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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

SYNE2 / Nesprin-2 (UniProt Q8WXH0): Functional-Annotation Research Report

Executive conclusion

Identity is verified. Human SYNE2 encodes nesprin-2 (also Syne-2, NUANCE, KASH2), the protein represented by UniProt Q8WXH0. The literature consistently describes a nesprin-family protein whose giant isoform is approximately 792–796 kDa, with paired N-terminal calponin-homology (CH) domains, an extended spectrin-repeat region, and a C-terminal transmembrane/KASH region. This matches the supplied accession, organism (Homo sapiens), aliases, family, and InterPro domain classes. No conflicting same-symbol gene was encountered. (young2021biallelicsyne2missense pages 1-2, young2021biallelicsyne2missense pages 11-12, holt2019nesprin1alpha2associateswith pages 1-2)

Nesprin-2 is not an enzyme or transporter. Its primary function is that of a mechanically active structural scaffold and cytoskeletal cargo adaptor at the nuclear envelope. It forms the outer-nuclear-membrane side of the LINC—linker of nucleoskeleton and cytoskeleton—complex, coupling F-actin and microtubule motors to SUN proteins, the nuclear lamina, and ultimately the nuclear interior. Its best-supported immediate functions are nuclear positioning and movement, maintenance of nuclear shape and stiffness, force transmission, and coordination of cytoskeleton-dependent cell polarization and migration. (kuwako2024diverserolesof pages 1-2, ziyi2024nesprinproteinsbridging pages 2-4, ziyi2024nesprinproteinsbridging pages 4-5)

Table: Compact evidence map for human SYNE2/Q8WXH0, separating established molecular architecture from human, mouse, and in-vitro functional findings. Quantitative 2024 results and major causality limitations are highlighted.

1. Molecular identity, architecture, and isoforms

1.1 Identity and nomenclature

The target is unambiguously human SYNE2/nesprin-2, not SYNE1/nesprin-1 or a similarly named nonhuman gene. Human SYNE2 produces numerous isoforms that differ in size, domain composition, localization, and tissue expression. The largest, nesprin-2 giant, is approximately 0.8 MDa; reported estimates of 792 and 796 kDa reflect transcript or annotation conventions rather than evidence for a different protein. (young2021biallelicsyne2missense pages 1-2, young2021biallelicsyne2missense pages 11-12, holt2019nesprin1alpha2associateswith pages 1-2)

1.2 Domain organization

The giant isoform has three functionally coherent regions:

1. N-terminal actin-binding domain. Two CH domains form an actinin-like actin-binding module. Mouse deletion evidence indicates that CH1 provides principal F-actin binding and CH2 enhances CH1 function. (zhou2018mousemodelsof pages 10-14)
2. Long spectrin-repeat rod. Numerous spectrin repeats produce an elongated, potentially extensible scaffold and provide sites for protein interactions. Human disease variants within individual repeats can reduce giant-protein stability without preventing nuclear-envelope targeting. (young2021biallelicsyne2missense pages 11-12, ziyi2024nesprinproteinsbridging pages 4-5)
3. C-terminal membrane/KASH region. A transmembrane segment anchors KASH-containing isoforms in the outer nuclear membrane; the short C-terminal KASH tail projects into the perinuclear lumen and binds SUN-domain proteins. (kuwako2024diverserolesof pages 1-2, ziyi2024nesprinproteinsbridging pages 4-5)

Alternative promoters, termination sites, and splicing generate shorter proteins that may lack the N-terminal actin-binding module, parts of the spectrin rod, or the KASH domain. Consequently, “SYNE2 expression” is not a single functional variable: different assays may measure giant, α, β, ε, or KASH-less forms. Reported examples include nesprin-2α1 at approximately 61–62 kDa, nesprin-2ε at 103 kDa, and nesprin-2ε-1 at 122 kDa. (holt2019nesprin1alpha2associateswith pages 1-2, liu2024commonsyne2genetic pages 13-16, ziyi2024nesprinproteinsbridging pages 4-5)

This isoform complexity is a central annotation caveat. A phenotype from pan-SYNE2 knockdown cannot automatically be attributed to nesprin-2 giant, and overexpressing a short KASH-containing isoform can act dominantly rather than reproduce its normal endogenous function.

2. Cellular location and immediate molecular mechanism

2.1 Nuclear-envelope topology

KASH-containing nesprin-2 is principally an outer nuclear membrane protein. Most of the giant molecule lies in the cytoplasm, where its CH domains bind actin and its C-terminal region can recruit motor complexes. The KASH tail occupies the nuclear-envelope lumen and binds SUN1/SUN2, which span the inner nuclear membrane and connect to lamins and other nuclear structures. The resulting SUN–KASH assembly is the core LINC bridge. (kuwako2024diverserolesof pages 1-2, ziyi2024nesprinproteinsbridging pages 2-4, ziyi2024nesprinproteinsbridging pages 1-2)

Thus, nesprin-2 acts at the mechanical boundary between cytoplasm and nucleus. Its broader subcellular distribution depends on isoform and cell state: shorter or KASH-less forms have been reported at stress fibers, focal adhesions, Golgi-associated regions, sarcomeric structures, cytoplasm, or nucleoplasm. These non-envelope localizations should not be generalized to every isoform. (ziyi2024nesprinproteinsbridging pages 4-5)

2.2 Principal interaction classes

• F-actin: direct binding through the paired N-terminal CH domains of nesprin-2 giant.
• SUN proteins: luminal binding through the KASH tail, anchoring nesprin-2 in LINC complexes.
• Dynein–dynactin–BicD2: recruited near the membrane-proximal C terminus through BicD2-dependent interactions.
• Kinesin-1: recruited through a distinct LEWD motif, permitting simultaneous coordination of oppositely directed microtubule motors.
• Nuclear-envelope proteins and signaling factors: functional interactions with lamin/emerin organization and context-dependent α-catenin/β-catenin signaling have been reported. (young2021biallelicsyne2missense pages 13-15, zhou2024nesprin2coordinatesopposing pages 5-6, zhou2024nesprin2coordinatesopposing pages 6-8, zhang2007nesprin1and2 pages 4-5)

SUN specificity is not fully resolved. Co-immunoprecipitation has sometimes favored SUN1–nesprin-2 association, whereas biophysical KASH-binding measurements found no important SUN1-versus-SUN2 affinity difference. Redundancy and cell-specific assembly therefore remain likely. (bougaran2024lifeatthe pages 5-6)

3. Core biological functions and pathways

3.1 Actin-coupled nuclear positioning

In polarized fibroblast models, nesprin-2 giant and SUN2 assemble in transmembrane actin-associated nuclear lines, or TAN lines, that couple retrograde dorsal actin flow to rearward nuclear movement. This moves the nucleus relative to the centrosome and helps establish front–rear polarity. Myosin-dependent tension across nesprin-2 supports the interpretation that it is a load-bearing component rather than merely a static marker. These are strong mechanistic cell-model findings, although their magnitude in intact human tissues is less well quantified. (kuwako2024diverserolesof pages 16-18, young2021biallelicsyne2missense pages 13-15)

3.2 Microtubule-motor coordination and neuronal nuclear migration

A major 2024 advance showed that nesprin-2 is not simply a passive motor attachment site. In mouse cerebellar granule neurons, membrane-proximal nesprin-2 recruited kinesin-1 through the LEWD motif and recruited BicD2–dynein/dynactin through separate motifs. Mutating either motor-binding system prevented rescue of nuclear migration, indicating that both minus- and plus-end motors contribute productively. (zhou2024nesprin2coordinatesopposing pages 1-2, zhou2024nesprin2coordinatesopposing pages 5-6, zhou2024nesprin2coordinatesopposing pages 6-8)

Nesprin-2-associated artificial cargo moved bidirectionally at approximately 1 μm/s, with 60 ± 10% of movement toward microtubule minus ends. Nesprin-2-mutant cerebellar neurons displaced nuclei at 7.46 ± 9.68 μm/h, compared with 12.91 ± 10.24 μm/h in wild type. Kinesin inhibition reduced, rather than accelerated, forward migration, arguing against a simple tug-of-war. The authors instead propose that bidirectional stepping and nuclear rotation keep the large nucleus mobile while the surrounding microtubule array advances. Published August 2024: Zhou et al., Journal of Cell Biology, DOI 10.1083/jcb.202405032. (zhou2024nesprin2coordinatesopposing pages 5-6, zhou2024nesprin2coordinatesopposing pages 6-8, zhou2024nesprin2coordinatesopposing pages 10-13)

Consistent developmental evidence from mouse retina and cortex shows that loss of nesprin-2 disrupts interkinetic nuclear migration, mislocalizes mitotic progenitors, depletes progenitor pools, and impairs migration of newborn neurons. In this setting, actin binding appears dispensable, emphasizing that different nesprin-2 domains dominate in different cell types. (kuwako2024diverserolesof pages 8-10)

3.3 Nuclear mechanics and mechanotransduction

By physically coupling the cytoskeleton to the nuclear envelope, nesprin-2 controls nuclear shape, prestress, stiffness, and deformation. These mechanical effects can influence downstream transcriptional regulators rather than constituting a conventional ligand-activated signaling pathway. The clearest recent human-cell example involves YAP–TEAD mechanosignaling: both pan-SYNE2 knockdown and overexpression of short nesprin-2α1 reduced YAP activity, illustrating that either loss of coupling or dominant-negative remodeling can perturb the same pathway. (liu2024commonsyne2genetic pages 5-6, liu2024commonsyne2genetic pages 8-10)

Nesprin-2 can therefore be placed in a mechanochemical route:

extracellular matrix/cell junctions → actomyosin or microtubules → nesprin-2–SUN LINC complex → lamina/nuclear mechanics → chromatin and mechanosensitive transcription.

The first three links are strongly supported structurally and experimentally. Direct, gene-specific transmission from nesprin-2 to particular chromatin loci is less firmly established and is likely cell- and isoform-dependent.

3.4 Migration, epithelia, and vascular responses

In endothelial models, nesprin-2 depletion increased cell spreading and reduced collective migration and Matrigel network formation. Joint depletion of nesprin-1 and nesprin-2 impaired pulsatile-shear induction of ZO-1 and occludin. Low shear reduced nesprin-2 expression in rat aortic endothelial cells, and restoring nesprin-2 under low shear altered proliferation and apoptosis. These findings implicate nesprin-2 in endothelial morphology, barrier adaptation, and flow responses. However, combined knockdowns and LINC redundancy prevent assigning all these effects uniquely to SYNE2; direct SYNE2-specific vascular-disease causality remains unproven. Bougaran and Bautch, published May 20, 2024; DOI 10.3389/fphys.2024.1411995. (bougaran2024lifeatthe pages 2-3, bougaran2024lifeatthe pages 5-6, bougaran2024lifeatthe pages 6-7, bougaran2024lifeatthe pages 1-2)

3.5 Ciliogenesis and Wnt-related functions

Nesprin-2 has been reported to interact with meckelin and promote ciliogenesis through actin-cytoskeleton remodeling. Separately, interaction with α-catenin can influence β-catenin nuclear distribution and Wnt signaling. Mouse skin studies connect loss of nesprin-2 giant to altered perinuclear actin, reduced keratinocyte migration, enhanced focal adhesions, and delayed wound closure. These observations broaden SYNE2 beyond nuclear positioning, but the evidence is substantially more context-specific than its core LINC role. Dawe et al., 2009, DOI 10.1242/jcs.043794; Rashmi et al., 2012, DOI 10.4161/nucl.19090. (young2021biallelicsyne2missense pages 13-15)

4. Recent developments, 2024

4.1 Atrial-fibrillation regulatory variant and nesprin-2α1

Liu et al. provided the strongest recent link between a common human SYNE2 variant and a defined molecular mechanism. In 235 human left-atrial-appendage samples, AF-risk allele dosage at rs1152591 was inversely associated with the short SYNE2α1 transcript; genotype-specific qPCR used ten samples per genotype and found no corresponding effect on the long transcript or SYNE2β2. The variant lies approximately 10 bp upstream of the presumed internal SYNE2α1 transcription start site. Reporter assays and CRISPR-edited isogenic human stem-cell-derived cardiomyocytes supported rs1152591 as a causal regulatory allele. Risk-allele cardiomyocytes had approximately 60% less endogenous SYNE2α1 mRNA. (liu2024commonsyne2genetic pages 5-6, liu2024commonsyne2genetic pages 8-10, liu2024commonsyne2genetic pages 13-16)

Functional perturbation produced several quantitative phenotypes:

• SYNE2α1 overexpression increased nuclear area 12.5%; pan-SYNE2 knockdown increased it 12.6%.
• Nuclear stiffness fell 33%, from 3.17 ± 0.42 to 2.11 ± 0.13 kPa, after α1 overexpression.
• Pan-SYNE2 knockdown reduced stiffness 57%, from 3.09 ± 0.43 to 1.31 ± 0.19 kPa.
• YAP activity fell 23% after α1 overexpression and 20% after knockdown.
• RNA sequencing identified 1,975 differentially expressed genes after knockdown and 5,719 after α1 overexpression.
• α1 overexpression accelerated calcium release and reuptake and shortened action-potential duration; pan-SYNE2 knockdown shortened action-potential duration and reduced conduction velocity. (liu2024commonsyne2genetic pages 5-6, liu2024commonsyne2genetic pages 1-3, liu2024commonsyne2genetic pages 16-21)

The similar nuclear phenotypes from α1 overexpression and pan-SYNE2 depletion suggest that excessive short α1 can act dominantly against normal giant-LINC coupling. Nevertheless, the direction from reduced α1 expression to AF remains biologically complex because experimental overexpression is not the inverse of physiological risk-allele dosage. Limitations include immature cardiomyocytes, some ventricular-like rather than atrial-like cells, low endogenous α1, cell fragility that prevented patch-clamp confirmation, and inability to map altered transcripts directly to individual ion currents. Published October 2024: DOI 10.1161/CIRCGEN.124.004750. (liu2024commonsyne2genetic pages 10-12)

4.2 PDI-dependent LINC remodeling in breast-cancer cells

In human MDA-MB-231 triple-negative breast-cancer cells, PDI inhibitors 16F16 (5 μM) and PACMA31 (2.5 μM) downregulated SUN proteins and lamins and displaced nesprin-2 from the nuclear envelope. Robust giant-nesprin-2 nuclear-rim staining fell from 25.7% in untreated cells to 7.0% with 16F16 and 4.8% with PACMA31; generic nesprin-2 rim staining fell from 28.8% to 5.7% and 3.0%, respectively. Perinuclear F-actin increased from 3.7% untreated to 11.4% and 33.8%. PACMA31 reduced SUN1 and SUN2 to 0.24- and 0.36-fold, respectively. (young2024inhibitionofpdis pages 13-15, young2024inhibitionofpdis pages 12-13)

PDI inhibition reduced proliferation, two-dimensional migration, and polarity but increased passage through restrictive 5-μm pores, consistent with a more deformable nucleus. This remains a pharmacological in-vitro association: broad redox and endoplasmic-reticulum effects, inhibitor-specific targets, and simultaneous loss of lamins/SUN proteins prevent attributing invasion specifically to nesprin-2. Published May 24, 2024: DOI 10.3390/cells13110906. (young2024inhibitionofpdis pages 1-2, young2024inhibitionofpdis pages 21-22, young2024inhibitionofpdis pages 17-19)

4.3 New rare-variant evidence in muscle disease

A March 2024 case report described a 70-year-old man with progressive proximal myalgia and creatine kinase levels up to 1,355 U/L, but no overt weakness or cardiac symptoms. He carried heterozygous SYNE2 c.15306+2T>G, predicted to disrupt the intron-82 donor site. Patient fibroblasts showed abnormal nuclear shape and reduced or discontinuous nuclear-envelope nesprin-2 giant. (paulus2024anintronicheterozygous pages 4-7, paulus2024anintronicheterozygous pages 2-4)

The variant should remain cautiously interpreted: it was classified as a variant of uncertain significance, direct aberrant-transcript evidence was not definitive, biopsy findings were nonspecific, and two reportedly unaffected children carried the variant. Published March 15, 2024: DOI 10.3390/muscles3010010. (paulus2024anintronicheterozygous pages 2-4, paulus2024anintronicheterozygous pages 1-2, paulus2024anintronicheterozygous pages 7-8)

5. Human disease relevance and evidence quality

5.1 Emery–Dreifuss muscular dystrophy and cardiomyopathy

SYNE2 has long been considered a candidate nuclear-envelopathy gene. A foundational study screened 190 probands with EDMD or EDMD-like phenotypes lacking LMNA or EMD mutations. Patient cells showed abnormal nuclei, reduced nuclear-envelope nesprin staining, emerin/SUN2 mislocalization, and disrupted nuclear-envelope organization; siRNA depletion of nesprin-2 reproduced aspects of these defects. (zhang2007nesprin1and2 pages 4-5, zhang2007nesprin1and2 pages 1-2, zhang2007nesprin1and2 pages 8-9)

Variant-level evidence was less decisive than the cellular evidence. Reported SYNE2 changes included T89M and a 5′-UTR variant found in 0.53% of 380 patient alleles versus 0/384 reference alleles; segregation and functional effects were incomplete, and T89M did not alter the tested emerin-binding interaction. The correct interpretation is therefore that SYNE2 disruption can produce EDMD-relevant cellular mechanisms, while not every historical variant is securely pathogenic. Zhang et al., advance publication August 29, 2007; DOI 10.1093/hmg/ddm238. (zhang2007nesprin1and2 pages 2-4, zhang2007nesprin1and2 pages 6-7)

Open Targets aggregates associations of SYNE2 with EDMD, atrial fibrillation/cardiac arrhythmia, and neurodegenerative phenotypes, but such scores combine heterogeneous genetic and functional evidence and should not be treated as clinical diagnostic validity by themselves. (OpenTargets Search: -SYNE2)

5.2 Neurodevelopmental disease

A 2021 study found compound-heterozygous p.E788K and p.V828G substitutions in spectrin repeat 5 in one child with autism, developmental delay, and intellectual disability. Patient cells had normal SYNE2 transcript abundance and retained nuclear-envelope localization but significantly reduced nesprin-2 giant protein, suggesting defective stability. This is useful human functional evidence for a hypomorphic mechanism but, as a single-family observation, is not definitive proof that SYNE2 is a common monogenic cause of autism. Published August 2021; DOI 10.3390/genes12091294. (young2021biallelicsyne2missense pages 11-12)

6. Current applications and translational status

Established or near-term applications

1. Genetic interpretation: SYNE2 is included in some nuclear-envelopathy, muscular-dystrophy, cardiomyopathy, arrhythmia, or neurodevelopmental analyses. Because of transcript size, extensive alternative splicing, and incomplete penetrance, variant interpretation requires isoform-aware annotation, population frequency, segregation, RNA analysis, and patient-cell localization studies.
2. Cellular disease phenotyping: Nuclear shape, nesprin-2 nuclear-rim localization, nuclear stiffness, and LINC-partner organization are useful research readouts for candidate variants. These are supportive functional assays, not standalone clinical diagnostics.
3. Mechanobiology models: Nesprin-2 constructs, dominant-negative KASH fragments, CRISPR perturbations, motor-binding mutants, and tension sensors are used to study nuclear force transmission, cell migration, neural development, and cardiomyocyte mechanics.
4. Risk-mechanism studies: The rs1152591 work illustrates how an AF GWAS locus can be resolved to an internal SYNE2 promoter and a specific short isoform, providing a model for functional fine-mapping. (liu2024commonsyne2genetic pages 5-6, liu2024commonsyne2genetic pages 8-10)

What is not yet implemented

There is no evidence in the retrieved literature of an approved drug, gene therapy, or clinical intervention that directly targets SYNE2/nesprin-2. Proposed strategies—CRISPR correction, gene replacement, antisense or RNA modulation, pharmacological restoration of LINC function, and cell therapy—remain preclinical concepts. The giant coding sequence, tissue-specific isoforms, and the danger of disturbing a ubiquitous mechanical bridge are major delivery and safety obstacles. (ziyi2024nesprinproteinsbridging pages 9-10)

7. Expert synthesis and unresolved questions

Authoritative 2024 reviews converge on a primary interpretation: nesprin-2 is a mechanical and organizational hub, especially important in mechanically stressed tissues and migrating cells. Its disease effects likely arise from failure of nuclear–cytoskeletal coupling, abnormal nuclear mechanics, altered positioning, and secondary changes in chromatin or signaling—not from loss of catalytic activity. (ziyi2024nesprinproteinsbridging pages 2-4, ziyi2024nesprinproteinsbridging pages 1-2, ziyi2024nesprinproteinsbridging pages 5-7)

The major unresolved issues are:

• Isoform specificity: Which phenotypes belong to giant, α1, or other short/KASH-less forms?
• Redundancy: When can nesprin-1 or alternative SUN–KASH assemblies compensate for nesprin-2?
• Variant validity: Many reported human variants lack robust segregation, RNA evidence, or multiple unrelated families.
• Mechanics-to-transcription causality: Nuclear stiffness and YAP or β-catenin changes are reproducible, but the direct molecular steps from a specific nesprin-2 lesion to a stable transcriptional program remain incompletely mapped.
• Tissue selectivity: Ubiquitously expressed LINC components can cause predominantly muscle, cardiac, neural, retinal, or skin phenotypes; differential isoform use and mechanical load are plausible explanations but not complete ones.
• Therapeutic window: Both depletion and excess of a short isoform can produce similar nuclear defects, implying that restoring correct stoichiometry and localization may matter more than simply increasing total SYNE2 expression. (liu2024commonsyne2genetic pages 5-6, ziyi2024nesprinproteinsbridging pages 4-5, ziyi2024nesprinproteinsbridging pages 5-7)

Overall functional annotation

Recommended primary annotation: Outer-nuclear-membrane spectrin-repeat scaffold and bidirectional cytoskeletal adaptor that forms SUN–KASH LINC complexes, directly links F-actin and microtubule motors to the nucleus, and thereby controls nuclear positioning, morphology, mechanics, mechanosensitive signaling, and migration.

The strongest evidence supports this structural/mechanical role. Cardiac electrophysiology, neural development, endothelial responses, ciliogenesis, Wnt signaling, wound repair, and disease associations are biologically credible downstream manifestations, but their dependence on particular SYNE2 isoforms and their clinical penetrance remain context-dependent.

References

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16. (liu2024commonsyne2genetic pages 13-16): Nana Liu, Jeffrey Hsu, Gautam Mahajan, Han Sun, Kenneth R. Laurita, Sathyamangla V. Naga Prasad, John Barnard, David R. Van Wagoner, Chandrasekhar R. Kothapalli, Mina K. Chung, and Jonathan D. Smith. Common syne2 genetic variant associated with atrial fibrillation lowers expression of nesprin-2α1 with downstream effects on nuclear and electrophysiological traits. Circulation: Genomic and Precision Medicine, 17:e004750, Oct 2024. URL: https://doi.org/10.1161/circgen.124.004750, doi:10.1161/circgen.124.004750. This article has 2 citations.

17. (young2024inhibitionofpdis pages 1-2): Natalie Young, Zizhao Gui, Suleiman Mustafa, Kleopatra Papa, Emily Jessop, Elizabeth Ruddell, Laura Bevington, Roy A. Quinlan, Adam M. Benham, Martin W. Goldberg, Boguslaw Obara, and Iakowos Karakesisoglou. Inhibition of pdis downregulates core linc complex proteins, promoting the invasiveness of mda-mb-231 breast cancer cells in confined spaces in vitro. Cells, 13:906, May 2024. URL: https://doi.org/10.3390/cells13110906, doi:10.3390/cells13110906. This article has 5 citations.

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20. (young2024inhibitionofpdis pages 17-19): Natalie Young, Zizhao Gui, Suleiman Mustafa, Kleopatra Papa, Emily Jessop, Elizabeth Ruddell, Laura Bevington, Roy A. Quinlan, Adam M. Benham, Martin W. Goldberg, Boguslaw Obara, and Iakowos Karakesisoglou. Inhibition of pdis downregulates core linc complex proteins, promoting the invasiveness of mda-mb-231 breast cancer cells in confined spaces in vitro. Cells, 13:906, May 2024. URL: https://doi.org/10.3390/cells13110906, doi:10.3390/cells13110906. This article has 5 citations.

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Artifacts

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Citations

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