Affinage

MARCKSL1

MARCKS-related protein · UniProt P49006

Length
195 aa
Mass
19.5 kDa
Annotated
2026-06-10
35 papers in source corpus 23 papers cited in narrative 23 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 5/6 claims corpus-supported (83%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MARCKSL1 (MacMARCKS/F52) is a myristoylated, peripherally membrane-associated PKC substrate that integrates protein kinase C and Ca2+/calmodulin signals to remodel the cortical actin cytoskeleton (PMID:1516135, PMID:1618855). Through a central basic effector domain it binds calmodulin with high affinity and binds and bundles F-actin, with PKC phosphorylation disrupting calmodulin binding; together with its N-terminal myristoylation this effector domain directs the protein to specific membrane domains and confers its actin-regulatory activity (PMID:1516135, PMID:1618855, PMID:9637918). JNK directly phosphorylates MARCKSL1 at S120/T148/T183, switching it toward F-actin bundling and stabilization that increases filopodia and retards migration, whereas non-phosphorylatable protein favors lamellipodia and motility (PMID:22751924). This actin-shaping function operates across contexts: it is genetically essential for cranial neural tube closure, where its loss causes neural tube defects and it behaves as haploinsufficient (PMID:8692805, PMID:8700893); it governs dendritic spine and dendrite morphology in neurons with consequences for anxiety behavior and HPA axis activity (PMID:29580842, PMID:31155484); and it controls endothelial cortical mechanics, vessel diameter, and JNK1-driven apical filopodia that establish neutrophil transmigration hotspots (PMID:33127887, PMID:37559902). MARCKSL1 also modulates membrane signaling and trafficking, binding the C-terminal tails of the serotonin transporter and metabotropic glutamate receptor 7 to regulate transport activity and VSCC tonic inhibition in a calmodulin-antagonized manner (PMID:12051706, PMID:16987251), and influencing integrin-dependent adhesion in a phosphorylation-state-dependent fashion (PMID:10497314). In cancer it promotes invadopodia formation and matrix degradation via F-actin and cortactin (PMID:35894387).

Mechanistic history

Synthesis pass · year-by-year structured walk · 9 steps
  1. 1992 High

    Established the core biochemical identity of MARCKSL1 as a myristoylated PKC substrate whose effector domain reciprocally couples calmodulin binding and actin binding to phosphorylation state, defining the molecular switch underlying all later functions.

    Evidence Protein purification, cDNA cloning, in vitro PKC phosphorylation and calmodulin/actin binding assays with defined kinetics, replicated across two labs

    PMID:1516135 PMID:1618855

    Open questions at the time
    • Did not establish which cellular processes the actin/calmodulin switch controls
    • No structural model of the membrane-bound effector domain
  2. 1996 High

    Demonstrated that MARCKSL1 is genetically essential in vivo, with knockout causing failure of cranial neural tube closure and dose-sensitive (haploinsufficient) penetrance, linking its actin function to morphogenetic movement.

    Evidence Independent gene knockout mouse studies with developmental phenotyping

    PMID:8692805 PMID:8700893

    Open questions at the time
    • Did not resolve which cell movements at the neural plate require MARCKSL1
    • Phosphorylation-dependence of the developmental role untested at the time
  3. 1998 High

    Resolved a conflict over MARCKSL1's role in phagocytosis: dominant-negative effector-domain mutants implicated it, but genetic null macrophages phagocytose and spread normally, showing it is recruited but not absolutely required.

    Evidence Comparison of dominant-negative mutant phenotypes versus MacMARCKS null macrophage phagocytosis and spreading assays

    PMID:9837946

    Open questions at the time
    • Possible redundancy with MARCKS not directly tested
    • Why dominant-negative and null phenotypes diverge mechanistically unresolved
  4. 1998 Medium

    Showed that the myristoyl moiety plus basic effector domain are sufficient for targeting MARCKSL1 to a specific (basolateral) membrane domain and that PKC activation displaces it, mechanistically connecting phosphorylation to membrane localization.

    Evidence GFP-fusion domain dissection in polarized MDCK cells with PKC activation

    PMID:9637918

    Open questions at the time
    • Single lab
    • Targeting determinants in non-epithelial cells not addressed
  5. 2006 High

    Identified direct receptor-tail binding partners (SERT, mGluR7) showing MARCKSL1 modulates membrane transporter/receptor function, with mGluR7 binding antagonized by Ca2+/calmodulin and controlling VSCC tonic inhibition.

    Evidence Yeast two-hybrid, pulldown, co-IP, colocalization, transporter uptake and electrophysiology assays

    PMID:12051706 PMID:16987251

    Open questions at the time
    • Physiological relevance of these interactions in vivo not established
    • Stoichiometry and regulation by PKC phosphorylation incompletely defined
  6. 2012 High

    Defined the JNK-MARCKSL1 axis: direct JNK phosphorylation at S120/T148/T183 switches MARCKSL1 toward F-actin bundling/stabilization that builds filopodia and slows migration, while the unphosphorylatable form drives lamellipodia and motility.

    Evidence In vitro JNK kinase assay, phosphosite mutagenesis, F-actin bundling assays, live imaging and migration assays in neurons and prostate cancer cells

    PMID:22751924

    Open questions at the time
    • Upstream signals activating JNK toward MARCKSL1 not delineated here
    • Relationship between JNK sites and PKC/calmodulin switch unresolved
  7. 2020 High

    Extended the actin function to tissue mechanics, showing MARCKSL1 sets endothelial cortical stiffness by promoting linear over branched actin, thereby controlling cell size, vessel diameter, and flow-dependent blebbing.

    Evidence Zebrafish in vivo gain/loss-of-function, high-resolution imaging, actin network analysis, blood flow manipulation

    PMID:33127887

    Open questions at the time
    • Molecular basis for linear vs branched actin preference not defined
    • Link to JNK phosphorylation in this context not tested
  8. 2023 Medium

    Connected upstream signaling to physiology, showing endothelial JNK1 (not JNK2) phosphorylates MARCKSL1 to form apical filopodia that establish neutrophil transmigration hotspots.

    Evidence Kinase translocation reporters, Cdc42 FRET biosensors, JNK1/2-specific perturbation, MARCKSL1 knockdown, neutrophil adhesion assays

    PMID:37559902

    Open questions at the time
    • Single lab
    • Whether the same S120/T148/T183 sites mediate this remains inferential
  9. 2025 Medium

    Implicated MARCKSL1 in plasma-membrane-derived extracellular vesicle secretion in collaboration with Radixin and STXBP3, expanding its role from cortical actin to membrane budding/trafficking.

    Evidence Genome-wide CRISPR activation screen, genomic activation/ablation, electron microscopy, proteomics, interaction studies (preprint)

    PMID:bio_10.1101_2025.07.24.665424

    Open questions at the time
    • Preprint, not yet peer-reviewed
    • Direct binding to Radixin/STXBP3 versus pathway co-dependence not fully separated

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the JNK (S120/T148/T183), PKC, and Ca2+/calmodulin inputs are integrated on a single effector domain to select between filopodia, lamellipodia, cortical stiffening, and membrane trafficking outputs remains unresolved.
  • No unified structural/biophysical model reconciling the three phosphoregulatory inputs
  • Tissue-specific partner sets that bias output are incompletely mapped

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008092 cytoskeletal protein binding 4 GO:0098772 molecular function regulator activity 3
Localization
GO:0005856 cytoskeleton 3 GO:0005886 plasma membrane 3
Pathway
R-HSA-1266738 Developmental Biology 3
Partners
CALM1CTTNGRM7LOXL2RDXSLC6A4STXBP3

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1992 MacMARCKS (MARCKSL1) is a PKC substrate that binds calmodulin in a phosphorylation-regulated manner; phosphorylation by PKC disrupts calmodulin binding. It also binds actin and shares structural homology with MARCKS including an amino-terminal myristoylation sequence and a central effector/calmodulin-binding/PKC phosphorylation domain. Protein purification, cDNA cloning, calmodulin binding assays, PKC phosphorylation assays Cell High 1516135 1618855
1992 The F52/MARCKSL1 protein is myristoylated at its N-terminus; it is a PKC substrate with high-affinity calmodulin binding (Kd <3 nM) that is disrupted upon PKC phosphorylation. A 24-amino acid peptide from the effector domain recapitulated these properties (S0.5 for PKC = 173 nM, KH = 5.4). E. coli expression, co-expression with N-myristoyltransferase, PKC phosphorylation assay, calmodulin binding assay, peptide substrate kinetics The Journal of biological chemistry High 1618855
1996 Deletion of the MacMARCKS gene in mice prevents cranial neural tube closure, resulting in anencephaly, demonstrating an essential role for MARCKSL1 in PKC-dependent actin-based morphogenic movement of the anterior neural plate. Gene knockout (homologous recombination), developmental phenotypic analysis Proceedings of the National Academy of Sciences of the United States of America High 8692805
1996 F52/MARCKSL1-deficient mice develop neural tube defects (exencephaly and spina bifida) with partial penetrance (~60% homozygous), and ~10% of heterozygotes also show defects, establishing MARCKSL1 as haploinsufficient for neural tube closure. Gene targeting/knockout in mice, developmental phenotype analysis Proceedings of the National Academy of Sciences of the United States of America High 8700893
1995 MacMARCKS concentrates around nascent phagosomes in macrophages during zymosan phagocytosis; expression of effector-domain deletion mutants reduced phagocytic capacity by ~90% without affecting receptor-mediated endocytosis of acetylated LDL, implicating the effector domain in phagocytosis. Immunofluorescence microscopy, stable transfection of effector-domain deletion mutants, phagocytosis assay, endocytosis assay The Journal of biological chemistry Medium 7629059
1998 MacMARCKS null macrophages phagocytose and spread normally, indicating that MacMARCKS is recruited to phagosomes but is not absolutely required for phagocytosis, contradicting findings from dominant-negative mutant studies. MacMARCKS null mouse macrophages (KO), phagocytosis assay, cell spreading assay The Journal of biological chemistry High 9837946
1996 MacMARCKS participates in integrin-dependent macrophage spreading and phorbol ester-stimulated spreading requiring multiple integrins; dominant-negative effector-domain mutant blocks macrophage binding to iC3b-opsonized targets (complement receptor 3/beta2 integrin), integrin-dependent paxillin tyrosine phosphorylation, and colocalizes with paxillin at leading-edge membrane ruffles. Dominant-negative mutant expression, cell spreading assay, rosette formation assay, immunofluorescence colocalization, paxillin phosphorylation assay The Journal of biological chemistry Medium 8662782
1996 MacMARCKS is phosphorylated in a Ca2+-dependent manner upon depolarization in PC12 cells and synaptosomes; it colocalizes with synaptophysin at neurite tips and associates with synaptic vesicles by subcellular fractionation, consistent with a role in integrating Ca2+/calmodulin and PKC signals in neurosecretion. Immunoprecipitation, immunofluorescence microscopy, subcellular fractionation, Percoll-purified synaptosomes, KCl depolarization, phorbol ester stimulation The Journal of biological chemistry Medium 8557647
1998 MacMARCKS is targeted specifically to the basolateral membrane domain of polarized MDCK cells; the effector domain (24-amino acid basic region with PKC phosphorylation and calmodulin/actin-binding sites) combined with a myristoyl moiety is sufficient for basolateral targeting, and PKC activation displaces it from this location. Transfection into polarized MDCK cells, immunofluorescence microscopy, GFP-fusion domain targeting experiments, PKC activation Current biology : CB Medium 9637918
1999 Phosphorylated MacMARCKS is required for LFA-1 (beta2 integrin)-mediated cell-cell adhesion in U937 monocytic cells; phosphomimetic (phosphorylated) MacMARCKS enhances adhesion while unphosphorylatable mutant inhibits it, demonstrating that PKC-mediated phosphorylation state determines integrin activation. Transfection of wild-type and phosphorylation-site mutants, PMA stimulation, cell-cell adhesion assay, okadaic acid phosphatase inhibition Journal of cellular physiology Medium 10497314
2001 MacMARCKS interacts with dynamitin (a dynactin complex subunit) in living cells; interaction is concentrated at the cell periphery in resting macrophages and is lost upon PMA stimulation as both proteins redistribute to perinuclear regions, linking MacMARCKS to microtubule motor-dependent functions. FRET (CFP/YFP fusion proteins), in vitro pulldown, live-cell imaging in RAW macrophages and HEK293 cells The Journal of biological chemistry Medium 11278693
2002 MacMARCKS interacts with the C-terminal cytoplasmic tail of the serotonin transporter (SERT) as identified by yeast two-hybrid and confirmed by co-transfection; MacMARCKS co-expression reduces maximal 5-HT uptake rate and attenuates PKC-induced SERT downregulation. Yeast two-hybrid screen, co-transfection in HEK293 cells, [3H]serotonin uptake assay Biochemical and biophysical research communications Medium 12051706
2006 MacMARCKS binds to the cytoplasmic C-terminal tail of metabotropic glutamate receptor 7 (mGluR7); binding is antagonized by Ca2+/calmodulin. Co-transfection of MacMARCKS with mGluR7 reduces G-protein-mediated tonic inhibition of voltage-sensitive Ca2+ channels (VSCCs), an effect dependent on MacMARCKS–mGluR7 interaction. Yeast two-hybrid, in vitro pulldown, co-immunoprecipitation, colocalization in transfected HEK293 and cerebellar granule cells, electrophysiology (VSCC inhibition) Journal of neurochemistry High 16987251
2012 JNK directly phosphorylates MARCKSL1 on C-terminal residues S120, T148, and T183. Phosphorylation by JNK enables MARCKSL1 to bundle and stabilize F-actin, increase filopodium numbers/dynamics, and retard cell migration. Conversely, non-phosphorylatable MARCKSL1 enhances lamellipodia formation and cell migration while reducing filopodia. This mechanism operates in neurons and prostate cancer cells. In vitro kinase assay (JNK phosphorylation), site-directed mutagenesis (S120A/T148A/T183A and S120D/T148D/T183D), F-actin bundling/stabilization assay, live-cell imaging of filopodia/lamellipodia, migration assay (neurons and prostate cancer cells), siRNA knockdown Molecular and cellular biology High 22751924
2014 LOXL2 interacts with MARCKSL1 via its scavenger-receptor domain binding to the N-terminal domain of MARCKSL1; LOXL2 promotes cell proliferation by inhibiting MARCKSL1-induced apoptosis, and MARCKSL1 suppresses LOXL2-induced oncogenesis and reduces luciferase reporter activity in a dose-dependent manner. Co-immunoprecipitation, domain-mapping pulldown assays, luciferase reporter assay, flow cytometry (cell cycle/apoptosis), siRNA knockdown Cellular signalling Medium 24863880
2015 MARCKSL1 suppresses angiogenesis by interacting with VEGFR-2 and inhibiting VEGF-induced phosphorylation of VEGFR-2 and downstream PI3K/Akt/PDK-1/mTOR signaling; it reduces VEGF-induced HUVEC proliferation and tubular structure formation in vitro, and decreases HIF-1α and VEGF expression. HUVEC proliferation assay, tube formation assay, Western blot for VEGFR-2 phosphorylation and downstream kinase phosphorylation, MARCKSL1 overexpression Oncology reports Medium 26555156
2018 MARCKSL1 overexpression in the amygdala increases dendritic spine formation in the central amygdala and elevates HPA axis activity and anxiety-like behaviors; knockdown of MARCKSL1 specifically in the amygdala normalizes both HPA axis activity and anxiety behaviors in transgenic mice. MARCKSL1 transgenic mice, site-specific knockdown in amygdala, behavioral assays (anxiety), spine morphology analysis, corticotropin-releasing hormone dependence assay EBioMedicine Medium 29580842
2019 VPA-induced transcriptional downregulation of MARCKSL1 (an actin-stabilizing protein) underlies impairment of dendritic morphology and functional properties in developing but not mature human neurons; these effects are mediated through HDAC and GSK-3 pathway inhibition. Direct reprogramming of human neurons, VPA treatment, RNA sequencing, dendritic morphology quantification, functional electrophysiology, pathway inhibitor experiments Cell stem cell Medium 31155484
2020 Marcksl1 modulates the mechanical properties of the endothelial cell cortex to regulate cell shape and vessel diameter during angiogenesis. Overexpression increases EC size, microvessel diameter, and induces ectopic blebbing suppressed by reduced blood flow; Marcksl1 promotes formation of linear actin bundles and decreases branched actin density at the cortex. In vivo overexpression/depletion in zebrafish, high-resolution live imaging, actin network analysis, microvessel diameter quantification, blood flow manipulation Nature communications High 33127887
2022 MARCKSL1 promotes esophageal squamous cell carcinoma cell migration and invasion by interacting with F-actin and cortactin to regulate invadopodia formation and extracellular matrix degradation. siRNA knockdown and overexpression, immunofluorescence colocalization of F-actin and cortactin, gelatin degradation assay, Transwell/wound-healing assays, RNA sequencing Cancer medicine Medium 35894387
2023 Endothelial JNK1 (but not JNK2) is activated by neutrophil adhesion and phosphorylates MARCKSL1 to promote formation of apical filopodia; these filopodia facilitate adhesion of secondary neutrophils and establish transmigration hotspots. Chemical JNK inhibition prevents neutrophil adhesion. Kinase translocation reporters, FRET-based Cdc42 biosensors, JNK1/JNK2 specific inhibition/knockdown, MARCKSL1 knockdown, live-cell imaging of filopodia, neutrophil adhesion assay iScience Medium 37559902
2025 MARCKSL1 promotes EV secretion from the plasma membrane (in part at the expense of late endosome-PM fusion); MARCKSL1 collaborates with PM-bridging cytoskeletal components (e.g., Radixin) and SNARE-associated proteins (e.g., STXBP3) in this process, as identified by CRISPR activation screen and genomic activation/ablation with microscopic and proteomic follow-up. Genome-wide CRISPR activation screen (CD63 surface levels), genomic activation/ablation, electron microscopy, proteomics, co-immunoprecipitation/interaction studies with Radixin and STXBP3 bioRxivpreprint Medium bio_10.1101_2025.07.24.665424
2026 MARCKSL1 expression in dendritic cells is upregulated by TGF-β1 and is required for dendritic cell-mediated promotion of fibroblast differentiation into myofibroblasts during wound healing; MARCKSL1 shRNA knockdown in dendritic cells diminishes their ability to induce myofibroblast differentiation, and systemic MANS peptide inhibition attenuates scar formation in vivo. TGF-β1 stimulation of mouse dendritic cells, MARCKSL1 shRNA knockdown, co-culture with fibroblasts, myofibroblast differentiation assay, MANS peptide treatment in mouse wound model, single-cell RNA sequencing Wound repair and regeneration Medium 41782175

Source papers

Stage 0 corpus · 35 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1992 MacMARCKS, a novel member of the MARCKS family of protein kinase C substrates. Cell 117 1516135
1996 Disruption of the MacMARCKS gene prevents cranial neural tube closure and results in anencephaly. Proceedings of the National Academy of Sciences of the United States of America 81 8692805
1996 Neural tube defects and abnormal brain development in F52-deficient mice. Proceedings of the National Academy of Sciences of the United States of America 79 8700893
2012 c-Jun N-terminal kinase phosphorylation of MARCKSL1 determines actin stability and migration in neurons and in cancer cells. Molecular and cellular biology 76 22751924
1992 Characteristics of the F52 protein, a MARCKS homologue. The Journal of biological chemistry 70 1618855
1995 MacMARCKS mutation blocks macrophage phagocytosis of zymosan. The Journal of biological chemistry 55 7629059
2022 MARCKSL1-2 reverses docetaxel-resistance of lung adenocarcinoma cells by recruiting SUZ12 to suppress HDAC1 and elevate miR-200b. Molecular cancer 48 35864549
2019 Direct Reprogramming of Human Neurons Identifies MARCKSL1 as a Pathogenic Mediator of Valproic Acid-Induced Teratogenicity. Cell stem cell 45 31155484
1996 Role of MacMARCKS in integrin-dependent macrophage spreading and tyrosine phosphorylation of paxillin. The Journal of biological chemistry 45 8662782
2002 Interaction of the C-terminal region of the rat serotonin transporter with MacMARCKS modulates 5-HT uptake regulation by protein kinase C. Biochemical and biophysical research communications 38 12051706
2020 MARCKSL1 promotes the proliferation, migration and invasion of lung adenocarcinoma cells. Oncology letters 33 32194726
2014 Lysyl oxidase-like 2 (LOXL2) controls tumor-associated cell proliferation through the interaction with MARCKSL1. Cellular signalling 33 24863880
1998 MacMARCKS is not essential for phagocytosis in macrophages. The Journal of biological chemistry 30 9837946
2020 Marcksl1 modulates endothelial cell mechanoresponse to haemodynamic forces to control blood vessel shape and size. Nature communications 28 33127887
2018 Withdrawal:The long noncoding RNA lncZic2 drives the self-renewal of liver tumor-initiating cells via the protein kinase C substrates MARCKS and MARCKSL1. The Journal of biological chemistry 25 29588366
1998 Identification of the basolateral targeting determinant of a peripheral membrane protein, MacMARCKS, in polarized cells. Current biology : CB 23 9637918
1996 Stimulus-dependent phosphorylation of MacMARCKS, a protein kinase C substrate, in nerve termini and PC12 cells. The Journal of biological chemistry 23 8557647
2021 METTL14-Mediated miR-30c-1-3p Maturation Represses the Progression of Lung Cancer via Regulation of MARCKSL1 Expression. Molecular biotechnology 19 34586620
2006 MacMARCKS interacts with the metabotropic glutamate receptor type 7 and modulates G protein-mediated constitutive inhibition of calcium channels. Journal of neurochemistry 19 16987251
2015 MARCKSL1 exhibits anti-angiogenic effects through suppression of VEGFR-2-dependent Akt/PDK-1/mTOR phosphorylation. Oncology reports 15 26555156
1999 Mechanisms of regulation of the MacMARCKS gene in macrophages by bacterial lipopolysaccharide. Journal of leukocyte biology 15 10496325
2001 In vivo interaction between dynamitin and MacMARCKS detected by the fluorescent resonance energy transfer method. The Journal of biological chemistry 13 11278693
2000 Expression of MacMARCKS restores cell adhesion to ICAM-1-coated surface. Cell adhesion and communication 13 10830615
1999 Phosphorylated form of MacMARCKS is essential to LFA-1-dependent cell-cell adhesion of U937 monocytic cells. Journal of cellular physiology 12 10497314
2018 MARCKSL1 Regulates Spine Formation in the Amygdala and Controls the Hypothalamic-Pituitary-Adrenal Axis and Anxiety-Like Behaviors. EBioMedicine 10 29580842
2023 Emerging role of microRNAs as regulators of protein kinase C substrate MARCKS and MARCKSL1 in cancer. Experimental cell research 8 38104645
2022 IncRNA TYMSOS Promotes Epithelial-Mesenchymal Transition and Metastasis in Thyroid Carcinoma through Regulating MARCKSL1 and Activating the PI3K/Akt Signaling Pathway. Critical reviews in eukaryotic gene expression 8 36374807
2022 MARCKSL1 interacted with F-actin to promote esophageal squamous cell carcinoma mobility by modulating the formation of invadopodia. Cancer medicine 7 35894387
2002 Ammonia assimilation in Klebsiella pneumoniae F-5-2 that can utilize ammonium and nitrate ions simultaneously: purification and characterization of glutamate dehydrogenase and glutamine synthetase. Journal of bioscience and bioengineering 7 16233253
2023 Primary adhered neutrophils increase JNK1-MARCKSL1-mediated filopodia to promote secondary neutrophil transmigration. iScience 6 37559902
2023 Circulating extracellular vesicle-derived MARCKSL1 is a potential diagnostic non-invasive biomarker in metastatic colorectal cancer patients. Scientific reports 5 37340044
2007 The regulation of MacMARCKS expression by integrin beta3. Experimental cell research 5 17292354
2025 Roles of MARCKSL1, MCM6, RFC4, and PLAU genes in esophageal cancer and their association with radiotherapy response. Scientific reports 2 40603489
2025 Changes in the Aqueous Solvent do not Impact the Internal Ring-Flip Dynamic of Fully Buried F52 in Protein GB1. Chembiochem : a European journal of chemical biology 1 40375829
2026 Dendritic Cell-Associated MARCKSL1 Regulates Fibroblast Differentiation During Wound Healing. Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society 0 41782175

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