Affinage

ERP29

Endoplasmic reticulum resident protein 29 · UniProt P30040

Length
261 aa
Mass
29.0 kDa
Annotated
2026-04-28
72 papers in source corpus 26 papers cited in narrative 26 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ERp29 is a redox-inactive, PDI-family member that functions as a non-classical escort and folding factor in the endoplasmic reticulum, facilitating the maturation, conformational regulation, and ER-to-Golgi transport of diverse client proteins. Its N-terminal thioredoxin domain mediates obligate homodimerization essential for function, while its C-terminal all-helical domain serves as the principal substrate-binding surface, recognizing peptides with aromatic and basic character (PMID:11435111, PMID:19084538, PMID:17267685). ERp29 lacks disulfide isomerase, reductase, and classical chaperone activities (PMID:15500441), yet it promotes secretion of thyroglobulin, facilitates ER exit of CFTR, ENaC, and proinsulin via interaction with the COPII component Sec24D, restricts premature Connexin43 oligomerization, unfolds polyomavirus to enable ER membrane penetration, bridges calnexin and calreticulin into lectin chaperone complexes, and selectively modulates ATF6-branch UPR signaling (PMID:16380091, PMID:21525008, PMID:24944201, PMID:19321666, PMID:16246730, PMID:33360823, PMID:24370996). ERp29 also functions outside the canonical ER quality-control pathway by stabilizing MSec to promote tunneling nanotube formation and by binding IP3R2 at mitochondria-associated ER membranes to regulate calcium transfer (PMID:30877198, PMID:36302455).

Mechanistic history

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

    Establishing ERp29 as an ER-resident, stress-responsive protein that homodimerizes and associates with BiP resolved its basic subcellular context and oligomeric state, distinguishing it as a new member of the ER quality-control machinery.

    Evidence Immunofluorescence, proteinase protection, co-IP, size-exclusion chromatography, and chemical cross-linking in rat hepatoma cells

    PMID:9492298 PMID:9714535

    Open questions at the time
    • Functional role of BiP interaction unclear
    • No enzymatic or chaperone activity assigned
  2. 2001 High

    NMR structures revealed that ERp29 dimerizes through its N-terminal thioredoxin domain and possesses a novel C-terminal all-helical fold, providing the first structural framework for understanding how a thioredoxin fold mediates non-covalent homodimerization.

    Evidence NMR spectroscopy with gadolinium relaxation agent interface mapping

    PMID:11435111

    Open questions at the time
    • No client-binding site identified at this stage
    • Functional significance of dimerization not yet tested
  3. 2002 High

    Identification of ERp29 within the thyroglobulin folding complex in thyroid cells provided the first evidence that ERp29 participates in client protein maturation, preferentially engaging unfolded substrates.

    Evidence Chemical cross-linking, co-IP, sucrose gradient analysis, and affinity chromatography with denatured thyroglobulin in thyroid cells

    PMID:11884402

    Open questions at the time
    • Whether ERp29 directly contacts thyroglobulin or acts through other chaperones not resolved
    • Mechanism of client recognition unknown
  4. 2004 High

    Biochemical characterization definitively excluded classical chaperone, disulfide isomerase/reductase, and calcium-binding activities for ERp29, forcing reclassification as a non-classical ER factor and motivating the search for an alternative mechanism.

    Evidence Purified native ERp29 tested in thermal aggregation protection, disulfide isomerase/reductase, and calcium-binding assays

    PMID:15500441 PMID:15572350

    Open questions at the time
    • What ERp29 actually does to clients remained undefined
    • Functional consequence of Cys125 for client handling unknown
  5. 2005 High

    Two parallel discoveries established ERp29 as an active escort factor: it catalytically unfolds polyomavirus to expose hydrophobic VP1 determinants for ER membrane penetration, and it directly promotes thyroglobulin secretion with defined interaction residues.

    Evidence In vitro viral unfolding/lipid-binding assay with dominant-negative ERp29; overexpression/RNAi with secretion readout and site-directed mutagenesis in thyroid cells

    PMID:16246730 PMID:16380091

    Open questions at the time
    • Whether the unfolding activity is purely conformational or involves cofactors unknown
    • Structural basis of client selectivity not resolved
  6. 2007 High

    Demonstration that dimerization-deficient ERp29 mutants lost both viral unfolding and thyroglobulin escort function—rescued by a compensatory mutation—established homodimerization as an obligate prerequisite for ERp29 activity.

    Evidence D42A and G37D/D42A compensatory mutagenesis with viral infection and thyroglobulin secretion assays

    PMID:17267685

    Open questions at the time
    • Why dimerization is mechanistically required (avidity vs. allosteric activation) not distinguished
  7. 2008 High

    Crystal structure and mutagenesis pinpointed the C-terminal D-domain as the principal substrate-binding surface, with hydrophobic residues in its last helix essential for polyomavirus engagement, while the same domain recognizes peptides with aromatic/basic character from multiple clients.

    Evidence X-ray crystallography at 2.9 Å, in vitro peptide/protein binding with D-domain and monomeric mutants; CTD hydrophobic-to-charged mutagenesis with infection, cross-linking, and unfolding assays

    PMID:19019959 PMID:19084538

    Open questions at the time
    • Client selectivity determinants beyond aromatic/basic motif not defined
    • CTD mutations separating Py from Tg function raise question of whether different clients use overlapping or distinct surfaces
  8. 2009 High

    ERp29 was shown to restrict premature Connexin43 oligomerization in the ER, establishing a quality-control role beyond simple escort—loss of ERp29 function destabilized monomeric Cx43 and impaired gap junctional communication.

    Evidence Co-IP of ERp29-monomeric Cx43, dominant-negative interference, trafficking analysis, and gap junction dye transfer assay

    PMID:19321666

    Open questions at the time
    • Whether ERp29 directly shields Cx43 oligomerization interfaces or acts indirectly unknown
    • Stoichiometry of ERp29-Cx43 complex not determined
  9. 2011 High

    ERp29 was found to regulate CFTR trafficking to the plasma membrane, including rescue of ΔF508-CFTR, broadening its client repertoire to a medically important ion channel and suggesting a general role in promoting ER exit of polytopic membrane proteins.

    Evidence Xenopus oocyte expression, co-IP of ERp29-ΔF508-CFTR, siRNA knockdown, Ussing chamber electrophysiology, and surface biotinylation

    PMID:21525008

    Open questions at the time
    • Whether ERp29's effect on CFTR is direct or mediated through quality-control machinery not resolved
    • No structural information on ERp29-CFTR interaction
  10. 2014 High

    ERp29 was linked to ER-to-Golgi cargo selection through interaction with Sec24D/COPII (demonstrated for ENaC) and to selective regulation of the ATF6 UPR branch (demonstrated in knockout mice), revealing functions in both anterograde transport and stress signaling.

    Evidence Sec24D co-IP with mutagenesis and Ussing chamber for ENaC; ERp29-knockout mouse with UPR branch dissection and apoptosis assays

    PMID:24370996 PMID:24944201

    Open questions at the time
    • How ERp29 facilitates ATF6 transport mechanistically is unclear
    • Whether Sec24D interaction is direct or through client cargo not determined
  11. 2014 Medium

    Quantitative binding studies showed ERp29 forms 1:1 complexes with calreticulin and calnexin with affinities comparable to ERp57, but through distinct binding sites, positioning ERp29 as an alternative bridge within the lectin chaperone cycle.

    Evidence SPR binding assays with calnexin P-domain mutants and calreticulin

    PMID:25130463 PMID:28456374

    Open questions at the time
    • Functional consequence of ERp29-lectin chaperone complexes for client folding not tested
    • In-cell validation of these interactions limited
  12. 2019 High

    Discovery that ERp29 stabilizes MSec post-translationally to promote tunneling nanotube formation expanded ERp29's functional scope beyond classical ER quality control to intercellular communication.

    Evidence AP-MS identification, confocal imaging, siRNA/overexpression with TNT quantification, limited proteolysis

    PMID:30877198

    Open questions at the time
    • Whether ERp29-MSec interaction is direct or bridged remains ambiguous
    • ER vs. cytoplasmic site of MSec stabilization not resolved
  13. 2020 Medium

    ERp29 dimers were shown to bridge calnexin-calnexin and calnexin-calreticulin into heteromeric complexes in vitro, and ERp29 was found to associate with proinsulin and Sec24D, extending the Sec24D-dependent ER exit mechanism to a new secretory client.

    Evidence In vitro complex formation/SPR for lectin bridging; co-IP and knockdown/overexpression for proinsulin-Sec24D in pancreatic cells

    PMID:32433667 PMID:33360823

    Open questions at the time
    • In-cell reconstitution of lectin bridging complexes not performed
    • Proinsulin study relies on single co-IP without reciprocal pull-down
  14. 2022 Medium

    Two studies identified ERp29 as a regulator of mitochondria-associated ER membrane (MAM) calcium signaling via stabilization of IP3R2, linking ERp29 to mitochondrial calcium overload in disease contexts.

    Evidence Co-IP of ERp29-IP3R2, siRNA/overexpression, pathway inhibitor studies, in vivo diabetic mouse models (Tregs and hippocampal neurons)

    PMID:36302455 PMID:36936785

    Open questions at the time
    • Whether ERp29-IP3R2 interaction is direct or occurs within a larger complex is unclear
    • Mechanism by which ERp29 prevents IP3R2 degradation not defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include the structural basis of client selectivity across ERp29's diverse substrates, the mechanistic link between ERp29 and ATF6 transport, whether ERp29's Sec24D interaction is direct, and how ERp29 coordinates its escort and quality-control functions with the calnexin/calreticulin cycle in vivo.
  • No co-crystal structure of ERp29 with any client protein
  • No reconstituted system showing ERp29-dependent COPII vesicle formation
  • In vivo significance of lectin-chaperone bridging untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 3 GO:0044183 protein folding chaperone 2
Localization
GO:0005783 endoplasmic reticulum 3
Pathway
R-HSA-9609507 Protein localization 5 R-HSA-392499 Metabolism of proteins 2 R-HSA-5653656 Vesicle-mediated transport 2 R-HSA-8953897 Cellular responses to stimuli 1
Partners
CALRCANXCFTRGJA1GRP78ITPR2SEC24DTNFAIP2
Complex memberships
Calnexin-calreticulin bridging complexERp29 homodimerThyroglobulin folding complex

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 NMR structures of the N- and C-terminal domains of ERp29 revealed a thioredoxin fold for the N-terminal domain and a novel all-helical fold for the C-terminal domain. The N-terminal thioredoxin domain mediates homodimerization, making ERp29 the first protein where the thioredoxin fold acts as a specific homodimerization module without covalent linkages. NMR spectroscopy, gadolinium relaxation agent-based interface mapping Structure High 11435111
1998 ERp29 is an ER-localized, stress-inducible protein that associates with the molecular chaperone BiP/GRP78 in rat hepatoma cells, and this interaction is enhanced under ER stress conditions (tunicamycin, calcium ionophore treatment). Immunofluorescence microscopy, topology studies (in vitro translation, proteinase protection assay), co-immunoprecipitation European journal of biochemistry High 9492298
1998 ERp29 self-associates predominantly into homodimers in solution and in cells, as shown by size exclusion chromatography and chemical cross-linking. ERp29 also interacts with multiple ER proteins including BiP/GRP78. Size exclusion chromatography, chemical cross-linking followed by immunoprecipitation FEBS letters High 9714535
2002 ERp29 is a member of the thyroglobulin (Tg) folding complex in the ER of thyroid cells, associating with Tg and major ER chaperones BiP and GRP94. ERp29 showed preferential binding to denatured Tg-Sepharose, indicating chaperone-like interactions. Chemical cross-linking, co-immunoprecipitation, sucrose density gradient analysis, immunofluorescent microscopy, affinity chromatography with Tg as ligand The Journal of biological chemistry High 11884402
2005 ERp29 triggers a conformational change in polyomavirus (Py) in the ER lumen by exposing the C-terminal arm of VP1, generating a hydrophobic particle that binds lipid bilayers. Expression of dominant-negative ERp29 decreases Py infection, establishing ERp29 as an ER factor mediating membrane penetration of a nonenveloped virus. In vitro conformational change assay, lipid bilayer binding assay, dominant-negative expression with infection assay Molecular cell High 16246730
2005 ERp29 overexpression in FRTL-5 thyroid cells enhanced thyroglobulin (Tg) secretion ~2-fold, while RNAi-mediated ERp29 silencing attenuated Tg export. Mutational analysis identified two loci important for ERp29-Tg interactions: the interdomain linker including Cys157 and an uncharged surface on the N-terminal domain flanked by Tyr64 and Gln70. Transient overexpression, RNAi knockdown, site-directed mutagenesis, secretion assay Biochemical and biophysical research communications High 16380091
2007 Dimerization of ERp29 via its N-terminal thioredoxin domain is essential for both its polyomavirus-unfolding activity and its escort function for thyroglobulin secretion. A dimerization-deficient mutant (D42A) lost both activities, and a compensatory mutation (G37D/D42A) that partially restored dimerization rescued activity. Site-directed mutagenesis, viral infection assay, thyroglobulin secretion assay, dimerization assays Molecular biology of the cell High 17267685
2008 Crystal structure of human ERp29 resolved to 2.9 Å showed significant structural homology to its Drosophila homolog Wind. ERp29 binds directly to thyroglobulin, thyroglobulin-derived peptides, the Wind client Pipe, and Pipe-derived peptides in vitro. The C-terminal D domain contains a peptide-binding site; a monomeric mutant and a D-domain mutant retaining the thioredoxin N-terminal domain alone were sufficient for client protein binding. Interacting peptides share two or more aromatic residues with overall basic character. X-ray crystallography, in vitro binding assays (peptide/protein binding), monomeric and D-domain mutant analysis Journal of molecular biology High 19084538
2008 The C-terminal all-helical domain (CTD) of ERp29 is required for polyomavirus binding, unfolding, and infection. Three hydrophobic residues in the last helix of the CTD (individually mutated to lysine or alanine) abolished ERp29's ability to stimulate Py unfolding and infection and reduced physical interaction with Py. The CTD mutants retained dimerization ability and could still facilitate thyroglobulin secretion. Site-directed mutagenesis, viral infection assay, cross-linking co-immunoprecipitation, protease sensitivity assay Journal of virology High 19019959
2009 ERp29 restricts Connexin43 (Cx43) oligomerization in the ER, forming a specific complex with monomeric Cx43. Interference with ERp29 function destabilized monomeric Cx43 in the ER, caused increased Cx43 accumulation in the Golgi, reduced plasma membrane transport, and inhibited gap junctional communication. Co-immunoprecipitation, dominant-negative interference, gap junction communication assay, trafficking/localization analysis Molecular biology of the cell High 19321666
2010 ERp57, PDI, and ERp72 facilitate polyomavirus infection downstream of ERp29. ERp57 and PDI operate in concert with ERp29 to unfold the VP1 C-terminal arm, while ERp72 can reduce the virus but does not collaborate with ERp29 for VP1 unfolding. ERp57 principally isomerizes Py using free viral cysteines; VP1 residues C11 and C15 were identified as important for ERp57-mediated isomerization and for stabilizing interpentamer interactions. In vitro disulfide disruption assays, isomerization assays, site-directed mutagenesis of VP1, infection assays with alkylated virus Journal of virology High 21159867
2004 Purified native ERp29 lacks classical chaperone activity (does not protect substrates against thermal aggregation or bind denatured proteins stably), disulfide reductase activity, disulfide isomerase activity, and calcium-binding activity, distinguishing it functionally from PDI and other classical ER chaperones. Purification to homogeneity, chaperone aggregation protection assays, cross-linking assays, disulfide reductase/isomerase assays, calcium-binding assays The Biochemical journal High 15500441
2004 Cys-125 is critical for ERp29's structural integrity and surface hydrophobicity. The Cys125Ser mutant shows reduced surface hydrophobicity and increased susceptibility to proteolytic degradation. Native ERp29 exists as tight homodimers (Kd <50 nM), and His-tagged ERp29 artifactually forms ~670 kDa oligomers. Sedimentation analysis, dynamic light scattering, hydrophobic probe assays, site-directed mutagenesis, proteolytic sensitivity assay The Journal of biological chemistry High 15572350
2011 ERp29 regulates wild-type and ΔF508-CFTR trafficking to the plasma membrane. ERp29 overexpression in Xenopus oocytes increased functional expression of both WT and ΔF508-CFTR >3-fold. ΔF508-CFTR co-immunoprecipitated with endogenous ERp29 in CF cells. ERp29 depletion decreased CFTR maturation and plasma membrane expression. Xenopus oocyte expression, co-immunoprecipitation, siRNA knockdown, Ussing chamber short-circuit current measurement, surface biotinylation The Journal of biological chemistry High 21525008
2014 ERp29 deficiency impairs ATF6 activation and transport from the ER to the Golgi under ER stress, without affecting other UPR branches (ATF4-eIF2α-XBP1). As a result, ERp29-knockout mouse thyrocytes and fibroblasts display reduced apoptosis sensitivity to tunicamycin and hydrogen peroxide. ERp29 knockout mouse model, UPR branch analysis, apoptosis assays in primary cells Apoptosis High 24370996
2014 ERp29 promotes ENaC functional expression by facilitating γ-ENaC cleavage and promoting β-ENaC interaction with the Sec24D COPII cargo recognition component, directing ENaC toward the Golgi. A cysteine-157 mutant (C157S ERp29) lost this activity. Ussing chamber (short-circuit current), siRNA knockdown, overexpression, apical trypsin activation assay, Cys mutant analysis, co-immunoprecipitation with Sec24D American journal of physiology. Cell physiology High 24944201
2011 ERp29 physically interacts with PERK (eIF2α kinase 3), and ERp29 overexpression enhances endogenous PERK levels. This interaction links ERp29 to regulation of ER stress signaling and chemotherapeutic response. Co-immunoprecipitation, overexpression, clonogenic cell survival assay Biochimica et biophysica acta Medium 21419175
2019 ERp29 is required for tunneling nanotube (TNT) formation by stabilizing MSec protein (TNFAIP2) post-translationally. ERp29 interacts with MSec (interaction requiring bridging proteins), and ERp29 depletion reduces TNT formation while overexpression induces TNTs in an MSec-dependent manner. Affinity purification-mass spectrometry, confocal immunofluorescence, siRNA depletion, overexpression, ER fractionation with limited proteolysis, TNT quantification The Journal of biological chemistry High 30877198
2017 ERp29 interacts with calnexin (CNX), recognizing the P-domain of CNX with a dissociation constant similar to that of ERp57. ERp29 and ERp57 recognize the same domain of CNX but with different modes of interaction. SPR (surface plasmon resonance) binding assays, CNX P-domain mutant analysis Biochemical and biophysical research communications Medium 28456374
2014 ERp29 forms a 1:1 complex with the lectin chaperone calreticulin (CRT), with a dissociation constant similar to the ERp57-CRT interaction, but through a different binding site on CRT. SPR (surface plasmon resonance) binding assays Biochemical and biophysical research communications Medium 25130463
2020 ERp29 mediates dimerization of ER lectin chaperones: ERp29 (itself a dimer) acts as a bridge linking two molecules of calnexin (CNX-CNX dimers) or connecting CNX and calreticulin (CRT) into CNX-CRT complexes. In vitro binding/complex formation assay, SPR Biochemical and biophysical research communications Medium 33360823
2020 ERp29 associates with Proinsulin and with the COPII cargo recognition component Sec24D. Overexpression of ERp29 increases whole-cell Proinsulin levels while ERp29 depletion decreases them, suggesting ERp29 promotes ER exit of Proinsulin via Sec24D/COPII vesicles. Co-immunoprecipitation (ERp29-Proinsulin, ERp29-Sec24D), overexpression and siRNA knockdown with western blot readout PloS one Medium 32433667
2022 ERp29 overexpression in astrocytes infected with murine β-coronavirus (MHV-A59) rescues Cx43 transport to the cell surface, restores gap junctional intercellular communication, and reduces ER stress. Cells expressing exogenous ERp29 were less susceptible to MHV-A59 infection. Exogenous ERp29 expression, confocal imaging of Cx43 localization, gap junction dye transfer assay, viral infection assay, chemical chaperone (4-PBA) treatment The Journal of biological chemistry Medium 36572185
2022 ERp29 expression is upregulated via PKA/SP1 signaling downstream of DPP4 binding to IGF2-R; elevated ERp29 promotes its binding to IP3R2, inhibiting IP3R2 degradation and promoting mitochondria-associated ER membrane (MAM) formation and mitochondrial calcium overload in regulatory T cells. Co-immunoprecipitation (ERp29-IP3R2), siRNA/knockdown experiments, signaling pathway inhibition, in vivo db/db mouse model Metabolism: clinical and experimental Medium 36302455
2023 ERp29 expression is upregulated via DPP4-PAR2-ERK1/2-CEBPB signaling in hippocampal neurons; elevated ERp29 binds IP3R2 and inhibits its degradation, promoting MAM formation and mitochondrial calcium overload contributing to cognitive impairment in diabetic mice. Co-immunoprecipitation (ERp29-IP3R2), DPP4 knockdown/overexpression, pathway inhibitor studies, in vivo mouse model iScience Medium 36936785
2010 ERp29 overexpression upregulates Hsp27 expression through downregulation of eIF2α, and Hsp27 mediates ERp29-conferred resistance to doxorubicin-induced apoptosis in breast cancer cells. Proteomics, western blot, siRNA knockdown of Hsp27, cell viability assay, apoptosis assay Experimental cell research Medium 20833165

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 142 16246730
2010 A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection. Journal of virology 88 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 74 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
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
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 57 24370996
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
2010 Over-expression of ERp29 attenuates doxorubicin-induced cell apoptosis through up-regulation of Hsp27 in breast cancer cells. Experimental cell research 41 20833165
2009 Cytokeratin 19 regulates endoplasmic reticulum stress and inhibits ERp29 expression via p38 MAPK/XBP-1 signaling in breast cancer cells. Experimental cell research 40 19265690
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 38 36302455
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 34 26431474
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
2019 The chaperone ERp29 is required for tunneling nanotube formation by stabilizing MSec. The Journal of biological chemistry 33 30877198
2007 Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions. Molecular biology of the cell 33 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
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
2014 High concentraction of taurocholic acid induced apoptosis in HTR-8/SVneo cells via overexpression of ERp29 and activation of p38. Placenta 25 24780196
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 13 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 9 36936785
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
2018 ERp29 counteracts the suppression of malignancy mediated by endoplasmic reticulum stress and promotes the metastasis of colorectal cancer. Oncology reports 9 30569094
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 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
2024 The role of ERp29/FOS/EMT pathway in excessive apoptosis of placental trophoblast cells in intrahepatic cholestasis of pregnancy. Placenta 1 38346375
2020 [Silencing ERp29 promotes the invasiveness of human PCa cells in vitro: Molecular mechanisms]. Zhonghua nan ke xue = National journal of andrology 1 33377711