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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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

Research report: Zebrafish spns1 (UniProt Q7ZU13) — functional annotation and biological roles

0) Target verification (critical disambiguation)

The target is Danio rerio spns1 (synonyms nrs, spinl), encoding Protein spinster homolog 1, a major facilitator superfamily (MFS) spinster-like multi-pass membrane protein (UniProt Q7ZU13). The literature synthesized here explicitly concerns zebrafish spns1/nrs and/or orthologous SPNS1/Spns1 that matches the same MFS-spinster family and lysosomal transporter role; studies focused on SPNS2 are not used to annotate spns1 function except as contextual comparison. (he2022spns1isa pages 3-5, chavez2024spns1dependentendocardiallysosomal pages 1-4, ha2024lackofspns1 pages 1-2)

1) Key concepts and definitions (current understanding)

1.1 Spinster (SPNS) family and MFS transporters

SPNS1 is part of the spinster-like branch of the MFS transporter superfamily, which typically mediates small-molecule transport across membranes using ion gradients (often H+ coupling). In the context of SPNS1, the key concept is lysosomal metabolite efflux: lysosomes hydrolyze complex lipids, but the breakdown products must exit the lysosome for reuse; impaired efflux can lead to lysosomal storage–like phenotypes. (he2022spns1isa pages 1-2, he2022spns1isa pages 5-7)

1.2 “Lysosomal phospholipid salvage”

He et al. define a lysosomal salvage pathway in which lysophospholipids generated during lysosomal phospholipid catabolism (notably LPC from phosphatidylcholine and LPE from phosphatidylethanolamine) are exported from lysosomes and subsequently re-acylated to replenish cytosolic membrane phospholipids. They emphasize that LPC and LPE are zwitterionic and do not readily diffuse across membranes, motivating the need for a transporter. (he2022spns1isa pages 1-2, he2022spns1isa pages 3-5)

2) Primary molecular function of zebrafish Spns1 (substrate specificity and mechanism)

2.1 Demonstrated substrate: LPC and LPE (primary, best-supported)

A major advance is the functional deorphanization of SPNS1/Spns1 as a proton-dependent lysophospholipid transporter with specificity for lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE). Transport assays show significant uptake activity for labeled LPC, with specificity excluding several other lipid classes (e.g., sphingosine-1-phosphate and multiple anionic lysolipids in the tested assay conditions). (he2022spns1isa pages 1-2, he2022spns1isa pages 2-3)

Visual support from the primary paper’s transport-assay figure (showing mutant effects, pH dependence, and lysolipid specificity) is provided in the retrieved figure crops. (he2022spns1isa media 37123e07, he2022spns1isa media 9b17cfa8, he2022spns1isa media 455e4d18, he2022spns1isa media 26578186, he2022spns1isa media 9b281958)

2.2 Coupling and key residues (mechanistic inference)

Transport is pH-dependent with an optimum in the acidic pH range (~5–6), consistent with proton coupling expected for an MFS transporter operating at the lysosome. Conserved residues R76, E164, and H427 are experimentally implicated: mutating these markedly reduces/abolishes transport activity, consistent with essential roles in substrate/ion coupling or conformational cycling. (he2022spns1isa pages 2-3, he2022spns1isa media 37123e07)

2.3 Is SPNS1 also a sphingosine exporter?

A 2024 mouse/human genetics study argues that SPNS1 is required for lysosomal sphingosine release in addition to lysoglycerophospholipid export, supported by lipid accumulation patterns and lysosome-release assays, and noting that some assays show reduced S1P synthesis consistent with impaired sphingosine availability. However, this work also acknowledges that direct demonstration of sphingosine transport by the same cell-surface uptake approach used for LPC has been challenging in prior work, so the highest-confidence substrate assignment remains LPC/LPE across studies. (ha2024lackofspns1 pages 1-2, ha2024lackofspns1 pages 6-7, ha2024lackofspns1 pages 9-11)

3) Subcellular localization and site of action

SPNS1/Spns1 is primarily a lysosomal/late endosomal membrane protein. In mammals, it colocalizes with LAMP1 (lysosomes) and Rab7 (late endosomes), consistent with trafficking through the endocytic system and a role in lysosomal efflux. In zebrafish, functional imaging and ultrastructure place spns1 activity in autolysosomal/lysosomal compartments in specific tissues such as the endocardium during valve morphogenesis, with abnormal lysosomal cargo accumulation upon loss of spns1. (ha2024lackofspns1 pages 2-4, chavez2024spns1dependentendocardiallysosomal pages 8-10)

4) Biological processes and pathways in zebrafish

4.1 Lysosome homeostasis and autophagy-associated processes

Loss of Spns1 causes enlarged/abnormal lysosomes and biochemical signatures consistent with lysosomal dysfunction and perturbation of autophagy-associated flux (e.g., elevated LC3 markers in mammalian knockdown/KO contexts; zebrafish tissues show accumulated autolysosomal/lysosomal structures and partially degraded cargo by TEM). These phenotypes are consistent with a model in which lysosomal lipid efflux is required to maintain normal lysosomal composition, pH-dependent hydrolase function, and degradative capacity. (he2022spns1isa pages 2-3, he2022spns1isa pages 5-7, chavez2024spns1dependentendocardiallysosomal pages 8-10)

4.2 Valve morphogenesis via endocardial lysosomal function and Notch1 signaling (2024 zebrafish development)

A 2024 iScience study provides direct zebrafish mechanistic insight: spns1 (nrs) is required cell-autonomously in endocardial cells for lysosomal/autophagic processing that enables cardiac valve morphogenesis through notch1 signaling. The study reports strong penetrance of valve-cell marker loss: ALCAM+ valve endothelial cells were frequent in siblings but substantially reduced in mutants (e.g., at 3 dpf OFT 91% siblings vs 40% mutants; AVC 73% vs 26%; and at 4 dpf OFT 100% vs 31%; AVC 85% vs 28%, with reported sample sizes in the paper). Endocardial-specific spns1 overexpression partially rescues valve structure/function and reduces accumulation of partially degraded lysosomal contents by TEM. (chavez2024spns1dependentendocardiallysosomal pages 10-12, chavez2024spns1dependentendocardiallysosomal pages 12-13, chavez2024spns1dependentendocardiallysosomal pages 8-10)

This positions zebrafish spns1 as a key node linking lysosome functional state to developmental signaling output (Notch-dependent valve morphogenesis). (chavez2024spns1dependentendocardiallysosomal pages 12-13)

4.3 Lysosomal pH-linked tissue degeneration (zebrafish skeletal muscle)

In zebrafish, spns1 loss has been linked to dysregulated lysosomal pH with downstream tissue consequences. A muscle-focused study reports that muscle development is initially normal, but degeneration appears around 3.5 dpf, with evidence of altered ECM regulation and strong upregulation of MMP-9 (reported as ~15.1-fold mRNA increase) and statistically significant protein-level differences in their assays; the authors emphasize lysosomal acidity as essential for hydrolase activity (pH ~4.5–5) and connect spns1 loss to impaired lysosomal proteolysis. (coffey2021lysosomalfunctionimpacts pages 17-19, coffey2021lysosomalfunctionimpacts pages 19-20)

5) Quantitative evidence and key statistics (selected)

5.1 Transport and lipidomics metrics supporting the lysolipid-export model

• In Spns1 KO cells, lysosome-enriched fractions show ~5-fold higher labeled LPC accumulation, and KO cells show ~25% less incorporation of [14C]-oleate into phosphatidylcholine over a short labeling interval, consistent with impaired lysosomal lysolipid salvage into PC pools. (he2022spns1isa pages 2-3)
• In mouse liver Spns1 knockdown, lysosome-enriched fractions show 8–13-fold accumulation of LPC/LPE/LPG species, ~12-fold higher BMP, and ~3-fold higher total lysosomal lipid (normalized to protein), consistent with lysosomal lipid storage driven by export failure. (he2022spns1isa pages 5-7)

5.2 Zebrafish in vivo statistics from valve morphogenesis study (2024)

Chávez et al. provide quantification of valve marker penetrance and functional scores. For example, ALCAM+ valve endothelium is frequent in siblings but markedly reduced in spns1 mutants (percentages above), and crispant experiments phenocopy reduced ALCAM+ nascent valve structures (e.g., 68% controls vs 36% crispants for ALCAM+ nascent AV leaflets in the excerpt). (chavez2024spns1dependentendocardiallysosomal pages 10-12, chavez2024spns1dependentendocardiallysosomal pages 8-10)

5.3 Mouse/human disease-variant functional statistics (2024)

Ha et al. report that disease-associated missense variants show significantly reduced LPC transport activity and provide typical sample sizes (n ~3–4) and p-value thresholds (e.g., P<0.05 to ***P<0.0001). (ha2024lackofspns1 pages 6-7)

6) Recent developments (prioritizing 2023–2024)

6.1 2024: Human disease relevance and expanded substrate considerations

A 2024 JCI Insight study links SPNS1 dysfunction to lysosomal storage disease–like phenotypes in mouse models and reports three human siblings with a homozygous SPNS1 variant presenting neurodevelopmental impairment (developmental delay, neurological impairment/intellectual disability, cerebellar hypoplasia). The study supports a model in which SPNS1 is required for export of LPC (and other lysolipids) and sphingosine from lysosomes, and identifies downstream impacts including altered PI3K/AKT signaling (reduced Akt phosphorylation in their assays). (ha2024lackofspns1 pages 1-2, ha2024lackofspns1 pages 7-9, ha2024lackofspns1 pages 6-7)

6.2 2024: Developmental organogenesis mechanism (zebrafish heart valves)

The 2024 iScience work is a major zebrafish-specific advance because it connects spns1-dependent lysosomal function to a defined developmental signaling program (Notch1) and a discrete morphogenetic outcome (valve formation), supported by transcriptomics, imaging reporters, and rescue. (chavez2024spns1dependentendocardiallysosomal pages 1-4, chavez2024spns1dependentendocardiallysosomal pages 12-13)

7) Current applications and real-world implementations

1. Zebrafish as an in vivo lysosome/autophagy and organogenesis model: spns1 mutants/crispants provide a tractable vertebrate system to interrogate how lysosomal lipid transport affects autolysosomal function, tissue remodeling, and developmental signaling (Notch-driven valve morphogenesis). (chavez2024spns1dependentendocardiallysosomal pages 1-4, chavez2024spns1dependentendocardiallysosomal pages 8-10)
2. Disease modeling for lysosomal storage-like disorders: Mammalian KO/KD phenotypes and emerging human genetics support SPNS1 as a candidate in lysosome-related lipid storage pathologies, motivating SPNS1 pathway interrogation in translational research. (ha2024lackofspns1 pages 1-2, ha2024lackofspns1 pages 7-9)
3. Metabolic stress/nutrient limitation implications: The lysosomal phospholipid salvage pathway provides a mechanistic basis for why SPNS1 could be important when lipid precursors are limiting, since export/recycling of lysolipids contributes to membrane lipid maintenance and broader cellular homeostasis. (he2022spns1isa pages 5-7, ha2024lackofspns1 pages 13-14)

8) Expert opinions and interpretation (evidence-weighted synthesis)

Best-supported primary function in zebrafish (DANRE/Q7ZU13): Spns1 is most strongly supported as a lysosomal proton-coupled exporter of LPC and LPE, enabling lysosomal phospholipid salvage and maintaining lysosome functional integrity. (he2022spns1isa pages 1-2, he2022spns1isa pages 2-3, he2022spns1isa pages 3-5)

How this explains zebrafish phenotypes: Failure to export lysolipids likely leads to lysosomal lipid buildup, altered membrane properties/pH regulation, impaired degradative processing, and tissue-specific consequences. In the heart endocardium, impaired lysosomal processing is linked to altered Notch pathway output and valve morphogenesis defects; in muscle, lysosomal dysfunction correlates with degeneration and ECM remodeling responses. (chavez2024spns1dependentendocardiallysosomal pages 8-10, chavez2024spns1dependentendocardiallysosomal pages 10-12, coffey2021lysosomalfunctionimpacts pages 17-19)

Open questions: Whether zebrafish Spns1 transports sphingosine directly (as suggested by mammalian physiology/genetics) remains less certain mechanistically than LPC/LPE export, and may depend on assay context or additional factors. (ha2024lackofspns1 pages 9-11, ha2024lackofspns1 pages 1-2)

9) Evidence map (summary table)

The following table compiles the main evidence categories for functional annotation of zebrafish spns1.

Table: This table summarizes the strongest evidence for zebrafish spns1 (UniProt Q7ZU13), covering substrate, mechanism, localization, phenotypes, pathways, quantitative results, and recent 2024 advances. It is useful as a compact evidence map for functional annotation grounded only in the gathered cited contexts.

10) Key source list (URLs and publication dates)

• He M. et al. “Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage.” PNAS (Publication month: Sep 2022). https://doi.org/10.1073/pnas.2210353119 (he2022spns1isa pages 1-2)
• Chávez M.N. et al. “Spns1-dependent endocardial lysosomal function drives valve morphogenesis through Notch1-signaling.” iScience (Publication month: Dec 2024). https://doi.org/10.1016/j.isci.2024.111406 (chavez2024spns1dependentendocardiallysosomal pages 1-4)
• Ha H.T.T. et al. “Lack of SPNS1 results in accumulation of lysolipids and lysosomal storage disease in mouse models.” JCI Insight (Publication month: Mar 2024). https://doi.org/10.1172/jci.insight.175462 (ha2024lackofspns1 pages 1-2)
• Coffey E.C. et al. “Lysosomal Function Impacts the Skeletal Muscle Extracellular Matrix.” Journal of Developmental Biology (Publication month: Nov 2021). https://doi.org/10.3390/jdb9040052 (coffey2021lysosomalfunctionimpacts pages 19-20)

References

1. (he2022spns1isa pages 3-5): Menglan He, Alvin C. Y. Kuk, Mei Ding, Cheen Fei Chin, Dwight L.A. Galam, Jie Min Nah, Bryan C. Tan, Hui Li Yeo, Geok Lin Chua, Peter I. Benke, Markus R. Wenk, Lena Ho, Federico Torta, and David L. Silver. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage. Proceedings of the National Academy of Sciences of the United States of America, Sep 2022. URL: https://doi.org/10.1073/pnas.2210353119, doi:10.1073/pnas.2210353119. This article has 62 citations and is from a highest quality peer-reviewed journal.

2. (chavez2024spns1dependentendocardiallysosomal pages 1-4): Myra N. Chávez, Prateek Arora, Marco Meer, Ines J. Marques, Alexander Ernst, Rodrigo A. Morales Castro, and Nadia Mercader. Spns1-dependent endocardial lysosomal function drives valve morphogenesis through notch1-signaling. Dec 2024. URL: https://doi.org/10.1016/j.isci.2024.111406, doi:10.1016/j.isci.2024.111406. This article has 2 citations and is from a peer-reviewed journal.

3. (ha2024lackofspns1 pages 1-2): Hoa T.T. Ha, SiYi Liu, Xuan T.A. Nguyen, Linh K. Vo, Nancy C.P. Leong, Dat T. Nguyen, Shivaranjani Balamurugan, Pei Yen Lim, YaJun Wu, Eunju Seong, Toan Q. Nguyen, Jeongah Oh, Markus R. Wenk, Amaury Cazenave-Gassiot, Zuhal Yapici, Wei-Yi Ong, Margit Burmeister, and Long N. Nguyen. Lack of spns1 results in accumulation of lysolipids and lysosomal storage disease in mouse models. JCI Insight, Mar 2024. URL: https://doi.org/10.1172/jci.insight.175462, doi:10.1172/jci.insight.175462. This article has 12 citations and is from a domain leading peer-reviewed journal.

4. (he2022spns1isa pages 1-2): Menglan He, Alvin C. Y. Kuk, Mei Ding, Cheen Fei Chin, Dwight L.A. Galam, Jie Min Nah, Bryan C. Tan, Hui Li Yeo, Geok Lin Chua, Peter I. Benke, Markus R. Wenk, Lena Ho, Federico Torta, and David L. Silver. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage. Proceedings of the National Academy of Sciences of the United States of America, Sep 2022. URL: https://doi.org/10.1073/pnas.2210353119, doi:10.1073/pnas.2210353119. This article has 62 citations and is from a highest quality peer-reviewed journal.

5. (he2022spns1isa pages 5-7): Menglan He, Alvin C. Y. Kuk, Mei Ding, Cheen Fei Chin, Dwight L.A. Galam, Jie Min Nah, Bryan C. Tan, Hui Li Yeo, Geok Lin Chua, Peter I. Benke, Markus R. Wenk, Lena Ho, Federico Torta, and David L. Silver. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage. Proceedings of the National Academy of Sciences of the United States of America, Sep 2022. URL: https://doi.org/10.1073/pnas.2210353119, doi:10.1073/pnas.2210353119. This article has 62 citations and is from a highest quality peer-reviewed journal.

6. (he2022spns1isa pages 2-3): Menglan He, Alvin C. Y. Kuk, Mei Ding, Cheen Fei Chin, Dwight L.A. Galam, Jie Min Nah, Bryan C. Tan, Hui Li Yeo, Geok Lin Chua, Peter I. Benke, Markus R. Wenk, Lena Ho, Federico Torta, and David L. Silver. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage. Proceedings of the National Academy of Sciences of the United States of America, Sep 2022. URL: https://doi.org/10.1073/pnas.2210353119, doi:10.1073/pnas.2210353119. This article has 62 citations and is from a highest quality peer-reviewed journal.

7. (he2022spns1isa media 37123e07): Menglan He, Alvin C. Y. Kuk, Mei Ding, Cheen Fei Chin, Dwight L.A. Galam, Jie Min Nah, Bryan C. Tan, Hui Li Yeo, Geok Lin Chua, Peter I. Benke, Markus R. Wenk, Lena Ho, Federico Torta, and David L. Silver. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage. Proceedings of the National Academy of Sciences of the United States of America, Sep 2022. URL: https://doi.org/10.1073/pnas.2210353119, doi:10.1073/pnas.2210353119. This article has 62 citations and is from a highest quality peer-reviewed journal.

8. (he2022spns1isa media 9b17cfa8): Menglan He, Alvin C. Y. Kuk, Mei Ding, Cheen Fei Chin, Dwight L.A. Galam, Jie Min Nah, Bryan C. Tan, Hui Li Yeo, Geok Lin Chua, Peter I. Benke, Markus R. Wenk, Lena Ho, Federico Torta, and David L. Silver. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage. Proceedings of the National Academy of Sciences of the United States of America, Sep 2022. URL: https://doi.org/10.1073/pnas.2210353119, doi:10.1073/pnas.2210353119. This article has 62 citations and is from a highest quality peer-reviewed journal.

9. (he2022spns1isa media 455e4d18): Menglan He, Alvin C. Y. Kuk, Mei Ding, Cheen Fei Chin, Dwight L.A. Galam, Jie Min Nah, Bryan C. Tan, Hui Li Yeo, Geok Lin Chua, Peter I. Benke, Markus R. Wenk, Lena Ho, Federico Torta, and David L. Silver. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage. Proceedings of the National Academy of Sciences of the United States of America, Sep 2022. URL: https://doi.org/10.1073/pnas.2210353119, doi:10.1073/pnas.2210353119. This article has 62 citations and is from a highest quality peer-reviewed journal.

10. (he2022spns1isa media 26578186): Menglan He, Alvin C. Y. Kuk, Mei Ding, Cheen Fei Chin, Dwight L.A. Galam, Jie Min Nah, Bryan C. Tan, Hui Li Yeo, Geok Lin Chua, Peter I. Benke, Markus R. Wenk, Lena Ho, Federico Torta, and David L. Silver. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage. Proceedings of the National Academy of Sciences of the United States of America, Sep 2022. URL: https://doi.org/10.1073/pnas.2210353119, doi:10.1073/pnas.2210353119. This article has 62 citations and is from a highest quality peer-reviewed journal.

11. (he2022spns1isa media 9b281958): Menglan He, Alvin C. Y. Kuk, Mei Ding, Cheen Fei Chin, Dwight L.A. Galam, Jie Min Nah, Bryan C. Tan, Hui Li Yeo, Geok Lin Chua, Peter I. Benke, Markus R. Wenk, Lena Ho, Federico Torta, and David L. Silver. Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid salvage. Proceedings of the National Academy of Sciences of the United States of America, Sep 2022. URL: https://doi.org/10.1073/pnas.2210353119, doi:10.1073/pnas.2210353119. This article has 62 citations and is from a highest quality peer-reviewed journal.

12. (ha2024lackofspns1 pages 6-7): Hoa T.T. Ha, SiYi Liu, Xuan T.A. Nguyen, Linh K. Vo, Nancy C.P. Leong, Dat T. Nguyen, Shivaranjani Balamurugan, Pei Yen Lim, YaJun Wu, Eunju Seong, Toan Q. Nguyen, Jeongah Oh, Markus R. Wenk, Amaury Cazenave-Gassiot, Zuhal Yapici, Wei-Yi Ong, Margit Burmeister, and Long N. Nguyen. Lack of spns1 results in accumulation of lysolipids and lysosomal storage disease in mouse models. JCI Insight, Mar 2024. URL: https://doi.org/10.1172/jci.insight.175462, doi:10.1172/jci.insight.175462. This article has 12 citations and is from a domain leading peer-reviewed journal.

13. (ha2024lackofspns1 pages 9-11): Hoa T.T. Ha, SiYi Liu, Xuan T.A. Nguyen, Linh K. Vo, Nancy C.P. Leong, Dat T. Nguyen, Shivaranjani Balamurugan, Pei Yen Lim, YaJun Wu, Eunju Seong, Toan Q. Nguyen, Jeongah Oh, Markus R. Wenk, Amaury Cazenave-Gassiot, Zuhal Yapici, Wei-Yi Ong, Margit Burmeister, and Long N. Nguyen. Lack of spns1 results in accumulation of lysolipids and lysosomal storage disease in mouse models. JCI Insight, Mar 2024. URL: https://doi.org/10.1172/jci.insight.175462, doi:10.1172/jci.insight.175462. This article has 12 citations and is from a domain leading peer-reviewed journal.

14. (ha2024lackofspns1 pages 2-4): Hoa T.T. Ha, SiYi Liu, Xuan T.A. Nguyen, Linh K. Vo, Nancy C.P. Leong, Dat T. Nguyen, Shivaranjani Balamurugan, Pei Yen Lim, YaJun Wu, Eunju Seong, Toan Q. Nguyen, Jeongah Oh, Markus R. Wenk, Amaury Cazenave-Gassiot, Zuhal Yapici, Wei-Yi Ong, Margit Burmeister, and Long N. Nguyen. Lack of spns1 results in accumulation of lysolipids and lysosomal storage disease in mouse models. JCI Insight, Mar 2024. URL: https://doi.org/10.1172/jci.insight.175462, doi:10.1172/jci.insight.175462. This article has 12 citations and is from a domain leading peer-reviewed journal.

15. (chavez2024spns1dependentendocardiallysosomal pages 8-10): Myra N. Chávez, Prateek Arora, Marco Meer, Ines J. Marques, Alexander Ernst, Rodrigo A. Morales Castro, and Nadia Mercader. Spns1-dependent endocardial lysosomal function drives valve morphogenesis through notch1-signaling. Dec 2024. URL: https://doi.org/10.1016/j.isci.2024.111406, doi:10.1016/j.isci.2024.111406. This article has 2 citations and is from a peer-reviewed journal.

16. (chavez2024spns1dependentendocardiallysosomal pages 10-12): Myra N. Chávez, Prateek Arora, Marco Meer, Ines J. Marques, Alexander Ernst, Rodrigo A. Morales Castro, and Nadia Mercader. Spns1-dependent endocardial lysosomal function drives valve morphogenesis through notch1-signaling. Dec 2024. URL: https://doi.org/10.1016/j.isci.2024.111406, doi:10.1016/j.isci.2024.111406. This article has 2 citations and is from a peer-reviewed journal.

17. (chavez2024spns1dependentendocardiallysosomal pages 12-13): Myra N. Chávez, Prateek Arora, Marco Meer, Ines J. Marques, Alexander Ernst, Rodrigo A. Morales Castro, and Nadia Mercader. Spns1-dependent endocardial lysosomal function drives valve morphogenesis through notch1-signaling. Dec 2024. URL: https://doi.org/10.1016/j.isci.2024.111406, doi:10.1016/j.isci.2024.111406. This article has 2 citations and is from a peer-reviewed journal.

18. (coffey2021lysosomalfunctionimpacts pages 17-19): Elizabeth C. Coffey, Mary Astumian, Sarah S. Alrowaished, Claire Schaffer, and Clarissa A. Henry. Lysosomal function impacts the skeletal muscle extracellular matrix. Journal of Developmental Biology, 9:52, Nov 2021. URL: https://doi.org/10.3390/jdb9040052, doi:10.3390/jdb9040052. This article has 11 citations.

19. (coffey2021lysosomalfunctionimpacts pages 19-20): Elizabeth C. Coffey, Mary Astumian, Sarah S. Alrowaished, Claire Schaffer, and Clarissa A. Henry. Lysosomal function impacts the skeletal muscle extracellular matrix. Journal of Developmental Biology, 9:52, Nov 2021. URL: https://doi.org/10.3390/jdb9040052, doi:10.3390/jdb9040052. This article has 11 citations.

20. (ha2024lackofspns1 pages 7-9): Hoa T.T. Ha, SiYi Liu, Xuan T.A. Nguyen, Linh K. Vo, Nancy C.P. Leong, Dat T. Nguyen, Shivaranjani Balamurugan, Pei Yen Lim, YaJun Wu, Eunju Seong, Toan Q. Nguyen, Jeongah Oh, Markus R. Wenk, Amaury Cazenave-Gassiot, Zuhal Yapici, Wei-Yi Ong, Margit Burmeister, and Long N. Nguyen. Lack of spns1 results in accumulation of lysolipids and lysosomal storage disease in mouse models. JCI Insight, Mar 2024. URL: https://doi.org/10.1172/jci.insight.175462, doi:10.1172/jci.insight.175462. This article has 12 citations and is from a domain leading peer-reviewed journal.

21. (ha2024lackofspns1 pages 13-14): Hoa T.T. Ha, SiYi Liu, Xuan T.A. Nguyen, Linh K. Vo, Nancy C.P. Leong, Dat T. Nguyen, Shivaranjani Balamurugan, Pei Yen Lim, YaJun Wu, Eunju Seong, Toan Q. Nguyen, Jeongah Oh, Markus R. Wenk, Amaury Cazenave-Gassiot, Zuhal Yapici, Wei-Yi Ong, Margit Burmeister, and Long N. Nguyen. Lack of spns1 results in accumulation of lysolipids and lysosomal storage disease in mouse models. JCI Insight, Mar 2024. URL: https://doi.org/10.1172/jci.insight.175462, doi:10.1172/jci.insight.175462. This article has 12 citations and is from a domain leading peer-reviewed journal.

Artifacts

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Citations

1. coffey2021lysosomalfunctionimpacts pages 19-20
2. coffey2021lysosomalfunctionimpacts pages 17-19
3. 14C
4. https://doi.org/10.1073/pnas.2210353119
5. https://doi.org/10.1172/jci.insight.175462
6. https://doi.org/10.1016/j.isci.2024.111406
7. https://doi.org/10.3390/jdb9040052
8. https://doi.org/10.1073/pnas.2210353119,
9. https://doi.org/10.1016/j.isci.2024.111406,
10. https://doi.org/10.1172/jci.insight.175462,
11. https://doi.org/10.3390/jdb9040052,