The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
UBAC2 (UBA domain–containing protein 2; UniProt Q8NBM4; synonym PHGDHL1) encodes an ER-resident, rhomboid-like multi-pass membrane pseudoprotein with a cytosolic ubiquitin-associated (UBA) domain that has been historically linked to ER-associated degradation (ERAD) and ubiquitin-dependent protein quality control (proteostasis). (adrain2020thecomplexlife pages 15-18, kandel2020theroleof pages 10-14, lemberg2016inactiverhomboidproteins pages 16-21, choi2019lmbr1lregulateslymphopoiesis pages 1-2)
A major 2024 advance is the discovery that UBAC2 also functions as a selective autophagy receptor for ER-phagy (reticulophagy): it binds GABARAP via a cytosolic LC3-interacting region (LIR) and is activated by MARK2 phosphorylation at S223, which promotes UBAC2 dimerization and increased GABARAP binding. This UBAC2-driven ER-phagy restrains ER stress/UPR-linked inflammation and protects against DSS-induced colitis in vivo. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 12-13, he2024erphagyrestrainsinflammatory pages 15-16, he2024erphagyrestrainsinflammatory pages 7-8)
“Rhomboid-like” proteins share a rhomboid fold (typically multiple transmembrane helices) but may lack protease activity; such proteins are often termed rhomboid pseudoproteases and can act as adapters/scaffolds that regulate client protein trafficking, turnover, and signaling rather than catalyzing proteolysis. Reviews place UBAC2 within this class and connect rhomboid-like factors to ER protein quality control. (lemberg2016inactiverhomboidproteins pages 16-21, adrain2020thecomplexlife pages 1-5)
UBA (ubiquitin-associated) domains are small protein modules that can bind ubiquitin or polyubiquitin chains and thereby link proteins to ubiquitin signaling and degradation pathways. Reviews specifically describe UBAC2 as having a conserved C-terminal UBA domain that binds polyubiquitin chains, consistent with an adapter role in ubiquitin-dependent quality control. (kandel2020theroleof pages 10-14, lemberg2016inactiverhomboidproteins pages 16-21)
ERAD is a canonical ER quality-control process in which misfolded or orphaned ER proteins are recognized, ubiquitinated, extracted (often via the p97/VCP machinery), and degraded by the proteasome. Reviews place UBAC2 within ERAD-related networks (including the GP78 pathway) and highlight its interactions with UBXD8/p97 axis components relevant to substrate processing. (adrain2020thecomplexlife pages 15-18, kandel2020theroleof pages 10-14, lemberg2016inactiverhomboidproteins pages 16-21)
ER-phagy is selective autophagic degradation of ER fragments. ER-phagy receptors often contain a LIR motif that binds ATG8-family proteins (e.g., GABARAP/LC3) to couple ER membranes to autophagosomes. In 2024, UBAC2 was shown to be such a receptor via its cytosolic LIR and GABARAP binding. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 12-13, he2024erphagyrestrainsinflammatory pages 7-8)
The literature sources retrieved here consistently describe human UBAC2 as “ubiquitin-associated domain–containing protein 2,” and genetic studies explicitly note that PHGDHL1 is alternatively called UBAC2, supporting the UniProt synonym set and mitigating symbol ambiguity. (nan2011genomewideassociationstudy pages 1-2, hou2012replicationstudyconfirms pages 1-2)
Multiple sources place UBAC2 at the endoplasmic reticulum (ER).
A 2024 EMBO Journal study provides direct mechanistic evidence that UBAC2 is an ER-phagy receptor.
Core mechanism
* UBAC2 contains a canonical LIR in its cytosolic domain that binds GABARAP. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 12-13)
* Under ER stress or autophagy activation, MARK2 phosphorylates UBAC2 at S223, promoting UBAC2 dimerization and stronger GABARAP binding, thereby enhancing ER-phagy. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 12-13)
Experimental readouts and quantitative design features
* ER-phagy flux was monitored with an ER luminal reporter ss-RFP-GFP-KDEL, in which lysosomal delivery quenches GFP and yields an RFP fragment; UBAC2 knockout reduces reporter processing under starvation conditions, while UBAC2 WT rescues and a LIR mutant (LIRm) fails to rescue. (he2024erphagyrestrainsinflammatory pages 7-8)
* Quantification in microscopy includes 20 cells scored/condition and statistics reported across 3 biological replicates (mean ± SEM). (he2024erphagyrestrainsinflammatory pages 12-13)
Physiological/in vivo implications
* In a DSS acute ulcerative colitis mouse model, AAV-mediated expression of UBAC2 variants (WT vs LIRm vs S223A and disease-associated variants) was tested with n = 6 mice/group and multiple outcome measures including body weight, colon length, histology, and qPCR markers of ER stress and inflammation. (he2024erphagyrestrainsinflammatory pages 15-16)
* The study concludes that UBAC2-mediated ER-phagy restrains inflammatory responses and protects against colitis pathology. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 15-16)
Figure-level support
Cropped panels of Figure 3 directly show: the ER-phagy reporter concept and quantification; rescue by UBAC2 WT but not LIRm; immunoblot readouts under starvation; and UBAC2–GABARAP co-immunoprecipitation. (he2024erphagyrestrainsinflammatory media 2051f18f, he2024erphagyrestrainsinflammatory media 4a49bd3c, he2024erphagyrestrainsinflammatory media 87f2e417, he2024erphagyrestrainsinflammatory media a2146745)
Prior to 2024, UBAC2’s best-supported mechanistic placement was in ER-associated ubiquitin-dependent quality control.
The central 2024 discovery is that UBAC2 is a regulated ER-phagy receptor, with an explicit upstream kinase (MARK2) and a defined regulatory site (S223 phosphorylation) that modulates receptor activity through dimerization and strengthened GABARAP binding. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 12-13)
A 2023 Cold Spring Harbor Perspectives in Biology review summarizes the roles of rhomboid superfamily members in ER protein quality control and includes UBAC2 within this proteostasis context, providing a recent synthesis that anticipates why a rhomboid-like ER membrane factor may integrate multiple quality-control outputs (e.g., ubiquitin pathways and autophagy). (OpenTargets Search: -UBAC2)
Because UBAC2-driven ER-phagy restrains ER stress/UPR-linked inflammation and mitigates colitis phenotypes in vivo (DSS model), the UBAC2–MARK2–GABARAP axis provides a mechanistically grounded target pathway for therapeutic exploration in inflammatory disease contexts where ER stress contributes to pathology. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 15-16)
The LMBR1L–GP78–UBAC2 complex was proposed as a second “brake” on Wnt signaling in lymphocytes by promoting ER-localized ubiquitination and degradation of Wnt receptors and β-catenin, suggesting a potential lever for contexts where Wnt signaling needs to be constrained. (choi2019lmbr1lregulateslymphopoiesis pages 1-2)
UBAC2 is implicated as a susceptibility locus across several diseases by genetics and aggregated evidence.
Across authoritative reviews, UBAC2 is repeatedly positioned as an ER membrane rhomboid-like factor with a ubiquitin-binding UBA module that participates in ER quality control, including ERAD-linked networks and lipid-droplet related trafficking (via UBXD8). (adrain2020thecomplexlife pages 15-18, kandel2020theroleof pages 10-14, lemberg2016inactiverhomboidproteins pages 16-21)
The 2024 identification of UBAC2 as an ER-phagy receptor provides a coherent functional extension: UBAC2 appears capable of routing ER components to both proteasome-associated and autophagy-associated disposal pathways depending on stress context and regulatory state (e.g., MARK2 phosphorylation), consistent with modern views that ER proteostasis involves coordinated and partially redundant degradation systems. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 12-13)
Genetic associations at the UBAC2/PHGDHL1 locus (e.g., skin cancer GWAS) establish medical relevance but do not alone demonstrate UBAC2 as the causal gene or define causal mechanisms; mechanistic interpretation should primarily rely on direct experiments such as the 2019 Science and 2024 EMBO Journal studies. (nan2011genomewideassociationstudy pages 1-2, choi2019lmbr1lregulateslymphopoiesis pages 1-2, he2024erphagyrestrainsinflammatory pages 1-2)
In a two-stage study totaling 477 BD cases and 1,334 controls, UBAC2 showed replicated association, including (selected examples):
For basal cell carcinoma (BCC), rs7335046 near UBAC2 showed combined OR 1.26 (95% CI 1.18–1.34) with P = 2.9 × 10^-8 (genome-wide significant) in a discovery + replication GWAS design. (nan2011genomewideassociationstudy pages 1-2)
The EMBO Journal 2024 study reports multiple statistically significant effects of UBAC2 perturbation/mutants on ER-phagy and inflammation-linked phenotypes, including comparisons with p < 0.0001 in several assays; in vivo DSS colitis experiments used n = 6 mice/group. (he2024erphagyrestrainsinflammatory pages 15-16, he2024erphagyrestrainsinflammatory pages 7-8)
| Year | Citation (first author journal) | URL | Evidence type (primary/review/database) | Key findings relevant to UBAC2 (function/pathway/localization/domains) | Key quantitative/statistical data (p-values, ORs, n) | Notes/limitations |
|---|---|---|---|---|---|---|
| 2024 | He, EMBO Journal | https://doi.org/10.1038/s44318-024-00232-z | Primary | Identifies human UBAC2 as an ER-resident ER-phagy receptor. UBAC2 contains a cytoplasmic canonical LIR that binds GABARAP; MARK2 phosphorylates UBAC2 at S223, promoting dimerization and stronger GABARAP binding. UBAC2-mediated ER-phagy restrains UPR/inflammatory signaling and protects against DSS colitis. UBAC2 also undergoes autophagic turnover during ER stress/starvation. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 12-13, he2024erphagyrestrainsinflammatory pages 15-16, he2024erphagyrestrainsinflammatory pages 7-8, he2024erphagyrestrainsinflammatory pages 14-15, he2024erphagyrestrainsinflammatory pages 3-4) | HeLa ER-phagy reporter quantified across 3 biological replicates; 20 cells scored/condition in microscopy analyses; DSS colitis experiments used n=6 mice/group; multiple comparisons reported including p<0.0001, p=0.0100, p=0.0071, p=0.0012, p=0.0080. (he2024erphagyrestrainsinflammatory pages 12-13, he2024erphagyrestrainsinflammatory pages 15-16, he2024erphagyrestrainsinflammatory pages 7-8, he2024erphagyrestrainsinflammatory pages 3-4) | Strongest recent mechanistic study; extends UBAC2 function beyond ERAD into selective autophagy. Context excerpts do not provide all effect sizes/fold changes. |
| 2019 | Choi, Science | https://doi.org/10.1126/science.aau0812 | Primary | Places UBAC2 in an ER-localized LMBR1L-GP78-UBAC2 complex that promotes ubiquitin-mediated degradation of FZD6/LRP6 and helps limit Wnt/β-catenin signaling in lymphocytes. Supports ER quality-control/ERAD-like function and ER localization. (choi2019lmbr1lregulateslymphopoiesis pages 1-2) | Paper reports impaired lymphoid development/function in mutant mice and restoration experiments involving β-catenin knockout, but quantitative values were not present in the available excerpt. (choi2019lmbr1lregulateslymphopoiesis pages 1-2) | Direct primary evidence for pathway-specific UBAC2 function, but excerpt does not state membrane topology or UBA-domain position. |
| 2023 | Bhaduri, Cold Spring Harbor Perspectives in Biology | https://doi.org/10.1101/cshperspect.a041248 | Review | Reviews rhomboid superfamily roles in ER protein quality control and includes UBAC2 among rhomboid-like proteins linked to ERAD/proteostasis. Helps place UBAC2 in current ER quality-control framework. (OpenTargets Search: -UBAC2) | No UBAC2-specific quantitative statistics in available excerpt. | High-authority recent review; useful for current conceptual understanding, but mostly secondary synthesis rather than direct UBAC2 experiments. |
| 2020 | Adrain, FEBS Journal | https://doi.org/10.1111/febs.15548 | Review | Describes UBAC2 as an ER-localized rhomboid pseudoprotease with a conserved C-terminal UBA domain; links UBAC2 to UBXD8, GP78-ERAD, delivery of substrates to GP78, and LMBR1L-GP78-UBAC2-mediated Wnt regulation. Notes Derlin-like behavior and unresolved physiology. (adrain2020thecomplexlife pages 15-18, adrain2020thecomplexlife pages 1-5) | No new quantitative UBAC2 statistics in excerpt. | Strong synthesis of mechanistic literature; some claims are review-level interpretations and precise physiological roles remain incompletely established. |
| 2020 | Kandel, BBA Mol Cell Res | https://doi.org/10.1016/j.bbamcr.2020.118793 | Review | Summarizes UBAC2 as a rhomboid-like multi-pass membrane protein with a C-terminal UBA domain that binds polyubiquitin; UBAC2 knockdown stabilizes mutant α1-antitrypsin (an ERAD substrate) and UBAC2 restricts UBXD8 trafficking from ER to lipid droplets, linking proteostasis to lipid homeostasis. (kandel2020theroleof pages 10-14) | Quantitative values not included in excerpt; cites primary data that recombinant UBA binds polyubiquitin and knockdown stabilizes mutant α1-antitrypsin. (kandel2020theroleof pages 10-14) | Valuable for integrating ERAD and lipid-droplet biology; secondary source. |
| 2016 | Lemberg, Seminars in Cell & Developmental Biology | https://doi.org/10.1016/j.semcdb.2016.06.022 | Review | Classifies UBAC2 as a rhomboid-family pseudoprotease predicted to bind ubiquitin via a conserved cytoplasmic C-terminal UBA domain; places it in the ERAD network with gp78 and identifies UBAC2 as an ER tether for UBXD8, affecting lipid-droplet trafficking and triglyceride turnover. (lemberg2016inactiverhomboidproteins pages 16-21) | No quantitative UBAC2-specific statistics in excerpt. | Foundational review; older and predates ER-phagy findings. |
| 2013 | Olzmann, Cold Spring Harbor Perspectives in Biology | https://doi.org/10.1101/cshperspect.a013185 | Review | Early authoritative ERAD review explicitly mentions UBAC2 as a recently identified UBA-domain-containing, rhomboid-like factor in mammalian ERAD, helping establish the historical basis for UBAC2’s ER quality-control annotation. (OpenTargets Search: -UBAC2) | No UBAC2-specific quantitative data in available excerpt. | Important historical context, but limited UBAC2 detail in excerpt. |
| 2012 | Hou, Arthritis Research & Therapy | https://doi.org/10.1186/ar3789 | Primary genetics/functional | Validates UBAC2 as a Behçet’s disease susceptibility locus in Han Chinese. Promoter SNP rs3825427 risk T allele reduces promoter activity and lowers UBAC2 transcript variant 1 in PBMCs/skin; variant 1 is decreased in BD, while variant 2 is increased in BD skin. (hou2012replicationstudyconfirms pages 4-5, hou2012replicationstudyconfirms pages 5-6, hou2012replicationstudyconfirms pages 1-2, hou2012replicationstudyconfirms pages 2-4, hou2012replicationstudyconfirms pages 6-7) | Two-stage study totaling 477 BD patients and 1,334 controls; rs9513584 Pc=0.018, OR=1.4; rs3825427 combined Pc=6.9×10^-6, OR=1.5; rs9517668 combined Pc=3.3×10^-4, OR=1.4; rs9517701 combined Pc=2.9×10^-5, OR=1.4; rs3825427 promoter assay P=0.002; transcript variant 1 genotype-expression P=0.045 and P=0.025; BD vs control expression P=0.025 and P=0.047; variant 2 in BD skin P=0.004. (hou2012replicationstudyconfirms pages 4-5, hou2012replicationstudyconfirms pages 5-6, hou2012replicationstudyconfirms pages 1-2, hou2012replicationstudyconfirms pages 2-4) | Strong disease-association and functional-regulatory evidence, but does not define biochemical mechanism of UBAC2 protein action. |
| 2011 | Nan, Human Molecular Genetics | https://doi.org/10.1093/hmg/ddr287 | Primary genetics | GWAS implicates the UBAC2/PHGDHL1 region in skin cancer susceptibility, supporting medical relevance of the locus. (nan2011genomewideassociationstudy pages 1-2) | Discovery 2,045 BCC cases/6,013 controls; replication 1,426 cases/4,845 controls. rs7335046 near UBAC2: BCC OR 1.26 (95% CI 1.18–1.34), P=2.9×10^-8; SCC OR 1.21 (95% CI 1.02–1.44), P=0.03; rs12210050[T] SCC OR 1.35 (95% CI 1.16–1.57), P=7.6×10^-5. (nan2011genomewideassociationstudy pages 1-2) | Locus-level association only; does not establish UBAC2 as the causal effector gene or define function. |
| Current | Open Targets Platform | https://platform.opentargets.org/target/ENSG00000134882 | Database | Aggregates disease-target associations for UBAC2, including asthma, childhood-onset asthma, psoriasis, actinic keratosis, and hypothyroidism, useful for prioritizing translational hypotheses. (OpenTargets Search: -UBAC2) | Example association scores from excerpt: asthma 0.4426; hypothyroidism 0.3475; actinic keratosis 0.3268; psoriasis 0.3055; childhood-onset asthma 0.3054; 5 literature-linked evidences per listed disease. (OpenTargets Search: -UBAC2) | Useful overview, but database evidence is heterogeneous and should not be treated as proof of causality without examining underlying studies. |
Table: This table summarizes the main evidence base for human UBAC2 (Q8NBM4), highlighting the 2024 ER-phagy discovery paper, the 2019 Wnt/ERAD study, key reviews, and disease-genetics sources. It is useful for quickly separating direct mechanistic evidence from review synthesis and locus-level association data.
The best-supported “primary function” assignment for human UBAC2 has shifted from being primarily an ERAD-associated adapter in ubiquitin-dependent quality control to a broader role as a regulated ER-phagy receptor that connects ER stress to selective autophagy and inflammatory restraint. Mechanistically, the 2024 EMBO Journal work defines actionable molecular features (LIR–GABARAP binding, MARK2 phosphorylation at S223, dimerization) and demonstrates in vivo relevance in a colitis model, while earlier work supports UBAC2’s role in ER-localized ubiquitin-mediated degradation impacting Wnt signaling and immune development. (he2024erphagyrestrainsinflammatory pages 1-2, he2024erphagyrestrainsinflammatory pages 12-13, he2024erphagyrestrainsinflammatory pages 15-16, choi2019lmbr1lregulateslymphopoiesis pages 1-2)
References
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(choi2019lmbr1lregulateslymphopoiesis pages 1-2): Jin Huk Choi, Xue Zhong, William McAlpine, Tzu-Chieh Liao, Duanwu Zhang, Beibei Fang, Jamie Russell, Sara Ludwig, Evan Nair-Gill, Zhao Zhang, Kuan-wen Wang, Takuma Misawa, Xiaoming Zhan, Mihwa Choi, Tao Wang, Xiaohong Li, Miao Tang, Qihua Sun, Liyang Yu, Anne R. Murray, Eva Marie Y. Moresco, and Bruce Beutler. Lmbr1l regulates lymphopoiesis through wnt/β-catenin signaling. May 2019. URL: https://doi.org/10.1126/science.aau0812, doi:10.1126/science.aau0812. This article has 66 citations and is from a highest quality peer-reviewed journal.
(he2024erphagyrestrainsinflammatory pages 1-2): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
(he2024erphagyrestrainsinflammatory pages 12-13): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
(he2024erphagyrestrainsinflammatory pages 15-16): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
(he2024erphagyrestrainsinflammatory pages 7-8): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
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(nan2011genomewideassociationstudy pages 1-2): Hongmei Nan, Mousheng Xu, Peter Kraft, Abrar A. Qureshi, Constance Chen, Qun Guo, Frank B. Hu, Gary Curhan, Christopher I. Amos, Li-E. Wang, Jeffrey E. Lee, Qingyi Wei, David J. Hunter, and Jiali Han. Genome-wide association study identifies novel alleles associated with risk of cutaneous basal cell carcinoma and squamous cell carcinoma. Human Molecular Genetics, 20:3718-3724, Jun 2011. URL: https://doi.org/10.1093/hmg/ddr287, doi:10.1093/hmg/ddr287. This article has 127 citations and is from a domain leading peer-reviewed journal.
(hou2012replicationstudyconfirms pages 1-2): Shengping Hou, Qinmeng Shu, Zhengxuan Jiang, Yuanyuan Chen, Fuzhen Li, Feilan Chen, Aize Kijlstra, and Peizeng Yang. Replication study confirms the association between ubac2 and behçet's disease in two independent chinese sets of patients and controls. Arthritis Research & Therapy, 14:R70-R70, Mar 2012. URL: https://doi.org/10.1186/ar3789, doi:10.1186/ar3789. This article has 50 citations and is from a domain leading peer-reviewed journal.
(he2024erphagyrestrainsinflammatory pages 3-4): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
(he2024erphagyrestrainsinflammatory media 2051f18f): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
(he2024erphagyrestrainsinflammatory media 4a49bd3c): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
(he2024erphagyrestrainsinflammatory media 87f2e417): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
(he2024erphagyrestrainsinflammatory media a2146745): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
(OpenTargets Search: -UBAC2): Open Targets Query (-UBAC2, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(hou2012replicationstudyconfirms pages 4-5): Shengping Hou, Qinmeng Shu, Zhengxuan Jiang, Yuanyuan Chen, Fuzhen Li, Feilan Chen, Aize Kijlstra, and Peizeng Yang. Replication study confirms the association between ubac2 and behçet's disease in two independent chinese sets of patients and controls. Arthritis Research & Therapy, 14:R70-R70, Mar 2012. URL: https://doi.org/10.1186/ar3789, doi:10.1186/ar3789. This article has 50 citations and is from a domain leading peer-reviewed journal.
(hou2012replicationstudyconfirms pages 5-6): Shengping Hou, Qinmeng Shu, Zhengxuan Jiang, Yuanyuan Chen, Fuzhen Li, Feilan Chen, Aize Kijlstra, and Peizeng Yang. Replication study confirms the association between ubac2 and behçet's disease in two independent chinese sets of patients and controls. Arthritis Research & Therapy, 14:R70-R70, Mar 2012. URL: https://doi.org/10.1186/ar3789, doi:10.1186/ar3789. This article has 50 citations and is from a domain leading peer-reviewed journal.
(he2024erphagyrestrainsinflammatory pages 14-15): Xing He, Haowei He, Zitong Hou, Zheyu Wang, Qinglin Shi, Tao Zhou, Yaoxing Wu, Yunfei Qin, Jun Wang, Zhe Cai, Jun Cui, and Shouheng Jin. Er-phagy restrains inflammatory responses through its receptor ubac2. The EMBO Journal, 43:5057-5084, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00232-z, doi:10.1038/s44318-024-00232-z. This article has 13 citations.
(hou2012replicationstudyconfirms pages 2-4): Shengping Hou, Qinmeng Shu, Zhengxuan Jiang, Yuanyuan Chen, Fuzhen Li, Feilan Chen, Aize Kijlstra, and Peizeng Yang. Replication study confirms the association between ubac2 and behçet's disease in two independent chinese sets of patients and controls. Arthritis Research & Therapy, 14:R70-R70, Mar 2012. URL: https://doi.org/10.1186/ar3789, doi:10.1186/ar3789. This article has 50 citations and is from a domain leading peer-reviewed journal.
(hou2012replicationstudyconfirms pages 6-7): Shengping Hou, Qinmeng Shu, Zhengxuan Jiang, Yuanyuan Chen, Fuzhen Li, Feilan Chen, Aize Kijlstra, and Peizeng Yang. Replication study confirms the association between ubac2 and behçet's disease in two independent chinese sets of patients and controls. Arthritis Research & Therapy, 14:R70-R70, Mar 2012. URL: https://doi.org/10.1186/ar3789, doi:10.1186/ar3789. This article has 50 citations and is from a domain leading peer-reviewed journal.