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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Target confirmed: the UniProt accession Q12907 corresponds to human LMAN2, encoding Vesicular integral-membrane protein VIP36 (VIP36/GP36b), a type I transmembrane L-type (legume-like) lectin in the early secretory pathway. This report summarizes experimentally supported function, localization, binding specificity, and recent (2023–2024 prioritized) disease/proteomics associations.
LMAN2/VIP36 is part of the animal L-type lectin family, defined by a luminal carbohydrate recognition domain (CRD) structurally homologous to plant legume lectins and specialized for high-mannose N-glycan recognition in luminal secretory compartments. L-type lectins in animals are frequently membrane-anchored and implicated in protein sorting/trafficking and glycoprotein quality control rather than extracellular lectin functions. (gupta2012ltypelectinsin pages 1-2, yamamoto2014intracellularlectinsare pages 8-10)
VIP36 is a type I transmembrane protein with an N-terminal signal peptide, a luminal lectin CRD, a single-pass transmembrane helix, and a short cytosolic tail. Review-level summaries describe L-type cargo lectins (ERGIC-53/LMAN1 and VIP36/LMAN2) as having: (i) an N-terminal L-type lectin domain, (ii) a proline-rich/stalk region, and (iii) a region near the membrane involved in Ca2+ coordination in family members. (gupta2012ltypelectinsin pages 2-3, veronika2010theroleof pages 22-25)
VIP36 localizes primarily to Golgi / pre-Golgi (ERGIC) compartments and exhibits cycling within the early secretory pathway. It has been described in cis/medial Golgi, ERGIC, and transport vesicles; under some contexts it can be detected in post-Golgi compartments and at the plasma membrane in polarized epithelial cells. This distribution is consistent with a role as a sorting receptor that binds luminal glycans in one compartment and releases them in another (e.g., driven by pH differences). (gupta2012ltypelectinsin pages 12-13, veronika2010theroleof pages 25-28)
The primary experimentally supported biochemical function of VIP36 is binding to high-mannose N-glycans, particularly glycan determinants enriched early in the secretory pathway.
Specificity: VIP36 preferentially recognizes Man7–Man9GlcNAc2 and shows strong preference for isomers containing the D1/A-arm Manα1-2–Manα1-2–Man motif; trimming or masking terminal α1,2-mannose residues abolishes binding in biochemical assays. (gupta2012ltypelectinsin pages 13-15, veronika2010theroleof pages 25-28, yamamoto2014intracellularlectinsare pages 10-11)
Environmental dependence: binding is pH sensitive, with optimal binding reported around pH ~6–6.5, aligning with early Golgi/ERGIC conditions and supporting a compartment-dependent binding/release model. (gupta2012ltypelectinsin pages 12-13, veronika2010theroleof pages 25-28, yamamoto2014intracellularlectinsare pages 10-11)
Ca2+ dependence: structural work indicates VIP36 binds one Ca2+ adjacent to the carbohydrate-binding site, supporting Ca2+-dependent ligand coordination, although some biochemical reports describe partial Ca2+ independence under certain assay conditions, indicating that Ca2+ dependence may be context- and/or method-dependent. (gupta2012ltypelectinsin pages 13-15, veronika2010theroleof pages 25-28, gupta2012ltypelectinsin pages 12-13)
High-resolution structural summaries indicate that Ca2+ positions and/or stabilizes the binding geometry such that Asp131, Asn166, and His190 form key direct contacts with the ligand, with additional residues (e.g., Gly260, Asp261, Leu262) contributing hydrogen bonds to mannose. These details provide a mechanistic basis for the D1/A-arm preference. (gupta2012ltypelectinsin pages 13-15, veronika2010theroleof pages 25-28)
VIP36 is widely framed as an intracellular cargo receptor/sorting lectin that recognizes high-mannose glycans and participates in Golgi/early secretory sorting. A prominent model is that VIP36 can bind glycoproteins that retain immature high-mannose glycans (e.g., that escaped earlier processing) and help recycle them for further glycan maturation, consistent with a quality-control role in glycosylation state. (gupta2012ltypelectinsin pages 2-3, gupta2012ltypelectinsin pages 12-13)
VIP36 is described as predominantly Golgi/ERGIC-localized and cycling between compartments of the early secretory pathway. Quantitative FRAP measurements reported in one compiled experimental account indicate approximate half-times of ER→Golgi t1/2 ~105 ± 39 min and Golgi→ER t1/2 ~1.67 ± 0.45 min, consistent with relatively rapid retrograde movement. (veronika2010theroleof pages 25-28)
In polarized epithelial contexts, VIP36 has been reported at the plasma membrane with an apical/basolateral ratio ~7, consistent with proposed roles in polarized trafficking/sorting. (gupta2012ltypelectinsin pages 12-13)
The cytosolic sorting logic of VIP36 is not as consistently described across sources as for ERGIC-53/LMAN1. One review describes VIP36 as lacking a canonical dilysine ER-localization motif and being mainly Golgi-localized (in contrast to ERGIC-53). (yamamoto2014intracellularlectinsare pages 8-10) In contrast, another compiled account proposes a C-terminal KRXX retrieval-like signal and reports rapid retrograde cycling consistent with COPI-mediated retrieval. (veronika2010theroleof pages 25-28) A third source discusses a short C-terminal motif (KRFY) associated with cycling in the VIP36/VIPL family, while VIPL has additional determinants for ER retention. (gupta2012ltypelectinsin pages 15-16)
Interpretation: overall evidence supports that VIP36 cycles and that its luminal lectin activity is tuned to Golgi/ERGIC conditions; however, the exact cytosolic motif logic (KRXX vs other motifs; whether “no dilysine” applies universally) is not fully reconciled within the retrieved evidence and likely depends on isoform/context and/or historical annotation differences. (veronika2010theroleof pages 25-28, yamamoto2014intracellularlectinsare pages 8-10, gupta2012ltypelectinsin pages 15-16)
Quantitative protein terminomics identified VIP36/LMAN2 as a metalloprotease-regulated shedding substrate with a reproducible cleavage site at F298↓L299 (reported as SVNF↓LKSP) detected across multiple cell lines, and downregulated by the broad-spectrum metalloprotease inhibitor BB-94. (tsumagari2021exploringthelandscape pages 6-8, tsumagari2021exploringthelandscape pages 8-11, tsumagari2021exploringthelandscape pages 11-12)
The cropped figure/table evidence documenting the cleavage site and inhibitor-dependent reduction is available here. (tsumagari2021exploringthelandscape media 6d3163dc, tsumagari2021exploringthelandscape media ed8c04ed, tsumagari2021exploringthelandscape media a19a5e2b)
Implication: VIP36 can generate a soluble ectodomain fragment under metalloprotease activity, offering a mechanistic basis for detecting VIP36-derived peptides/fragments in extracellular compartments and suggesting regulated remodeling of its lectin function at membranes. (tsumagari2021exploringthelandscape pages 8-11, tsumagari2021exploringthelandscape pages 11-12)
A 2024 proteome-wide association study (PWAS) integrating plasma proteomics (SOMAmer) with GWAS datasets identified LMAN2 among proteins associated with chronic kidney disease (CKD) and replicated signals in related traits (eGFR and BUN). The study used ARIC proteomics with n=7,213 European-ancestry participants and followed PWAS with Mendelian randomization (MR) and colocalization.
MR results reported: association strongest for BUN (OR 1.032, FDR 5.85×10−3); MR evidence for CKD was marginal (OR 1.283, FDR 5.63×10−2) and not significant for eGFR (OR 0.989, FDR 0.141). Colocalization did not support a shared causal cis-variant for LMAN2 with CKD/eGFR/BUN (PP4 < 0.01), weakening causal interpretation and indicating that LMAN2 is currently better viewed as an associated marker/candidate pathway component rather than a confirmed causal effector. (xiong2024plasmaproteomeanalysis pages 1-2, xiong2024plasmaproteomeanalysis pages 7-9)
Publication details: Xiong et al., Heliyon, Jun 2024. URL: https://doi.org/10.1016/j.heliyon.2024.e31704. (xiong2024plasmaproteomeanalysis pages 1-2)
In a 2023 study of cultured human granulosa cells treated with 30 µM cannabidiol (CBD) for 24 h (n=5 biological replicates), LMAN2 (VIP36) was reported as differentially abundant with log2 fold-change = 1.23 and q = 0.04. While this does not define mechanism, it places LMAN2 among regulated proteins under conditions that induced inflammatory/secretory changes in granulosa cells. (eubler2023trpv2anovel pages 9-10)
Publication details: Eubler et al., Molecular Human Reproduction, Aug 2023. URL: https://doi.org/10.1093/molehr/gaad029. (eubler2023trpv2anovel pages 9-10)
Authoritative syntheses emphasize that VIP36’s pH-dependent and high-mannose-specific recognition is well matched to the chemistry of early Golgi/ERGIC glycan maturation and positions VIP36 as a glycan-state sensor that can influence forward trafficking vs retrieval/recycling decisions for glycoproteins. (gupta2012ltypelectinsin pages 12-13, yamamoto2014intracellularlectinsare pages 8-10, yamamoto2014intracellularlectinsare pages 10-11)
Given the PWAS/MR associations, LMAN2 is being discussed as a candidate plasma protein marker linked to CKD-related traits; however, the limited colocalization support indicates caution in interpreting LMAN2 as a drug target without further causal validation. (xiong2024plasmaproteomeanalysis pages 1-2, xiong2024plasmaproteomeanalysis pages 7-9)
Because VIP36 undergoes metalloprotease-sensitive ectodomain shedding at a specific site (F298↓L299), assays targeting shed ectodomain fragments could, in principle, serve as readouts of membrane protease activity and/or secretory-pathway remodeling, though clinical utility remains to be established. (tsumagari2021exploringthelandscape pages 6-8, tsumagari2021exploringthelandscape pages 8-11, tsumagari2021exploringthelandscape media 6d3163dc)
A ClinicalTrials.gov-style search performed in this run returned no clearly relevant interventional clinical trials targeting LMAN2/VIP36 specifically. (clinical-trials search result context in pqac tool state; no citeable trial context was returned)
The most coherent pathway placement for VIP36 is within secretory-pathway cargo selection and glycoprotein quality control, coupling N-glycan processing state (high mannose vs processed complex glycans) to sorting and recycling in ERGIC/cis-Golgi/TGN trafficking routes. The pH-tuned binding profile (maximal near mildly acidic Golgi conditions) provides a plausible biophysical switch for ligand engagement and release across compartments. (gupta2012ltypelectinsin pages 12-13, yamamoto2014intracellularlectinsare pages 8-10, yamamoto2014intracellularlectinsare pages 10-11)
The retrieved reviews emphasize family context with ERGIC-53/LMAN1 and VIPL/LMAN2L, noting that paralogues differ in localization (e.g., VIPL being ER-localized) and sorting signals, reinforcing that LMAN2/VIP36 is the Golgi/ERGIC cycling lectin among close homologs. (yamamoto2014intracellularlectinsare pages 8-10, gupta2012ltypelectinsin pages 15-16)
The following table consolidates quantitative parameters and recent association statistics relevant for functional annotation.
| Finding | Quantitative value(s) | Experimental basis | Source (include DOI URL if available) |
|---|---|---|---|
| Glycan specificity | Prefers high-mannose Man7–9GlcNAc2 glycans; strongest recognition of D1/A-arm Manα1-2Manα1-2Man motif; trimming or glucosylation of the terminal α1,2-mannose abolishes/reduces binding; one FAC-derived affinity value is reported in review text as “7.1 × 10^8 M^-1” for immobilized VIP36 with Man7–9 glycans | Frontal affinity chromatography, competition with Man7–9 glycopeptides, glycan trimming/glucosylation perturbation, and co-crystal structural analysis of the VIP36 CRD | Gupta 2012, https://doi.org/10.1007/978-3-7091-1065-2_7; Reiterer 2010, https://doi.org/10.5451/unibas-005405317; Yamamoto 2014, https://doi.org/10.2183/pjab.90.67 (gupta2012ltypelectinsin pages 13-15, veronika2010theroleof pages 25-28, yamamoto2014intracellularlectinsare pages 10-11, gupta2012ltypelectinsin pages 10-12) |
| pH optimum for sugar binding | Optimal binding reported at ~pH 6.5; other assays reported ~pH 6.0; binding increases under mildly acidic conditions consistent with Golgi localization | Recombinant CRD binding assays and FAC; review synthesis of primary studies | Reiterer 2010, https://doi.org/10.5451/unibas-005405317; Gupta 2012, https://doi.org/10.1007/978-3-7091-1065-2_7; Yamamoto 2014, https://doi.org/10.2183/pjab.90.67 (gupta2012ltypelectinsin pages 12-13, veronika2010theroleof pages 25-28, yamamoto2014intracellularlectinsare pages 10-11) |
| Ca2+ dependence evidence | Structural evidence supports 1 Ca2+ bound adjacent to the carbohydrate-binding site; key residues Asp131, Asn166, His190 directly contact ligand; however, some biochemical studies reported binding at pH 6.0 without strict Ca2+ dependence, so evidence is mixed | X-ray crystallography of VIP36 CRD with mannosyl ligands plus biochemical glycan-binding assays | Gupta 2012, https://doi.org/10.1007/978-3-7091-1065-2_7; Reiterer 2010, https://doi.org/10.5451/unibas-005405317 (gupta2012ltypelectinsin pages 13-15, veronika2010theroleof pages 25-28, gupta2012ltypelectinsin pages 12-13) |
| Cycling kinetics | ER→Golgi t1/2 = 105 ± 39 min; Golgi→ER t1/2 = 1.67 ± 0.45 min | FRAP analysis of cycling in the early secretory pathway | Reiterer 2010, https://doi.org/10.5451/unibas-005405317 (veronika2010theroleof pages 25-28) |
| Localization polarity | Apical/basolateral ratio ≈ 7 in polarized cells | Cell biological localization studies in polarized epithelial cells summarized in review literature | Gupta 2012, https://doi.org/10.1007/978-3-7091-1065-2_7 (gupta2012ltypelectinsin pages 12-13) |
| Ectodomain shedding site | Cleavage at F298↓L299; local sequence reported as SVNF↓LKSP; detected across all analyzed cell lines and scored as a high-confidence metalloprotease-sensitive shedding site | Quantitative protein terminomics with metalloprotease inhibitor BB-94; cleavage-site mapping and PWM-based sheddase analysis | Tsumagari et al. 2021, https://doi.org/10.1101/2020.09.23.310102 (tsumagari2021exploringthelandscape pages 6-8, tsumagari2021exploringthelandscape pages 8-11, tsumagari2021exploringthelandscape pages 11-12, tsumagari2021exploringthelandscape media 6d3163dc) |
| Recent proteomics association: granulosa cells | Log2FC = 1.23, q = 0.04, n = 5 biological replicates | Mass-spectrometry proteomics of cultured human granulosa cells treated 24 h with 30 µM CBD versus ethanol control | Eubler et al. 2023, https://doi.org/10.1093/molehr/gaad029 (eubler2023trpv2anovel pages 9-10) |
| Recent CKD genetics/proteomics association | PWAS identified LMAN2 among 22 CKD-associated plasma proteins; ARIC proteomics n = 7,213 European-ancestry participants; MR for BUN OR = 1.032, FDR = 5.85 × 10^-3; MR for CKD OR = 1.283, FDR = 5.63 × 10^-2; MR for eGFR OR = 0.989, FDR = 0.141; colocalization PP4 < 0.01 for CKD/eGFR/BUN | Proteome-wide association study integrating cis-pQTLs with CKD/eGFR/BUN GWAS, followed by Mendelian randomization and Bayesian colocalization | Xiong et al. 2024, https://doi.org/10.1016/j.heliyon.2024.e31704 (xiong2024plasmaproteomeanalysis pages 1-2, xiong2024plasmaproteomeanalysis pages 9-10, xiong2024plasmaproteomeanalysis pages 7-9) |
Table: This table compiles the main experimentally supported functional parameters and the most relevant recent quantitative disease/proteomics associations for human LMAN2/VIP36. It is useful as a compact evidence summary for annotation, emphasizing what is measured directly versus what remains inferential or mixed.
Open Targets lists modest disease-association evidence for LMAN2 across several disease categories (e.g., metabolic syndrome, atopic eczema, allergic disease, respiratory system disease, eye disease), supported by a small set of PubMed-indexed studies (PubMed IDs provided in the Open Targets evidence rows). These associations are not mechanistic proofs of VIP36 function in those diseases but can guide hypothesis generation and prioritization. (OpenTargets Search: -LMAN2)
References
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(yamamoto2014intracellularlectinsare pages 8-10): Kazuo YAMAMOTO. Intracellular lectins are involved in quality control of glycoproteins. Proceedings of the Japan Academy. Series B, Physical and Biological Sciences, 90:67-82, Feb 2014. URL: https://doi.org/10.2183/pjab.90.67, doi:10.2183/pjab.90.67. This article has 38 citations.
(gupta2012ltypelectinsin pages 2-3): G. S. Gupta. L-type lectins in er-golgi intermediate compartment. Animal Lectins: Form, Function and Clinical Applications, pages 145-161, Mar 2012. URL: https://doi.org/10.1007/978-3-7091-1065-2_7, doi:10.1007/978-3-7091-1065-2_7. This article has 3 citations.
(veronika2010theroleof pages 22-25): Veronika Reiterer. The role of the lectin vip36 in the early secretory pathway. ArXiv, 2010. URL: https://doi.org/10.5451/unibas-005405317, doi:10.5451/unibas-005405317. This article has 0 citations.
(gupta2012ltypelectinsin pages 12-13): G. S. Gupta. L-type lectins in er-golgi intermediate compartment. Animal Lectins: Form, Function and Clinical Applications, pages 145-161, Mar 2012. URL: https://doi.org/10.1007/978-3-7091-1065-2_7, doi:10.1007/978-3-7091-1065-2_7. This article has 3 citations.
(veronika2010theroleof pages 25-28): Veronika Reiterer. The role of the lectin vip36 in the early secretory pathway. ArXiv, 2010. URL: https://doi.org/10.5451/unibas-005405317, doi:10.5451/unibas-005405317. This article has 0 citations.
(gupta2012ltypelectinsin pages 13-15): G. S. Gupta. L-type lectins in er-golgi intermediate compartment. Animal Lectins: Form, Function and Clinical Applications, pages 145-161, Mar 2012. URL: https://doi.org/10.1007/978-3-7091-1065-2_7, doi:10.1007/978-3-7091-1065-2_7. This article has 3 citations.
(yamamoto2014intracellularlectinsare pages 10-11): Kazuo YAMAMOTO. Intracellular lectins are involved in quality control of glycoproteins. Proceedings of the Japan Academy. Series B, Physical and Biological Sciences, 90:67-82, Feb 2014. URL: https://doi.org/10.2183/pjab.90.67, doi:10.2183/pjab.90.67. This article has 38 citations.
(gupta2012ltypelectinsin pages 15-16): G. S. Gupta. L-type lectins in er-golgi intermediate compartment. Animal Lectins: Form, Function and Clinical Applications, pages 145-161, Mar 2012. URL: https://doi.org/10.1007/978-3-7091-1065-2_7, doi:10.1007/978-3-7091-1065-2_7. This article has 3 citations.
(tsumagari2021exploringthelandscape pages 6-8): Kazuya Tsumagari, Chih-Hsiang Chang, and Yasushi Ishihama. Exploring the landscape of ectodomain shedding by quantitative protein terminomics. iScience, Sep 2021. URL: https://doi.org/10.1101/2020.09.23.310102, doi:10.1101/2020.09.23.310102. This article has 26 citations and is from a peer-reviewed journal.
(tsumagari2021exploringthelandscape pages 8-11): Kazuya Tsumagari, Chih-Hsiang Chang, and Yasushi Ishihama. Exploring the landscape of ectodomain shedding by quantitative protein terminomics. iScience, Sep 2021. URL: https://doi.org/10.1101/2020.09.23.310102, doi:10.1101/2020.09.23.310102. This article has 26 citations and is from a peer-reviewed journal.
(tsumagari2021exploringthelandscape pages 11-12): Kazuya Tsumagari, Chih-Hsiang Chang, and Yasushi Ishihama. Exploring the landscape of ectodomain shedding by quantitative protein terminomics. iScience, Sep 2021. URL: https://doi.org/10.1101/2020.09.23.310102, doi:10.1101/2020.09.23.310102. This article has 26 citations and is from a peer-reviewed journal.
(tsumagari2021exploringthelandscape media 6d3163dc): Kazuya Tsumagari, Chih-Hsiang Chang, and Yasushi Ishihama. Exploring the landscape of ectodomain shedding by quantitative protein terminomics. iScience, Sep 2021. URL: https://doi.org/10.1101/2020.09.23.310102, doi:10.1101/2020.09.23.310102. This article has 26 citations and is from a peer-reviewed journal.
(tsumagari2021exploringthelandscape media ed8c04ed): Kazuya Tsumagari, Chih-Hsiang Chang, and Yasushi Ishihama. Exploring the landscape of ectodomain shedding by quantitative protein terminomics. iScience, Sep 2021. URL: https://doi.org/10.1101/2020.09.23.310102, doi:10.1101/2020.09.23.310102. This article has 26 citations and is from a peer-reviewed journal.
(tsumagari2021exploringthelandscape media a19a5e2b): Kazuya Tsumagari, Chih-Hsiang Chang, and Yasushi Ishihama. Exploring the landscape of ectodomain shedding by quantitative protein terminomics. iScience, Sep 2021. URL: https://doi.org/10.1101/2020.09.23.310102, doi:10.1101/2020.09.23.310102. This article has 26 citations and is from a peer-reviewed journal.
(xiong2024plasmaproteomeanalysis pages 1-2): Yang Xiong, Tianhong Wang, Wei Wang, Yangchang Zhang, Fuxun Zhang, Jiuhong Yuan, Feng Qin, and Xianding Wang. Plasma proteome analysis implicates novel proteins as potential therapeutic targets for chronic kidney disease: a proteome-wide association study. Heliyon, 10:e31704, Jun 2024. URL: https://doi.org/10.1016/j.heliyon.2024.e31704, doi:10.1016/j.heliyon.2024.e31704. This article has 11 citations.
(xiong2024plasmaproteomeanalysis pages 7-9): Yang Xiong, Tianhong Wang, Wei Wang, Yangchang Zhang, Fuxun Zhang, Jiuhong Yuan, Feng Qin, and Xianding Wang. Plasma proteome analysis implicates novel proteins as potential therapeutic targets for chronic kidney disease: a proteome-wide association study. Heliyon, 10:e31704, Jun 2024. URL: https://doi.org/10.1016/j.heliyon.2024.e31704, doi:10.1016/j.heliyon.2024.e31704. This article has 11 citations.
(eubler2023trpv2anovel pages 9-10): Katja Eubler, Karolina M Caban, Gregory A Dissen, Ulrike Berg, Dieter Berg, Carola Herrmann, Nicole Kreitmair, Astrid Tiefenbacher, Thomas Fröhlich, and Artur Mayerhofer. Trpv2, a novel player in the human ovary and human granulosa cells. Molecular human reproduction, Aug 2023. URL: https://doi.org/10.1093/molehr/gaad029, doi:10.1093/molehr/gaad029. This article has 8 citations and is from a peer-reviewed journal.
(gupta2012ltypelectinsin pages 10-12): G. S. Gupta. L-type lectins in er-golgi intermediate compartment. Animal Lectins: Form, Function and Clinical Applications, pages 145-161, Mar 2012. URL: https://doi.org/10.1007/978-3-7091-1065-2_7, doi:10.1007/978-3-7091-1065-2_7. This article has 3 citations.
(xiong2024plasmaproteomeanalysis pages 9-10): Yang Xiong, Tianhong Wang, Wei Wang, Yangchang Zhang, Fuxun Zhang, Jiuhong Yuan, Feng Qin, and Xianding Wang. Plasma proteome analysis implicates novel proteins as potential therapeutic targets for chronic kidney disease: a proteome-wide association study. Heliyon, 10:e31704, Jun 2024. URL: https://doi.org/10.1016/j.heliyon.2024.e31704, doi:10.1016/j.heliyon.2024.e31704. This article has 11 citations.
(OpenTargets Search: -LMAN2): Open Targets Query (-LMAN2, 7 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
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