The Key Starting Point for Phosphatidylserine Research: Changes in Membrane Localization, Functional Shifts, and Interpretation of Findings

1. To Understand Phosphatidylserine, Start with Changes in Membrane Localization and Functional Transition

 

Phosphatidylserine (PS) is an important anionic phospholipid in cell membranes. Any discussion of PS should begin with a clear view of its positional state within membranes. In discussions of plasma membrane lipid asymmetry, PS under steady-state conditions is located predominantly on the cytoplasmic leaflet of the plasma membrane; however, at the whole-cell level, PS is also distributed across the membranes of multiple organelles. With respect to the plasma membrane, enrichment of PS on the cytoplasmic side helps maintain a negatively charged membrane surface environment and influences the recruitment, localization, and intracellular signaling organization of many membrane-associated proteins. In this state, PS primarily functions as part of membrane structure and the intracellular signaling system.

 

When lipid asymmetry is disrupted and PS becomes exposed on the outer leaflet of the membrane, its functional role in the cell changes accordingly. At that point, PS is no longer merely a structural phospholipid on the inner side of the plasma membrane, but instead becomes a surface signal that can be recognized externally. Importantly, PS externalization does not correspond to a single function. Its biological significance depends on the specific state of the cell: in apoptotic cells, externalized PS is a classic phagocytic clearance signal; in activated platelets, externalized PS mainly provides a procoagulant surface for coagulation factor complexes; in tumor cells and tumor-associated endothelium, persistent or abnormal PS exposure is associated with the formation of an immunosuppressive microenvironment and with immune evasion. Viewed this way, PS externalization is better understood as a state-dependent change in membrane signaling rather than a single process with a fixed outcome.

 

1.1 Changes in PS Localization and Functional Reorientation Across Different Cellular States

 

Scenario	Primary Location of PS	Mechanism/Driver of Localization Change	Main Function or Recognition Significance
Healthy cells	Mainly on the inner leaflet of the plasma membrane	Maintenance of membrane lipid asymmetry	Maintains a negatively charged membrane environment and supports membrane protein recruitment, localization, and intracellular signaling organization
Apoptotic cells	Exposed on the outer leaflet of the membrane	Loss of membrane lipid asymmetry and PS externalization	Serves as a classic phagocytic clearance signal, promoting recognition and removal of apoptotic cells
Activated platelets	Exposed on the outer leaflet of the membrane	Calcium-dependent membrane lipid rearrangement	Provides a procoagulant surface for coagulation factor complexes and promotes blood coagulation
Tumor cells and tumor-associated endothelium	Persistently or abnormally exposed on the outer leaflet of the membrane	Jointly driven by stress, oxidative stress, treatment responses, and the tumor microenvironment	Associated with the formation of an immunosuppressive tumor microenvironment and related immunoregulatory processes

 

2. The Current Position of PS in Oncology: Strong Mechanistic Basis, but Clinical Positioning Is Not Yet Defined

 

2.1 Why PS Has Entered Tumor-Targeting Research

 

PS has entered cancer research not only because it can become exposed on the surface of tumor cells or tumor-associated endothelium, but also because externalized PS is thought to be associated with an immunosuppressive tumor microenvironment. Recent reviews have characterized PS externalization as a conceptual, non-canonical immunosuppressive signal: it is linked to the resolution of inflammation, tissue-repair-like clearance programs, and tumor immune evasion, and therefore has a theoretical basis for inclusion in discussions of cancer immunotherapy. This positioning is reasonable, but it is not equivalent to a classical checkpoint pathway that has already undergone clinical stratification and achieved broad therapeutic establishment.

 

2.2 Key Evidence

 

1) At the mechanistic level: PS-related signaling has a rationale for inclusion in tumor immunology research.

The reason recent mechanistic studies continue to focus on PS is not simply that it can be exposed on the surface of tumor cells or tumor-associated endothelium, but also that externalized PS is thought to participate in immunosuppressive regulation within the tumor microenvironment. A 2024 review noted that PS externalization is associated with the resolution of inflammation, tissue-repair-like clearance, and downregulation of immune responses, and therefore may be proposed as an immunosuppressive signaling axis with checkpoint-like features, or regarded as a conceptual immune-checkpoint-like pathway. This suggests that the significance of PS in cancer research lies not only in its role as a recognizable membrane surface marker, but also in how tumors may use this class of signal to influence immune responses. However, this positioning is still based mainly on mechanistic and translational research.

 

2) Randomized phase III results: a valid mechanism does not mean clinical benefit has already been established.

A randomized phase III study published in 2018 enrolled 597 previously treated patients with advanced nonsquamous non-small cell lung cancer and compared bavituximab plus docetaxel with docetaxel alone. The results showed median overall survival of 10.5 months and 10.9 months, respectively, with no difference in progression-free survival either. However, the study also reported two exploratory subgroup signals: among patients with higher baseline serum β2-glycoprotein 1 (β2GP1) levels, overall survival showed a trend toward benefit that did not reach statistical significance; among patients who subsequently received immune checkpoint inhibitor therapy, overall survival also showed a result favoring the combination-treatment group. These findings suggest that PS-targeted strategies are not entirely without leads worth further study; however, they remain exploratory observations and cannot overturn the conclusion that the primary trial result was negative.

 

3) Combination-treatment signals: this route still leaves room for further validation.

A single-arm phase II study published in 2024 showed that, in unresectable hepatocellular carcinoma, bavituximab, a monoclonal antibody that recognizes PS-related membrane surfaces in the presence of β2-glycoprotein 1 (β2GP1), combined with pembrolizumab achieved a confirmed objective response rate of 32.1% and a median progression-free survival of 6.3 months among 28 evaluable patients, meeting the prespecified primary endpoint. At present, results of this kind are still insufficient to establish a standard-of-care role, but PS targeting in combination with immunotherapy remains a strategy with room for further validation.

 

2.3 Current Positioning

 

Taken together, the current evidence suggests that, in oncology, PS is better understood as a research direction with a relatively strong mechanistic basis and early signals in combination therapy, but with a clinical position that has not yet been firmly defined.

 

3. When Discussing PS, First Distinguish the Research Object and the Level of Conclusion

 

PS-related research is not a single question. The existing literature involves at least three levels:

1. Changes in the intracellular versus extracellular distribution of membrane PS and disruption of lipid asymmetry;

2. Functional interpretation of externalized PS in apoptotic clearance, platelet procoagulant activity, and tumor immune regulation;

3. Application-oriented research in which externalized PS is used as a recognition target, or PS is incorporated as a component of liposomes or nanodelivery systems.

All of these are related to PS, but the object of study and the conclusions that can be drawn are not the same.

 

Here, it is more appropriate to focus on the first two levels: first, positional changes in endogenous membrane PS; second, the functional significance of those changes in different cellular states. Under normal conditions, PS is maintained predominantly on the inner leaflet of the plasma membrane. Only when membrane lipid asymmetry is disrupted and PS becomes exposed on the outer leaflet does it then enter into distinct biological processes such as phagocytic recognition, formation of a procoagulant surface, and tumor-related immune regulation.

 

When evaluating the literature on PS, at least three issues need to be distinguished first.

 

1) Determine what the study actually measured.

Some studies measure changes in total PS content, whereas others measure increased PS exposure on the outer leaflet of the membrane. These two kinds of results are not equivalent. The former reflects changes in lipid composition or metabolism, while the latter reflects a change in membrane localization state.

 

2) Determine what function externalized PS indicates in that system.

Externalized PS is not, by itself, a single functional signal. In apoptotic cells, it mainly serves as a phagocytic clearance signal; in activated platelets, it mainly provides a procoagulant surface; in tumor-associated settings, it may be related to immunosuppressive regulation. Only when cell type, stimulus conditions, and research context are considered together can the functional significance of externalized PS be accurately understood.

 

3) Determine the level at which the conclusion stops.

Detecting PS externalization shows that the membrane localization state has changed; demonstrating that externalized PS participates in a given functional process belongs to mechanistic interpretation; further developing antibodies, ligands, or nanodelivery systems for targeted intervention already moves into the level of applied research. Changes in localization, functional interpretation, and interventional value should not be merged directly.

 

Once these levels are separated, the meaning of PS-related research becomes easier to understand accurately. Detecting externalized PS indicates first and foremost that the membrane localization state has changed. Whether this further involves immunosuppression still needs to be judged in light of cell type, stimulus conditions, and the specific microenvironment. As for whether externalized PS can serve as an interventional target, that belongs to a later-stage question in applied research. Therefore, detecting PS externalization does not mean that its function in that system has already been clearly established; and being able to explain its function does not mean that the change can already be translated directly into stable therapeutic value.

 

4. Three Issues That Commonly Affect the Interpretation of PS Externalization Studies

 

In experiments and in the interpretation of the literature surrounding PS externalization, three issues are especially prone to affecting conclusions: whether PS externalization is equivalent to apoptosis, what Annexin V positivity actually indicates, and whether different PS probes can be used interchangeably. Existing studies have repeatedly shown that, unless these three points are clearly distinguished, PS-related results are easily overinterpreted.

 

Key Question	More Accurate Understanding	Why It Matters
Does PS externalization equal apoptosis?	No. PS exposure is an important feature of apoptosis, but it does not occur only during apoptosis; PS externalization can also be seen in some viable cells, cells undergoing programmed necrosis, and extracellular vesicles.	This means that detecting positive PS externalization cannot automatically be interpreted as proof that cells are in an apoptotic state.
Can Annexin V positivity alone define the cellular state?	No. Annexin V staining indicates that externalized PS has been detected; in essence, it reports membrane localization status rather than directly classifying the mode of cell death. When membrane integrity is compromised, Annexin V can also bind cells, so it usually needs to be interpreted together with membrane integrity dyes and related indicators.	Annexin V positivity alone cannot distinguish early apoptosis from other death processes accompanied by PS externalization, or from certain non-apoptotic states involving membrane lipid rearrangement; membrane integrity, caspase activation, and other indicators are usually needed for joint interpretation.
Can different PS probes be used as equivalents?	They should not be treated as simply equivalent. Annexin V binding to PS is Ca²⁺-dependent; lactadherin binding to PS is Ca²⁺-independent, and in some platelet, erythrocyte, and apoptotic cell models it is more sensitive to PS exposure.	This means that the percentage of positive events and signal intensity obtained with different probes may not be the same, and the experimental system, ionic conditions, and membrane surface state can all affect interpretation.

 

5. Product Navigation Table for PS Externalization Detection, Model Membrane Construction, and Cellular Interpretation(Table 1–Table 3)

 

Research or Experimental Goal	Table to Consult First	Why This Table Comes First	Suggested Companion Table(s)	Navigation Notes
You want to build an overall understanding of phosphatidylserine (PS) research systems and determine which class of PS molecular species to start with	Table 1	Table 1 focuses on defined PS molecular species such as DOPS, POPS, DPPS, and DSPS, making it the best starting point for deciding whether the experiment requires a highly fluid, mixed-acyl, or saturated PS species	Then see Table 2	First determine the PS molecular species itself, then supplement with membrane scaffold lipids and control lipids; this is a more reliable way to establish a stable model membrane or liposome system
You want to compare how different fatty acyl compositions of PS affect membrane fluidity, membrane order, protein recognition, or surface presentation	Table 1	Table 1 directly corresponds to PS species with different acyl-chain compositions and is most suitable for parallel comparisons among DOPS, POPS, DPPS, and DSPS	Then see Table 2	In this type of comparison, it is usually best to keep the PC, PE, or cholesterol background in Table 2 constant and change only the PS species, which makes the results easier to interpret
You want to construct PS-containing liposomes, supported membranes, or bilayer models to simulate the cellular membrane environment	Table 2	Table 2 focuses on membrane scaffold and control lipids such as DOPC, DOPE, PA, PI, sphingomyelin, and cholesterol, making it the best place to define the overall membrane composition first	Then see Table 1	First define the membrane background and control-lipid framework, then add specific PS molecular species from Table 1; this is more suitable for building a comparable model membrane system
You want to determine whether PS recognition is truly due to the PS headgroup itself or simply due to an anionic membrane surface	Table 2	Table 2 contains anionic control phospholipids such as PA and PI, which are most suitable for distinguishing “PS-specific recognition” from “general negative-charge effects”	Then see Table 1	These experiments usually use one PS species from Table 1 as the main line and PA or PI from Table 2 as anionic controls, allowing clearer interpretation
You want to study how cholesterol, sphingomyelin, or PE affects PS exposure, clustering, membrane-domain distribution, and protein binding	Table 2	Table 2 covers lipids related to membrane order, membrane curvature, and membrane-domain formation, making it the best choice for membrane-environment modulation experiments	Then see Table 1	First use Table 2 to tune the membrane environment, then combine it with specific PS species from Table 1; this makes it easier to distinguish “changes in membrane background” from “changes in PS molecular species”
You want to perform Annexin V recognition, PS externalization detection, or early apoptosis analysis	Table 3	Table 3 focuses on CaCl2, PI, 7-AAD, and commonly used inducers, making it the best direct starting point for establishing PS externalization detection and dual-staining workflows	Then see Table 1	For cell-level PS externalization detection, Table 3 is primary; if extracellular reconstitution systems or liposome controls are also needed, then supplement with Table 1
You want to establish an apoptosis model and observe whether PS externalization occurs after DNA damage or broad-spectrum kinase inhibition	Table 3	Camptothecin, etoposide, and staurosporine in Table 3 are all classic apoptosis inducers and are best suited for building different types of cell-death models	Then see Table 1	First establish the cellular model with Table 3; if you also want to test whether PS recognition is influenced by molecular species, further combine it with membrane-model experiments from Table 1
You want to study Ca²⁺-dependent membrane lipid scrambling, PS exposure, or procoagulant phenotype formation	Table 3	Ionomycin calcium salt, A23187, and calcium chloride in Table 3 directly correspond to Ca²⁺-dependent PS externalization and detection conditions	Then see Table 1 and Table 2	For cell or platelet experiments, start with Table 3; if you want to further compare how different PS species or membrane backgrounds affect externalization recognition in artificial membranes, then link to Table 1 and Table 2
You want to move from cell experiments to reconstituted membrane systems to test whether a given PS-recognition phenomenon can be reproduced in a simplified system	Table 1	Table 1 is best suited for first determining which PS molecular species should be used to reconstruct the membrane surface	Then see Table 2 and Table 3	This type of work usually begins with selecting the PS species in Table 1, then uses Table 2 to define the membrane background; if correspondence with Annexin V detection results is needed, the detection conditions in Table 3 can also be referenced
You want to establish a relatively complete PS research platform covering “membrane model–externalization induction–detection and interpretation”	First Table 1, then Table 2, and finally Table 3	Table 1 addresses the choice of PS molecular species itself, Table 2 addresses membrane-system and control design, and Table 3 addresses externalization induction and detection/interpretation	All three tables in combination	This route is suitable for stepwise work across the molecular, membrane, and cellular levels, enabling both mechanistic comparison and coherent linkage among results

 

Table 1 | Phosphatidylserine Molecular Species with Different Fatty Acyl Compositions

 

Category	CAS No.	Aladdin SKU	Name	Specification or Purity	Product Features and Applications
Defined phosphatidylserine molecular species	90693-88-2	D130321	1,2-dioleoyl-sn-glycero-3-phospho-L-serine (sodium salt) (DOPS)	Moligand™, ≥99%	A commonly used PS species with relatively high membrane fluidity, suitable for constructing PS-containing liposomes or model membranes for studies of membrane asymmetry, Annexin V recognition, procoagulant interfaces, and protein–lipid interactions.
Saturated phosphatidylserine molecular species	321595-13-5	D130315	1,2-distearoyl-sn-glycero-3-phospho-L-serine (sodium salt)	≥99%	A saturated PS species with a high phase-transition temperature, suitable for comparing how acyl composition affects membrane order, phase behavior, and PS surface presentation.
Saturated phosphatidylserine molecular species	145849-32-7	D130323	1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine (sodium salt)	≥98%	Commonly used to construct PS model membranes with relatively high order, suitable for evaluating how membrane rigidity affects Annexin V binding, recognition of PS exposure, and membrane protein assembly.
Mixed-acyl phosphatidylserine molecular species	321863-21-2	P130320	16:0-18:1 PS (POPS)	≥97%	A mixed-acyl PS species commonly used in semi-natural model membrane construction; suitable for introducing acyl-chain combinations that are closer to certain natural membranes into defined membrane systems, and for comparing PS presentation modes, membrane surface charge properties, and protein-recognition behavior.
Defined phosphatidylserine molecular species	70614-14-1	D462978	1,2-Dioleoyl-sn-glycero-3-phospho-L-serine sodium salt	≥95%	A commonly used dioleoyl PS species, suitable for establishing PS-containing liposome, bilayer, and protein-binding systems, and for reproducing and validating the membrane behavior observed in DOPS-type models.

 

Table 2 | Membrane Models and Control Lipids

 

Category	CAS No.	Aladdin SKU	Name	Specification or Purity	Product Features and Applications
Membrane-order-modulating lipid	57-88-5	C104036	Cholesterol	For cell culture, ≥99% (GC)	One of the classic membrane components, commonly used to regulate the order, fluidity, and phase-separation behavior of liposomes and model membranes; suitable for combination with PS to evaluate changes in the membrane microenvironment.
Neutral phosphatidylcholine control lipid	4235-95-4	D130438	1,2-dioleoyl-sn-glycero-3-phosphocholine	Moligand™, ≥99%	A commonly used neutral bilayer scaffold lipid, suitable for constructing basic liposomes or model membranes together with PS, and for use as a non-anionic phospholipid control.
Sphingolipid membrane-order control lipid	383907-87-7	S130559	Sphingomyelin	≥99%, from egg, chicken	Commonly used together with cholesterol to construct more ordered membrane regions, suitable for comparing how ordered membrane domains affect PS exposure, clustering, and protein recognition.
Anionic control phospholipid	108392-02-5	D130369	1,2-dioleoyl-sn-glycero-3-phosphate (sodium salt) (18:1 PA)	≥99%	A commonly used anionic phospholipid control, useful for distinguishing PS-specific recognition from general negatively charged membrane-surface effects, and also suitable for constructing PA-containing signaling-lipid model membranes.
Anionic control phospholipid	383907-36-6	L130328	L-α-phosphatidylinositol (Soy) (sodium salt)	≥99%	A PI-class anionic phospholipid suitable for side-by-side comparison with PS to assess how different anionic headgroups influence membrane-protein recruitment and membrane surface electrostatics.
Helper curvature-type membrane lipid	4004-05-1	D155634	1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE)	≥98%	Displays a strong tendency toward negative curvature and is commonly used to modulate liposome morphology, membrane-fusion tendency, and membrane rearrangement behavior; suitable for building membrane systems closer to biological membranes in combination with PS and PC.

 

Table 3 | Reagents for PS Externalization Induction, Detection Probes, and Interpretation Support

 

Category	CAS No.	Aladdin SKU	Name	Specification or Purity	Product Features and Applications
Inorganic salt for Annexin V binding buffer	10043-52-4	C431202	Calcium chloride	Anhydrous, ≥97%	Annexin V binding to externalized PS depends on Ca²⁺; commonly used to prepare binding buffers or supplement calcium conditions in reaction systems.
DNA-damage-type apoptosis inducer	7689-03-4	C111282	(S)-(+)-Camptothecin	Moligand™, ≥97%	A topoisomerase I inhibitor commonly used to induce apoptosis and to analyze early PS externalization together with Annexin V/PI or Annexin V/7-AAD.
DNA-damage-type apoptosis inducer	33419-42-0	E121713	Etoposide	Moligand™, ≥98%	A topoisomerase II inhibitor commonly used to establish DNA-damage-related apoptosis models and observe the loss of PS asymmetry during cell death progression.
Broad-spectrum kinase-inhibition-type apoptosis inducer	62996-74-1	S102392	Staurosporine	Moligand™, ≥98%	A classic, highly efficient apoptosis inducer commonly used to rapidly establish PS externalization models; suitable for comparing early apoptosis, membrane rearrangement, and subsequent changes in membrane integrity.
Dye for assessing cell membrane integrity	7240-37-1	A131295	7-Aminoactinomycin D	Moligand™, ≥97% (HPLC)	Commonly used together with Annexin V to distinguish early apoptotic cells from late apoptotic/dead cells; suitable for membrane-integrity assessment in flow cytometry.
Nucleic-acid-intercalating dye for cell-death assessment	25535-16-4	P266304	Propidium iodide (PI)	≥98% (HPLC)	Commonly used in dual staining with Annexin V to distinguish membrane-intact cells, early apoptotic cells, and late apoptotic/necrotic cells.
Ca²⁺ ionophore-type PS externalization inducer	56092-82-1	I133497	Ionomycin (Calcium salt)	≥98% (HPLC)	Commonly used to rapidly elevate intracellular Ca²⁺ and induce PS externalization; suitable for studying Ca²⁺-dependent membrane-lipid rearrangement and procoagulant phenotype formation.
Ca²⁺ ionophore-type PS externalization inducer	52665-69-7	C137844	Calcium Ionophore A23187	≥97%	Commonly used to induce Ca²⁺-dependent membrane-lipid scrambling and PS externalization; suitable for establishing platelet or cellular membrane externalization models and comparing externalization kinetics.
Annexin V binding buffer system	—	A377916	Annexin V Binding Buffer	2.5 mM Calcium Chloride in HEPES buffered saline	Annexin V binding to externalized PS depends on appropriate Ca²⁺ and buffering conditions; this product is suitable for establishing PS externalization detection systems and for joint interpretation with PI, 7-AAD, and related reagents.
Single-probe PS externalization detection probe	—	rp226053	Annexin V-FITC	BioReagent, biological stain, for microscopy, suitable for immunofluorescence (IF), 5 μL/test	A classic fluorescent Annexin V probe that directly recognizes externalized PS; suitable for early apoptosis analysis, PS externalization detection, and flow-cytometric or fluorescence-imaging experiments.
Single-probe PS externalization detection probe	—	rp226054	Annexin V-APC	BioReagent, biological stain, for microscopy, suitable for immunofluorescence (IF), 5 μL/test	An APC-channel Annexin V probe suitable for detecting externalized PS in multicolor flow-cytometry systems; especially useful when the FITC channel must be reserved for other markers.
Annexin V/PI dual-staining detection kit	—	A1372286	Annexin V-FITC/PI Apoptosis Detection Kit	Suitable for immunofluorescence (IF), BioReagent, biological stain, for microscopy	Suitable for the combined detection of PS externalization and changes in membrane integrity, enabling distinction among membrane-intact cells, early apoptotic cells, and late apoptotic/dead cells; one of the most common combinations for PS externalization interpretation.
Annexin V/7-AAD dual-staining detection kit	—	A1456530	Annexin V-FITC/7-AAD Apoptosis Detection Kit	BioReagent, biological stain, for microscopy, suitable for immunofluorescence (IF), ready to use	Suitable for the combined detection of externalized PS and cell membrane integrity, commonly used in flow-cytometric stratification of apoptosis; compared with the PI-based route, it serves as another widely used dual-staining interpretation system.
Multicolor flow-cytometry extended dual-staining kit	—	A1456533	Annexin V-APC/7-AAD Apoptosis Detection Kit	Bioactive, ready to use, biological stain, for microscopy, suitable for fluorescence analysis	Suitable for combined interpretation of externalized PS and membrane integrity in multicolor flow-cytometry experiments; particularly advantageous when the FITC channel must be avoided or used together with other green fluorescent markers.

 

Note: The products listed above are representative Aladdin products. For more product specifications, please refer to the product list at the end of the article or search by product name/CAS number/SKU on the Aladdin website.

 

References

 

[1] Kay JG, Fairn GD. Distribution, dynamics and functional roles of phosphatidylserine within the cell. Cell Communication and Signaling. 2019;17(1):126. doi:10.1186/s12964-019-0438-z.

 

[2] Nagata S, Sakuragi T, Segawa K. Flippase and scramblase for phosphatidylserine exposure. Current Opinion in Immunology. 2020;62:31-38. doi:10.1016/j.coi.2019.11.009.

 

[3] Kur IM, Weigert A. Phosphatidylserine externalization as immune checkpoint in cancer. Pflügers Archiv. 2024;476(12):1789-1802. doi:10.1007/s00424-024-02948-7.

 

[4] Gerber DE, Horn L, Boyer M, et al. Randomized phase III study of docetaxel plus bavituximab in previously treated

advanced non-squamous non-small-cell lung cancer. Annals of Oncology. 2018;29(7):1548-1553. doi:10.1093/annonc/mdy177.

 

[5] Hsiehchen D, Beg MS, Kainthla R, et al. The phosphatidylserine targeting antibody bavituximab plus pembrolizumab in unresectable hepatocellular carcinoma: a phase 2 trial. Nature Communications. 2024;15(1):2178. doi:10.1038/s41467-024-46542-y.

 

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