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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 requested target is unambiguously human LYN proto-oncogene, Src-family tyrosine kinase—the protein represented by UniProt P07948, not a similarly named gene or product. The literature agrees with the supplied annotation: LYN is an intracellular, membrane-associated, non-receptor protein-tyrosine kinase with SH4, unique, SH3, SH2 and catalytic SH1 domains. Alternative splicing produces LynA/p56 and LynB/p53. The unrelated product name “Oral-lyn” refers to oral insulin and was excluded. (weerawarna2023lynkinasestructure pages 1-3, l’estrangestranieri2024thedualisticrole pages 2-4, williams2009crystalstructuresof pages 1-1)
LYN’s primary biochemical function is ATP-dependent phosphorylation of tyrosine residues in receptor-associated and cytosolic proteins. Its defining physiological role is not simply to turn immune signaling on: at the plasma-membrane cytosolic leaflet, LYN initiates ITAM-dependent signaling but also phosphorylates ITIMs that recruit SHP and SHIP phosphatases. It therefore establishes both the initial signal and its inhibitory threshold. This duality explains why either loss or constitutive activation can produce inflammatory or lupus-like disease. (weerawarna2023lynkinasestructure pages 8-10, l’estrangestranieri2024thedualisticrole pages 4-6, l’estrangestranieri2024thedualisticrole pages 1-2)
The strongest recent human functional evidence is a 2023 study of three boys with de novo activating variants affecting the inhibitory C-terminal Tyr508 region. Their neonatal systemic inflammation, neutrophilic vasculitis and liver fibrosis directly demonstrate the importance of LYN autoinhibition in humans. A 2024 review, however, concluded that common SLE evidence remains heterogeneous. A separate 2024 study identified LYN/Src-family inhibition as a contributor to the in-vitro antiviral effects of several nominal FGFR inhibitors, but this is not yet a clinical application. (l’estrangestranieri2024thedualisticrole pages 9-10, stefanova2024fgfreceptorkinase pages 14-15, jesus2023constitutivelyactivelyn pages 6-7, jesus2023constitutivelyactivelyn pages 2-3)
| Topic | High-confidence conclusion | Key evidence/model | Interpretation/caveat |
|---|---|---|---|
| Identity, isoforms, domains | The target is human LYN (UniProt P07948), a Src-family non-receptor tyrosine kinase—not an ambiguous namesake. Alternative splicing produces LynA/p56 and LynB/p53; LynA is 512 aa and contains a 21-aa N-terminal insert. Architecture: lipidated SH4 → unique region → SH3 → SH2 → SH1 kinase domain. (weerawarna2023lynkinasestructure pages 1-3, l’estrangestranieri2024thedualisticrole pages 2-4) | Concordant structural and immunological reviews; Lyn kinase-domain crystallography confirms canonical Src-family organization. (williams2009crystalstructuresof pages 1-1) | “Oral-lyn” insulin is an unrelated product name and must not be conflated with the LYN gene. |
| Catalytic reaction and substrate specificity | LYN catalyzes ATP-dependent transfer of phosphate to protein tyrosine residues: protein-Tyr + ATP → protein-phospho-Tyr + ADP. Peptide profiling indicates preferences for acidic residues around −2/−3 and hydrophobic or neutral residues at +2 to +4, but specificity overlaps with BLK, SRC and SYK. (weerawarna2023lynkinasestructure pages 1-3, schmitz1996catalyticspecificityof pages 5-8) | Phage-display-derived peptides and biochemical kinase assays showed that a LYN-selected peptide was efficiently phosphorylated by LYN, but also by SYK. (schmitz1996catalyticspecificityof pages 5-8) | Physiological specificity is determined not only by the local peptide motif but also by membrane colocalization, receptor docking, and SH2/SH3 interactions; no unique “LYN-only” consensus substrate is established. |
| Regulation and localization | N-terminal myristoylation and palmitoylation anchor LYN mainly to the cytoplasmic leaflet of the plasma membrane and lipid rafts; Golgi and nuclear pools are also reported. Autophosphorylation of Tyr397 activates LYN, whereas Csk/Chk phosphorylation of Tyr508 stabilizes SH2-mediated autoinhibition; SH3 binding to the SH2–kinase linker further closes the enzyme. (weerawarna2023lynkinasestructure pages 1-3, ingley2012functionsofthe pages 1-2, l’estrangestranieri2024thedualisticrole pages 2-4) | Structural analysis and mutational/localization studies support the closed Src-family conformation and lipidation-dependent compartmentalization. (williams2009crystalstructuresof pages 1-1) | LYN is membrane-associated but not transmembrane. Localization is dynamic and cell-state dependent; nuclear/Golgi functions are less firmly characterized than plasma-membrane signaling. |
| Activating BCR/ITAM signaling | After B-cell receptor aggregation, LYN phosphorylates Igα/Igβ ITAMs, enabling SYK recruitment and activation. Downstream signaling engages PI3K, BTK, PLCγ, IP3/Ca²⁺, MAPK, NF-κB and Akt. (weerawarna2023lynkinasestructure pages 8-10, l’estrangestranieri2024thedualisticrole pages 2-4) | Mechanistic B-cell studies and immune-signaling reviews; LYN also phosphorylates ITAM-associated Fc receptors in myeloid cells. (l’estrangestranieri2024thedualisticrole pages 2-4, l’estrangestranieri2024thedualisticrole pages 4-6) | Positive initiation is partly redundant with other Src-family kinases such as FYN; LYN’s less-redundant physiological contribution is often inhibitory feedback. |
| Inhibitory FcγRIIB/ITIM signaling | LYN phosphorylates the FcγRIIB ITIM, recruiting SHIP1; reduced PIP3 then limits membrane recruitment of BTK/PLCγ and suppresses Ca²⁺ signaling. LYN also phosphorylates ITIM receptors such as PIR-B/LILRB, SIRPα, PECAM1 and CEACAM1, recruiting SHP-1, SHP-2 and/or SHIP phosphatases. (weerawarna2023lynkinasestructure pages 8-10, l’estrangestranieri2024thedualisticrole pages 4-6, l’estrangestranieri2024thedualisticrole pages 8-9) | Receptor-coligation experiments, immune-cell genetics and Lyn-deficient mouse phenotypes support this negative-feedback role. | ITAM phosphorylation can also generate inhibitory “ITAMi” signaling under partial or monovalent receptor engagement; the outcome depends on receptor, ligand geometry and cell type. (weerawarna2023lynkinasestructure pages 1-3, weerawarna2023lynkinasestructure pages 8-10) |
| 2023 human gain-of-function disease | Three unrelated boys had perinatal systemic inflammation and neutrophilic small-vessel vasculitis caused by de novo activating variants p.Q507*, p.Y508F, or p.Y508*. Patient CRP ranges were 14–86.5, 46–166, and 6.5–107.6 mg/L; two developed early liver fibrosis. (jesus2023constitutivelyactivelyn pages 2-3, jesus2023constitutivelyactivelyn pages 1-2, jesus2023constitutivelyactivelyn pages 11-12) | Mutants lacked normal Tyr508-tail inhibition and showed constitutive Tyr397 phosphorylation. Patient-derived endothelial cells exhibited increased ICAM-1, neutrophil adhesion and transmigration; dasatinib or TNF inhibition reduced several abnormalities. In one patient, 30 months of dasatinib monotherapy accompanied bile-duct recovery and regression of fibrosis. (jesus2023constitutivelyactivelyn pages 6-7, jesus2023constitutivelyactivelyn pages 7-9) | Strong genotype–mechanism evidence, but only three patients and uncontrolled compassionate treatment; dasatinib inhibits multiple kinases, so clinical improvement cannot be assigned exclusively to LYN inhibition. |
| 2024 SLE evidence | Human SLE data are heterogeneous: several studies report reduced B-cell LYN protein/mRNA and increased ubiquitination, whereas transcriptomic datasets report increased LYN RNA in antibody-secreting cells or blood. Protective associations reported for rs7829816 (OR 0.77) and rs2667978 (OR 0.81) in European-ancestry women; rs6983130 associated with hematologic SLE and anti-dsDNA/anti-Sm antibodies. (l’estrangestranieri2024thedualisticrole pages 8-9, l’estrangestranieri2024thedualisticrole pages 9-10) | A 2024 expert review integrates human genetics/expression with mouse findings that both Lyn deficiency and constitutive activation can produce lupus-like disease. (l’estrangestranieri2024thedualisticrole pages 1-2) | Associations are noncoding and incompletely functionally annotated; RNA and protein findings conflict, myeloid cells are under-sampled, and direct LYN inhibition could worsen rather than improve disease in some biological subsets. |
| 2024 antiviral study | Several nominal FGFR inhibitors showed in-vitro antiviral activity partly through Src-family inhibition, particularly LYN. AZD4547 inhibited Lyn Tyr397 phosphorylation and recombinant LynA at approximately 5–10 µM; antiviral activity required roughly 1–10 µM, versus about 0.1 µM for canonical FGFR-pathway inhibition. (stefanova2024fgfreceptorkinase pages 14-15, stefanova2024fgfreceptorkinase pages 11-14) | Experiments included HSV-1 in HaCaT and primary human keratinocytes and HCoV-229E in Huh7 cells. LYN siRNA reduced viral release and weakened or abolished later AZD4547 effects; the pan-SFK inhibitor AZD0530 phenocopied antiviral activity. (stefanova2024fgfreceptorkinase pages 14-15, stefanova2024fgfreceptorkinase pages 15-18, stefanova2024fgfreceptorkinase pages 1-2) | Preclinical repurposing hypothesis only. Incomplete knockdown, residual drug activity, micromolar exposures and other SFKs prevent attribution to LYN alone; no clinical antiviral efficacy was demonstrated. |
| Inhibitors and clinical translation | Dasatinib, PP2, AZD0530 and bafetinib bind or inhibit LYN, but available compounds are multi-kinase inhibitors. Crystal structures show PP2 and dasatinib occupying the ATP site and an adjacent hydrophobic pocket. (williams2009crystalstructuresof pages 1-1) | Bafetinib, described as a dual BCR-ABL/LYN inhibitor, entered a completed Phase 1 study in recurrent high-grade glioma or brain metastases (NCT01234740; enrollment 7). (NCT01234740 chunk 2) | There is no established LYN-selective approved therapy or validated LYN-specific clinical indication. Small trial size, absent efficacy evidence in the retrieved record, blood–brain exposure concerns and broad kinase inhibition limit conclusions; monogenic LYN disease currently provides the clearest precision-treatment rationale. |
Table: Compact evidence matrix covering the verified identity, molecular function, localization, pathways, recent disease findings, and translational status of human LYN (UniProt P07948). Quantitative findings are paired with model and interpretation caveats.
The literature identifies LYN as “Lck/Yes-related novel tyrosine kinase,” a Src-family non-receptor protein-tyrosine kinase expressed prominently in hematopoietic cells and also in selected nonhematopoietic cells. This matches the supplied human UniProt P07948 description, alternative names p53Lyn/p56Lyn and gene synonym JTK8. No evidence was found that the query had retrieved a different organism or a different gene with the same symbol. (weerawarna2023lynkinasestructure pages 1-3, l’estrangestranieri2024thedualisticrole pages 2-4)
Current human nomenclature databases represented through Open Targets identify the corresponding gene as LYN proto-oncogene, Src family tyrosine kinase, Ensembl ENSG00000254087. Disease-association data link this same target to cancer, CML, ALL, neurodegenerative disease and systemic autoinflammatory vasculitis, although database association scores do not themselves prove causality. (OpenTargets Search: -LYN)
Humans express two major splice isoforms:
The apparent 20-versus-21-residue wording in older sources reflects counting/annotation conventions, not a different protein identity. Both forms contain the canonical Src-family organization: SH4 membrane-targeting segment → unique domain → SH3 domain → SH2 domain → SH1 protein-kinase domain → short C-terminal regulatory tail. This directly aligns with the supplied InterPro kinase, Lyn-SH2 and Lyn-SH3 annotations. (weerawarna2023lynkinasestructure pages 1-3, ingley2012functionsofthe pages 1-2, l’estrangestranieri2024thedualisticrole pages 2-4)
LYN is an EC 2.7.10.2 non-receptor protein-tyrosine kinase. Its net reaction is:
ATP + protein-L-tyrosine → ADP + protein-O-phospho-L-tyrosine.
The kinase domain binds ATP/Mg²⁺ and transfers the γ-phosphate to a substrate tyrosine hydroxyl group. The product phosphotyrosine can alter catalytic activity or create docking sites for SH2- and PTB-domain proteins. LYN is thus a signaling enzyme rather than a transporter, structural protein or extracellular ligand. Structural work showed the isolated kinase domain in an active-like conformation and demonstrated binding of AMP-PNP, PP2 and dasatinib in the ATP pocket; PP2 and dasatinib also extend into an adjacent hydrophobic pocket. (weerawarna2023lynkinasestructure pages 1-3, williams2009crystalstructuresof pages 1-1)
LYN does not have one exclusive substrate. Biochemical peptide selection found preferences shared by several tyrosine kinases: acidic residues are favored around positions −2/−3 relative to the phosphoacceptor Tyr, while neutral or hydrophobic residues are preferred around +2 to +4; basic residues were disfavored. A phage-selected LYN peptide was efficiently phosphorylated by LYN but also by BLK and SYK, demonstrating overlapping intrinsic specificity. Reported apparent Km values were 24 mM for LYN, 28 mM for BLK, 37 mM for SRC and 17 mM for SYK with that peptide, although the unusually high peptide concentrations and historical assay format limit direct physiological interpretation. (schmitz1996catalyticspecificityof pages 5-8)
Consequently, physiological specificity is predominantly combinatorial: local peptide sequence plus membrane colocalization, receptor clustering, SH2 recognition of pre-existing phosphotyrosine, SH3 recognition of proline-rich partners and scaffold/adaptor interactions. Established substrate classes include BCR Igα/Igβ ITAMs, Fc-receptor ITAMs and ITIMs, inhibitory receptors, SYK, PI3K-associated proteins, PLCγ2, Cbp/PAG1, STAT5 and cytoskeletal or adhesion regulators. (weerawarna2023lynkinasestructure pages 8-10, williams2009crystalstructuresof pages 1-1, l’estrangestranieri2024thedualisticrole pages 4-6)
Two conserved phosphorylation sites dominate LYN regulation:
Tail engagement by SH2, together with SH3 binding to the proline-rich SH2–kinase linker, produces the compact autoinhibited conformation. Dephosphorylation of Tyr508 by receptor-like phosphatases including CD45 or CD148 permits opening; subsequent Tyr397 autophosphorylation raises activity. The kinase domain’s DFG motif and αC helix adopt active “in” arrangements in the active state. (weerawarna2023lynkinasestructure pages 1-3, ingley2012functionsofthe pages 1-2, l’estrangestranieri2024thedualisticrole pages 2-4, williams2009crystalstructuresof pages 1-1)
This model is strongly validated in humans by activating variants that remove Tyr508 or prevent its phosphorylation. The p.Q507, p.Y508 and p.Y508F variants produce constitutive Tyr397 phosphorylation and downstream-substrate phosphorylation. (jesus2023constitutivelyactivelyn pages 2-3, jesus2023constitutivelyactivelyn pages 11-12)
Cbp/PAG1-associated CSK helps restrain raft-localized LYN. Phosphorylation within the LYN SH2 domain, including Tyr194, can alter phosphopeptide-binding affinity and specificity, adding another layer of regulation. Ubiquitination and degradation also affect LYN abundance; increased ubiquitination has been reported in B cells from some SLE cohorts. (ingley2012functionsofthe pages 1-2, l’estrangestranieri2024thedualisticrole pages 9-10)
LYN is not a transmembrane protein. N-terminal myristoylation and palmitoylation of the SH4 region attach it to the cytoplasmic leaflet of the plasma membrane and enrich it in cholesterol/sphingolipid-associated signaling microdomains commonly termed lipid rafts. This location places LYN next to clustered BCRs, Fc receptors, growth-factor receptors and inhibitory coreceptors. (weerawarna2023lynkinasestructure pages 1-3, ingley2012functionsofthe pages 1-2)
The predominant functional pool is plasma-membrane associated, but Golgi and nuclear pools have been reported. Golgi localization can change during oxidative stress, and nuclear LYN has been linked to DNA-damage responses. These secondary compartments are less comprehensively defined than membrane immunoreceptor signaling and should not be treated as the protein’s principal location. (l’estrangestranieri2024thedualisticrole pages 2-4, l’estrangestranieri2024thedualisticrole pages 4-6)
After antigen-induced BCR clustering, raft-associated LYN phosphorylates tyrosines in the ITAMs of CD79A/Igα and CD79B/Igβ. Doubly phosphorylated ITAMs recruit SYK through its tandem SH2 domains. SYK and LYN then promote signaling through PI3K, BTK and PLCγ2, generating IP3, mobilizing intracellular Ca²⁺ and activating MAPK, NF-κB and Akt pathways. These outputs control B-cell activation, survival, antigen processing and differentiation. (weerawarna2023lynkinasestructure pages 8-10, l’estrangestranieri2024thedualisticrole pages 2-4)
Positive initiation is partly redundant: FYN and other Src-family kinases can phosphorylate ITAMs when LYN is absent. LYN’s inhibitory function is less readily replaced, explaining the counterintuitive BCR hyperresponsiveness of Lyn-deficient mouse B cells. (weerawarna2023lynkinasestructure pages 8-10, l’estrangestranieri2024thedualisticrole pages 8-9)
When BCR is co-ligated with FcγRIIB, LYN phosphorylates the receptor’s ITIM. The ITIM recruits SHIP1, which dephosphorylates PI(3,4,5)P3 and thereby limits membrane recruitment of BTK and PLCγ, suppressing Ca²⁺ flux and B-cell activation. LYN can likewise phosphorylate inhibitory receptors such as PIR-B/LILRB and SIRPα, recruiting SHP-1, SHP-2 and/or SHIP phosphatases. (weerawarna2023lynkinasestructure pages 8-10)
This establishes a mechanistic interpretation of LYN as a receptor-proximal rheostat. Strong or appropriately clustered receptor signals can yield conventional activating ITAM phosphorylation, whereas partial or monovalent engagement can produce inhibitory ITAMi signaling, favoring SHP-1 rather than SYK recruitment. (weerawarna2023lynkinasestructure pages 1-3, weerawarna2023lynkinasestructure pages 8-10)
In macrophages, neutrophils, dendritic cells and mast cells, LYN couples Fc receptors, integrins, growth-factor receptors and innate receptors to both activation and feedback inhibition. Inhibitory substrates include PECAM1 and CEACAM1 ITIMs, which recruit SHP-family phosphatases. Mouse genetics indicate that LYN constrains TLR, integrin and growth-factor signaling and that MyD88/TLR signals contribute substantially to inflammatory disease in Lyn-deficient animals. LYN can also bind and suppress IRF5 downstream of TLR7/9 through a mechanism with a kinase-independent component. (l’estrangestranieri2024thedualisticrole pages 4-6, l’estrangestranieri2024thedualisticrole pages 8-9, l’estrangestranieri2024thedualisticrole pages 9-10, scapini2009multiplerolesof pages 5-6)
In mast cells, LYN can phosphorylate FcεRI ITAMs and initiate SYK-dependent activation, but it simultaneously engages inhibitory circuits. Thus its net effect varies with stimulus strength, timing, genetic background and the activity of other Src kinases such as FYN and HCK. This context dependence is experimentally real, rather than an annotation inconsistency. (l’estrangestranieri2024thedualisticrole pages 4-6)
LYN participates in signaling downstream of c-KIT, erythropoietin and thrombopoietin receptors and contributes to platelet, erythroid, endothelial and neuronal signaling. In human erythrocytes, sequential phosphorylation provides a precise example: SYK first phosphorylates band 3 at Tyr8 and Tyr21, enabling SH2-dependent LYN recruitment; LYN then phosphorylates Tyr359 and Tyr904. (williams2009crystalstructuresof pages 1-1, schmitz1996catalyticspecificityof pages 5-8)
In Alzheimer-related experimental systems, Aβ oligomers activated LYN through neuronal FcγRIIb2, leading to ITIM Tyr273 phosphorylation, SHIP2 recruitment and tau-related toxicity. Human AD hippocampal samples reportedly showed approximately threefold higher LYN Tyr397 phosphorylation than controls, but the causal and therapeutic implications remain preclinical. (weerawarna2023lynkinasestructure pages 12-13)
The best-supported systems-level function is setting the amplitude and duration of receptor-proximal signaling, particularly in B and myeloid cells. LYN’s kinase activity generates activating phosphotyrosine docking sites, but also creates inhibitory sites that recruit lipid and protein phosphatases. This explains three otherwise paradoxical findings:
Expert reviews therefore caution against classifying LYN simply as pro-inflammatory or anti-inflammatory. Its effect depends on receptor identity, phosphorylation geometry, cell type, subcellular compartment, isoform and timing. (weerawarna2023lynkinasestructure pages 1-3, l’estrangestranieri2024thedualisticrole pages 2-4)
A March 2023 Nature Communications study identified three unrelated boys with neonatal-onset systemic inflammation and de novo variants p.Q507, p.Y508F or p.Y508**. The truncations remove the inhibitory tail, while Y508F prevents inhibitory phosphorylation. All three developed recurrent neutrophilic small-vessel vasculitis; two developed early liver fibrosis. Reported CRP ranges were 14–86.5, 46–166 and 6.5–107.6 mg/L, respectively; liver elastography reached 6.7 and 18.7 kPa in two patients. (jesus2023constitutivelyactivelyn pages 2-3, jesus2023constitutivelyactivelyn pages 1-2)
Patient-derived induced endothelial cells displayed prolonged ICAM1/E-selectin responses, impaired VE-cadherin barrier integrity and increased neutrophil adhesion and transendothelial migration. Mutant endothelial cells supported greater adhesion than isogenic-corrected and healthy-control cells, with reported p=0.0058 and p=0.0019; dasatinib and TNF inhibition reduced transmigration, with p=0.0158 and p=0.0496. Genetic correction normalized barrier resistance more completely than pharmacological treatment. (jesus2023constitutivelyactivelyn pages 6-7, jesus2023constitutivelyactivelyn pages 7-9)
Clinically, TNF inhibition improved systemic inflammation. In one patient, compassionate dasatinib progressively normalized inflammatory and liver measures; withdrawal was followed by recurrent rash and inflammation, and 30 months of monotherapy accompanied bile-duct reconstitution and regression of fibrosis. This is compelling precision-medicine evidence, but it remains an uncontrolled observation in one patient, and dasatinib is a broad kinase inhibitor. [Published March 2023; DOI/URL: https://doi.org/10.1038/s41467-023-36941-y.] (jesus2023constitutivelyactivelyn pages 6-7)
A June 2024 Frontiers in Immunology review concluded that both inadequate and excessive LYN signaling can disrupt immune tolerance. Human SLE studies are inconsistent: several report lower LYN protein or mRNA and increased ubiquitination in circulating B cells, whereas transcriptomic studies report elevated LYN RNA in antibody-secreting cells, whole blood or pediatric SLE, sometimes correlated with type-I-interferon signatures or disease activity. Protein-level confirmation of the latter observations is limited, and myeloid cells are underrepresented. [Published June 2024; DOI/URL: https://doi.org/10.3389/fimmu.2024.1395427.] (l’estrangestranieri2024thedualisticrole pages 1-2, l’estrangestranieri2024thedualisticrole pages 9-10)
Reported genetic associations include protective effects for rs7829816 (OR 0.77) and rs2667978 (OR 0.81) in European-ancestry women and association of rs6983130 with hematologic SLE and anti-dsDNA/anti-Sm antibodies. These are noncoding variants with incomplete functional annotation and weaker evidence than the rare activating Tyr508-region mutations. (l’estrangestranieri2024thedualisticrole pages 8-9, l’estrangestranieri2024thedualisticrole pages 9-10)
A May 2024 Nature study systematically profiled the intrinsic peptide specificity of the human tyrosine kinome. Its broader significance for LYN annotation is conceptual: kinase motifs help rank candidate sites, but cellular substrates are selected jointly by intrinsic sequence preference and interaction/localization networks. This supports avoiding overconfident assignment of high-throughput phosphosites to LYN solely from motif similarity. [Published May 2024; DOI/URL: https://doi.org/10.1038/s41586-024-07407-y.]
A December 2024 Cellular and Molecular Life Sciences study found that several FGFR1–3 inhibitors suppressed DNA- and RNA-virus infection largely independently of canonical FGFR blockade. Kinome analysis identified Src-family kinases, particularly LYN, as candidate off-target mediators. In HaCaT keratinocytes and primary human keratinocytes, AZD4547 suppressed LYN Tyr397 phosphorylation; recombinant LynA was directly inhibited. LYN knockdown reduced extracellular HSV-1 DNA and weakened or abolished the later antiviral effect of AZD4547. The pan-SFK inhibitor AZD0530 reproduced much of the phenotype; HCoV-229E infection in Huh7 cells was also reduced. (stefanova2024fgfreceptorkinase pages 14-15, stefanova2024fgfreceptorkinase pages 11-14, stefanova2024fgfreceptorkinase pages 15-18)
The dose relationship is important: antiviral and LYN-inhibitory effects generally required approximately 1–10 µM, compared with about 0.1 µM for canonical FGFR signaling inhibition. Incomplete knockdown, residual drug activity and effects on other Src-family kinases mean the data identify a LYN/SFK-dependent mechanism, not a uniquely LYN-specific one. No human antiviral efficacy was tested. [Published December 2024; DOI/URL: https://doi.org/10.1007/s00018-024-05502-x.] (stefanova2024fgfreceptorkinase pages 14-15, stefanova2024fgfreceptorkinase pages 9-11, stefanova2024fgfreceptorkinase pages 18-19)
Activating germline LYN variants now support a causal disease entity characterized by neonatal systemic inflammation, neutrophilic cutaneous vasculitis, endothelial-barrier dysfunction, thrombocytopenia and variable liver fibrosis. Molecular diagnosis can therefore influence management, including consideration of TNF blockade and, in severe cases, carefully monitored broad Src-family inhibition. Evidence remains limited to very small case series. (jesus2023constitutivelyactivelyn pages 6-7, jesus2023constitutivelyactivelyn pages 2-3, gul2025thepathogenesisclinical pages 5-6)
LYN is central to B-cell tolerance in animal models and is plausibly dysregulated in subsets of human SLE. However, opposing loss- and gain-of-function disease mechanisms mean that an unstratified “LYN inhibitor for lupus” strategy is biologically risky. Expert interpretation favors measuring cell type, protein abundance, activation state and pathway phenotype rather than using bulk-blood LYN RNA alone. (l’estrangestranieri2024thedualisticrole pages 1-2, l’estrangestranieri2024thedualisticrole pages 9-10)
Hyperactive LYN supports survival and drug resistance in subsets of AML, CML and B-cell malignancies, and has been implicated in aggressive breast, prostate, colorectal and brain tumors. In CML models, LYN/SYK signaling contributes to nilotinib resistance; in solid-tumor models, LYN can support Akt survival, migration or invasion. These associations are context-specific and do not establish a universal LYN dependency. (ingley2012functionsofthe pages 7-8, williams2009crystalstructuresof pages 1-1, scapini2009multiplerolesof pages 5-6)
Open Targets aggregates LYN evidence for CML, ALL and cancer, but much clinical-stage evidence comes from multi-target inhibitors such as dasatinib or related BCR-ABL/Src inhibitors. Clinical benefit from those drugs cannot be attributed specifically to LYN. (OpenTargets Search: -LYN)
The 2023 structural review highlights emerging LYN involvement in Aβ/FcγRIIb2/SHIP2 signaling and Chorea-acanthocytosis models. Nilotinib improved autophagy and neuroinflammation in Vps13a-deficient mice, and a broad Src inhibitor reduced Aβ-related toxicity in experimental systems. These are mechanistically interesting but remain preclinical and are confounded by inhibitor polypharmacology. [Published January 2023; DOI/URL: https://doi.org/10.3390/kinasesphosphatases1010004.] (weerawarna2023lynkinasestructure pages 12-13)
Available LYN inhibitors are generally ATP-competitive and poorly selective across Src-family or other kinases. Examples include dasatinib, PP1/PP2, AZD0530/saracatinib, nilotinib and bafetinib. Their utility is therefore usually pathway-level or disease-specific rather than clean pharmacological validation of LYN. (weerawarna2023lynkinasestructure pages 12-13, williams2009crystalstructuresof pages 1-1, stefanova2024fgfreceptorkinase pages 11-14)
Bafetinib was explicitly described as a second-generation dual BCR-ABL/LYN inhibitor in NCT01234740, a completed Phase 1 study in recurrent high-grade glioma or brain metastases. The retrieved registry metadata report only seven participants and did not establish efficacy. Trial URL: https://clinicaltrials.gov/study/NCT01234740. (NCT01234740 chunk 2)
A search also retrieved NCT00827138, a Phase 1 dose-finding study of DCC-2036/rebastinib in Philadelphia-positive leukemia. The available record did not identify LYN as an intended target, so it should not be presented as a LYN-directed trial. Likewise, NCT00668850 “Oral-lyn” is an insulin spray and is unrelated to the LYN gene. (NCT00827138 chunk 2)
As of the assessed literature, there is no established LYN-selective approved drug and no clinically validated LYN-specific indication. The most persuasive current real-world use is individualized treatment of rare activating LYN disease with broad Src-family inhibition, supported by molecular diagnosis and pharmacodynamic monitoring—not routine LYN targeting in cancer, lupus, infection or neurodegeneration.
Human LYN is best annotated as a lipid-anchored Src-family tyrosine kinase that converts receptor clustering into both activating and inhibitory phosphotyrosine signals. At BCRs and Fc receptors it phosphorylates ITAMs to recruit SYK and activate PI3K–BTK–PLCγ/Ca²⁺, MAPK, NF-κB and Akt, while also phosphorylating ITIM-bearing receptors to recruit SHIP1 and SHP-1/2 and terminate or reshape those signals. Its plasma-membrane localization and Tyr397/Tyr508 conformational switch are integral to function, not incidental annotations. (weerawarna2023lynkinasestructure pages 1-3, weerawarna2023lynkinasestructure pages 8-10, williams2009crystalstructuresof pages 1-1)
The 2023 human Tyr508-region mutation study provides unusually direct causal validation: removing C-terminal inhibition causes constitutive LYN signaling, neonatal vasculitis and endothelial/neutrophil pathology, with preliminary evidence for mechanism-guided treatment. The 2024 literature expands LYN’s possible translational scope to SLE stratification and host-directed antiviral therapy, but also reinforces the central caveat: because LYN is both an activator and inhibitor and current drugs are multi-kinase, therapeutic manipulation must be genotype-, cell- and pathway-specific. (l’estrangestranieri2024thedualisticrole pages 1-2, stefanova2024fgfreceptorkinase pages 14-15, jesus2023constitutivelyactivelyn pages 6-7, jesus2023constitutivelyactivelyn pages 2-3)
References
(weerawarna2023lynkinasestructure pages 1-3): Pathum M. Weerawarna and Timothy I. Richardson. Lyn kinase structure, regulation, and involvement in neurodegenerative diseases: a mini review. Kinases and Phosphatases, 1:23-38, Jan 2023. URL: https://doi.org/10.3390/kinasesphosphatases1010004, doi:10.3390/kinasesphosphatases1010004. This article has 20 citations.
(l’estrangestranieri2024thedualisticrole pages 2-4): Elan L’Estrange-Stranieri, Timothy A. Gottschalk, Mark D. Wright, and Margaret L. Hibbs. The dualistic role of lyn tyrosine kinase in immune cell signaling: implications for systemic lupus erythematosus. Frontiers in Immunology, Jun 2024. URL: https://doi.org/10.3389/fimmu.2024.1395427, doi:10.3389/fimmu.2024.1395427. This article has 23 citations and is from a peer-reviewed journal.
(williams2009crystalstructuresof pages 1-1): Neal K. Williams, Isabelle S. Lucet, S. Peter Klinken, Evan Ingley, and Jamie Rossjohn. Crystal structures of the lyn protein tyrosine kinase domain in its apo- and inhibitor-bound state. Journal of Biological Chemistry, 284:284-291, Jan 2009. URL: https://doi.org/10.1074/jbc.m807850200, doi:10.1074/jbc.m807850200. This article has 84 citations and is from a domain leading peer-reviewed journal.
(weerawarna2023lynkinasestructure pages 8-10): Pathum M. Weerawarna and Timothy I. Richardson. Lyn kinase structure, regulation, and involvement in neurodegenerative diseases: a mini review. Kinases and Phosphatases, 1:23-38, Jan 2023. URL: https://doi.org/10.3390/kinasesphosphatases1010004, doi:10.3390/kinasesphosphatases1010004. This article has 20 citations.
(l’estrangestranieri2024thedualisticrole pages 4-6): Elan L’Estrange-Stranieri, Timothy A. Gottschalk, Mark D. Wright, and Margaret L. Hibbs. The dualistic role of lyn tyrosine kinase in immune cell signaling: implications for systemic lupus erythematosus. Frontiers in Immunology, Jun 2024. URL: https://doi.org/10.3389/fimmu.2024.1395427, doi:10.3389/fimmu.2024.1395427. This article has 23 citations and is from a peer-reviewed journal.
(l’estrangestranieri2024thedualisticrole pages 1-2): Elan L’Estrange-Stranieri, Timothy A. Gottschalk, Mark D. Wright, and Margaret L. Hibbs. The dualistic role of lyn tyrosine kinase in immune cell signaling: implications for systemic lupus erythematosus. Frontiers in Immunology, Jun 2024. URL: https://doi.org/10.3389/fimmu.2024.1395427, doi:10.3389/fimmu.2024.1395427. This article has 23 citations and is from a peer-reviewed journal.
(l’estrangestranieri2024thedualisticrole pages 9-10): Elan L’Estrange-Stranieri, Timothy A. Gottschalk, Mark D. Wright, and Margaret L. Hibbs. The dualistic role of lyn tyrosine kinase in immune cell signaling: implications for systemic lupus erythematosus. Frontiers in Immunology, Jun 2024. URL: https://doi.org/10.3389/fimmu.2024.1395427, doi:10.3389/fimmu.2024.1395427. This article has 23 citations and is from a peer-reviewed journal.
(stefanova2024fgfreceptorkinase pages 14-15): Debora Stefanova, Dominik Olszewski, Mirco Glitscher, Michael Bauer, Luca Ferrarese, Daria Wüst, Eberhard Hildt, Urs F. Greber, and Sabine Werner. Fgf receptor kinase inhibitors exhibit broad antiviral activity by targeting src family kinases. Cellular and Molecular Life Sciences: CMLS, Dec 2024. URL: https://doi.org/10.1007/s00018-024-05502-x, doi:10.1007/s00018-024-05502-x. This article has 6 citations.
(jesus2023constitutivelyactivelyn pages 6-7): Adriana A. de Jesus, Guibin Chen, Dan Yang, Tomas Brdicka, Natasha M. Ruth, David Bennin, Dita Cebecauerova, Hana Malcova, Helen Freeman, Neil Martin, Karel Svojgr, Murray H. Passo, Farzana Bhuyan, Sara Alehashemi, Andre T. Rastegar, Katsiaryna Uss, Lela Kardava, Bernadette Marrero, Iris Duric, Ebun Omoyinmi, Petra Peldova, Chyi-Chia Richard Lee, David E. Kleiner, Colleen M. Hadigan, Stephen M. Hewitt, Stefania Pittaluga, Carmelo Carmona-Rivera, Katherine R. Calvo, Nirali Shah, Miroslava Balascakova, Danielle L. Fink, Radana Kotalova, Zuzana Parackova, Lucie Peterkova, Daniela Kuzilkova, Vit Campr, Lucie Sramkova, Angelique Biancotto, Stephen R. Brooks, Cameron Manes, Eric Meffre, Rebecca L. Harper, Hyesun Kuehn, Mariana J. Kaplan, Paul Brogan, Sergio D. Rosenzweig, Melinda Merchant, Zuoming Deng, Anna Huttenlocher, Susan L. Moir, Douglas B. Kuhns, Manfred Boehm, Karolina Skvarova Kramarzova, and Raphaela Goldbach-Mansky. Constitutively active lyn kinase causes a cutaneous small vessel vasculitis and liver fibrosis syndrome. Nature Communications, Mar 2023. URL: https://doi.org/10.1038/s41467-023-36941-y, doi:10.1038/s41467-023-36941-y. This article has 40 citations and is from a highest quality peer-reviewed journal.
(jesus2023constitutivelyactivelyn pages 2-3): Adriana A. de Jesus, Guibin Chen, Dan Yang, Tomas Brdicka, Natasha M. Ruth, David Bennin, Dita Cebecauerova, Hana Malcova, Helen Freeman, Neil Martin, Karel Svojgr, Murray H. Passo, Farzana Bhuyan, Sara Alehashemi, Andre T. Rastegar, Katsiaryna Uss, Lela Kardava, Bernadette Marrero, Iris Duric, Ebun Omoyinmi, Petra Peldova, Chyi-Chia Richard Lee, David E. Kleiner, Colleen M. Hadigan, Stephen M. Hewitt, Stefania Pittaluga, Carmelo Carmona-Rivera, Katherine R. Calvo, Nirali Shah, Miroslava Balascakova, Danielle L. Fink, Radana Kotalova, Zuzana Parackova, Lucie Peterkova, Daniela Kuzilkova, Vit Campr, Lucie Sramkova, Angelique Biancotto, Stephen R. Brooks, Cameron Manes, Eric Meffre, Rebecca L. Harper, Hyesun Kuehn, Mariana J. Kaplan, Paul Brogan, Sergio D. Rosenzweig, Melinda Merchant, Zuoming Deng, Anna Huttenlocher, Susan L. Moir, Douglas B. Kuhns, Manfred Boehm, Karolina Skvarova Kramarzova, and Raphaela Goldbach-Mansky. Constitutively active lyn kinase causes a cutaneous small vessel vasculitis and liver fibrosis syndrome. Nature Communications, Mar 2023. URL: https://doi.org/10.1038/s41467-023-36941-y, doi:10.1038/s41467-023-36941-y. This article has 40 citations and is from a highest quality peer-reviewed journal.
(schmitz1996catalyticspecificityof pages 5-8): Rita Schmitz, Götz Baumann, and Hermann Gram. Catalytic specificity of phosphotyrosine kinases blk, lyn, c-src and syk as assessed by phage display. Journal of molecular biology, 260 5:664-77, Aug 1996. URL: https://doi.org/10.1006/jmbi.1996.0429, doi:10.1006/jmbi.1996.0429. This article has 202 citations and is from a domain leading peer-reviewed journal.
(ingley2012functionsofthe pages 1-2): Evan Ingley. Functions of the lyn tyrosine kinase in health and disease. Cell Communication and Signaling : CCS, 10:21-21, Jul 2012. URL: https://doi.org/10.1186/1478-811x-10-21, doi:10.1186/1478-811x-10-21. This article has 248 citations.
(l’estrangestranieri2024thedualisticrole pages 8-9): Elan L’Estrange-Stranieri, Timothy A. Gottschalk, Mark D. Wright, and Margaret L. Hibbs. The dualistic role of lyn tyrosine kinase in immune cell signaling: implications for systemic lupus erythematosus. Frontiers in Immunology, Jun 2024. URL: https://doi.org/10.3389/fimmu.2024.1395427, doi:10.3389/fimmu.2024.1395427. This article has 23 citations and is from a peer-reviewed journal.
(jesus2023constitutivelyactivelyn pages 1-2): Adriana A. de Jesus, Guibin Chen, Dan Yang, Tomas Brdicka, Natasha M. Ruth, David Bennin, Dita Cebecauerova, Hana Malcova, Helen Freeman, Neil Martin, Karel Svojgr, Murray H. Passo, Farzana Bhuyan, Sara Alehashemi, Andre T. Rastegar, Katsiaryna Uss, Lela Kardava, Bernadette Marrero, Iris Duric, Ebun Omoyinmi, Petra Peldova, Chyi-Chia Richard Lee, David E. Kleiner, Colleen M. Hadigan, Stephen M. Hewitt, Stefania Pittaluga, Carmelo Carmona-Rivera, Katherine R. Calvo, Nirali Shah, Miroslava Balascakova, Danielle L. Fink, Radana Kotalova, Zuzana Parackova, Lucie Peterkova, Daniela Kuzilkova, Vit Campr, Lucie Sramkova, Angelique Biancotto, Stephen R. Brooks, Cameron Manes, Eric Meffre, Rebecca L. Harper, Hyesun Kuehn, Mariana J. Kaplan, Paul Brogan, Sergio D. Rosenzweig, Melinda Merchant, Zuoming Deng, Anna Huttenlocher, Susan L. Moir, Douglas B. Kuhns, Manfred Boehm, Karolina Skvarova Kramarzova, and Raphaela Goldbach-Mansky. Constitutively active lyn kinase causes a cutaneous small vessel vasculitis and liver fibrosis syndrome. Nature Communications, Mar 2023. URL: https://doi.org/10.1038/s41467-023-36941-y, doi:10.1038/s41467-023-36941-y. This article has 40 citations and is from a highest quality peer-reviewed journal.
(jesus2023constitutivelyactivelyn pages 11-12): Adriana A. de Jesus, Guibin Chen, Dan Yang, Tomas Brdicka, Natasha M. Ruth, David Bennin, Dita Cebecauerova, Hana Malcova, Helen Freeman, Neil Martin, Karel Svojgr, Murray H. Passo, Farzana Bhuyan, Sara Alehashemi, Andre T. Rastegar, Katsiaryna Uss, Lela Kardava, Bernadette Marrero, Iris Duric, Ebun Omoyinmi, Petra Peldova, Chyi-Chia Richard Lee, David E. Kleiner, Colleen M. Hadigan, Stephen M. Hewitt, Stefania Pittaluga, Carmelo Carmona-Rivera, Katherine R. Calvo, Nirali Shah, Miroslava Balascakova, Danielle L. Fink, Radana Kotalova, Zuzana Parackova, Lucie Peterkova, Daniela Kuzilkova, Vit Campr, Lucie Sramkova, Angelique Biancotto, Stephen R. Brooks, Cameron Manes, Eric Meffre, Rebecca L. Harper, Hyesun Kuehn, Mariana J. Kaplan, Paul Brogan, Sergio D. Rosenzweig, Melinda Merchant, Zuoming Deng, Anna Huttenlocher, Susan L. Moir, Douglas B. Kuhns, Manfred Boehm, Karolina Skvarova Kramarzova, and Raphaela Goldbach-Mansky. Constitutively active lyn kinase causes a cutaneous small vessel vasculitis and liver fibrosis syndrome. Nature Communications, Mar 2023. URL: https://doi.org/10.1038/s41467-023-36941-y, doi:10.1038/s41467-023-36941-y. This article has 40 citations and is from a highest quality peer-reviewed journal.
(jesus2023constitutivelyactivelyn pages 7-9): Adriana A. de Jesus, Guibin Chen, Dan Yang, Tomas Brdicka, Natasha M. Ruth, David Bennin, Dita Cebecauerova, Hana Malcova, Helen Freeman, Neil Martin, Karel Svojgr, Murray H. Passo, Farzana Bhuyan, Sara Alehashemi, Andre T. Rastegar, Katsiaryna Uss, Lela Kardava, Bernadette Marrero, Iris Duric, Ebun Omoyinmi, Petra Peldova, Chyi-Chia Richard Lee, David E. Kleiner, Colleen M. Hadigan, Stephen M. Hewitt, Stefania Pittaluga, Carmelo Carmona-Rivera, Katherine R. Calvo, Nirali Shah, Miroslava Balascakova, Danielle L. Fink, Radana Kotalova, Zuzana Parackova, Lucie Peterkova, Daniela Kuzilkova, Vit Campr, Lucie Sramkova, Angelique Biancotto, Stephen R. Brooks, Cameron Manes, Eric Meffre, Rebecca L. Harper, Hyesun Kuehn, Mariana J. Kaplan, Paul Brogan, Sergio D. Rosenzweig, Melinda Merchant, Zuoming Deng, Anna Huttenlocher, Susan L. Moir, Douglas B. Kuhns, Manfred Boehm, Karolina Skvarova Kramarzova, and Raphaela Goldbach-Mansky. Constitutively active lyn kinase causes a cutaneous small vessel vasculitis and liver fibrosis syndrome. Nature Communications, Mar 2023. URL: https://doi.org/10.1038/s41467-023-36941-y, doi:10.1038/s41467-023-36941-y. This article has 40 citations and is from a highest quality peer-reviewed journal.
(stefanova2024fgfreceptorkinase pages 11-14): Debora Stefanova, Dominik Olszewski, Mirco Glitscher, Michael Bauer, Luca Ferrarese, Daria Wüst, Eberhard Hildt, Urs F. Greber, and Sabine Werner. Fgf receptor kinase inhibitors exhibit broad antiviral activity by targeting src family kinases. Cellular and Molecular Life Sciences: CMLS, Dec 2024. URL: https://doi.org/10.1007/s00018-024-05502-x, doi:10.1007/s00018-024-05502-x. This article has 6 citations.
(stefanova2024fgfreceptorkinase pages 15-18): Debora Stefanova, Dominik Olszewski, Mirco Glitscher, Michael Bauer, Luca Ferrarese, Daria Wüst, Eberhard Hildt, Urs F. Greber, and Sabine Werner. Fgf receptor kinase inhibitors exhibit broad antiviral activity by targeting src family kinases. Cellular and Molecular Life Sciences: CMLS, Dec 2024. URL: https://doi.org/10.1007/s00018-024-05502-x, doi:10.1007/s00018-024-05502-x. This article has 6 citations.
(stefanova2024fgfreceptorkinase pages 1-2): Debora Stefanova, Dominik Olszewski, Mirco Glitscher, Michael Bauer, Luca Ferrarese, Daria Wüst, Eberhard Hildt, Urs F. Greber, and Sabine Werner. Fgf receptor kinase inhibitors exhibit broad antiviral activity by targeting src family kinases. Cellular and Molecular Life Sciences: CMLS, Dec 2024. URL: https://doi.org/10.1007/s00018-024-05502-x, doi:10.1007/s00018-024-05502-x. This article has 6 citations.
(NCT01234740 chunk 2): Bafetinib in Treating Patients With Recurrent High-Grade Glioma or Brain Metastases. City of Hope Medical Center. 2010. ClinicalTrials.gov Identifier: NCT01234740
(OpenTargets Search: -LYN): Open Targets Query (-LYN, 42 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(scapini2009multiplerolesof pages 5-6): Patrizia Scapini, Shalini Pereira, Hong Zhang, and Clifford A. Lowell. Multiple roles of lyn kinase in myeloid cell signaling and function. Immunological Reviews, 228:23-40, Mar 2009. URL: https://doi.org/10.1111/j.1600-065x.2008.00758.x, doi:10.1111/j.1600-065x.2008.00758.x. This article has 178 citations and is from a domain leading peer-reviewed journal.
(weerawarna2023lynkinasestructure pages 12-13): Pathum M. Weerawarna and Timothy I. Richardson. Lyn kinase structure, regulation, and involvement in neurodegenerative diseases: a mini review. Kinases and Phosphatases, 1:23-38, Jan 2023. URL: https://doi.org/10.3390/kinasesphosphatases1010004, doi:10.3390/kinasesphosphatases1010004. This article has 20 citations.
(stefanova2024fgfreceptorkinase pages 9-11): Debora Stefanova, Dominik Olszewski, Mirco Glitscher, Michael Bauer, Luca Ferrarese, Daria Wüst, Eberhard Hildt, Urs F. Greber, and Sabine Werner. Fgf receptor kinase inhibitors exhibit broad antiviral activity by targeting src family kinases. Cellular and Molecular Life Sciences: CMLS, Dec 2024. URL: https://doi.org/10.1007/s00018-024-05502-x, doi:10.1007/s00018-024-05502-x. This article has 6 citations.
(stefanova2024fgfreceptorkinase pages 18-19): Debora Stefanova, Dominik Olszewski, Mirco Glitscher, Michael Bauer, Luca Ferrarese, Daria Wüst, Eberhard Hildt, Urs F. Greber, and Sabine Werner. Fgf receptor kinase inhibitors exhibit broad antiviral activity by targeting src family kinases. Cellular and Molecular Life Sciences: CMLS, Dec 2024. URL: https://doi.org/10.1007/s00018-024-05502-x, doi:10.1007/s00018-024-05502-x. This article has 6 citations.
(gul2025thepathogenesisclinical pages 5-6): Ahmet Gül, Ivona Aksentijevich, Paul Brogan, Marco Gattorno, Peter C. Grayson, and Seza Ozen. The pathogenesis, clinical presentations and treatment of monogenic systemic vasculitis. Nature reviews. Rheumatology, 21:414-425, May 2025. URL: https://doi.org/10.1038/s41584-025-01250-9, doi:10.1038/s41584-025-01250-9. This article has 19 citations.
(ingley2012functionsofthe pages 7-8): Evan Ingley. Functions of the lyn tyrosine kinase in health and disease. Cell Communication and Signaling : CCS, 10:21-21, Jul 2012. URL: https://doi.org/10.1186/1478-811x-10-21, doi:10.1186/1478-811x-10-21. This article has 248 citations.
(NCT00827138 chunk 2): Study Safety and Preliminary Efficacy of DCC-2036 in Patients With Leukemias (Ph+ CML With T315I Mutation). Deciphera Pharmaceuticals, LLC. 2009. ClinicalTrials.gov Identifier: NCT00827138