ArticleFrontiers in immunology2011
The EMILIN/Multimerin family.
Article in Frontiers in immunology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 112 citations in OpenAlex.
- Behind the scenes: how the EMILIN/Multimerin family shapes the cancer landscape.The FEBS journal · 2026Review
- Article
- EMILIN1 emerges as a TGFβ/SETDB1-regulated secreted biomarker in Duchenne muscular dystrophy.Cell death & disease · 2026Article
- EMILIN-1 in the tumor microenvironment: insights from CNS tumors and beyond.Frontiers in oncology · 2026Review
- Roles and molecular mechanisms of EMILIN-1 in physiology and disease: a narrative review.Frontiers in medicine · 2026Review
- The role of MEGF10 in myoblast fusion and hypertrophic response to overload of skeletal muscle.Journal of muscle research and cell motility · 2025Article
- CD93 in Health and Disease: Bridging Physiological Functions and Clinical Applications.International journal of molecular sciences · 2025Review
- Intestinal lymphatic vasculature is functionally adapted to different drainage regions and is altered by helminth infection.The Journal of experimental medicine · 2025Article
- MMRN1 Facilitates Renal Cell Carcinoma by Activating AMPK/MMPs Axis.Cancer medicine · 2025Article
- Review
- FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains.Nature chemical biology · 2025Article
- ProteinMolecules (Basel, Switzerland) · 2025Review
- Embryonic reprogramming of the tumor vasculature reveals targets for cancer therapy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- New insights into the structural role of EMILINs within the human skin microenvironment.Scientific reports · 2024Article
- FeCell adhesion & migration · 2024Article
- Label-Free Quantitative Proteomics Analysis of Nasal Lavage Fluid in Chronic Rhinosinusitis with Nasal Polyposis.Biology · 2024Article
- Article
- HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to promote WNT signaling.Journal of virology · 2024Article
- Emilin2 marks the target region for mesenchymal cell accumulation in bone regeneration.Inflammation and regeneration · 2024Article
- Generation of Tailored Extracellular Matrix Hydrogels for the Study of In Vitro Folliculogenesis in Response to Matrisome-Dependent Biochemical Cues.Bioengineering (Basel, Switzerland) · 2024Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elastin microfibrillar interface proteins (EMILINs) and Multimerins (EMILIN1, EMILIN2, Multimerin1, and Multimerin2) constitute a four member family that in addition to the shared C-terminus gC1q domain typical of the gC1q/TNF superfamily members contain a N-terminus unique cysteine-rich EMI domain. These glycoproteins are homotrimeric and assemble into high molecular weight multimers. They are predominantly expressed in the extracellular matrix and contribute to several cellular functions in part associated with the gC1q domain and in part not yet assigned nor linked to other specific regions of the sequence. Among the latter is the control of arterial blood pressure, the inhibition of Bacillus anthracis cell cytotoxicity, the promotion of cell death, the proangiogenic function, and a role in platelet hemostasis. The focus of this review is to highlight the multiplicity of functions and domains of the EMILIN/Multimerin family with a particular emphasis on the regulatory role played by the ligand-receptor interactions of the gC1q domain. EMILIN1 is the most extensively studied member both from the structural and functional point of view. The structure of the gC1q of EMILIN1 solved by NMR highlights unique characteristics compared to other gC1q domains: it shows a marked decrease of the contact surface of the trimeric assembly and while conserving the jelly-roll topology with two β-sheets of antiparallel strands it presents a nine-stranded β-sandwich fold instead of the usual 10-stranded fold. This is likely due to the insertion of nine residues that disrupt the ordered strand organization and forma a highly dynamic protruding loop. In this loop the residue E933 is the site of interaction between gC1q and the α4β1 and α9β1 integrins, and contrary to integrin occupancy that usually upregulates cell growth, when gC1q is ligated by the integrin the cells reduce their proliferative activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.