERp 57 also interacts with calreticulin through the N domain of the protein . 0.5711834^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
A carbohydrate dependent interaction between newly synthesized glycoproteins , the thiol dependent reductase ERp 57 , and either calnexin or calreticulin was identified . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
These components are calnexin , calreticulin and ERp 57 , and this review focuses on the molecular basis for their capacity to influence glycoprotein folding . . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Association of ERp 57 with mouse MHC class 1 molecules is tapasin dependent and mimics that of calreticulin and not calnexin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Only wild type hTpn efficiently recruited HC and calreticulin ( Crt ) into complexes with TAP and endoplasmic reticulum p 57 ( ERp 57 ) . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
This modification mediates glycoprotein interaction with the folding machinery comprised of calnexin or calreticulin in conjunction with ERp 57 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
The glycan specific oxidoreductase ERp 57 was cross linked to tyrosinase when calnexin and calreticulin were associated . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.66713254
ERp 57 is a protein chaperone with thiol dependent protein disulfide isomerase and additional activities and recently it has been shown to be involved , in cooperation with calnexin or with calreticulin , in the correct folding of glycoproteins . 0.66713254^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
A subset of these luminal components are specific for glycoproteins , and , like calnexin and calreticulin , the thiol dependent reductase ERp 57 has been shown to interact specifically with soluble secretory proteins bearing N linked carbohydrate . ^^^ Calnexin and calreticulin also interact with glycosylated integral membrane proteins , and in this study we have examined the interaction of ERp 57 with these substrates . ^^^ Furthermore , ERp 57 binds to newly synthesized glycoproteins in combination with either calnexin or calreticulin . ^^^ We propose that ERp 57 acts in concert with calnexin and calreticulin to modulate glycoprotein folding and enforce the glycoprotein specific quality control mechanism operating in the endoplasmic reticulum . . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
In young and old energy restricted mice , hepatic expression of the endoplasmic reticulum chaperones ERp 57 ( 37 % ) , GRP 170 ( 51 % ) , ERp 72 ( 43 % ) , calreticulin ( 54 % ) and calnexin ( 23 % ) was significantly and specifically reduced . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp 57 . ^^^ The endoplasmic reticulum protein ERp 57 is homologous to protein disulfide isomerase and can be cross linked to the same monoglucosylated glycoproteins that bind to calnexin and calreticulin . ^^^ The present study demonstrates that the disulfide isomerase activity of ERp 57 on the refolding of monoglucosylated ribonuclease B is much greater when this glycoprotein is associated with calnexin or calreticulin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Recently , the thiol oxidoreductase ERp 57 also known as GRP 58 , ERp 61 , ER 60 , Q 2 , HIP 70 , and CPT and first misidentified as phospholipase C alpha has been shown to bind in conjunction with calnexin or calreticulin to a number of newly synthesized ER glycoproteins when their N linked glycans are trimmed by glucosidases 1 and 2 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
We demonstrate that ERp 57 interacts preferentially with the glycosylated versions of soluble and membrane proteins , and that this interaction occurs in combination with calnexin and calreticulin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Therefore , Myc SERT was co expressed with the endoplasmic reticulum ( ER ) molecular chaperones calnexin , calreticulin and immunoglobulin heavy chain binding protein ( BiP ) , and the foldase , ERp 57 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
ERp 57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin . ^^^ In this study we demonstrate that ERp 57 forms discrete complexes with the ER lectins , calnexin and calreticulin . ^^^ After in vitro translation and import into microsomes , radiolabeled ERp 57 can be cross linked to endogenous calreticulin and calnexin while radiolabeled PDI can not . ^^^ Likewise , radiolabeled calreticulin is cross linked to endogenous ERp 57 but not PDI . ^^^ This result was confirmed by a specific interaction between in vitro synthesized calreticulin and ERp 57 prepared in solution in the absence of other ER components . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
We show that the endoplasmic reticulum resident oxidoreductases PDI and ERp 57 are directly involved in disulphide oxidation and isomerization , and , together with the lectins calnexin and calreticulin , are central in glycoprotein folding in the endoplasmic reticulum of mammalian cells . . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
These pathways may or may not include the interaction of class 1 molecules with the accessory proteins tapasin , calreticulin , ERp 57 , or TAP . 1 would like to suggest that the particular pathway utilized by a given class 1 molecule depends more upon the availability of appropriate peptides rather than on an intrinsic property of the class 1 molecule , and that tapasin may serve a peptide editing function . . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
In addition to these specialized components two soluble ' house keeping ' proteins , the chaperone calreticulin and the thiol oxidoreductase ERp 57 , are also components of this complex . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Three of these , calreticulin precursor , p 58 microsomal protein ( ERp 57 ) and protein disulfide isomerase ( p 55 ) have been identified by matrix assisted laser desorption and ionization mass spectrometry and the pI / molecular weight parameters of the affected proteins were estimated by computer analysis . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
In the assembly of active prolyl 4 hydroxylase tetramers , the a and b domains of PDI , but not b ' and a ' , can in part be substituted by the corresponding domains of ERp 57 , a PDI isoform that functions naturally in association with the lectins calnexin and calreticulin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Before peptide binding these molecules form part of a multisubunit loading complex that also contains the two subunits of the TAP , the transmembrane glycoprotein tapasin , the soluble chaperone calreticulin , and the thiol oxidoreductase ERp 57 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Once MHC class 1 heavy chain binds beta ( 2 ) microglobulin ( beta ( 2 ) m ) within the endoplasmic reticulum , an assembly complex comprising the class 1 heterodimer , TAP , TAPasin , calreticulin , and possibly Erp 57 is formed before the binding of high affinity peptide . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
During the assembly of major histocompatibility complex ( MHC ) class 1 molecules transient associations are formed with the endoplasmic reticulum resident chaperones calnexin and calreticulin , ERp 57 oxidoreductase , and also with tapasin , the latter mediating binding of the class 1 molecules to the transporter associated with antigen processing ( TAP ) . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
TROSY NMR reveals interaction between ERp 57 and the tip of the calreticulin P domain . ^^^ We found that ERp 57 binds to the P domain of calreticulin , an independently folding domain comprising residues 189 288 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Peptide binding occurs when assembling class 1 molecules associate with a loading complex consisting of the transporter associated with antigen processing ( TAP ) peptide transporter , tapasin , ERp 57 and calreticulin ( CRT ) / calnexin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
It can be hypothesized that ERp 57 , which is known to associate with other proteins , in particular STAT 3 and calreticulin , may contribute to their nuclear import , DNA binding , or other functions that they fulfil inside the nucleus . . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Localization of the lectin , ERp 57 binding , and polypeptide binding sites of calnexin and calreticulin . ^^^ In addition to sharing substantial sequence identity , both calnexin and calreticulin bind to monoglucosylated oligosaccharides of the form Glc ( 1 ) Man ( 5 9 ) GlcNAc ( 2 ) , interact with the thiol oxidoreductase , ERp 57 , and are capable of acting as chaperones in vitro to suppress the aggregation of non native proteins . ^^^ To understand how these diverse functions are coordinated , we have localized the lectin , ERp 57 binding , and polypeptide binding sites of calnexin and calreticulin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
The ER resident molecule tapasin ( Tpn ) is uniquely dedicated to tether class 1 molecules jointly with the chaperone calreticulin ( Crt ) and the oxidoreductase ERp 57 to TAP . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Identification of specific glycoforms of major histocompatibility complex class 1 heavy chains suggests that class 1 peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp 57 . ^^^ Heavy chains were also isolated from Raji cells in multimolecular complexes ( peptide loading complexes ) containing the transporter associated with antigen processing , tapasin and ERp 57 with and without the lectin like folding chaperone , calreticulin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Calnexin , calreticulin , and ERp 57 cooperate in disulfide bond formation in human CD1d heavy chain . ^^^ Here we show that CD1d associates in the ER with both calnexin and calreticulin and with the thiol oxidoreductase ERp 57 in a manner dependent on glucose trimming of its N linked glycans . ^^^ The formation of at least one of the disulfide bonds in the CD1d heavy chain is coupled to its glucose trimming dependent association with ERp 57 , calnexin , and calreticulin . . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Antigenic peptides are loaded onto class 1 MHC molecules in the endoplasmic reticulum ( ER ) by a complex consisting of the MHC class 1 heavy chain , beta ( 2 ) microglobulin , calreticulin , tapasin , Erp 57 ( ER 60 ) and the transporter associated with antigen processing ( TAP ) . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
These proteins include the lectin chaperones calnexin ( CNX ) and calreticulin ( CRT ) , the thiol dependent oxidoreductase ERp 57 , the transporter associated with antigen processing ( TAP ) , and the protein tapasin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
These steps include cleavage of the signal sequence , glycosylation , binding by the chaperones calnexin and calreticulin , and the oxidoreductase ERp 57 , and oxidation . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
These cells were systematically characterized by Northern and / or Western blotting ( e . g . , mini transcriptome / mini proteome analysis ) for the expression of HLA A , B , C , beta ( 2 ) microglobulin , and the members of the `` antigen processing machinery ' ' of class 1 molecules ( LMP 2 , LMP 7 , TAP 1 , TAP 2 , tapasin , calreticulin , calnexin , and ERp 57 ) . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
The resulting peptides are thought to be translocated into the lumen of the endoplasmic reticulum ( ER ) by specific transporters associated with antigen presentation ( TAP ) , and loaded onto MHC class 1 molecules by a complex `` loading machinery ' ' ( which includes tapasin , calreticulin and Erp 57 ) . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
RESULTS : Calnexin , ERp 57 , calreticulin , tapasin , and HLA class 1 antigens were down regulated in 13 , 13 , 24 , 69 , and 78 % of the 70 lesions tested , respectively . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Here we show that early phagosomes from human dendritic cells ( DCs ) contain the peptide loading complex , incorporating MHC class 1 , beta 2 microglobulin , transporter associated with Ag processing ( TAP ) , calreticulin , tapasin , and ERp 57 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
To overcome this limitation , we have generated human calnexin , ERp 57 , calreticulin and tapasin specific mAb secreting hybridomas from BALB / c mice immunized with peptides and recombinant proteins . ^^^ The mAb TO 5 , TO 2 , TO 11 and TO 3 were shown to be specific for calnexin , ERp 57 , calreticulin and tapasin , respectively , as they react specifically with the corresponding immunizing peptides in ELISA and with the corresponding proteins when tested with human lymphoid cell lysates in Western blotting . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
The loading of newly synthesised MHC class 1 molecules ( MHCI ) with peptides requires the involvement of several endoplasmic reticulum ( ER ) resident cofactors including calnexin , calreticulin , transporter associated with antigen processing , ERp 57 and tapasin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Calnexin , calreticulin , and ERp 57 : teammates in glycoprotein folding . ^^^ Essential components of this system include the lectin chaperones calnexin ( CNX ) and calreticulin ( CRT ) and their associated co chaperone ERp 57 , a glycoprotein specific thiol disulfide oxidoreductase . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Identification and characterization of structural domains of human ERp 57 : association with calreticulin requires several domains . ^^^ The amino acid sequence of ERp 57 , which functions in the endoplasmic reticulum together with the lectins calreticulin and calnexin to achieve folding of newly synthesized glycoproteins , is highly similar to that of protein disulfide isomerase ( PDI ) , but they have their own distinct roles in protein folding . ^^^ Interaction of the soluble ERp 57 domains with the P domain of calreticulin was studied by chemical cross linking in vitro . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
A dynamic multimolecular assembly termed the peptide loading complex ( PLC ) participates in this process and is composed of MHC class 1 molecules , calreticulin , ERp 57 , and tapasin bound to the transporter associated with antigen processing ( TAP ) peptide transporter . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Substrate selection by ERp 57 is dependent upon its formation of discrete complexes with two ER resident lectins , soluble calreticulin and membrane bound calnexin . ^^^ Thus , ERp 57 is presented with a preselected set of substrates upon which it can act , and the specific binding of calreticulin and calnexin to ERp 57 is pivotal to the functions of the resulting complexes . ^^^ To gain further insights into the formation of these ERp 57 ER lectin complexes , we have investigated the regions of ERp 57 that are specifically required for its binding to calreticulin . ^^^ Using a quantitative pull down assay to investigate the binding of ERp57 / PDI chimeras to calreticulin , we define the b and b ' domains of ERp 57 as the minimal elements that are sufficient for complex formation . ^^^ Using our understanding of substrate binding to the b ' domain of PDI as a paradigm , we show that alterations to specific residues in the b ' domain of ERp 57 dramatically reduce or completely abolish its binding to calreticulin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Toward this end , we examined the potential associations of calnexin , calreticulin , Grp 94 , BiP , ERp 57 , and protein disulfide isomerase with each of the three glycoprotein hormone receptors . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
This hierarchy broke down in cells lacking tapasin but not in cells lacking calreticulin or in cells lacking transporter associated with antigen processing associated ERp 57 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
For both of these safeguard mechanisms , the MHC class 1 loading complex ( which consists of the peptide transporter TAP , the chaperones tapasin and calreticulin , and the protein disulfide isomerase ERp 57 ) plays a central role . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
The assembly of MHC class 1 molecules with beta ( 2 ) microglobulin and peptides is assisted by the housekeeping chaperones calnexin , calreticulin , and Erp 57 and the dedicated accessory protein , tapasin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Tapasin is the central stabilizer of this complex , which also includes the transporter associated with antigen processing ( TAP ) , MHC class 1 molecules , the ER chaperone , calreticulin , and the thiol oxidoreductase ERp 57 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
ERp 57 binds competitively to protein disulfide isomerase and calreticulin . ^^^ Additionally , following pre incubation of ERp 57 with calreticulin ( CRT ) , decreased interactions were observed between ERp 57 and PDI , and vice versa . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
In cerebrospinal fluid ER chaperones ERp 57 and calreticulin bind beta amyloid . ^^^ Based on immunoblotting studies of cerebrospinal fluid ( CSF ) from normals , we find that the bulk of the abetas are bound to the ER chaperones , ERp 57 and calreticulin , suggesting that these may be carrier proteins which prevent aggregation of the abetas and that the deposits are due to faulty ER posttranslational processing of APP with the failure to form this complex . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
This cell line synthesized normal levels of the MHC class 1 H chain and beta ( 2 ) microglobulin , as well as normal levels of TAP , tapasin , GRP 78 , calnexin , calreticulin , ERp 57 , and protein disulfide isomerase . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Cellular functions of endoplasmic reticulum chaperones calreticulin , calnexin , and ERp 57 . ^^^ Calreticulin , calnexin , and ERp 57 are among the endoplasmic chaperones that interact with partially folded glycoproteins and determine if the proteins are to be released from the endoplasmic reticulum to be expressed , or alternatively , if they are to be sent to the proteosome for degradation . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
The PLC contains a peptide transporter ( transporter associated with antigen processing ) , a thiooxido reductase ( ERp 57 ) , a glycoprotein chaperone ( calreticulin ) , and tapasin , a class 1 specific chaperone . ^^^ We suggest that tapasin is the key chaperone that directs this action of the PLC with secondary contributions from calreticulin and possibly ERp 57 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
The rate of tapasin ERp 57 conjugate formation is unaffected by the absence of beta 2 microglubulin ( beta2m ) , and is independent of calnexin or calreticulin interactions with monoglucosylated N linked glycans . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
We identified four amino acid residues ( Glu ( 239 ) , Asp ( 241 ) , Glu ( 243 ) , and Trp ( 244 ) ) at the hairpin tip of the P domain that are critical in the formation of a complex between ERp 57 and calreticulin . ^^^ This indicates that binding of ERp 57 to calreticulin may not be critical for the chaperone function of calreticulin with respect to the bradykinin receptor . . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Estrogen increased levels of the more acidic isoforms of growth hormone and prolactin and of proteins involved in protein synthesis , folding , and secretion ( e . g . , eukaryotic translation elongation factor 2 , ERp 57 , ERp 29 , Hsc 70 ps1 , calreticulin , coatomer delta subunit , and secretogranin 2 ) and of some metabolic enzymes ( e . g . , arginosuccinate synthetase , enolase 1 , creatine kinase B , phosphoglycerate mutase , malate dehydrogenase , pyruvate kinase , and aldolase A ) . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
ApoK 1 er assembles with calreticulin and the protein disulfide isomerase ERp 57 and undergoes a conformational shift in a Ca2+ dependent manner that allows fluorescence resonance energy transfer between the two fluorophores . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
In addition , calnexin and calreticulin possess binding sites for ATP , Ca2+ , non native polypeptides and ERp 57 , an enzyme that catalyzes disulfide bond formation , reduction and isomerization . ^^^ Furthermore , there is clear evidence that ERp 57 participates in glycoprotein biogenesis either alone or in tandem with calnexin and calreticulin . . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
ERp 57 is a thiol oxidoreductase of the endoplasmic reticulum that appears to be recruited to substrates indirectly through its association with the molecular chaperones calnexin and calreticulin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
These include the molecular chaperones calnexin and calreticulin , which enhance the proper folding and subunit assembly of class 1 molecules and also retain assembly intermediates within the ER ; ERp 57 , a thiol oxidoreductase that promotes heavy chain disulfide formation and proper assembly of the peptide loading complex ; tapasin , which recruits class 1 molecules to the TAP peptide transporter and enhances the loading of high affinity peptide ligands ; and Bap 31 , which is involved in clustering assembled class 1 molecules at ER exit sites for export along the secretory pathway . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
An analysis of the N terminal sequence of the luminal endoplasmic reticulum protein , ERp 60 , showed that it was identical to the well characterized Ca2+ binding protein , calregulin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Two dimensional electrophoresis in conjunction with N terminal sequencing , immunoblot , matrix assisted laser desorption / ionization time of flight analysis or computer matching with protein databases further revealed that the LPS induced apoptosis is accompanied by an augmented level of calreticulin , calcium binding protein 50 , endoplasmic reticulum protein 60 ( ERP 60 ) , heat shock protein 60 ( HSP 60 ) or HSP 90 , and a reduced level of amphoterin , cytochrome c oxidase polypeptide VIa liver or ERP 29 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
In contrast with PDI and parallel purified co residents ( calreticulin , ERp 60 ) , native ERp 29 lacked classical chaperone , disulphide reductase and isomerase , and calcium binding activities . ^^^ ERp 29 also did not exhibit helper activity toward calreticulin ( chaperone ) or PDI and ERp 60 ( disulphide reductase ) . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
ERp 60 ( also known as ERp 61 or GRP 58 ) is an isoform of protein disulfide isomerase ( PDI ) that has two thioredoxin like domains a and a ' in positions corresponding to those of domains a and a ' in the PDI polypeptide and shows a significant amino acid sequence similarity to PDI in almost all parts . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
This work reveals that a 65 % reduction in the cellular UDP Glc level causes up regulation of the mitochondrial chaperone GRP 75 and the endoplasmic reticulum ( ER ) resident chaperones GRP 58 , ERp 72 , GRP 78 , GRP 94 , GRP 170 , and calreticulin . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Analysis of message levels for the ER stress genes BiP ( grp 78 ) , CHOP ( Gadd 153 ) , calreticulin , and grp 58 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 . ^^^
Interacting proteins: P30101 and P27797 Pubmed SVM Score :0.0
Proteolytic cleavage accounted for the discrepancies between messenger RNA and protein level changes for 7 genes including calreticulin , PDIA 3 , PDI , and GRP 78 . ^^^ We also detected calreticulin and PDIA 3 cleavage products in sera of patients with HCC . ^^^ A statistically highly significant difference in calreticulin and PDIA 3 fragment serum levels between patients with HCC and healthy individuals was observed . ^^^ Amounts of calreticulin and PDIA 3 fragments were also significantly different between patients with HCC and at risk patients ( patients with chronic hepatitis or cirrhosis ) . ^^^