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Showing OS9 — OS-9 is a alias.

OS9

Protein OS-9 · UniProt Q13438

Length
667 aa
Mass
75.6 kDa
Annotated
2026-06-10
33 papers in source corpus 23 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

OS9 is an ER-luminal lectin that triages misfolded glycoproteins for endoplasmic-reticulum-associated degradation (ERAD) by recognizing mannose-trimmed N-glycans and delivering substrates to the membrane ubiquitin ligase machinery (PMID:18264092, PMID:19346256). Its mannose-6-phosphate-receptor-homology (MRH) domain binds high-mannose glycans bearing terminal alpha1,6-linked mannose on the trimmed C-arm (Man7 isomers), and this lectin activity is required for OS9 to promote degradation of glycosylated substrates such as the alpha1-antitrypsin NHK variant (PMID:19346256, PMID:19914915); crystallography defined a P-type lectin fold with a distinctive double-tryptophan site recognizing Manalpha1,6Manalpha1,6Man residues (PMID:21172656). OS9 bridges captured substrates to the HRD1 E3 ligase through the SEL1L adaptor, with the MRH domain required for SEL1L binding (PMID:18264092), and cryo-EM of the OS9-SEL1L-HRD1 core complex shows SEL1L and OS9 forming a claw-like luminal substrate-engagement module above a membrane HRD1 dimer that translocates substrate (PMID:41593065, PMID:40661598). Degradation of soluble ERAD-L substrates strictly requires HRD1, SEL1L, and the interchangeable lectins OS9 and XTP3B, whereas membrane-tethered substrates bypass this requirement, defining OS9 as a pathway-selective luminal recognition factor (PMID:20100910); OS9 and XTP3B act redundantly to promote glycoprotein degradation and stabilize the SEL1L/HRD1 dislocon, and their expression ratio tunes triage fidelity, with OS9 antagonizing XTP3B-mediated inhibition of non-glycosylated substrate degradation (PMID:29706535). OS9 is induced by ER stress through the IRE1/XBP1 pathway and selectively retains and disposes of folding-defective conformers (PMID:18417469), and is required for ubiquitination of glycosylated ERAD substrates (PMID:19084021). Beyond canonical glycan-dependent ERAD, OS9 also recognizes certain misfolded substrates through the polypeptide backbone in an MRH-independent manner, as shown for NKCC2 and sonic hedgehog (PMID:26721884, PMID:24910992). OS9 is required for ERAD of mutant neuroserpin in a cell and mouse model of familial encephalopathy with neuroserpin inclusion bodies (FENIB) (PMID:24795221).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2002 Medium

    Established OS-9 as an ER-membrane-associated protein that transiently engages a client (meprin beta) during early secretory transport, providing the first localization and interaction context.

    Evidence Yeast two-hybrid, co-IP, subcellular fractionation, and pulse-chase in mammalian cells

    PMID:12093806

    Open questions at the time
    • Topology assigned as cytoplasm-exposed, later revised to luminal
    • No link to ERAD machinery yet
  2. 2005 Medium

    Proposed a cytoplasmic role linking OS-9 to HIF-1alpha hydroxylation and degradation, raising the question of whether OS-9 acts outside the ER lumen.

    Evidence Co-IP, RNAi, reporter and HIF stability assays

    PMID:15721254

    Open questions at the time
    • Topologically incompatible with later luminal localization data
    • Directly contradicted by subsequent study
  3. 2008 High

    Defined OS-9 as the core ERAD lectin-adaptor by showing it binds misfolded substrates and bridges them, via SEL1L, to the HRD1 E3 ligase, with the MRH domain required for SEL1L (but not substrate) binding.

    Evidence Reciprocal Co-IP, RNAi functional ERAD assays, MRH domain mutagenesis

    PMID:18264092

    Open questions at the time
    • Glycan ligand of MRH domain not yet defined
    • Structural basis of complex assembly unknown
  4. 2008 Medium

    Connected OS-9 to the unfolded protein response and partitioned its function into retention of misfolded conformers and promotion of their disposal, while flagging an unproductive association with non-glycosylated clients.

    Evidence Co-IP, RNAi, pulse-chase, secretion assays, XBP1 induction

    PMID:18417469

    Open questions at the time
    • Mechanistic basis for productive vs unproductive binding unresolved
    • Single lab
  5. 2008 Medium

    Showed OS-9 is required for ubiquitination specifically of glycosylated ERAD substrates, localizing its functional requirement to the N-glycan signal.

    Evidence RNAi, ubiquitination assays, Co-IP

    PMID:19084021

    Open questions at the time
    • Did not define which glycan species are recognized
    • Single lab
  6. 2009 High

    Resolved the molecular recognition signal by demonstrating the MRH domain binds trimmed-C-arm Man7 glycans (terminal alpha1,6-mannose), and that this lectin activity is required for ERAD of glycosylated substrates in vivo.

    Evidence Frontal affinity chromatography with defined glycan panels, MRH mutagenesis, in-cell Co-IP, in vivo ERAD assays

    PMID:19346256 PMID:19914915

    Open questions at the time
    • Atomic basis of glycan selectivity not yet structurally defined
  7. 2010 High

    Defined the structural basis of glycan recognition, revealing a P-type lectin fold with a double-tryptophan binding site engaging Manalpha1,6Manalpha1,6Man on the trimmed C-arm.

    Evidence X-ray crystallography with mannopentaose, NMR, biochemical binding

    PMID:21172656

    Open questions at the time
    • Did not show how MRH-bound substrate is handed to SEL1L/HRD1
  8. 2010 High

    Established pathway selectivity by showing OS-9/XTP3-B (with HRD1 and SEL1L) are strictly required only for soluble ERAD-L substrates and dispensable when substrates are membrane-tethered.

    Evidence RNAi epistasis with soluble vs membrane-tethered substrates, pulse-chase

    PMID:20100910

    Open questions at the time
    • Functional division between OS-9 and XTP3-B not yet defined
  9. 2011 Medium

    Refuted the cytoplasmic HIF model by establishing OS-9 as a luminal ER protein incapable of in vivo interaction with cytoplasmic PHD2, consolidating its role within the ER lumen.

    Evidence Subcellular fractionation, glycosylation assays, FRET, lentiviral knockdown

    PMID:21559462

    Open questions at the time
    • Cannot exclude indirect effects on HIF in some contexts
    • Single lab
  10. 2014 Medium

    Broadened OS-9's substrate repertoire and showed glycan-independent recognition modes, including disease-mutant neuroserpin (FENIB) ERAD and backbone-based recognition of sonic hedgehog and a GRP94-specific lysosomal turnover route.

    Evidence Co-IP, RNAi, glycosylation-site mutagenesis, pulse-chase, mouse FENIB model, lysosome inhibitor studies

    PMID:24795221 PMID:24899641 PMID:24910992 PMID:25193139

    Open questions at the time
    • How OS-9 discriminates glycan vs polypeptide signals unresolved
    • GRP94 lysosomal route mechanism unclear
  11. 2015 Medium

    Demonstrated MRH-independent, N-glycan-dependent recognition of immature NKCC2, showing OS-9 can target substrates through glycan signals not read by its MRH domain.

    Evidence Yeast two-hybrid, Co-IP, immunocytochemistry, chase assays, MRH and glycosylation-site mutagenesis

    PMID:26721884

    Open questions at the time
    • The MRH-independent recognition determinant not identified
    • Single lab
  12. 2018 High

    Defined the functional relationship between the two lectins, showing OS9 and XTP3B redundantly promote glycoprotein degradation, stabilize the SEL1L/HRD1 dislocon, and that their expression ratio tunes triage fidelity with OS9 antagonizing XTP3B repression of non-glycosylated substrate disposal.

    Evidence CRISPR homozygous deletions, quantitative ERAD assays, SEL1L/HRD1 complex Co-IP, double-KO epistasis

    PMID:29706535

    Open questions at the time
    • Structural basis of dislocon stabilization not resolved here
    • Physiological substrates governed by the ratio not enumerated
  13. 2025 High

    Provided the architectural basis of ERAD by resolving the OS9-SEL1L-HRD1 core complex, showing a luminal claw-like SEL1L-OS9 substrate-engagement module over a membrane HRD1 dimer, and validating a pathogenic SEL1L-OS9 interface mutation that impairs ERAD.

    Evidence Cryo-EM, site-directed mutagenesis, crosslinking, ERAD functional assays

    PMID:40661598 PMID:41593065

    Open questions at the time
    • Dynamics of substrate handoff from MRH to HRD1 not captured
    • How non-glycosylated substrates are accommodated structurally unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How OS9 mechanistically reconciles glycan-dependent (MRH-mediated) and glycan-independent/polypeptide-based substrate recognition, and how the OS9:XTP3B ratio is physiologically regulated, remain open.
  • No unified model of dual recognition modes
  • Regulation of lectin expression ratio in tissues unknown
  • Structural account of backbone-based recognition lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008289 lipid binding 3 GO:0060090 molecular adaptor activity 2
Localization
GO:0005783 endoplasmic reticulum 4
Pathway
R-HSA-392499 Metabolism of proteins 3 R-HSA-8953897 Cellular responses to stimuli 1
Partners
CASRGRP94HRD1MEPRIN BETANKCC2SEL1LTRPV4XTP3B
Complex memberships
HRD1-SEL1L ERAD dislocon complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2008 OS-9 is an ER-resident glycoprotein that binds to ERAD substrates (including mutant alpha1-antitrypsin) and, through the SEL1L adaptor, to the ER-membrane-embedded E3 ubiquitin ligase HRD1. The MRH domain of OS-9 is required for interaction with SEL1L but not with substrate. OS-9 also associates with the ER chaperone GRP94, and both HRD1 and SEL1L are required for degradation of mutant alpha1-antitrypsin. Co-immunoprecipitation, RNAi knockdown, functional ERAD degradation assays, domain mutagenesis (MRH domain) Nature cell biology High 18264092
2005 OS-9 interacts with both HIF-1alpha and HIF-1alpha prolyl hydroxylases (PHDs). OS-9 gain-of-function promotes HIF-1alpha hydroxylation, VHL binding, proteasomal degradation of HIF-1alpha, and inhibition of HIF-1-mediated transcription. OS-9 loss-of-function via RNAi increases HIF-1alpha protein levels and HIF-1-mediated transcription under non-hypoxic conditions. Co-immunoprecipitation, RNAi knockdown, reporter assays, HIF-1alpha stability assays Molecular cell Medium 15721254
2011 A subsequent study contradicting OS-9/PHD interaction: OS-9 is a luminal ER protein (confirmed by subcellular fractionation and glycosylation tests) while PHD2 is cytoplasmic; FRET analysis showed no significant in vivo physical interaction between PHD2 and OS-9. Neither overexpression nor lentiviral knockdown of OS-9 affected HIF regulation. Subcellular fractionation, glycosylation assay, co-immunoprecipitation, FRET, lentiviral knockdown PloS one Medium 21559462
2009 The MRH domain of human OS-9 specifically binds N-glycans lacking the terminal mannose from the C branch (i.e., Man7 isomers with trimmed C-arm alpha1,2-mannose) as demonstrated by frontal affinity chromatography. This lectin activity is required for OS-9 to promote ERAD of the glycosylated substrate NHK in vivo. Frontal affinity chromatography with recombinant MRH domain, siRNA knockdown, overexpression of mannosidases, in vivo ERAD assays The Journal of biological chemistry High 19346256
2010 Crystal structure of the human OS-9 MRH domain complexed with alpha3,alpha6-mannopentaose reveals a flattened beta-barrel structure with P-type lectin fold and distinctive double tryptophan (WW) residues in the oligosaccharide-binding site that recognize Manalpha1,6Manalpha1,6Man residues on the processed C-arm of high-mannose glycans. X-ray crystallography, NMR spectroscopy, biochemical binding assays Molecular cell High 21172656
2010 Disposal of soluble ERAD-L substrates (ERAD-LS) is strictly dependent on HRD1, SEL1L, and the two interchangeable lectins OS-9 and XTP3-B. Tethering the same substrates to the membrane (ERAD-LM) renders these ERAD factors dispensable, demonstrating that OS-9/XTP3-B function is pathway-selective. RNAi knockdown, pulse-chase degradation assays, genetic epistasis using membrane-tethered vs. soluble substrates The Journal of cell biology High 20100910
2008 OS-9.1 and OS-9.2 (alternative splice variants) are transcriptionally induced by the IRE1/XBP1 ER-stress pathway. OS-9 variants selectively bind folding-defective proteins but not folding-competent ones, thereby inhibiting secretion of misfolded conformers (retention function) and promoting their ERAD (disposal function). OS-9 also transiently associates with non-glycosylated misfolded proteins but this association is unproductive for ERAD. Co-immunoprecipitation, RNAi knockdown, pulse-chase assays, secretion assays, XBP1 reporter/induction The Journal of biological chemistry Medium 18417469
2008 OS-9 is upregulated by ER stress and is required for efficient ubiquitination of glycosylated ERAD substrates (demonstrated by RNAi). OS-9 also binds a misfolded non-glycosylated ERAD substrate but is not required for its ubiquitination or degradation, indicating that OS-9's functional requirement is N-glycan-dependent. RNAi knockdown, ubiquitination assays, co-immunoprecipitation, Western blot Journal of molecular biology Medium 19084021
2007 OS-9 interacts with the cytosolic N-terminal tail of TRPV4 via co-immunoprecipitation. OS-9 preferentially binds TRPV4 monomers and immature ER-localized forms, impedes TRPV4 release from the ER, reduces TRPV4 at the plasma membrane, and attenuates polyubiquitination of TRPV4 subunits, suggesting a role as an auxiliary maturation factor protecting against premature ERAD. Co-immunoprecipitation, knockdown, cell-surface biotinylation, in vivo zebrafish expression, polyubiquitination assays The Journal of biological chemistry Medium 17932042
2018 Using homozygous deletion cell lines, OS9 and XTP3B were found to redundantly promote glycoprotein degradation and stabilize the SEL1L/HRD1 dislocon complex. OS9 antagonizes XTP3B-mediated inhibition of non-glycosylated protein degradation. The relative expression ratio of OS9 and XTP3B determines the fidelity of glycoprotein triage in the ER. CRISPR/Cas9 homozygous deletions, quantitative ERAD assays, co-immunoprecipitation of SEL1L/HRD1 complex, genetic epistasis Molecular cell High 29706535
2015 OS9 interacts specifically with the immature form of the renal Na-K-2Cl co-transporter NKCC2 (identified by yeast two-hybrid and confirmed by co-IP), co-localizes with NKCC2 in the ER, and promotes proteasomal degradation of immature NKCC2. Inactivation of the OS9 MRH domain does not affect this activity, but mutation of NKCC2 N-glycosylation sites abolishes OS9-induced degradation, indicating N-glycan-dependent but MRH-independent recognition. Yeast two-hybrid, co-immunoprecipitation, immunocytochemistry, pulse-chase and cycloheximide-chase assays, siRNA knockdown, MRH domain mutagenesis, glycosylation site mutagenesis The Journal of biological chemistry Medium 26721884
2014 OS-9 facilitates turnover of hyperglycosylated (nonnative) GRP94 via a lysosomal-like, ERAD-independent mechanism. OS-9 binds preferentially to a subpopulation of GRP94 that is hyperglycosylated on cryptic N-linked acceptor sites, and these GRP94 forms have nonnative conformations and are less active. GRP94 is not required for OS-9 folding and does not collaborate with OS-9 in ERAD of misfolded substrates. Co-immunoprecipitation, pulse-chase assays, glycosylation analysis, lysosome inhibitor experiments, RNAi Molecular biology of the cell Medium 24899641
2014 The C-terminal domain of mammalian OS-9 contains mammalian-specific inserts that are intrinsically disordered and specifically recognized by the middle and C-terminal domains of GRP94. Glycosylation of full-length GRP94 is essential for OS-9 binding, but this requirement is relieved by deletion of the GRP94 N-terminal domain, indicating an allosteric rather than direct glycan-mediated interaction. Domain mapping by co-immunoprecipitation, deletion mutagenesis, biochemical binding assays Journal of molecular biology Medium 25193139
2014 OS-9 (but not XTP3-B) is required for ERAD of mutant neuroserpin in familial encephalopathy with neuroserpin inclusion bodies. OS-9 binds mutant neuroserpin via glycan recognition; removal of glycosylation sites increases neuroserpin protein load, while OS-9 overexpression decreases it. This was validated in both cell culture and a murine FENIB model. Co-immunoprecipitation, RNAi, overexpression, glycosylation site mutagenesis, mouse model analysis Neurobiology of aging Medium 24795221
2014 OS-9 is required for ERAD of both glycosylated and non-glycosylated sonic hedgehog (SHH). OS-9 robustly interacts with a non-glycosylated SHH variant (N278A), indicating that the misfolded polypeptide backbone rather than a glycan signature can serve as the predominant recognition signal for OS-9 in certain substrates. RNAi knockdown, co-immunoprecipitation, pulse-chase ERAD assays, glycosylation mutant analysis PloS one Medium 24910992
2002 OS-9 interacts specifically with the cytoplasmic intracellular region of the membrane proteinase meprin beta. OS-9 is associated with ER membranes and exposed to the cytoplasm. OS-9 associates transiently with meprin beta coinciding with ER-to-Golgi transport of meprin beta. Only the non-spliced form of OS-9 binds meprin beta, implicating the alternatively spliced segment in binding specificity. Yeast two-hybrid, co-immunoprecipitation, subcellular fractionation, deletion mutagenesis, pulse-chase assays The Journal of biological chemistry Medium 12093806
2009 The OS-9 MRH domain binds N-glycans containing terminal alpha1,6-linked mannose in the Manalpha1,6(Manalpha1,3)Manalpha1,6(Manalpha1,3)Man structure (Ka ~10^4 M^-1), as determined by frontal affinity chromatography with 92 oligosaccharides. Trimming of either an alpha1,6-linked mannose from the C-arm or an alpha1,3-linked mannose from the B-arm abolishes OS-9 MRH binding. The alpha1-antitrypsin NHK variant (but not wild-type) interacts with OS-9 in cells in a sugar-dependent manner. Frontal affinity chromatography (92 glycan panel), tetramer binding assay, site-directed mutagenesis of MRH residues, co-immunoprecipitation Glycobiology High 19914915
2008 OS9 physically interacts with DC-STAMP and both proteins co-localize in the ER. Upon TLR-induced DC maturation, DC-STAMP translocates from the ER to the Golgi while OS9 localization is unchanged. The DC-STAMP/OS9 interaction is involved in this ER-to-Golgi translocation process. Yeast two-hybrid, co-immunoprecipitation, confocal co-localization, TLR stimulation experiments in CHO cells and dendritic cells Molecular immunology Low 18952287
1999 OS-9 interacts with N-copine (a two-C2-domain protein) via the second C2 domain of N-copine and the carboxy-terminal region of OS-9. This interaction is Ca2+-dependent as shown by in vitro binding assays and co-immunoprecipitation. Yeast two-hybrid, co-immunoprecipitation, in vitro Ca2+-dependent binding assay FEBS letters Low 10403379
2016 Meprin beta (but not meprin A) cleaves OS-9 in vitro and in vivo during ischemia/reperfusion-induced renal injury. Fragmentation of OS-9 by meprin beta was observed in WT mice subjected to IR but not in meprin αβKO mice. Transfection with meprin beta cDNA prevented accumulation of OS-9 under hypoxia mimic conditions. In vitro protease assay with purified proteins, meprin knockout mouse model, IR injury model, Western blot, cell transfection International journal of nephrology Medium 27478637
2017 OS-9 interacts with the immature form of the calcium-sensing receptor (CaSR) in the ER (identified by yeast two-hybrid and co-IP). OS-9 binding to CaSR requires the MRH domain. Two distinct binding interactions were identified: one involving both C-terminal domains and another involving both N-terminal domains of OS-9 and CaSR. However, OS-9 knockdown or overexpression did not significantly affect CaSR cell surface expression or CaSR-mediated ERK1/2 phosphorylation (negative functional result). Yeast two-hybrid, co-immunoprecipitation, confocal co-localization, MRH domain mutagenesis, siRNA knockdown, ERK phosphorylation assay Journal of cellular physiology Low 28419469
2025 Cryo-EM structure of the core mammalian ERAD complex comprising OS9, SEL1L, and HRD1 reveals a dimeric assembly where SEL1L and OS9 form a claw-like configuration in the ER lumen for substrate engagement while HRD1 dimerizes in the membrane for substrate translocation. Pathogenic SEL1L mutations at the SEL1L-OS9 interface (Gly585Asp) disrupt complex formation and impair ERAD activity, validated by mutagenesis and crosslinking assays. Cryo-EM structure determination, site-directed mutagenesis, crosslinking assays, ERAD functional assays Nature communications High 40661598 41593065

Source papers

Stage 0 corpus · 33 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2008 OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nature cell biology 420 18264092
2005 OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha. Molecular cell 193 15721254
2009 Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. The Journal of biological chemistry 167 19346256
2010 Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates. The Journal of cell biology 148 20100910
2008 A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal. The Journal of biological chemistry 102 18417469
2014 A novel long non-coding RNA ENST00000480739 suppresses tumour cell invasion by regulating OS-9 and HIF-1α in pancreatic ductal adenocarcinoma. British journal of cancer 96 25314054
2010 Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation. Molecular cell 67 21172656
2007 OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum. The Journal of biological chemistry 65 17932042
2016 Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9. Histochemistry and cell biology 63 27803995
2008 Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins. Journal of molecular biology 52 19084021
2009 The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation. Glycobiology 51 19914915
1996 Complete sequence analysis of a gene (OS-9) ubiquitously expressed in human tissues and amplified in sarcomas. Molecular carcinogenesis 48 8634085
2018 Redundant and Antagonistic Roles of XTP3B and OS9 in Decoding Glycan and Non-glycan Degrons in ER-Associated Degradation. Molecular cell 45 29706535
2002 A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta. The Journal of biological chemistry 38 12093806
1998 Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines. Journal of biochemistry 36 9562620
2015 OS9 Protein Interacts with Na-K-2Cl Co-transporter (NKCC2) and Targets Its Immature Form for the Endoplasmic Reticulum-associated Degradation Pathway. The Journal of biological chemistry 30 26721884
2014 OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation. Molecular biology of the cell 30 24899641
1999 Ca2(+)-dependent interaction of N-copine, a member of the two C2 domain protein family, with OS-9, the product of a gene frequently amplified in osteosarcoma. FEBS letters 24 10403379
2014 EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog. PloS one 23 24910992
2008 OS9 interacts with DC-STAMP and modulates its intracellular localization in response to TLR ligation. Molecular immunology 22 18952287
2014 Lectin OS-9 delivers mutant neuroserpin to endoplasmic reticulum associated degradation in familial encephalopathy with neuroserpin inclusion bodies. Neurobiology of aging 21 24795221
1994 OS9: a novel olfactory gene of Drosophila expressed in two olfactory organs. Journal of neurobiology 17 8021646
2014 Interaction of structural core protein of classical swine fever virus with endoplasmic reticulum-associated degradation pathway protein OS9. Virology 16 25010283
2014 Characterization of the Grp94/OS-9 chaperone-lectin complex. Journal of molecular biology 13 25193139
2015 A Novel Role of OS-9 in the Maintenance of Intestinal Barrier Function from Hypoxia-induced Injury via p38-dependent Pathway. International journal of biological sciences 12 25999789
1997 Genomic organization of the OS-9 gene amplified in human sarcomas. Journal of biochemistry 12 9498564
2011 The function of hypoxia-inducible factor (HIF) is independent of the endoplasmic reticulum protein OS-9. PloS one 10 21559462
2005 OS-9: another piece in the HIF complex story. Molecular cell 7 15721249
2017 The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor. Journal of cellular physiology 6 28419469
2025 Structural basis and pathological implications of the dimeric OS9-SEL1L-HRD1 ERAD Core Complex. bioRxiv : the preprint server for biology 3 40661598
2016 Hypoxia Associated Proteolytic Processing of OS-9 by the Metalloproteinase Meprin β. International journal of nephrology 3 27478637
2026 Structural basis and pathological implications of the dimeric OS9-SEL1L-HRD1 ERAD Core Complex. Nature communications 2 41593065
2009 [The cooperation of OS-9 and PHDs in hypoxia-induced pulmonary hypertension of rats]. Zhongguo ying yong sheng li xue za zhi = Zhongguo yingyong shenglixue zazhi = Chinese journal of applied physiology 0 21186601

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