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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
The research target is human LMAN2L (synonym VIPL, “VIP36-like protein”), consistent across genetics, cell-biology, and infection/proteomics studies that explicitly refer to LMAN2L/VIPL as an ER-resident L-type (legume-like) intracellular lectin involved in glycoprotein handling in the early secretory pathway. This aligns with the UniProt-provided description (VIP36-like; L-type lectin/ConA-like domain superfamily; precursor/type I membrane protein). (gupta2012ltypelectinsin pages 15-16, hunter2023functionalcharacterisationof pages 91-94, casalnuovo2024characterizationofthe pages 5-9)
L-type lectins are defined by a luminal carbohydrate-recognition domain (CRD) structurally related to legume seed lectins, typically a β-sandwich that binds Ca2+ adjacent to the carbohydrate-binding site; Ca2+ helps organize binding-site residues and supports glycan binding. (gupta2012ltypelectinsin pages 13-15)
In mammalian secretory trafficking, L-type lectins include ERGIC-53/LMAN1, VIP36/LMAN2, and VIPL/LMAN2L and are proposed to recognize high-mannose N-glycans in regulated ways (compared with high-affinity plant lectins). Binding is often Ca2+-dependent and pH-sensitive, allowing capture/release across the ER→ERGIC→Golgi pH gradient. (yamamoto2009intracellularlectinsinvolved pages 5-6, yamamoto2009intracellularlectinsinvolved pages 3-5)
A cargo receptor is a transmembrane protein that binds soluble secretory cargo in the ER lumen and links them to cytosolic coat machinery (e.g., COPII) for ER exit, then typically recycles via COPI. ERGIC-53 is described as a best-characterized example, with oligomerization enabling COPII-recognized sorting signals and selective export of folded cargo. (hunter2023functionalcharacterisationof pages 91-94, gupta2012ltypelectinsin pages 2-3)
LMAN2L is repeatedly distinguished from cycling receptors (ERGIC-53, VIP36) by being primarily ER-resident / non-cycling, consistent with cytosolic retention signals. (hunter2023functionalcharacterisationof pages 91-94, yamamoto2009intracellularlectinsinvolved pages 5-6)
Multiple sources converge on LMAN2L as an ER-resident L-type lectin implicated in glycoprotein trafficking/export rather than enzymatic catalysis. It has been framed as a cargo receptor or “secretion chaperone” whose specific endogenous glycoprotein clients remain incompletely defined. (alkhater2019dominantlman2lmutation pages 1-3, gupta2012ltypelectinsin pages 15-16, hunter2023functionalcharacterisationof pages 91-94)
Mechanistically, LMAN2L is proposed to bind native (properly folded) glycoproteins after they exit the calnexin/calreticulin (CNX/CRT) folding cycle, thereby helping them avoid mannose trimming that would otherwise target them to ER-associated degradation (ERAD), and possibly facilitating onward transport (including potential handoff to ERGIC-53). (hunter2023functionalcharacterisationof pages 91-94)
The strongest and most specific statements in the retrieved literature indicate that LMAN2L/VIPL:
- Binds high-mannose-type N-glycans, with selectivity for deglucosylated forms. (hunter2024hcmvus2coopts pages 5-7, hunter2023functionalcharacterisationof pages 91-94)
- Recognizes motifs including Manα1-2Manα1-2Man (reported from competition assays). (gupta2012ltypelectinsin pages 15-16)
- Shows Ca2+ and pH dependence, with stronger binding at neutral (ER-like) pH and weaker binding after glucosylation or mannose trimming. (hunter2023functionalcharacterisationof pages 91-94, gupta2012ltypelectinsin pages 15-16)
However, some experimental reports summarized in review text note conflicting results (e.g., failure of certain tagged constructs to detect binding to immobilized mannose/Glc/GlcNAc ligands), so glycan-binding activity is supported but not uniformly observed across assay formats. (gupta2012ltypelectinsin pages 15-16)
LMAN2L is described as primarily ER-resident with some partial Golgi localization, and not cycling like ERGIC-53/VIP36. (gupta2012ltypelectinsin pages 15-16, yamamoto2009intracellularlectinsinvolved pages 5-6)
Sorting/retention motifs reported for LMAN2L/VIPL include:
- A cytosolic KRFY motif (associated with ER/ERGIC/cis-Golgi recycling signals in the L-type lectin family context). (gupta2012ltypelectinsin pages 15-16)
- An RKR ER-retention/localization motif described in its cytosolic domain (noted as a determinant of ER residency). (hunter2023functionalcharacterisationof pages 91-94, yamamoto2009intracellularlectinsinvolved pages 5-6, gupta2012ltypelectinsin pages 15-16)
ERGIC-53 (LMAN1): LMAN2L has been proposed to interact with ERGIC-53; overexpression of LMAN2L can redistribute/retain ERGIC-53 in the ER, suggesting regulatory interplay in receptor-mediated export. (hunter2023functionalcharacterisationof pages 91-94, casalnuovo2024characterizationofthe pages 5-9)
Integrin trafficking (ITGA6): A key 2023–2024 development is the emergence of at least one plausible cell-surface client: ITGA6. In infection-linked and depletion experiments, surface ITGA6 was reduced in LMAN2L-deficient cells, and interactome work detected ITGB1 (ITGA6 partner) as a potential associated protein, supporting a model in which LMAN2L contributes to trafficking of specific glycoproteins to the plasma membrane. (hunter2023functionalcharacterisationof pages 121-124, hunter2024hcmvus2coopts pages 5-7)
Unbiased proteomics interaction screening (2024): A RUSH-based co-IP/MS workflow yielded 87 VIPL-associated candidate interactors/cargos after localization filtering, including proteins annotated to ER/Golgi and COPII-related components (e.g., SEC23A/SEC23B, COPB2) plus many cytoskeleton-associated proteins. This dataset is hypothesis-generating and requires orthogonal validation to separate direct interactors from indirect associations. (casalnuovo2024characterizationofthe pages 49-52, casalnuovo2024characterizationofthe pages 45-49)
A major 2024 advance is the demonstration that human cytomegalovirus (HCMV) pUS2 targets LMAN2L for degradation by co-opting the host ERAD machinery:
- LMAN2L is downregulated early (as early as 4 hours post-infection).
- Downregulation is rescued by proteasome inhibition (MG132) but not lysosomal inhibition (leupeptin), supporting proteasome-dependent degradation.
- Deletion mapping indicates pUS2 is necessary for LMAN2L downregulation during infection.
- LMAN2L degradation is TRC8-dependent (TRC8 knockdown strongly rescues LMAN2L), consistent with US2 recruiting TRC8 to ubiquitinate substrates for dislocation and proteasomal degradation.
- Proteomics supporting data deposition: PRIDE PXD050878 (reported in the paper). (hunter2024hcmvus2coopts pages 5-7, hunter2024hcmvus2coopts pages 4-5)
The study interprets these results as consistent with LMAN2L’s hypothesized role in glycoprotein trafficking and suggests US2-mediated targeting may indirectly affect specific surface proteins, including ITGA6. (hunter2024hcmvus2coopts pages 5-7)
URL and publication date: Hunter et al., Journal of General Virology, Apr 2024. https://doi.org/10.1099/jgv.0.001980 (hunter2024hcmvus2coopts pages 5-7)
A 2023 clinical report extends LMAN2L-related neurodevelopmental disease beyond homozygous consanguineous pedigrees by identifying compound heterozygous variants in a Chinese patient:
- Variants: c.256C>T (p.R86C) and c.902del (p.F301Sfs*8).
- Phenotype: global developmental delay, severe intellectual disability, seizures starting at 2 months; additional features include hearing loss and dystonia (phenotype expansion).
- Quantitative clinical details: tonic seizures lasting ~10 seconds; seizure frequency about twice per month on therapy; developmental indices <50 (mean 100).
- Diagnostic implementation: trio-WES, Sanger confirmation, ACMG classification, plus CMA noting a small duplication VUS. (zhou2023novelcompoundheterozygous pages 1-2, zhou2023novelcompoundheterozygous pages 2-3)
URL and publication date: Zhou et al., Chinese Medical Journal, Feb 2023. https://doi.org/10.1097/cm9.0000000000002285 (zhou2023novelcompoundheterozygous pages 1-2)
Autosomal recessive: The foundational Mendelian evidence is a 2016 consanguineous family where LMAN2L p.R53Q (c.158G>A) co-segregated with severe intellectual disability and infantile seizures until age 5, with 5 affected homozygotes and 7 unaffected relatives showing heterozygosity or non-carrier status, strongly supporting causality in that pedigree. (rafiullah2016homozygousmissensemutation pages 2-4)
Autosomal dominant: A 2019 report identified a heterozygous frameshift c.1073delT; p.(Phe358Serfs*16) that removes the ER-retention/localization motif and causes ID with remitting epilepsy in 4 affected family members. A central mechanistic interpretation is that loss of ER retention causes mislocalization and disrupts glycoprotein handling critical for neurodevelopment. (alkhater2019dominantlman2lmutation pages 1-3, alkhater2019dominantlman2lmutation pages 3-5)
Image-based evidence for mechanism (2019): Figure 2 provides direct evidence that the c.1073delT variant shifts LMAN2L into the plasma membrane fraction and produces peripheral cell-surface immunofluorescence, supporting mislocalization due to loss of ER retention. (alkhater2019dominantlman2lmutation media 119efd23)
Expert interpretation: The 2019 authors explicitly frame LMAN2L as among “glycoprotein secretion chaperone” family members and emphasize that its specific processed glycoproteins are unknown, while arguing that mislocalization or impaired glycoprotein interaction can disturb brain development and produce remitting childhood epilepsy. (alkhater2019dominantlman2lmutation pages 1-3, alkhater2019dominantlman2lmutation pages 3-5)
LMAN2L has been repeatedly mentioned as associated in GWAS contexts with disorders including bipolar disorder and schizophrenia in the genetics literature, but these do not establish causal mechanism in the same way as family segregation. (alkhater2019dominantlman2lmutation pages 1-3, rafiullah2016homozygousmissensemutation pages 2-4)
A disease-target association query in Open Targets lists associations for LMAN2L with autosomal dominant intellectual disability, autosomal recessive non-syndromic intellectual disability, and psychiatric phenotypes (major depressive disorder, bipolar disorder, schizophrenia), reflecting aggregated evidence links and literature mapping. (OpenTargets Search: -LMAN2L)
The most mature real-world application is rare-disease genetic diagnosis:
- LMAN2L variants are identified via whole-exome sequencing (WES) with segregation/Sanger validation in families and probands; trio-WES is used in contemporary diagnostics. (zhou2023novelcompoundheterozygous pages 1-2, rafiullah2016homozygousmissensemutation pages 2-4, alkhater2019dominantlman2lmutation pages 1-3)
- Reported inheritance spans autosomal recessive (homozygous or compound heterozygous) and autosomal dominant (ER-retention-loss frameshift) presentations, which is relevant for variant interpretation and counseling. (rafiullah2016homozygousmissensemutation pages 2-4, alkhater2019dominantlman2lmutation pages 1-3)
LMAN2L has emerging relevance as a host factor targeted by HCMV immune evasion. The pUS2–TRC8-mediated degradation of LMAN2L demonstrates a concrete host–virus interaction and provides a tool/perturbation axis for dissecting LMAN2L-dependent trafficking of specific glycoproteins. (hunter2024hcmvus2coopts pages 5-7)
The 2024 HCMV study reports proteomics deposition (PRIDE: PXD050878) supporting LMAN2L degradation and downstream surface-proteome analysis, enabling reanalysis and integration by other investigators. (hunter2024hcmvus2coopts pages 5-7, hunter2024hcmvus2coopts pages 4-5)
| Category | Key findings | Evidence type | Citation id(s) | Publication year | URL |
|---|---|---|---|---|---|
| Protein identity, localization, motifs | Human LMAN2L (VIPL; UniProt Q9H0V9) is a VIP36-like, ER-resident L-type intracellular lectin/cargo-receptor family member. It is largely non-cycling relative to ERGIC-53/LMAN1 and LMAN2/VIP36. Reported cytosolic sorting motifs include KRFY and an additional RKR ER-retention/localization signal; mutation of KR can redirect VIPL to the cell surface. | Reviews/summaries of prior cell biology; mechanistic thesis synthesis | (gupta2012ltypelectinsin pages 15-16, hunter2023functionalcharacterisationof pages 91-94, casalnuovo2024characterizationofthe pages 5-9) | 2012, 2023, 2024 | https://doi.org/10.1007/978-3-7091-1065-2_7; https://doi.org/10.17863/cam.108565 |
| Glycan binding and mechanistic role | VIPL/LMAN2L has been reported to recognize deglucosylated high-mannose N-glycans, especially Manα1-2Manα1-2Man motifs; binding is stronger at neutral ER-like pH and is Ca2+-dependent. Proposed role: bind native glycoproteins exiting the calnexin/calreticulin cycle, protect them from demannosylation/ERAD, and possibly hand cargo to ERGIC-53 for anterograde transport. siRNA knockdown delayed secretion of two glycoproteins. Some earlier assays failed to detect sugar binding, so this function remains supported but not fully settled. | Binding assays/competition data, knockdown experiments, mechanistic synthesis | (gupta2012ltypelectinsin pages 15-16, hunter2023functionalcharacterisationof pages 91-94) | 2012, 2023 | https://doi.org/10.1007/978-3-7091-1065-2_7; https://doi.org/10.17863/cam.108565 |
| 2016 clinical variant | Homozygous c.158G>A (p.R53Q) in a consanguineous Pakistani family co-segregated with severe intellectual disability and infantile epileptic seizures. Studied pedigree included 5 affected and 7 unaffected relatives; all affected were homozygous, unaffected relatives were heterozygous, supporting autosomal recessive inheritance. | Family-based WES, segregation, Sanger validation, homology modeling | (rafiullah2016homozygousmissensemutation pages 2-4) | 2016 | https://doi.org/10.1136/jmedgenet-2015-103179 |
| 2019 clinical variant | Heterozygous c.1073delT, p.(Phe358Serfs*16) disrupted the C-terminal KRFY ER-retention motif in a family with autosomal dominant intellectual disability and remitting epilepsy. Functional studies in HeLa cells showed mutant LMAN2L shifted from ER/light-membrane fractions to the plasma membrane; immunofluorescence showed a peripheral “shroud” consistent with surface mislocalization. | WES/segregation plus membrane fractionation and immunofluorescence | (alkhater2019dominantlman2lmutation pages 1-3, alkhater2019dominantlman2lmutation pages 3-5, alkhater2019dominantlman2lmutation media 119efd23) | 2019 | https://doi.org/10.1002/acn3.727 |
| 2023 clinical variant | A Chinese MRT52 proband carried compound heterozygous variants c.256C>T (p.R86C) and c.902del (p.F301Sfs*8), extending LMAN2L disease beyond homozygous cases. Phenotype included global developmental delay, severe ID, seizures beginning at 2 months, hearing loss, and dystonia; seizures occurred about twice monthly despite therapy. | Trio-WES, Sanger confirmation, ACMG classification, case report | (zhou2023novelcompoundheterozygous pages 1-2, zhou2023novelcompoundheterozygous pages 2-3) | 2023 | https://doi.org/10.1097/cm9.0000000000002285 |
| 2024 HCMV/ERAD finding | HCMV pUS2 targets LMAN2L for degradation through the host E3 ligase TRC8. LMAN2L was downregulated as early as 4 h post-infection, rescued by MG132 but not leupeptin, and restored in ΔUS2 infection. This supports a bona fide ER-resident role for LMAN2L and implicates it in host glycoprotein trafficking exploited by virus. | Quantitative proteomics, viral genetics, inhibitor rescue, knockdown | (hunter2024hcmvus2coopts pages 5-7, hunter2024hcmvus2coopts pages 4-5) | 2024 | https://doi.org/10.1099/jgv.0.001980 |
| 2024 trafficking/client evidence | In LMAN2L-deficient cells, surface ITGA6 was reproducibly reduced; 2023-2024 proteomic work also detected ITGB1 in the LMAN2L interactome, suggesting integrin-related client trafficking. Effect size reported for ITGA6 in the thesis was ~1.5-fold downregulation upon LMAN2L depletion. | Plasma-membrane profiling, CRISPR/siRNA depletion, interactome proteomics | (hunter2023functionalcharacterisationof pages 121-124, hunter2024hcmvus2coopts pages 5-7) | 2023, 2024 | https://doi.org/10.17863/cam.108565; https://doi.org/10.1099/jgv.0.001980 |
| 2024 proteomics interaction screening | A RUSH-based co-IP/MS study identified 87 candidate VIPL-associated proteins/cargos after localization filtering, including ER/Golgi and COPII-related proteins such as SEC23A, SEC23B, and COPB2, plus many cytoskeleton-associated proteins. Authors cautioned that these are candidate interactors/cargos requiring orthogonal validation. | RUSH live-cell trafficking, GFP-nanobody IP, mass spectrometry, imaging | (casalnuovo2024characterizationofthe pages 49-52, casalnuovo2024characterizationofthe pages 45-49) | 2024 | No stable journal URL available in retrieved context |
Table: This table condenses the main experimentally supported findings for human LMAN2L/VIPL, spanning identity, localization, glycan-binding biology, disease variants, and the most relevant 2023-2024 mechanistic studies. It is useful as a quick-reference evidence map linking each claim to specific cited contexts and source URLs.
References
(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.
(hunter2023functionalcharacterisationof pages 91-94): Functional Characterisation of Protein Degradation during Human Cytomegalovirus Infection This article has 0 citations.
(casalnuovo2024characterizationofthe pages 5-9): S Casalnuovo. Characterization of the protein vip36 and vipl and identification of their interaction partners. Unknown journal, 2024.
(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.
(yamamoto2009intracellularlectinsinvolved pages 5-6): Kazuo Yamamoto. Intracellular lectins involved in folding and transport in the endoplasmic reticulum. Biological & pharmaceutical bulletin, 32 5:767-73, May 2009. URL: https://doi.org/10.1248/bpb.32.767, doi:10.1248/bpb.32.767. This article has 29 citations and is from a peer-reviewed journal.
(yamamoto2009intracellularlectinsinvolved pages 3-5): Kazuo Yamamoto. Intracellular lectins involved in folding and transport in the endoplasmic reticulum. Biological & pharmaceutical bulletin, 32 5:767-73, May 2009. URL: https://doi.org/10.1248/bpb.32.767, doi:10.1248/bpb.32.767. This article has 29 citations and is from a peer-reviewed journal.
(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.
(alkhater2019dominantlman2lmutation pages 1-3): Reem A. Alkhater, Peixiang Wang, Alessandra Ruggieri, Lori Israelian, Susan Walker, Stephen W. Scherer, Mary Lou Smith, and Berge A. Minassian. Dominant lman2l mutation causes intellectual disability with remitting epilepsy. Annals of Clinical and Translational Neurology, 6:807-811, Mar 2019. URL: https://doi.org/10.1002/acn3.727, doi:10.1002/acn3.727. This article has 14 citations and is from a peer-reviewed journal.
(hunter2024hcmvus2coopts pages 5-7): Leah M. Hunter, Joanne Kite, Alice Fletcher-Etherington, Katie Nightingale, Luis Nobre, Robin Antrobus, Ceri A. Fielding, Richard J. Stanton, and Michael P. Weekes. Hcmv us2 co-opts trc8 to degrade the endoplasmic reticulum-resident protein lman2l. Apr 2024. URL: https://doi.org/10.1099/jgv.0.001980, doi:10.1099/jgv.0.001980. This article has 4 citations and is from a peer-reviewed journal.
(hunter2023functionalcharacterisationof pages 121-124): Functional Characterisation of Protein Degradation during Human Cytomegalovirus Infection This article has 0 citations.
(casalnuovo2024characterizationofthe pages 49-52): S Casalnuovo. Characterization of the protein vip36 and vipl and identification of their interaction partners. Unknown journal, 2024.
(casalnuovo2024characterizationofthe pages 45-49): S Casalnuovo. Characterization of the protein vip36 and vipl and identification of their interaction partners. Unknown journal, 2024.
(hunter2024hcmvus2coopts pages 4-5): Leah M. Hunter, Joanne Kite, Alice Fletcher-Etherington, Katie Nightingale, Luis Nobre, Robin Antrobus, Ceri A. Fielding, Richard J. Stanton, and Michael P. Weekes. Hcmv us2 co-opts trc8 to degrade the endoplasmic reticulum-resident protein lman2l. Apr 2024. URL: https://doi.org/10.1099/jgv.0.001980, doi:10.1099/jgv.0.001980. This article has 4 citations and is from a peer-reviewed journal.
(zhou2023novelcompoundheterozygous pages 1-2): Cong Zhou, Xing Wei, Yuanyuan Xiao, Shanling Liu, and Jing Wang. Novel compound heterozygous variants in lectin mannose-binding 2-like gene identified in a chinese autosomal recessive mental retardation-52 (mrt52) patient with phenotype expansion. Chinese Medical Journal, 136:2107-2109, Feb 2023. URL: https://doi.org/10.1097/cm9.0000000000002285, doi:10.1097/cm9.0000000000002285. This article has 2 citations and is from a peer-reviewed journal.
(zhou2023novelcompoundheterozygous pages 2-3): Cong Zhou, Xing Wei, Yuanyuan Xiao, Shanling Liu, and Jing Wang. Novel compound heterozygous variants in lectin mannose-binding 2-like gene identified in a chinese autosomal recessive mental retardation-52 (mrt52) patient with phenotype expansion. Chinese Medical Journal, 136:2107-2109, Feb 2023. URL: https://doi.org/10.1097/cm9.0000000000002285, doi:10.1097/cm9.0000000000002285. This article has 2 citations and is from a peer-reviewed journal.
(rafiullah2016homozygousmissensemutation pages 2-4): Rafiullah Rafiullah, Muhammad Aslamkhan, Nagarajan Paramasivam, Christian Thiel, Ghulam Mustafa, Stefan Wiemann, Matthias Schlesner, Rebecca C Wade, Gudrun A Rappold, and Simone Berkel. Homozygous missense mutation in the lman2l gene segregates with intellectual disability in a large consanguineous pakistani family. Journal of Medical Genetics, 53:138-144, Nov 2016. URL: https://doi.org/10.1136/jmedgenet-2015-103179, doi:10.1136/jmedgenet-2015-103179. This article has 25 citations and is from a domain leading peer-reviewed journal.
(alkhater2019dominantlman2lmutation pages 3-5): Reem A. Alkhater, Peixiang Wang, Alessandra Ruggieri, Lori Israelian, Susan Walker, Stephen W. Scherer, Mary Lou Smith, and Berge A. Minassian. Dominant lman2l mutation causes intellectual disability with remitting epilepsy. Annals of Clinical and Translational Neurology, 6:807-811, Mar 2019. URL: https://doi.org/10.1002/acn3.727, doi:10.1002/acn3.727. This article has 14 citations and is from a peer-reviewed journal.
(alkhater2019dominantlman2lmutation media 119efd23): Reem A. Alkhater, Peixiang Wang, Alessandra Ruggieri, Lori Israelian, Susan Walker, Stephen W. Scherer, Mary Lou Smith, and Berge A. Minassian. Dominant lman2l mutation causes intellectual disability with remitting epilepsy. Annals of Clinical and Translational Neurology, 6:807-811, Mar 2019. URL: https://doi.org/10.1002/acn3.727, doi:10.1002/acn3.727. This article has 14 citations and is from a peer-reviewed journal.
(OpenTargets Search: -LMAN2L): Open Targets Query (-LMAN2L, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.