Affinage

ERP29

Endoplasmic reticulum resident protein 29 · UniProt P30040

Length
261 aa
Mass
29.0 kDa
Annotated
2026-06-09
72 papers in source corpus 25 papers cited in narrative 25 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ERp29 is a redox-inactive, PDI-family endoplasmic reticulum lumenal protein that functions as a folding/escort assistant in the early secretory pathway, where it recognizes non-native client proteins and facilitates their conformational maturation, ER exit, or membrane penetration (PMID:11884402, PMID:15500441). Structurally it comprises an N-terminal thioredoxin-fold domain that mediates non-covalent homodimerization and a novel all-helical C-terminal (D) domain, and it exists predominantly as a tight 51 kDa homodimer (Kd <50 nM) (PMID:11435111, PMID:15500441). Unlike canonical PDIs, purified ERp29 lacks disulfide reductase, isomerase, classical anti-aggregation chaperone, and calcium-binding activities, consistent with a non-enzymatic escort role (PMID:15500441). Its C-terminal D domain is sufficient for binding peptide and protein substrates, which share aromatic residues and basic character, while dimerization via the thioredoxin domain is required for its functional activities (PMID:19084538, PMID:17267685). ERp29 binds and conformationally unfolds polyomavirus VP1 to expose its hydrophobic C-terminal arm and enable lipid-bilayer penetration during viral entry, acting together with the redox-active enzymes ERp57 and PDI (PMID:16246730, PMID:19019959, PMID:21159867). It associates with denatured thyroglobulin in a heterocomplex with BiP and GRP94 and promotes thyroglobulin secretion, and similarly promotes functional expression and ER exit of ΔF508/wild-type CFTR, γ-ENaC (via Sec24D-dependent COPII targeting), and proinsulin (PMID:11884402, PMID:16380091, PMID:21525008, PMID:24944201, PMID:32433667). ERp29 restricts Connexin43 oligomerization by stabilizing monomeric Cx43 in the ER to enable gap-junction trafficking, and stabilizes the cytosolic protein MSec to support tunneling-nanotube formation (PMID:19321666, PMID:30877198). It is stress-inducible, associates with BiP/GRP78, and modulates the ATF6-CHOP branch of the unfolded protein response, acting as an escort that promotes ATF6 transport from ER to Golgi (PMID:9492298, PMID:24370996). ERp29 additionally bridges the ER lectin chaperones calnexin and calreticulin into ternary complexes (PMID:28456374, PMID:33360823).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 1998 Medium

    Established ERp29's basic identity and stress responsiveness: it was unknown whether this ER protein was constitutive or regulated, and demonstrating ER lumenal localization plus stress-enhanced BiP association placed it in the ER stress chaperone network.

    Evidence Immunofluorescence, protease protection, and co-IP with BiP/GRP78 after tunicamycin/A23187 in cells, plus size exclusion chromatography and cross-linking

    PMID:9492298 PMID:9714535

    Open questions at the time
    • Functional consequence of BiP association not defined
    • Whether self-association is functionally required not yet tested
  2. 2001 High

    Resolved the architectural basis of ERp29 function: the question was how a PDI-like protein lacking enzymatic motifs is organized, answered by showing a thioredoxin-fold N-terminal domain serving as a non-covalent dimerization module and a novel helical C-terminal domain.

    Evidence NMR structures of both domains and full-length dimer model

    PMID:11435111

    Open questions at the time
    • Substrate-binding surface not localized to a domain
    • No catalytic activity defined
  3. 2004 High

    Defined what ERp29 is NOT: by testing for PDI-like reductase, isomerase, anti-aggregation, and calcium-binding activities on purified native protein and finding none, established ERp29 as a redox-inactive escort rather than a classical foldase.

    Evidence In vitro enzymatic assays, aggregation assays, calcium binding, cross-linking, plus mutagenesis of the single conserved Cys125

    PMID:15500441 PMID:15572350

    Open questions at the time
    • Positive functional mechanism not assigned by these negative assays
    • Physiological substrates not yet identified in this work
  4. 2002 High

    Provided the first endogenous client: it was unknown whether ERp29 binds folding clients in vivo, answered by showing preferential association with denatured thyroglobulin in a BiP/GRP94 heterocomplex.

    Evidence Cross-linking, co-IP, sucrose gradient sedimentation, and affinity chromatography in thyroid cells

    PMID:11884402

    Open questions at the time
    • Whether ERp29 actively promotes Tg export not yet shown here
    • Binding determinants on Tg not mapped
  5. 2005 High

    Linked ERp29 to secretory throughput and viral entry, two distinct readouts of escort function: gain/loss-of-function showed it accelerates thyroglobulin secretion, while unfolding assays showed it conformationally activates polyomavirus VP1 for membrane penetration.

    Evidence Overexpression/RNAi secretion assays with mutagenesis; biochemical unfolding, lipid binding, and dominant-negative infection assays

    PMID:16246730 PMID:16380091

    Open questions at the time
    • Domain responsible for substrate binding not yet defined
    • Whether dimerization is required for activity not yet tested
  6. 2007 High

    Established that the oligomeric state is mechanistically essential: a dimerization-deficient D42A mutant abolished both VP1 unfolding and Tg escort, and a compensatory G37D/D42A mutation restoring dimerization rescued activity, tying function to the thioredoxin-domain interface.

    Evidence Site-directed mutagenesis with compensatory rescue; unfolding, infection, and Tg secretion assays

    PMID:17267685

    Open questions at the time
    • How dimerization enables substrate engagement structurally unresolved
    • Generality across other clients not tested
  7. 2008 High

    Mapped substrate recognition to specific domains and residues: the crystal structure plus binding assays showed the C-terminal D domain is sufficient for substrate binding (preferring aromatic, basic peptides), while a monomeric mutant retained binding, and three CTD hydrophobic residues were specifically required for polyomavirus binding/unfolding.

    Evidence X-ray crystallography at 2.9 Å, in vitro peptide/protein binding, and CTD mutagenesis with viral and Tg functional readouts

    PMID:19019959 PMID:19084538

    Open questions at the time
    • Apparent tension between monomer binding and dimer-dependent activity not fully reconciled
    • Structural basis of substrate unfolding not visualized
  8. 2009 High

    Extended escort function to gap-junction biogenesis: it was unknown how monomeric connexin is protected before assembly, answered by showing ERp29 binds monomeric Cx43 in the ER to restrict premature oligomerization and enable plasma-membrane trafficking.

    Evidence Co-IP, confocal microscopy, Golgi accumulation, and dye-transfer GJIC assays

    PMID:19321666

    Open questions at the time
    • Binding site on Cx43 not mapped
    • Whether dimerization is required for Cx43 stabilization not tested here
  9. 2010 High

    Placed ERp29 in a multi-enzyme pathway and revealed a second tissue context: in vitro reconstitution showed ERp57/PDI cooperate with ERp29 to unfold VP1, while sperm-head localization plus antibody blocking implicated ERp29 in sperm-oocyte fusion.

    Evidence In vitro disulfide disruption and VP1 unfolding with cysteine mutants; confocal localization and antibody-blocking fertilization assays

    PMID:20132541 PMID:21159867

    Open questions at the time
    • How redox-inactive ERp29 coordinates with redox enzymes mechanistically unresolved
    • Sperm function based on antibody blocking, not genetic loss-of-function
  10. 2011 Medium

    Broadened the client repertoire to disease-relevant channels and connected ERp29 to ER-stress signaling: it promotes maturation and functional expression of WT and ΔF508 CFTR, and physically interacts with PERK to modulate eIF2α/Hsp27 and confer drug resistance.

    Evidence Co-IP, Xenopus oocyte expression, Ussing chamber, CFTR maturation Western blots; PERK co-IP with Hsp27 siRNA clonogenic rescue

    PMID:21419175 PMID:21525008

    Open questions at the time
    • PERK interaction rests on single co-IP without reciprocal validation
    • Mechanism of CFTR maturation assistance not resolved
  11. 2014 Medium

    Defined a COPII-coupled ER-exit mechanism and a specific UPR-branch role: ERp29 promotes β-ENaC interaction with the COPII cargo receptor Sec24D to drive γ-ENaC cleavage/activation, and ERp29 loss selectively impairs the ATF6-CHOP UPR branch, altering apoptosis sensitivity.

    Evidence Ussing chamber, ENaC cleavage Western blots, Sec24D siRNA, C157S mutagenesis; ERp29 knockout mouse with UPR branch and apoptosis assays; SPR calreticulin binding

    PMID:24370996 PMID:24944201 PMID:25130463

    Open questions at the time
    • Direct demonstration of ATF6 transport by ERp29 not shown
    • Whether Sec24D coupling generalizes to other cargo not established
  12. 2020 Medium

    Established ERp29 as a bridge between ER lectin chaperones and extended COPII escort to additional cargo: it binds the calnexin P-domain and forms CNX-ERp29-CNX and CNX-ERp29-CRT ternary complexes, and promotes proinsulin ER exit via Sec24D.

    Evidence In vitro binding/complex reconstitution and CNX domain mapping; proinsulin/Sec24D co-precipitation with gain/loss-of-function

    PMID:28456374 PMID:32433667 PMID:33360823

    Open questions at the time
    • Functional output of CNX/CRT bridging in cells not demonstrated
    • Proinsulin role based on co-precipitation without direct reconstitution
  13. 2022 Medium

    Extended the Cx43-escort role to disease and showed a cytosolic-facing client: ERp29 stabilizes MSec to drive tunneling-nanotube formation, and ERp29 restores Cx43 trafficking/GJIC and reduces coronavirus susceptibility in astrocytes.

    Evidence Affinity purification/MS, siRNA epistasis, ER fractionation, TNT quantification; viral infection model with exogenous ERp29 and 4-PBA

    PMID:30877198 PMID:36572185

    Open questions at the time
    • How an ER lumenal protein stabilizes the cytosolic/ER-outer-surface MSec mechanistically unclear
    • Cx43/viral findings are gain-of-function in one model
  14. 2023 Medium

    Implicated ERp29 in calcium signaling at ER-mitochondria contacts: DPP4/PAR2/ERK signaling upregulates ERp29, which binds and stabilizes IP3R2 to promote MAM formation and mitochondrial calcium overload in neurons.

    Evidence Co-IP, pathway inhibitors, DPP4 knockdown, and db/db in vivo model

    PMID:36936785

    Open questions at the time
    • Direct ERp29-IP3R2 interaction rests on co-IP in one model
    • Reconciliation of lumenal ERp29 acting on IP3R2 not addressed

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a redox-inactive, enzymatically silent dimer mechanically unfolds or stabilizes its diverse clients—and how this single escort selects between membrane penetration, oligomerization restriction, and COPII-coupled export—remains structurally and mechanistically unresolved.
  • No co-structure of ERp29 with any substrate
  • Molecular basis of client selectivity unknown
  • Reconciliation of lumenal localization with cytosolic-facing roles (MSec, IP3R2) unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0044183 protein folding chaperone 6 GO:0098772 molecular function regulator activity 4 GO:0060090 molecular adaptor activity 3
Localization
GO:0005783 endoplasmic reticulum 3
Pathway
R-HSA-392499 Metabolism of proteins 4 R-HSA-8953897 Cellular responses to stimuli 3 R-HSA-5653656 Vesicle-mediated transport 2
Partners
CALRCANXEIF2AK3GJA1HSPA5ITPR2SEC24DTNFAIP2
Complex memberships
CNX-ERp29-CNX / CNX-ERp29-CRT lectin-chaperone bridge complexERp29 homodimer

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 NMR structures of ERp29's N-terminal and C-terminal domains were determined: the N-terminal domain adopts a thioredoxin fold and mediates homodimerization, while the C-terminal domain has a novel all-helical fold. The thioredoxin fold acts as a specific homodimerization module without covalent linkages. ERp29 exists predominantly as a 51 kDa homodimer with a short flexible linker between domains. NMR spectroscopy, gadolinium-based relaxation agent, biochemical characterization Structure High 11435111
1998 ERp29 is a stress-inducible ER lumenal protein localized to the ER lumen (confirmed by immunofluorescence microscopy, in vitro translation, and proteinase protection assay). It associates with the ER chaperone BiP/GRP78, and this interaction is significantly enhanced after ER stress induction with tunicamycin or A23187. Immunofluorescence microscopy, proteinase protection assay, co-immunoprecipitation European journal of biochemistry Medium 9492298
1998 ERp29 self-associates predominantly into homodimers in solution and in rat hepatoma cells, as shown by size exclusion chromatography and chemical cross-linking. Cross-linking and immunoprecipitation also demonstrated interaction of ERp29 with BiP/GRP78 in cells. Size exclusion chromatography, chemical cross-linking, immunoprecipitation, [35S]methionine labeling FEBS letters Medium 9714535
2002 ERp29 associates with thyroglobulin (Tg) in the ER of thyroid cells as part of a large heterocomplex also containing BiP and GRP94. This was demonstrated by chemical cross-linking followed by immunoprecipitation, sucrose density gradient co-fractionation, and affinity chromatography using Tg as ligand. ERp29 preferentially associated with urea-denatured Tg-Sepharose, indicating chaperone-like binding to non-native protein. Chemical cross-linking, co-immunoprecipitation, sucrose density gradient sedimentation, affinity chromatography, immunofluorescence microscopy The Journal of biological chemistry High 11884402
2005 ERp29 triggers conformational unfolding of polyomavirus (Py) VP1 in the ER lumen, exposing the C-terminal arm of VP1 and creating a hydrophobic particle capable of binding lipid bilayers. Expression of dominant-negative ERp29 decreases Py infection, establishing ERp29 as required for ER membrane penetration during viral entry. Biochemical unfolding assay, lipid bilayer binding assay, dominant-negative expression, infection assay Molecular cell High 16246730
2005 Overexpression of ERp29 in FRTL-5 thyroid cells enhanced thyroglobulin (Tg) secretion ~2-fold, while RNAi-mediated ERp29 silencing attenuated Tg export. Mutational analysis identified two functional loci: the interdomain linker including Cys157 (important for C-terminal domain structural integrity) and an uncharged surface on the N-terminal domain flanked by Tyr64 and Gln70. Transient overexpression, RNAi knockdown, secretion assay, site-directed mutagenesis Biochemical and biophysical research communications Medium 16380091
2007 Dimerization of ERp29 via its N-terminal thioredoxin domain is essential for both its polyomavirus-unfolding activity and its thyroglobulin escort/secretion function. A dimerization-deficient mutant (D42A) failed to unfold Py or stimulate infection; a compensatory mutation (G37D/D42A) that partially restored dimerization rescued activity. The same dimerization requirement applied to the Tg escort function. Site-directed mutagenesis, polyomavirus unfolding assay, infection assay, thyroglobulin secretion assay Molecular biology of the cell High 17267685
2004 Purified native ERp29 lacks classical chaperone activity (does not protect substrate proteins against thermal aggregation, does not interact stably with chemically denatured proteins), lacks disulfide reductase and isomerase activities, and lacks calcium-binding activity. ERp29 exists as tight homodimers (Kd <50 nM) and has unusual affinity for heparin. Chaperone aggregation assay, disulfide reductase assay, isomerase assay, calcium binding assay, cross-linking, size exclusion chromatography, heparin affinity chromatography The Biochemical journal High 15500441
2004 Cys-125 (the single conserved cysteine of ERp29) plays a key structural role: its substitution with serine reduces surface hydrophobicity and increases proteolytic lability of the protein. No multimerization beyond tight homodimers was detected with untagged ERp29 (His-tag artifactually promoted higher oligomers). Analytical ultracentrifugation, dynamic light scattering, hydrophobic probe assay, limited proteolysis, mutagenesis The Journal of biological chemistry Medium 15572350
2008 Crystal structure of human ERp29 was determined at 2.9 Å resolution, confirming structural homology to the Drosophila homolog Wind. ERp29 binds directly to thyroglobulin, thyroglobulin-derived peptides, and Wind client protein Pipe in vitro. The C-terminal D domain alone is sufficient for peptide/protein substrate binding. Interacting peptides share two or more aromatic residues with overall basic character. A monomeric mutant still binds substrates, indicating the thioredoxin domain alone supports client binding. X-ray crystallography, in vitro binding assay, peptide binding assay, mutagenesis Journal of molecular biology High 19084538
2008 The C-terminal domain (CTD) of ERp29 is required for polyomavirus binding and unfolding. Three hydrophobic residues in the last helix of the CTD, when individually mutated to lysine or alanine, abolished ERp29's ability to stimulate Py unfolding and infection without affecting dimerization or Tg secretion. Cross-linking co-immunoprecipitation showed these CTD mutants bind Py inefficiently. Site-directed mutagenesis, Py unfolding assay, infection assay, Tg secretion assay, cross-linking co-immunoprecipitation Journal of virology High 19019959
2009 ERp29 restricts Connexin43 (Cx43) oligomerization in the ER. ERp29 forms a specific complex with monomeric Cx43 in the ER, and interference with ERp29 function destabilizes monomeric Cx43, causing increased Cx43 accumulation in the Golgi, reduced transport to the plasma membrane, and inhibited gap junctional communication. Co-immunoprecipitation, confocal microscopy, dye transfer assay (gap junction communication), Golgi accumulation assay Molecular biology of the cell High 19321666
2010 ERp57, PDI, and ERp72 facilitate polyomavirus (Py) infection by disrupting Py disulfide bonds. ERp57 and PDI, but not ERp72, operate in concert with ERp29 to unfold the VP1 C-terminal arm. ERp57 principally isomerizes Py (requiring free cysteines), while PDI and ERp72 reduce Py. VP1 residues C11 and C15 are important for infection and for isomerization, and also stabilize some interpentamer interactions via disulfide bonds. In vitro disulfide disruption assay, VP1 unfolding assay, site-directed mutagenesis of VP1 cysteines, infection assay, alkylation experiments Journal of virology High 21159867
2011 ERp29 co-immunoprecipitates with ΔF508-CFTR in CF bronchiolar epithelial cells. Overexpression of ERp29 increased functional expression of both wild-type and ΔF508-CFTR and increased WT-CFTR plasma membrane expression in Xenopus oocytes. Depletion of ERp29 decreased CFTR functional expression and maturation of newly synthesized CFTR. Co-immunoprecipitation, Xenopus oocyte expression, short circuit current (Ussing chamber), Western blot for CFTR maturation The Journal of biological chemistry High 21525008
2014 ERp29 deficiency impairs activation of the ATF6-CHOP branch of the unfolded protein response (UPR) without affecting ATF4-eIF2α-XBP1 signaling. As a result, ERp29-/- dermal fibroblasts and thyrocytes show reduced apoptosis sensitivity to tunicamycin and H2O2, suggesting ERp29 acts as an escort factor promoting ATF6 transport from the ER to the Golgi under ER stress. ERp29 knockout mouse model, UPR branch activation assays, apoptosis assay (tunicamycin, H2O2 treatment) Apoptosis Medium 24370996
2014 ERp29 regulates ENaC functional expression by promoting cleavage of γ-ENaC. ERp29 overexpression increases amiloride-sensitive short-circuit current and abundance of cleaved γ-ENaC. The single cysteine of ERp29 (Cys157) is required for this function. ERp29 promotes interaction of β-ENaC with the COPII cargo recognition component Sec24D, directing ENaC toward the Golgi. Ussing chamber electrophysiology, Western blot for ENaC cleavage, co-immunoprecipitation, Sec24D siRNA, mutagenesis (C157S ERp29) American journal of physiology. Cell physiology High 24944201
2011 ERp29 physically interacts with PERK (the ER stress kinase EIF2AK3) as shown by co-immunoprecipitation. Overexpression of ERp29 enhances endogenous PERK levels. ERp29 upregulates Hsp27 via downregulation of eIF2α phosphorylation, and this Hsp27 upregulation mediates ERp29-conferred resistance to doxorubicin. Co-immunoprecipitation, Western blotting, siRNA knockdown of Hsp27, clonogenic survival assay Biochimica et biophysica acta Medium 21419175
2019 ERp29 is required for tunneling nanotube (TNT) formation by stabilizing the TNT-essential protein MSec (TNFAIP2). ERp29 depletion reduces TNT formation; ERp29 overexpression promotes TNT formation in a strictly MSec-dependent manner. ERp29 stabilizes MSec at the protein (not mRNA) level, requiring ERp29 chaperone activity. MSec is associated with the outer surface of the ER. Affinity protein purification, mass spectrometry, siRNA depletion, confocal immunofluorescence, ER fractionation, limited proteolysis, TNT quantification The Journal of biological chemistry High 30877198
2014 ERp29 forms a 1:1 complex with lectin chaperone calreticulin (CRT) with a dissociation constant similar to that of the ERp57-calreticulin interaction, as measured by surface plasmon resonance. The recognition site of ERp29 on calreticulin may differ from that of ERp57. Surface plasmon resonance (SPR) analysis Biochemical and biophysical research communications Medium 25130463
2017 ERp29 directly interacts with calnexin (CNX), recognizing the P-domain of CNX. The interaction has an affinity similar to the ERp57-CNX interaction. ERp29 and ERp57 appear to recognize the same domain of CNX but with somewhat different modes of interaction. In vitro binding assay, CNX mutant analysis, dissociation constant determination Biochemical and biophysical research communications Medium 28456374
2020 ERp29, as a dimer, bridges two molecules of calnexin (CNX), forming CNX-ERp29-CNX complexes. Similar heterocomplexes including CNX-ERp29-CRT were also detected, establishing ERp29 as a molecular bridge between ER lectin chaperones. In vitro binding assays, biochemical complex formation analysis Biochemical and biophysical research communications Medium 33360823
2020 ERp29 associates with Proinsulin and with the COPII cargo recognition component Sec24D in co-precipitation experiments. ERp29 overexpression increases whole-cell Proinsulin levels and depletion decreases them, suggesting ERp29 promotes ER exit of Proinsulin via Sec24D/COPII vesicles. Co-immunoprecipitation/co-precipitation, overexpression, siRNA depletion, Western blotting PloS one Medium 32433667
2022 In MHV-A59 coronavirus-infected astrocytes, reduced ERp29 expression was associated with Cx43 retention in the ER and impaired gap junctional communication. Exogenous ERp29 expression reduced MHV-A59 susceptibility and restored Cx43-mediated GJIC. The chemical chaperone 4-PBA increased ERp29 expression and rescued Cx43 trafficking. Viral infection model, exogenous ERp29 expression, GJIC dye transfer assay, 4-PBA treatment, Western blotting The Journal of biological chemistry Medium 36572185
2010 ERp29 is localized to the equatorial and post-acrosomal regions of the sperm head after acrosome reaction in mice—the site of initial sperm-oocyte membrane fusion. Antibodies against ERp29 inhibited sperm penetration into zona pellucida-free oocytes and reduced fertilization rate and index without affecting sperm motility or acrosome reaction, implicating ERp29 in sperm-oocyte membrane fusion. Confocal immunofluorescence microscopy, functional antibody blocking assay, fertilization assay Reproductive biology and endocrinology Medium 20132541
2023 ERp29 promotes its binding to IP3R2 (inositol 1,4,5-trisphosphate receptor type 2), inhibiting IP3R2 degradation and promoting mitochondria-associated ER membrane (MAM) formation and mitochondrial calcium overload in hippocampal neurons. DPP4 activates PAR2/ERK1/2/CEBPB signaling to upregulate ERp29, which then binds IP3R2. Co-immunoprecipitation (ERp29-IP3R2), signaling pathway inhibitors, DPP4 knockdown, in vivo db/db mouse model iScience Medium 36936785

Source papers

Stage 0 corpus · 72 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Molecular cell 143 16246730
2010 A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection. Journal of virology 89 21159867
2002 Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex. The Journal of biological chemistry 87 11884402
2001 Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer. Structure (London, England : 1993) 84 11435111
1998 A stress-inducible rat liver endoplasmic reticulum protein, ERp29. European journal of biochemistry 83 9492298
2009 ERp29 restricts Connexin43 oligomerization in the endoplasmic reticulum. Molecular biology of the cell 75 19321666
1998 ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif. European journal of biochemistry 71 9738895
1997 Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum. FEBS letters 71 9037184
2014 ERp29 deficiency affects sensitivity to apoptosis via impairment of the ATF6-CHOP pathway of stress response. Apoptosis : an international journal on programmed cell death 58 24370996
2000 Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells. Evidence for a unique role in secretory-protein synthesis. European journal of biochemistry 58 10727933
2010 Endoplasmic reticulum protein 29 (ERp29): An emerging role in cancer. The international journal of biochemistry & cell biology 52 20920593
2006 ERp29, an unusual redox-inactive member of the thioredoxin family. Antioxidants & redox signaling 51 16677078
2008 Crystal structure and functional analysis of the protein disulfide isomerase-related protein ERp29. Journal of molecular biology 49 19084538
2005 ERp29 is an essential endoplasmic reticulum factor regulating secretion of thyroglobulin. Biochemical and biophysical research communications 48 16380091
2002 ERp29 is a ubiquitous resident of the endoplasmic reticulum with a distinct role in secretory protein production. The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society 47 11897809
2011 Identification of ERp29 as a biomarker for predicting nasopharyngeal carcinoma response to radiotherapy. Oncology reports 43 22160175
2022 Nonenzymatic function of DPP4 promotes diabetes-associated cognitive dysfunction through IGF-2R/PKA/SP1/ERp29/IP3R2 pathway-mediated impairment of Treg function and M1 microglia polarization. Metabolism: clinical and experimental 42 36302455
2009 Cytokeratin 19 regulates endoplasmic reticulum stress and inhibits ERp29 expression via p38 MAPK/XBP-1 signaling in breast cancer cells. Experimental cell research 42 19265690
2010 Over-expression of ERp29 attenuates doxorubicin-induced cell apoptosis through up-regulation of Hsp27 in breast cancer cells. Experimental cell research 41 20833165
1998 Oligomerization properties of ERp29, an endoplasmic reticulum stress protein. FEBS letters 36 9714535
2015 Erp29 Attenuates Cigarette Smoke Extract-Induced Endoplasmic Reticulum Stress and Mitigates Tight Junction Damage in Retinal Pigment Epithelial Cells. Investigative ophthalmology & visual science 35 26431474
2019 The chaperone ERp29 is required for tunneling nanotube formation by stabilizing MSec. The Journal of biological chemistry 34 30877198
2008 Triplex profiling of functionally distinct chaperones (ERp29/PDI/BiP) reveals marked heterogeneity of the endoplasmic reticulum proteome in cancer. Journal of proteome research 34 18598068
2007 Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions. Molecular biology of the cell 34 17267685
2002 Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29. Gene 33 12039039
2011 ERp29 regulates DeltaF508 and wild-type cystic fibrosis transmembrane conductance regulator (CFTR) trafficking to the plasma membrane in cystic fibrosis (CF) and non-CF epithelial cells. The Journal of biological chemistry 32 21525008
2000 Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis 31 11271497
2011 Inhibiting ERp29 expression enhances radiosensitivity in human nasopharyngeal carcinoma cell lines. Medical oncology (Northwood, London, England) 30 21479953
2011 ERp29 induces breast cancer cell growth arrest and survival through modulation of activation of p38 and upregulation of ER stress protein p58IPK. Laboratory investigation; a journal of technical methods and pathology 30 22064321
2005 Overexpression of ERp29 in the thyrocytes of FRTL-5 cells. Molecular biology reports 29 15865205
2011 ERp29 regulates response to doxorubicin by a PERK-mediated mechanism. Biochimica et biophysica acta 28 21419175
2006 Expression of ERp29, an endoplasmic reticulum secretion factor in basal-cell carcinoma. The American Journal of dermatopathology 28 17012915
2020 The Probable, Possible, and Novel Functions of ERp29. Frontiers in physiology 26 33013490
2017 Proteomic identification of ERP29 as a key chemoresistant factor activated by the aggregating p53 mutant Arg282Trp. Oncogene 26 28534505
2014 High concentraction of taurocholic acid induced apoptosis in HTR-8/SVneo cells via overexpression of ERp29 and activation of p38. Placenta 26 24780196
2004 Purification and biochemical characterization of native ERp29 from rat liver. The Biochemical journal 26 15500441
2019 High glucose regulates ERp29 in hepatocellular carcinoma by LncRNA MEG3-miRNA 483-3p pathway. Life sciences 25 31251997
2008 ERp29 is a radiation-responsive gene in IEC-6 cell. Journal of radiation research 25 18802324
2004 ERp29, a general endoplasmic reticulum marker, is highly expressed throughout the brain. The Journal of comparative neurology 25 15281078
2019 miR-205-5p downregulation decreases gemcitabine sensitivity of breast cancer cells via ERp29 upregulation. Experimental and therapeutic medicine 23 31602229
2008 ERp29, an endoplasmic reticulum secretion factor is involved in the growth of breast tumor xenografts. Molecular carcinogenesis 23 18395818
2008 The C-terminal domain of ERp29 mediates polyomavirus binding, unfolding, and infection. Journal of virology 23 19019959
2004 Biophysical characterization of ERp29. Evidence for a key structural role of cysteine 125. The Journal of biological chemistry 23 15572350
2017 ERp29 controls invasion and metastasis of gastric carcinoma by inhibition of epithelial-mesenchymal transition via PI3K/Aktsignaling pathway. BMC cancer 21 28874138
2015 Friend or foe: Endoplasmic reticulum protein 29 (ERp29) in epithelial cancer. FEBS open bio 21 25709888
2010 Endoplasmic reticulum protein 29 (ERp29), a protein related to sperm maturation is involved in sperm-oocyte fusion in mouse. Reproductive biology and endocrinology : RB&E 21 20132541
2018 Molecular Chaperone ERp29: A Potential Target for Cellular Protection in Retinal and Neurodegenerative Diseases. Advances in experimental medicine and biology 20 29721972
2017 PDI family protein ERp29 recognizes P-domain of molecular chaperone calnexin. Biochemical and biophysical research communications 19 28456374
2014 PDI family protein ERp29 forms 1:1 complex with lectin chaperone calreticulin. Biochemical and biophysical research communications 19 25130463
2014 ERp29 regulates epithelial sodium channel functional expression by promoting channel cleavage. American journal of physiology. Cell physiology 18 24944201
2007 Identification and characterization of ERp29 in rat spermatozoa during epididymal transit. Reproduction (Cambridge, England) 18 17379652
2015 Endoplasmic reticulum protein 29 (ERp29) confers radioresistance through the DNA repair gene, O(6)-methylguanine DNA-methyltransferase, in breast cancer cells. Scientific reports 16 26420420
2019 ERp29 inhibition attenuates TCA toxicity via affecting p38/p53- dependent pathway in human trophoblast HTR-8/SVeno cells. Archives of biochemistry and biophysics 14 31586554
2017 ERp29 inhibits tumorigenicity by suppressing epithelial mesenchymal transition in gastric cancer. Oncotarget 13 29108263
2023 Non-canonical function of DPP4 promotes cognitive impairment through ERp29-associated mitochondrial calcium overload in diabetes. iScience 11 36936785
2018 ERp29 counteracts the suppression of malignancy mediated by endoplasmic reticulum stress and promotes the metastasis of colorectal cancer. Oncology reports 10 30569094
2022 Regulatory role of endoplasmic reticulum resident chaperone protein ERp29 in anti-murine β-coronavirus host cell response. The Journal of biological chemistry 9 36572185
2021 Identification of Two Novel CIL-102 Upregulations of ERP29 and FUMH to Inhibit the Migration and Invasiveness of Colorectal Cancer Cells by Using the Proteomic Approach. Biomolecules 9 34572494
2021 ERp29 forms a feedback regulation loop with microRNA-135a-5p and promotes progression of colorectal cancer. Cell death & disease 9 34667160
2016 Comparison of ILK and ERP29 expressions in benign and malignant pancreatic lesions and their clinicopathological significances in pancreatic ductal adenocarcinomas. Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico 9 26887611
1991 Immunohistochemical assessment of ER-P31, a mouse anti-oestrogen receptor protein monoclonal antibody in human breast cancers: comparison with ER-ICA (Abbott) and radioligand assays. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 8 1705046
2020 ERp29 as a regulator of Insulin biosynthesis. PloS one 7 32433667
2023 ERp29 Attenuates Nicotine-Induced Endoplasmic Reticulum Stress and Inhibits Choroidal Neovascularization. International journal of molecular sciences 6 37958506
2018 ERp29 downregulation enhances lung adenocarcinoma cell chemosensitivity to gemcitabine by upregulating HSP27 phosphorylation. Experimental and therapeutic medicine 5 30651868
2008 Constancy of ERp29 expression in cultured retinal pigment epithelial cells in the Ccl2/Cx3cr1 deficient mouse model of age-related macular degeneration. Current eye research 5 18696346
2024 ERP29 regulates the proliferation of endometrial carcinoma via M6A modification. Life sciences 4 39142507
2006 Purification and structural characterization of human ERp29. Protein and peptide letters 3 17073718
2024 The role of ERp29/FOS/EMT pathway in excessive apoptosis of placental trophoblast cells in intrahepatic cholestasis of pregnancy. Placenta 2 38346375
2024 The impact of ERP29 on the progression of pharyngeal squamous cell carcinoma. Scientific reports 2 39465248
2020 ERp29 affects the migratory and invasive ability of human extravillous trophoblast HTR-8/SVneo cells via modulating the epithelial-mesenchymal transition. Journal of biochemical and molecular toxicology 2 31981282
2020 Dimerization of ER-resident molecular chaperones mediated by ERp29. Biochemical and biophysical research communications 2 33360823
2020 [Silencing ERp29 promotes the invasiveness of human PCa cells in vitro: Molecular mechanisms]. Zhonghua nan ke xue = National journal of andrology 1 33377711

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