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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 UniProt accession P49257 corresponds to human LMAN1, whose protein product is also known as ERGIC-53/p58/Gp58 and functions as a type I transmembrane L-type lectin cargo receptor in the early secretory pathway (ER→ERGIC→Golgi). This identity is consistent with (i) a luminal carbohydrate-recognition domain (CRD) that binds mannose/high-mannose glycans in a Ca2+-dependent manner, (ii) a long luminal coiled-coil stalk, (iii) a single-pass transmembrane helix, and (iv) a short cytosolic tail with a C-terminal KKFF trafficking motif required for ER–Golgi cycling. (watanabe2024structureoffulllength pages 1-2, tang2023cargoselectionin pages 5-7)
In mammalian cells, cargo receptors are transmembrane proteins that facilitate recruitment of selected luminal cargo into COPII carriers at ER exit sites, accelerating ER-to-Golgi transport compared with bulk flow. LMAN1/ERGIC-53 is a prototypical mammalian cargo receptor: it captures subsets of newly synthesized secretory and membrane proteins in the ER and promotes their export to the Golgi apparatus. (watanabe2024structureoffulllength pages 1-2, tang2023cargoselectionin pages 5-7)
LMAN1 is a type I transmembrane protein with an N-terminal luminal L-type lectin CRD (carbohydrate-recognition domain) and a long luminal stalk (coiled-coils), followed by a transmembrane helix and a short cytosolic tail. The cytosolic tail contains the KKFF motif that supports cycling between ER/ERGIC/Golgi. (watanabe2024structureoffulllength pages 1-2, tang2023cargoselectionin pages 5-7, watanabe2024structureoffulllength media cf25ea0c)
LMAN1 forms a functional complex with MCFD2, a small soluble EF-hand protein that binds Ca2+. The complex is Ca2+-dependent and is central to ER export of canonical cargos such as coagulation factors V and VIII. (zhang2023separaterolesof pages 1-2, tang2023cargoselectionin pages 5-7)
LMAN1’s luminal CRD binds mannose/high-mannose glycans in a Ca2+-dependent manner and contributes to selective trafficking of certain glycoprotein cargos. (watanabe2024structureoffulllength pages 1-2, tang2023cargoselectionin pages 5-7)
However, lectin binding is not universally required for all LMAN1-dependent cargos: in a mechanistic cell system, carbohydrate-binding mutants of LMAN1 retained the ability to rescue much of FVIII secretion, supporting at least partial lectin-independent cargo recognition (protein–protein interactions) for some cargos. (zhang2023separaterolesof pages 8-9)
A major 2024 advance is the cryo-EM structure of full-length human ERGIC-53 (LMAN1) in complex with MCFD2, revealing:
- A homotetrameric assembly (revising older hexamer models), with a “four-leaf clover-like” head region and a long stalk built from multiple four-helix coiled-coils leading to the transmembrane anchor. (watanabe2024structureoffulllength pages 1-2)
- Proposed regulation of cargo capture/release via stalk bending and metal binding, including an N-terminal Zn2+-binding site in MCFD2 that may modulate cargo binding. (watanabe2024structureoffulllength pages 1-2)
The corresponding figure panels provide a compact visual summary of the tetrameric architecture and domain organization (head/stalk/TM/tail). (watanabe2024structureoffulllength media cf25ea0c, watanabe2024structureoffulllength media 7e4fa169)
A 2023 mechanistic study supports a model in which MCFD2 is the primary interacting partner for FV/FVIII cargo, while LMAN1 primarily serves as the shuttling membrane carrier of MCFD2 within the ER–ERGIC cycling route. (zhang2023separaterolesof pages 1-2, zhang2023separaterolesof pages 8-9)
LMAN1/ERGIC-53 is primarily localized to the ER and ERGIC, and cycles through the ER → ERGIC → cis-Golgi compartments as part of early secretory trafficking. (tang2023cargoselectionin pages 5-7, tang2023cargoselectionin pages 9-10, watanabe2024structureoffulllength pages 1-2)
The KKFF motif in the cytosolic tail is functionally subdivided:
- FF acts as an ER exit determinant that promotes export (consistent with COPII-mediated trafficking from ER exit sites).
- KK mediates COPI-dependent retrieval to the ER, enabling receptor recycling. (tang2023cargoselectionin pages 5-7)
Oligomerization is an important determinant for sorting into COPII-coated carriers (notably dimerization is described as required for efficient exit in the review context, while the full-length structure resolves tetrameric architecture). (tang2023cargoselectionin pages 5-7, watanabe2024structureoffulllength pages 1-2)
The best-established physiological role for LMAN1 is facilitating ER-to-Golgi trafficking of FV and FVIII, via the LMAN1–MCFD2 complex. Loss-of-function variants in LMAN1 or MCFD2 cause the autosomal recessive bleeding disorder combined deficiency of FV and FVIII (F5F8D) due to impaired secretion/transport of both factors. (tang2023cargoselectionin pages 5-7, zhang2023separaterolesof pages 1-2)
Recent sources and cited evidence support an expanding (but still limited) cargo list including:
- α1-antitrypsin (A1AT), with experimental evidence of reduced secretion in LMAN1-deficient contexts and review-level synthesis that A1AT export requires both LMAN1 and MCFD2. (zhang2023separaterolesof pages 8-9, everett2024lman1servesas pages 6-7)
- Thrombopoietin (TPO) (new 2024 primary discovery): LMAN1 is required for efficient TPO secretion from hepatocytes, and this appears to be MCFD2-independent. (everett2024lman1servesas pages 1-2, everett2024lman1servesas pages 4-6)
- Review-level summary indicates some cargos are glycan-binding dependent (e.g., CTSC/CTSZ/A1AT/Mac-2BP/MMP-9), while FVIII and some neuroreceptors may not require carbohydrate binding. (tang2023cargoselectionin pages 5-7)
A 2023 expert review emphasizes that, despite LMAN1 being a prototypical cargo receptor, the recognition motif(s) and determinants for many LMAN1/MCFD2-dependent cargos remain unclear, and the full cargo spectrum is still incompletely defined. (tang2023cargoselectionin pages 5-7, tang2023cargoselectionin pages 7-8)
Etiology and genetics. F5F8D is caused by loss-of-function variants in LMAN1 (~70% of cases) or MCFD2 (~30%), disrupting ER-to-Golgi trafficking of FV and FVIII rather than directly mutating F5 or F8. (tang2023cargoselectionin pages 5-7, zhang2023separaterolesof pages 1-2)
Epidemiology. F5F8D is rare, with an estimated prevalence around 1:1,000,000 in the general population (higher in consanguineous populations). (yakovleva2024hereditarycombineddeficiency pages 1-3)
Clinical phenotype and statistics (2024 case series). In a 2024 Russian series (n=6), mean FV activity was 5.7%, mean FVIII activity 9.0%, mean aPTT 85 s, and bleeding severity (ISTH-BAT) ranged 17–29 (mean 23.5). (yakovleva2024hereditarycombineddeficiency pages 1-3)
Diagnostic implementation. Clinical evaluation and genetic confirmation (LMAN1/MCFD2) are used to establish diagnosis and inform counseling; 2024 work illustrates family sequencing approaches (e.g., Sanger sequencing for causal variants) integrated with coagulation assays (PT/aPTT and FV/FVIII activity). (ma2024rnaitargetinglman1mcfd2 pages 3-5)
A 2024 primary study links LMAN1 to platelet homeostasis via TPO secretion. In Lman1–/– mice, plasma TPO was reduced (about 230×10^3 pg/mL → 120×10^3 pg/mL, ELISA; P<0.0024) despite unchanged hepatic Tpo mRNA, consistent with a secretion defect. Hepatocyte-specific Lman1 deletion caused thrombocytopenia, and TPO physically interacted with LMAN1 by co-IP, while MCFD2 did not co-IP with TPO—supporting an MCFD2-independent LMAN1 cargo relationship. (everett2024lman1servesas pages 4-6)
A 2024 preclinical study explored GalNAc-conjugated siRNA knockdown of LMAN1/MCFD2 in mouse liver as an anticoagulation strategy. A single 3 mg/kg dose reduced hepatic LMAN1 mRNA to ~19.97%±3.78% and MCFD2 mRNA to ~32.22%±13.14% at 7 days; protein levels dropped to ~30% (LMAN1) and ~50% (MCFD2) of control in liver. Functional effects included APTT prolongation and reduced FVIII activity, with tail-bleeding generally not significantly increased in this model. (ma2024rnaitargetinglman1mcfd2 pages 1-3, ma2024rnaitargetinglman1mcfd2 pages 9-10, ma2024rnaitargetinglman1mcfd2 pages 10-12)
The following table summarizes the core functional annotation elements, evidence types, and quantitative highlights.
| Concept/Entity | Current understanding | Evidence type | Key quantitative/statistical data if available | Primary recent source(s) with year |
|---|---|---|---|---|
| Protein type / topology | Human LMAN1 (ERGIC-53; UniProt P49257) is a type I transmembrane L-type lectin cargo receptor of the early secretory pathway. It has an N-terminal luminal carbohydrate-recognition domain (CRD), a long luminal stalk, a single-pass TM helix, and a short cytosolic tail carrying trafficking motifs including KKFF for ER/Golgi cycling. (watanabe2024structureoffulllength pages 1-2, tang2023cargoselectionin pages 5-7) | Cryo-EM, structural analysis, review | Cytosolic tail is described as 12 residues in the 2023 review; full-length structure is ~340 Å long in cryo-EM figures. (tang2023cargoselectionin pages 5-7, watanabe2024structureoffulllength media cf25ea0c) | Watanabe et al., 2024; Tang & Ginsburg, 2023 |
| Lectin domain / glycan recognition | The luminal CRD binds mannose/high-mannose glycans in a Ca2+-dependent manner and contributes to selective recruitment of glycoprotein cargo. Some cargos appear glycan-dependent, whereas others can be recognized through lectin-independent protein interactions. (watanabe2024structureoffulllength pages 1-2, tang2023cargoselectionin pages 5-7, zhang2023separaterolesof pages 8-9) | Cryo-EM, prior structural/biochemical evidence summarized in review, rescue assays | No single universal cargo motif has been defined; carbohydrate-binding mutants can still rescue much of FVIII secretion in KO cells, supporting partial lectin-independent recognition. (zhang2023separaterolesof pages 8-9) | Watanabe et al., 2024; Tang & Ginsburg, 2023; Zhang et al., 2023 |
| Oligomerization | A major 2024 advance is that full-length ERGIC-53 was resolved as a homotetramer with a four-leaf-clover head and long flexible coiled-coil stalk, revising older hexamer models. Oligomerization is functionally linked to early secretory pathway trafficking. (watanabe2024structureoffulllength pages 1-2) | Cryo-EM, review | Cryo-EM consensus map at 3.51 Å; head substates at ~3.3–3.4 Å. (watanabe2024structureoffulllength pages 11-12) | Watanabe et al., 2024 |
| Binding partner MCFD2 | MCFD2 is a soluble EF-hand protein that forms a Ca2+-dependent 1:1 complex with LMAN1 and is required for efficient export of canonical cargos such as FV and FVIII. Recent structural work also indicates an N-terminal Zn2+-binding site in MCFD2 that may regulate cargo binding/release. (zhang2023separaterolesof pages 1-2, watanabe2024structureoffulllength pages 1-2, tang2023cargoselectionin pages 5-7) | Cryo-EM, structural analysis, review | F5F8D genetics are attributed to LMAN1 in ~70% of cases and MCFD2 in ~30% of cases. (tang2023cargoselectionin pages 5-7, zhang2023separaterolesof pages 1-2) | Watanabe et al., 2024; Tang & Ginsburg, 2023; Zhang et al., 2023 |
| Localization / trafficking cycle | LMAN1 cycles between the ER, ER-Golgi intermediate compartment (ERGIC), and Golgi/cis-Golgi, acting as a cargo receptor that helps recruit selected clients into COPII-mediated ER export and then recycles back through retrieval signals. (watanabe2024structureoffulllength pages 1-2, watanabe2024structureoffulllength pages 12-13, tang2023cargoselectionin pages 9-10) | Cryo-EM-informed structural analysis, review | Not quantified directly in the extracted evidence; pathway placement is consistent across review and structural sources. (watanabe2024structureoffulllength pages 1-2, tang2023cargoselectionin pages 9-10) | Watanabe et al., 2024; Tang & Ginsburg, 2023 |
| Canonical cargos: factor V and factor VIII | The best-established physiological role of the LMAN1-MCFD2 complex is ER-to-Golgi transport of coagulation factors V and VIII. Recent mechanistic work suggests MCFD2 is likely the primary interacting partner for FV/FVIII cargo, while LMAN1 mainly serves as the shuttling membrane carrier. (zhang2023separaterolesof pages 1-2, zhang2023separaterolesof pages 8-9) | Knockout/complementation, secretion assays, review | In human F5F8D, FV and FVIII are typically reduced to ~5%–30% of normal; some summaries cite average levels around 9%–15%. (ma2024rnaitargetinglman1mcfd2 pages 1-3, ma2024rnaitargetinglman1mcfd2 pages 10-12, zhang2023separaterolesof pages 1-2) | Zhang et al., 2023; Ma et al., 2024 |
| Additional cargos | Beyond FV/FVIII, evidence supports LMAN1-dependent trafficking of α1-antitrypsin (A1AT), Mac-2BP, MMP-9, and now thrombopoietin (TPO). A1AT appears to require both LMAN1 and MCFD2, whereas TPO is the first reported LMAN1-dependent cargo that is MCFD2-independent. (zhang2023separaterolesof pages 10-11, everett2024lman1servesas pages 4-6, watanabe2024structureoffulllength pages 11-12, everett2024lman1servesas pages 6-7, everett2024lman1servesas pages 1-2) | Knockout mice, hepatocyte-specific deletion, co-IP, secretion assays, review | In Lman1-deficient mice, plasma TPO fell from about 230 × 10^3 to 120 × 10^3 pg/mL; hepatocyte-specific loss caused significant thrombocytopenia. (everett2024lman1servesas pages 4-6) | Everett et al., 2024; Zhang et al., 2023; Watanabe et al., 2024 |
| Disease association: F5F8D | Biallelic loss-of-function variants in LMAN1 cause combined deficiency of coagulation factors V and VIII (F5F8D), a rare autosomal recessive bleeding disorder due to impaired cargo export rather than defects in F5 or F8 genes themselves. (tang2023cargoselectionin pages 5-7, yakovleva2024hereditarycombineddeficiency pages 1-3, zhang2023separaterolesof pages 1-2) | Human genetics, clinical case series, review | Prevalence is about 1:1,000,000 overall, but can be much higher in some consanguineous populations; a 2024 Russian series of 6 patients reported mean FV 5.7%, FVIII 9.0%, aPTT 85 s, and mean ISTH-BAT 23.5. (yakovleva2024hereditarycombineddeficiency pages 1-3, zhang2023separaterolesof pages 1-2) | Yakovleva et al., 2024; Tang & Ginsburg, 2023; Zhang et al., 2023 |
| Emerging therapeutic targeting | Experimental liver-directed GalNAc-siRNA knockdown of LMAN1 or MCFD2 reduces FVIII and prolongs coagulation times in mice, suggesting partial inhibition of the complex could be explored as an anticoagulation strategy. (ma2024rnaitargetinglman1mcfd2 pages 10-12, ma2024rnaitargetinglman1mcfd2 pages 9-10, ma2024rnaitargetinglman1mcfd2 pages 1-3) | Preclinical RNAi, RT-qPCR, western blot, coagulation assays | After a single 3 mg/kg dose, hepatic LMAN1 mRNA fell to 19.97% ± 3.78% and MCFD2 mRNA to 32.22% ± 13.14%; liver LMAN1 and MCFD2 proteins fell to ~30% and ~50% of control, respectively. APTT peaked around day 13, and tail bleeding was generally not significantly increased. (ma2024rnaitargetinglman1mcfd2 pages 9-10, ma2024rnaitargetinglman1mcfd2 pages 1-3) | Ma et al., 2024 |
| Open mechanistic questions | Expert reviews emphasize that the full cargo repertoire remains limited and incompletely defined, the recognition motifs for many cargos are still unclear, and secretion may involve backup receptors or bulk-flow pathways. Recent structure work clarifies architecture but not all determinants of cargo specificity or in vivo release dynamics. (watanabe2024structureoffulllength pages 1-2, tang2023cargoselectionin pages 5-7, tang2023cargoselectionin pages 7-8) | Review, cryo-EM primary study | No definitive quantitative estimate of total cargo repertoire is available in the extracted evidence. (tang2023cargoselectionin pages 5-7, tang2023cargoselectionin pages 7-8) | Tang & Ginsburg, 2023; Watanabe et al., 2024 |
Table: This table compiles compact, evidence-backed functional annotation points for human LMAN1/ERGIC-53, emphasizing mechanism, trafficking, cargo specificity, disease relevance, and recent 2023–2024 advances. It is useful as a quick reference for integrating structural, cell-biological, and clinical findings.
Despite extensive study of ER export, experts emphasize that only a small fraction of secreted proteins have known cargo receptors; for LMAN1 specifically, the complete cargo repertoire and generalizable cargo recognition rules remain incompletely defined, and secretion may rely on bulk flow and/or backup receptors for many proteins. (tang2023cargoselectionin pages 7-8, tang2023cargoselectionin pages 5-7)
References
(watanabe2024structureoffulllength pages 1-2): Satoshi Watanabe, Yoshiaki Kise, Kento Yonezawa, Mariko Inoue, Nobutaka Shimizu, Osamu Nureki, and Kenji Inaba. Structure of full-length ergic-53 in complex with mcfd2 for cargo transport. Nature Communications, Mar 2024. URL: https://doi.org/10.1038/s41467-024-46747-1, doi:10.1038/s41467-024-46747-1. This article has 14 citations and is from a highest quality peer-reviewed journal.
(tang2023cargoselectionin pages 5-7): Vi T. Tang and David Ginsburg. Cargo selection in endoplasmic reticulum–to–golgi transport and relevant diseases. The Journal of Clinical Investigation, Jan 2023. URL: https://doi.org/10.1172/jci163838, doi:10.1172/jci163838. This article has 60 citations.
(watanabe2024structureoffulllength media cf25ea0c): Satoshi Watanabe, Yoshiaki Kise, Kento Yonezawa, Mariko Inoue, Nobutaka Shimizu, Osamu Nureki, and Kenji Inaba. Structure of full-length ergic-53 in complex with mcfd2 for cargo transport. Nature Communications, Mar 2024. URL: https://doi.org/10.1038/s41467-024-46747-1, doi:10.1038/s41467-024-46747-1. This article has 14 citations and is from a highest quality peer-reviewed journal.
(zhang2023separaterolesof pages 1-2): Yuanbao Zhang, Zhigang Liu, and Bin Zhang. Separate roles of lman1 and mcfd2 in er-to-golgi trafficking of fv and fviii. Mar 2023. URL: https://doi.org/10.1182/bloodadvances.2022008788, doi:10.1182/bloodadvances.2022008788. This article has 15 citations and is from a peer-reviewed journal.
(zhang2023separaterolesof pages 8-9): Yuanbao Zhang, Zhigang Liu, and Bin Zhang. Separate roles of lman1 and mcfd2 in er-to-golgi trafficking of fv and fviii. Mar 2023. URL: https://doi.org/10.1182/bloodadvances.2022008788, doi:10.1182/bloodadvances.2022008788. This article has 15 citations and is from a peer-reviewed journal.
(watanabe2024structureoffulllength media 7e4fa169): Satoshi Watanabe, Yoshiaki Kise, Kento Yonezawa, Mariko Inoue, Nobutaka Shimizu, Osamu Nureki, and Kenji Inaba. Structure of full-length ergic-53 in complex with mcfd2 for cargo transport. Nature Communications, Mar 2024. URL: https://doi.org/10.1038/s41467-024-46747-1, doi:10.1038/s41467-024-46747-1. This article has 14 citations and is from a highest quality peer-reviewed journal.
(tang2023cargoselectionin pages 9-10): Vi T. Tang and David Ginsburg. Cargo selection in endoplasmic reticulum–to–golgi transport and relevant diseases. The Journal of Clinical Investigation, Jan 2023. URL: https://doi.org/10.1172/jci163838, doi:10.1172/jci163838. This article has 60 citations.
(everett2024lman1servesas pages 6-7): Lesley A. Everett, Zesen Lin, Ann Friedman, Vi T. Tang, Greggory Myers, Ginette Balbin-Cuesta, Richard King, Guojing Zhu, Beth McGee, and Rami Khoriaty. Lman1 serves as a cargo receptor for thrombopoietin. JCI Insight, Dec 2024. URL: https://doi.org/10.1172/jci.insight.175704, doi:10.1172/jci.insight.175704. This article has 1 citations and is from a domain leading peer-reviewed journal.
(everett2024lman1servesas pages 1-2): Lesley A. Everett, Zesen Lin, Ann Friedman, Vi T. Tang, Greggory Myers, Ginette Balbin-Cuesta, Richard King, Guojing Zhu, Beth McGee, and Rami Khoriaty. Lman1 serves as a cargo receptor for thrombopoietin. JCI Insight, Dec 2024. URL: https://doi.org/10.1172/jci.insight.175704, doi:10.1172/jci.insight.175704. This article has 1 citations and is from a domain leading peer-reviewed journal.
(everett2024lman1servesas pages 4-6): Lesley A. Everett, Zesen Lin, Ann Friedman, Vi T. Tang, Greggory Myers, Ginette Balbin-Cuesta, Richard King, Guojing Zhu, Beth McGee, and Rami Khoriaty. Lman1 serves as a cargo receptor for thrombopoietin. JCI Insight, Dec 2024. URL: https://doi.org/10.1172/jci.insight.175704, doi:10.1172/jci.insight.175704. This article has 1 citations and is from a domain leading peer-reviewed journal.
(tang2023cargoselectionin pages 7-8): Vi T. Tang and David Ginsburg. Cargo selection in endoplasmic reticulum–to–golgi transport and relevant diseases. The Journal of Clinical Investigation, Jan 2023. URL: https://doi.org/10.1172/jci163838, doi:10.1172/jci163838. This article has 60 citations.
(yakovleva2024hereditarycombineddeficiency pages 1-3): E. V. Yakovleva, N. I. Zozulya, O. S. Pshenichnikova, V. L. Surin V.L, N. V. Sats, E. B. Orel, A. A. Surenkov, and S. Yu. Mamleeva. Hereditary combined deficiency of factors v and viii: observations in the russian population. Russian journal of hematology and transfusiology, 69:344-355, Nov 2024. URL: https://doi.org/10.35754/0234-5730-2024-69-3-344-355, doi:10.35754/0234-5730-2024-69-3-344-355. This article has 1 citations.
(ma2024rnaitargetinglman1mcfd2 pages 3-5): Siqian Ma, Boyan Liu, Hong Du, Fei Yang, Jingjing Han, Xinqi Huang, Minyang Zhang, Shundong Ji, and Miao Jiang. Rnai targeting lman1-mcfd2 complex promotes anticoagulation in mice. Journal of Thrombosis and Thrombolysis, 57:1349-1362, Sep 2024. URL: https://doi.org/10.1007/s11239-024-03034-6, doi:10.1007/s11239-024-03034-6. This article has 1 citations and is from a peer-reviewed journal.
(ma2024rnaitargetinglman1mcfd2 pages 1-3): Siqian Ma, Boyan Liu, Hong Du, Fei Yang, Jingjing Han, Xinqi Huang, Minyang Zhang, Shundong Ji, and Miao Jiang. Rnai targeting lman1-mcfd2 complex promotes anticoagulation in mice. Journal of Thrombosis and Thrombolysis, 57:1349-1362, Sep 2024. URL: https://doi.org/10.1007/s11239-024-03034-6, doi:10.1007/s11239-024-03034-6. This article has 1 citations and is from a peer-reviewed journal.
(ma2024rnaitargetinglman1mcfd2 pages 9-10): Siqian Ma, Boyan Liu, Hong Du, Fei Yang, Jingjing Han, Xinqi Huang, Minyang Zhang, Shundong Ji, and Miao Jiang. Rnai targeting lman1-mcfd2 complex promotes anticoagulation in mice. Journal of Thrombosis and Thrombolysis, 57:1349-1362, Sep 2024. URL: https://doi.org/10.1007/s11239-024-03034-6, doi:10.1007/s11239-024-03034-6. This article has 1 citations and is from a peer-reviewed journal.
(ma2024rnaitargetinglman1mcfd2 pages 10-12): Siqian Ma, Boyan Liu, Hong Du, Fei Yang, Jingjing Han, Xinqi Huang, Minyang Zhang, Shundong Ji, and Miao Jiang. Rnai targeting lman1-mcfd2 complex promotes anticoagulation in mice. Journal of Thrombosis and Thrombolysis, 57:1349-1362, Sep 2024. URL: https://doi.org/10.1007/s11239-024-03034-6, doi:10.1007/s11239-024-03034-6. This article has 1 citations and is from a peer-reviewed journal.
(watanabe2024structureoffulllength pages 11-12): Satoshi Watanabe, Yoshiaki Kise, Kento Yonezawa, Mariko Inoue, Nobutaka Shimizu, Osamu Nureki, and Kenji Inaba. Structure of full-length ergic-53 in complex with mcfd2 for cargo transport. Nature Communications, Mar 2024. URL: https://doi.org/10.1038/s41467-024-46747-1, doi:10.1038/s41467-024-46747-1. This article has 14 citations and is from a highest quality peer-reviewed journal.
(watanabe2024structureoffulllength pages 12-13): Satoshi Watanabe, Yoshiaki Kise, Kento Yonezawa, Mariko Inoue, Nobutaka Shimizu, Osamu Nureki, and Kenji Inaba. Structure of full-length ergic-53 in complex with mcfd2 for cargo transport. Nature Communications, Mar 2024. URL: https://doi.org/10.1038/s41467-024-46747-1, doi:10.1038/s41467-024-46747-1. This article has 14 citations and is from a highest quality peer-reviewed journal.
(zhang2023separaterolesof pages 10-11): Yuanbao Zhang, Zhigang Liu, and Bin Zhang. Separate roles of lman1 and mcfd2 in er-to-golgi trafficking of fv and fviii. Mar 2023. URL: https://doi.org/10.1182/bloodadvances.2022008788, doi:10.1182/bloodadvances.2022008788. This article has 15 citations and is from a peer-reviewed journal.