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Showing ERLEC1 — XTP3-B is a alias.

ERLEC1

Endoplasmic reticulum lectin 1 · UniProt Q96DZ1

Length
483 aa
Mass
54.9 kDa
Annotated
2026-06-09
42 papers in source corpus 17 papers cited in narrative 17 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ERLEC1 (XTP3-B/Erlectin) is an ER-luminal lectin that functions in ER-associated degradation (ERAD), recognizing misfolded glycoproteins and coupling their surveillance to the membrane ubiquitin ligase machinery (PMID:18264092, PMID:20100910). It is directly recruited into the HRD1-SEL1L ubiquitin ligase scaffold through interaction with the adaptor SEL1L, an association that, together with OS-9 and BiP, builds a large (~27S) ER quality control complex; SEL1L-HRD1 engagement is prerequisite for ERLEC1 incorporation, and its MRH domain is required for SEL1L binding but not for substrate recognition (PMID:18264092, PMID:18502753, PMID:37333389). Substrate engagement is mediated by the C-terminal MRH domain, which recognizes mannose-trimmed high-mannose N-glycans, specifically Man9GlcNAc2, on misfolded glycoproteins such as the alpha1-antitrypsin variant NHK and unassembled CD147; conserved residues including Arg428 and Tyr457 are essential for this glycan-dependent binding (PMID:19917667, PMID:21062743, PMID:23097496, PMID:23356641). ERLEC1 and OS-9 act as partially redundant, interchangeable lectins selectively required for disposal of soluble luminal (ERAD-LS) substrates but dispensable when the same lesions are membrane-tethered (PMID:20100910). ERLEC1 can also engage non-glycosylated substrates through protein-protein interactions and receives substrates handed off from EDEM1 independently of glycan recognition (PMID:23233672, PMID:21917589). Functionally distinct from OS-9, ERLEC1 acts as a negative regulator of ERAD, protecting immature M9-glycan-bearing polypeptides from premature degradation (PMID:23356641), and it stabilizes the adaptor SEL1L against degradation (PMID:33576152). ERLEC1 is transcriptionally induced by ER stress through an ERSE-26 promoter element controlled by XBP1 (PMID:23737521), and its cotranslational ER translocation at the Sec61 translocon is signal-peptide-dependent and blocked by cyclotriazadisulfonamide (PMID:34481949). Rare missense variants in ERLEC1 co-segregate with Class III malocclusion, where the protein inhibits jaw osteoblast proliferation (PMID:32442352).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2006 Medium

    Established ERLEC1 as an ER-luminal MRH-domain lectin capable of glycan-dependent control of glycoprotein trafficking, the founding observation of its function.

    Evidence Proteomic interaction screen, Co-IP with deglycosylation, cell surface transport assay, and Xenopus morpholino knockdown

    PMID:16531414

    Open questions at the time
    • Did not connect ERLEC1 to ERAD or to the HRD1-SEL1L machinery
    • Kremen2 interaction not linked to degradation
  2. 2008 High

    Defined ERLEC1's core role: an ERAD lectin that binds substrate and bridges to the Hrd1 ligase via SEL1L, working in a pathway partially redundant with OS-9.

    Evidence Reciprocal Co-IP, siRNA knockdown, pulse-chase degradation assays; orthogonal sucrose density gradient fractionation defining the ~27S scaffold and isoform requirement

    PMID:18264092 PMID:18502753

    Open questions at the time
    • Glycan specificity of substrate recognition not yet defined
    • Mechanistic basis of redundancy with OS-9 unresolved
  3. 2009 High

    Localized substrate recognition to the C-terminal MRH domain and showed it is glycan-dependent, distinguishing substrate-binding from SEL1L-binding functions.

    Evidence Recombinant Fc-fusion binding to Lec1 cells, EndoH treatment, mannose competition, alanine mutagenesis (Arg428/Tyr457), Co-IP

    PMID:19917667

    Open questions at the time
    • Precise glycan species recognized not yet determined
    • Role of N-terminal MRH domain unexplained
  4. 2010 High

    Defined the substrate class strictly dependent on ERLEC1 and established that mannose trimming is required for substrate handoff to the ligase.

    Evidence siRNA epistasis with defined ERAD-LS/ERAD-LM substrate variants; Co-IP, kifunensine treatment, ERManI/SEL1L knockdown, confocal colocalization

    PMID:20100910 PMID:21062743

    Open questions at the time
    • Structural basis of mannose-trimmed glycan selectivity not resolved
    • Order of factor recruitment along the pathway not fully ordered
  5. 2010 Medium

    Proposed a moonlighting role in hypoxia signaling whereby ERLEC1 sequesters OS-9 to stabilize HIF-1α, linking it to BiP and the UPR.

    Evidence Proteomic approaches, Co-IP, ectopic expression, hypoxia tolerance assays

    PMID:21118962

    Open questions at the time
    • Single-lab overexpression-based; physiological relevance of OS-9 sequestration not independently validated
    • Quantitative competition mechanism not established
  6. 2011 Medium

    Showed substrate delivery to ERLEC1 can bypass glycan recognition via EDEM1 protein-protein interactions, broadening its substrate engagement modes.

    Evidence siRNA knockdown, overexpression, pulse-chase, confocal colocalization, Co-IP with EDEM1 CRD-deletion mutant

    PMID:21917589

    Open questions at the time
    • Direct vs. indirect nature of EDEM1-ERLEC1 transfer not resolved
    • Physiological frequency of glycan-independent handoff unknown
  7. 2012 Medium

    Extended ERLEC1 function to endogenous and non-glycosylated substrates, demonstrating engagement through both lectin and protein-protein interactions.

    Evidence MS substrate identification (CD147), Co-IP, lectin-domain mutagenesis, siRNA depletion, proteasome inhibitor assays; Co-IP/siRNA epistasis for non-glycosylated BiP substrates

    PMID:23097496 PMID:23233672

    Open questions at the time
    • Molecular basis of non-glycosylated substrate recognition undefined
    • Relative contribution of ERLEC1 vs OS-9 for endogenous substrates unclear
  8. 2013 High

    Defined the precise glycan ligand (Man9GlcNAc2) and revealed that ERLEC1 acts as a negative ERAD regulator protecting immature polypeptides, distinguishing it functionally from OS-9; also identified XBP1-driven ER-stress induction.

    Evidence Frontal affinity chromatography, Co-IP, siRNA, pulse-chase, lectin mutagenesis; luciferase reporter and XBP1 knockdown/overexpression with multiple ER stressors

    PMID:23356641 PMID:23737521

    Open questions at the time
    • Mechanism by which ERLEC1 protects vs. targets substrates not structurally explained
    • Switch between protective and degradative modes not defined
  9. 2021 Medium

    Identified ERLEC1 as a stabilizer of SEL1L and a determinant of cytosolic aggregation behavior, and showed its biogenesis is controlled at the Sec61 translocon.

    Evidence Proteasome inhibitor assays, Co-IP, GFP-aggregation reporters, OS-9/XTP3-B siRNA; SILAC-MS, Western blot, flow cytometry, and cell-free translation/translocation assay with CADA

    PMID:33576152 PMID:34481949

    Open questions at the time
    • Mechanism of SEL1L stabilization not biochemically defined
    • Functional consequence of CADA-mediated ERLEC1 depletion in vivo unknown
  10. 2023 Medium

    Confirmed SEL1L-HRD1 engagement as prerequisite for ERLEC1 recruitment into the functional ERAD complex and validated ERLEC1's ERAD role for misfolded ZAAT in vivo.

    Evidence SEL1L/HRD1 interactome screens, Co-IP, knockin mouse SEL1L variant (preprint); CRISPR erlec1 zebrafish knockout with transcriptomic/proteomic analysis

    PMID:36768797 PMID:37333389

    Open questions at the time
    • bioRxiv preprint not peer-reviewed for the recruitment hierarchy
    • Mechanistic link between ERAD defect and cholesterol pathway suppression unclear
  11. 2020 Medium

    Linked ERLEC1 to a human craniofacial phenotype, implicating it in osteoblast proliferation control.

    Evidence Exome/Sanger co-segregation of missense variants with Class III malocclusion; osteoblast expression and wild-type vs mutant proliferation/differentiation assays

    PMID:32442352

    Open questions at the time
    • Mechanistic connection between ERAD lectin function and osteoblast proliferation undefined
    • Causality of variants not established beyond co-segregation

Open questions

Synthesis pass · forward-looking unresolved questions
  • How ERLEC1 toggles between protecting immature glycoproteins and committing substrates to degradation, and how this is structurally coordinated within the HRD1-SEL1L complex, remains unresolved.
  • No structure of ERLEC1 within the assembled HRD1-SEL1L complex
  • Molecular switch between protective and degradative modes unknown
  • Physiological substrate repertoire incompletely mapped

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Localization
GO:0005783 endoplasmic reticulum 2
Pathway
R-HSA-392499 Metabolism of proteins 3 R-HSA-8953897 Cellular responses to stimuli 1
Partners
BIPDERLINEDEM1HRD1KREMEN2OS-9SEL1LUBE2J1
Complex memberships
HRD1-SEL1L ERAD complex

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2008 XTP3-B/ERLEC1 is an ER-resident glycoprotein that binds to ERAD substrates and, through the SEL1L adaptor, to the ER-membrane-embedded ubiquitin ligase Hrd1. Its MRH domain is required for interaction with SEL1L but not with substrate. XTP3-B and OS-9 form components of distinct, partially redundant quality control surveillance pathways coordinating protein folding with membrane dislocation and ubiquitin conjugation. Co-immunoprecipitation, siRNA knockdown, pulse-chase degradation assays Nature cell biology High 18264092
2008 The long isoform of human XTP3-B (hXTP3-B) associates with the HRD1-SEL1L membrane-anchored ubiquitin ligase complex and BiP, forming a ~27S ER quality control scaffold complex. The short isoform is excluded from scaffold formation. hOS-9 is also incorporated into this large complex. hXTP3-B long isoform inhibits ERAD of NHK (null Hong Kong alpha1-antitrypsin variant), including a non-glycosylated version (NHK-QQQ), while the short isoform has almost no effect. Immunoprecipitation, sucrose density gradient centrifugation fractionation, siRNA knockdown, pulse-chase degradation assays The Journal of biological chemistry High 18502753
2009 XTP3-B binds to the ERAD substrate alpha1-antitrypsin variant NHK (but not wild-type AT) specifically via its C-terminal MRH domain in a glycan-dependent manner. Mutation of Arg428 or Tyr457 in the C-terminal MRH domain abolishes glycan binding. The N-terminal MRH domain is dispensable for substrate binding. Recombinant Fc-fusion protein binding assays to Lec1 cells, EndoH treatment, competitive inhibition with mannose oligosaccharides, alanine mutagenesis, co-immunoprecipitation Glycobiology High 19917667
2010 Disposal of soluble ERAD-LS substrates (nontransmembrane polypeptides with luminal lesions) is strictly dependent on XTP3-B (and OS-9) acting as interchangeable ERAD lectins along with HRD1 and SEL1L. These ERAD factors become dispensable when the same polypeptides are membrane-tethered (ERAD-LM substrates), revealing a mammalian-specific distinction from yeast. siRNA knockdown, pulse-chase degradation assays, genetic epistasis with defined substrate variants The Journal of cell biology High 20100910
2010 Mannose trimming is required for substrate association with XTP3-B and with E3 ubiquitin ligases HRD1 and SCF(Fbs2). Inhibition of mannose trimming (kifunensine or ERManI knockdown) prevents substrate colocalization with HRD1 and Fbs2 at the ERQC but not with EDEM1. Substrate association with XTP3-B remained dependent on mannose trimming even upon SEL1L knockdown, suggesting XTP3-B recognizes mannose-trimmed glycans for late ERAD steps. Co-immunoprecipitation, mannosidase inhibitor (kifunensine) treatment, siRNA knockdown of ERManI and SEL1L, confocal colocalization The Journal of biological chemistry Medium 21062743
2012 XTP3-B interacts with unassembled core-glycosylated CD147 (an endogenous ERAD substrate), and this interaction is inhibited by mutations to conserved residues in the XTP3-B lectin domain. XTP3-B participates along with OS-9 in the OS-9/SEL1L/Hrd1 ERAD pathway for an endogenous constitutive substrate. Mass spectrometry identification, Co-immunoprecipitation, lectin domain mutagenesis, siRNA depletion, proteasome inhibitor assays Molecular biology of the cell Medium 23097496
2013 The C-terminal MRH domain of XTP3-B specifically recognizes Man9GlcNAc2 (M9) glycans in vitro and on the ERAD substrate NHK in vivo. Endogenous XTP3-B is a component of the HRD1-SEL1L complex via direct interaction with SEL1L. Lectin activity is required for NHK binding but not for SEL1L association. Unlike OS-9, XTP3-B inhibits ERAD of NHK bearing M9 oligosaccharides, acting as a negative regulator of ERAD and protecting newly synthesized immature polypeptides from premature degradation. Frontal affinity chromatography (FAC), co-immunoprecipitation, siRNA knockdown, pulse-chase degradation assays, lectin-domain mutagenesis The FEBS journal High 23356641
2012 Nonglycosylated BiP substrates (NS-1κ light chain and truncated Igγ heavy chain) interact with XTP3-B and OS-9, and require EDEM1 for degradation, revealing that XTP3-B can engage non-glycosylated ERAD substrates through protein-protein interactions, sharing the ERAD pathway with glycoproteins. Co-immunoprecipitation, siRNA knockdown, pulse-chase degradation assays The Journal of biological chemistry Medium 23233672
2006 Erlectin (XTP3-B/ERLEC1) is an ER luminal resident protein with two MRH domains. It interacts with the Wnt co-receptor Kremen2 (Krm2) via one MRH domain in a glycan-dependent manner (interaction abolished by Krm2 deglycosylation). Erlectin overexpression inhibits transport of Krm2 to the cell surface. Morpholino knockdown in Xenopus causes head and axial defects, placing Erlectin in ER glycoprotein trafficking regulation. Proteomic interaction screen, co-immunoprecipitation, deglycosylation assay, cell surface transport assay, Xenopus morpholino knockdown The Journal of biological chemistry Medium 16531414
2010 ERLEC1/CIM sequesters OS-9 away from the HIF-1α complex and PHD2, thereby preventing HIF-1α degradation and permitting HIF-1α accumulation under hypoxic conditions. ERLEC1 also modulates the unfolded protein response through interaction with the key ER stress protein BiP, influencing cell proliferation under ER stress. Proteomic approaches, co-immunoprecipitation, ectopic expression, hypoxia tolerance assays Cancer research Medium 21118962
2013 ERLEC1 expression is transcriptionally upregulated by ER stress via a novel ERSE-26 element (CCAAT-N26-CCACG) in its promoter, regulated by XBP1 but not ATF6α. XBP1 overexpression increased and siRNA knockdown of XBP1 reduced ERLEC1 mRNA levels. Luciferase reporter assays, ER stressor treatment (brefeldin A, tunicamycin, thapsigargin), siRNA knockdown of XBP1, mRNA quantification The Journal of biological chemistry Medium 23737521
2021 XTP3-B/ERLEC1 stabilizes SEL1L by inhibiting its degradation. When proteasome activity is inhibited, SEL1L generates degradation intermediates that interact with aggregation-prone proteins including polyglutamine-expanded Huntingtin (Htt-polyQ-GFP), stimulating their cytosolic aggregation. Proteasome inhibitor assays, co-immunoprecipitation, GFP-tagged aggregation reporters, siRNA knockdown of OS-9 and XTP3-B The FEBS journal Medium 33576152
2021 ERLEC1 is identified as a substrate for the ER translocation inhibitor cyclotriazadisulfonamide (CADA). CADA inhibits ERLEC1 protein expression in a signal peptide-dependent manner. Cell-free in vitro translation/translocation assays confirmed that ERLEC1's signal peptide is a target for CADA-mediated cotranslational translocation inhibition at the Sec61 translocon. Quantitative proteomics (SILAC-MS), Western blot, flow cytometry, cell-free in vitro translation/translocation assay Molecular & cellular proteomics Medium 34481949
2023 SEL1L recruits ERLEC1 (along with OS9, UBE2J1, and DERLIN) to HRD1 to form a functional HRD1 ERAD complex. Attenuation of the SEL1L-HRD1 interaction (via a SEL1L variant) impairs recruitment of ERLEC1 to HRD1, demonstrating that SEL1L-HRD1 interaction is prerequisite for ERLEC1 incorporation into the functional ERAD complex. Proteomic interactome screens of SEL1L and HRD1, co-immunoprecipitation, knockin mouse model with SEL1L variant bioRxivpreprint Medium 37333389
2023 Mutation of erlec1 in zebrafish results in further suppression of the cholesterol biosynthesis pathway in the context of misfolded Z-variant alpha1-antitrypsin (ZAAT) expression, confirming a role for this ER lectin in targeting misfolded ZAAT for ER-associated degradation (ERAD). CRISPR/Cas9 erlec1 knockout in zebrafish, transcriptomic and proteomic analysis International journal of molecular sciences Medium 36768797
2011 EDEM1 overexpression or its up-regulation by IRE1 can deliver ERAD substrates to XTP3-B and OS9 even when mannose trimming is bypassed. An EDEM1 deletion mutant lacking most of the carbohydrate-recognition domain still accelerates ERAD by delivering substrate to XTP3-B, suggesting that substrate delivery from EDEM1 to XTP3-B can occur through protein-protein interactions independent of glycan recognition. siRNA knockdown, overexpression, pulse-chase degradation assays, confocal colocalization, co-immunoprecipitation Molecular biology of the cell Medium 21917589
2020 Rare missense variants in ERLEC1 (including p.His413Tyr, p.Thr140Ser, p.Thr140Ile, p.Asn483Ser) co-segregate with Class III malocclusion. ERLEC1 is highly expressed in mouse jaw osteoblasts and inhibits osteoblast proliferation; the His413Tyr variant significantly enhanced this inhibitory effect on osteoblast proliferation. Proper ERLEC1 expression level is required for correct osteogenic differentiation. Exome sequencing, Sanger sequencing co-segregation, ERLEC1 expression analysis in osteoblasts, overexpression of wild-type vs. mutant ERLEC1 with cell proliferation and differentiation assays Human mutation Medium 32442352

Source papers

Stage 0 corpus · 42 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
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
2008 Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP. The Journal of biological chemistry 161 18502753
2010 Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates. The Journal of cell biology 148 20100910
2012 Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate. Molecular biology of the cell 78 23097496
2010 Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation. Molecular cell 67 21172656
2010 The role of MRH domain-containing lectins in ERAD. Glycobiology 53 20118070
2011 Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1. Molecular biology of the cell 52 21917589
2010 Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps. The Journal of biological chemistry 50 21062743
2012 A shared endoplasmic reticulum-associated degradation pathway involving the EDEM1 protein for glycosylated and nonglycosylated proteins. The Journal of biological chemistry 45 23233672
2013 Identification of a novel endoplasmic reticulum stress response element regulated by XBP1. The Journal of biological chemistry 40 23737521
2022 Human alpha cell transcriptomic signatures of types 1 and 2 diabetes highlight disease-specific dysfunction pathways. iScience 39 36134336
2022 Circulating Proteins Influencing Psychiatric Disease: A Mendelian Randomization Study. Biological psychiatry 39 36280454
2009 Human XTP3-B binds to alpha1-antitrypsin variant null(Hong Kong) via the C-terminal MRH domain in a glycan-dependent manner. Glycobiology 35 19917667
2006 The MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition. The Journal of biological chemistry 30 16531414
2013 Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant. The FEBS journal 28 23356641
2011 Mannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway. Biochimica et biophysica acta 28 21723917
2018 Abnormal expression of ER quality control and ER associated degradation proteins in the dorsolateral prefrontal cortex in schizophrenia. Schizophrenia research 26 29496332
2015 Glucosidase II and MRH-domain containing proteins in the secretory pathway. Current protein & peptide science 25 25692846
2010 Novel metastasis-related gene CIM functions in the regulation of multiple cellular stress-response pathways. Cancer research 24 21118962
2014 EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog. PloS one 23 24910992
2016 Classification of Cholestatic and Necrotic Hepatotoxicants Using Transcriptomics on Human Precision-Cut Liver Slices. Chemical research in toxicology 21 26881866
2014 Lectin OS-9 delivers mutant neuroserpin to endoplasmic reticulum associated degradation in familial encephalopathy with neuroserpin inclusion bodies. Neurobiology of aging 21 24795221
2017 Identification of FBXL4 as a Metastasis Associated Gene in Prostate Cancer. Scientific reports 18 28698647
2021 A Proteomic Study on the Membrane Protein Fraction of T Cells Confirms High Substrate Selectivity for the ER Translocation Inhibitor Cyclotriazadisulfonamide. Molecular & cellular proteomics : MCP 14 34481949
2008 Sweet bays of ERAD. Trends in biochemical sciences 12 18538572
2023 Molecular mechanism and diagnostic marker investigation of endoplasmic reticulum stress on periodontitis. BMC oral health 11 36894919
2015 Promotion of Endoplasmic Reticulum-Associated Degradation of Procathepsin D by Human Herpesvirus 8-Encoded Viral Interleukin-6. Journal of virology 11 26018151
2022 Reduced DNAJC3 Expression Affects Protein Translocation across the ER Membrane and Attenuates the Down-Modulating Effect of the Translocation Inhibitor Cyclotriazadisulfonamide. International journal of molecular sciences 10 35054769
2024 Gut microbiota and interstitial cystitis: exploring the gut-bladder axis through mendelian randomization, biological annotation and bulk RNA sequencing. Frontiers in immunology 9 39399486
2018 Genome-wide based model predicting recovery from portosystemic shunting after liver shunt attenuation in dogs. Journal of veterinary internal medicine 8 29770973
2015 Early postnatal feed restriction reduces liver connective tissue levels and affects H3K9 acetylation state of regulated genes associated with protein metabolism in low birth weight pigs. The Journal of nutritional biochemistry 7 26895664
2020 Identification of pathogenic variants of ERLEC1 in individuals with Class III malocclusion by exome sequencing. Human mutation 6 32442352
2025 Genetic overlap between schizophrenia and constipation: insights from a genome-wide association study in a European population. Annals of general psychiatry 4 40033405
2021 SEL1L degradation intermediates stimulate cytosolic aggregation of polyglutamine-expanded protein. The FEBS journal 4 33576152
2010 Mannose 6-phosphate receptor homology domain-containing lectins in mammalian endoplasmic reticulum-associated degradation. Methods in enzymology 4 20816211
2024 Identification of novel drug targets for osteoarthritis by integrating genetics and proteomes from blood. Journal of orthopaedic surgery and research 2 39261869
2023 Expression of the Z Variant of α1-Antitrypsin Suppresses Hepatic Cholesterol Biosynthesis in Transgenic Zebrafish. International journal of molecular sciences 2 36768797
2023 SEL1L-HRD1 interaction is prerequisite for the formation of a functional HRD1 ERAD complex. bioRxiv : the preprint server for biology 2 37333389
2023 The Distant Molecular Effects on the Brain by Cancer Treatment. Brain sciences 2 38248237
2026 Proteomic Profiling of Endometrial Cancer Tissues Reveals Differential Expression of Proteomes in Obese Versus Non-Obese Patients. Cells 1 41892289
2024 Mendelian Randomization Estimates the Effects of Plasma and Cerebrospinal Fluid Proteins on Intelligence, Fluid Intelligence Score, and Cognitive Performance. Molecular neurobiology 1 39495227

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