Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

Advertisement

Scientific Reports
  • View all journals
  • Search
  • My Account Login
  • Content Explore content
  • About the journal
  • Publish with us
  • Sign up for alerts
  • RSS feed
  1. nature
  2. scientific reports
  3. articles
  4. article
Choice of lipid supplementation for in vitro erythroid cell culture impacts reticulocyte yield and characteristics
Download PDF
Download PDF
  • Article
  • Open access
  • Published: 29 January 2026

Choice of lipid supplementation for in vitro erythroid cell culture impacts reticulocyte yield and characteristics

  • C. M. Freire1,
  • N. R. King1,
  • M. Dzieciatkowska2,
  • D. Stephenson2,
  • J. G. G. Dobbe3,
  • G. J. Streekstra3,
  • A. D’Alessandro2,
  • T. J. Satchwell4 na1 &
  • …
  • A. M. Toye1 na1 

Scientific Reports , Article number:  (2026) Cite this article

We are providing an unedited version of this manuscript to give early access to its findings. Before final publication, the manuscript will undergo further editing. Please note there may be errors present which affect the content, and all legal disclaimers apply.

Subjects

  • Biochemistry
  • Biological techniques
  • Biotechnology
  • Cell biology

Abstract

Lipids, particularly cholesterol, are critical components of red blood cell (RBC) membranes, influencing protein function, cell stability, and deformability. Reticulocytes (young RBC) derived from in vitro erythroid cultures have been reported to possess less cholesterol than their native counterparts, compromising their functional integrity and lifespan. However, variability in starting materials and culture protocols between studies has hindered definitive conclusions regarding the nature and consequences of this lipid deficiency. Here, we evaluated the influence of lipid sources on reticulocyte quality using a well-established CD34⁺ erythroid culture system. We compared the use of human AB serum and Octaplas (solvent/detergent (S/D)-extracted pooled plasma) as lipid sources. Our results reveal that S/D-extracted plasma leads to cholesterol-deficient reticulocytes with impaired characteristics, including reduced filtration yield, heightened osmotic fragility, and altered PIEZO1 activity. In contrast, AB serum supported the generation of functionally stable reticulocytes, with cholesterol supplementation required to rescue the majority of defects observed with culturing erythroid cells with plasma alone. Importantly, this study provides the first integrated lipidomic, metabolomic, and proteomic characterisation of in vitro-derived reticulocytes cultured under distinct lipid conditions. These multi-omic datasets offer new insights into the consequences of reduced lipid availability during erythroid culture and offer new insights into how culture media affects the development and functionality of lab grown blood.

Data availability

The proteomics data set is available at MassIVE. The MassIVE identifier is MSV000094204, and can be accessed directly through the link [https://massive.ucsd.edu/ProteoSAFe/private-dataset.jsp?task=ab88082fec2b43b2952a16535b013127] . The relevant samples include cultured reticulocytes ( *cultured_reticulocytes_07* to *_15* ), with subsets as follows: 07-09 cultured in AB serum, 10-12 in plasma, and 13-15 in plasma supplemented with CRL. Samples *RBCs_16* to *_18* correspond to erythrocyte controls.The metabolomics and lipidomics data sets are available at the National Institutes of Health Common Fund’s National Metabolomics Data Repository website, the Metabolomics Workbench, [https://www.metabolomicsworkbench.org] for which it has been assigned study ID ST003108. Samples under Assay 01CF19 are pertinent to this manuscript, following the same subsets are detailed above (see last number on *local_sample_id* for correct sample identification).

References

  1. Moreau, A. et al. Physical mechanisms of red blood cell Splenic filtration. Proc. Natl. Acad. Sci. U S A. 120 (44), e2300095120. https://doi.org/10.1073/PNAS.2300095120/SUPPL_FILE/PNAS.2300095120.SM06.AVI (2023).

    Google Scholar 

  2. Minetti, G., Dorn, I., Köfeler, H., Perotti, C. & Kaestner, L. Insights from lipidomics into the terminal maturation of Circulating human reticulocytes. Cell. Death Discovery 2025. 11 (1), 1. https://doi.org/10.1038/s41420-025-02318-x (2025).

    Google Scholar 

  3. Mohandas, N. & Evans, E. Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects. Annu. Rev. Biophys. Biomol. Struct. 23 (23, 1994), 787–818. https://doi.org/10.1146/ANNUREV.BB.23.060194.004035/CITE/REFWORKS (1994).

    Google Scholar 

  4. RA C. Abnormalities of cell-membrane fluidity in the pathogenesis of disease. N. Engl. J. Med. 297, 371–377 (2024). https://cir.nii.ac.jp/crid/1570572700582030592.

  5. Buchwald, H., O’Dea, T. J., Menchaca, H. J., Michalek, V. N. & Rohde, T. D. Effect of plasma cholesterol on red blood cell oxygen transport. Clin. Exp. Pharmacol. Physiol. 27 (12), 951–955. https://doi.org/10.1046/J.1440-1681.2000.03383.X (2000).

    Google Scholar 

  6. Forsyth, A. M., Braunmüller, S., Wan, J., Franke, T. & Stone, H. A. The effects of membrane cholesterol and Simvastatin on red blood cell deformability and ATP release. Microvasc Res. 83 (3), 347–351. https://doi.org/10.1016/J.MVR.2012.02.004 (2012).

    Google Scholar 

  7. Doole, F. T., Kumarage, T., Ashkar, R. & Brown, M. F. Cholesterol stiffening of lipid membranes. J. Membrane Biology 2022. 255 (4), 4. https://doi.org/10.1007/S00232-022-00263-9 (2022).

    Google Scholar 

  8. Nemkov, T. et al. Circulating primitive murine erythroblasts undergo complex proteomic and metabolomic changes during terminal maturation. Blood Adv. 6 (10), 3072–3089. https://doi.org/10.1182/BLOODADVANCES.2021005975 (2022).

    Google Scholar 

  9. Moon, S. H. et al. p53 represses the mevalonate pathway to mediate tumor suppression. Cell 176 (3), 564. https://doi.org/10.1016/J.CELL.2018.11.011 (2018).

    Google Scholar 

  10. D’Alessandro, A. et al. Ferroptosis regulates hemolysis in stored murine and human red blood cells. Blood 145 (7), 765–783. https://doi.org/10.1182/BLOOD.2024026109 (2025).

    Google Scholar 

  11. Mahdi, A. et al. The red blood cell as a mediator of endothelial dysfunction in patients with Familial hypercholesterolemia and dyslipidemia. J. Intern. Med. 293 (2), 228. https://doi.org/10.1111/JOIM.13580 (2022).

    Google Scholar 

  12. Himbert, S. et al. Blood bank storage of red blood cells increases RBC cytoplasmic membrane order and bending rigidity. PLoS One. 16 (11), e0259267. https://doi.org/10.1371/JOURNAL.PONE.0259267 (2021).

    Google Scholar 

  13. Peltier, S. et al. Proteostasis and metabolic dysfunction characterize a subset of storage-induced senescent erythrocytes targeted for post-transfusion clearance. J. Clin. Invest. 11 https://doi.org/10.1172/JCI183099 (2025).

  14. Hawksworth, J. et al. Enhancement of red blood cell transfusion compatibility using CRISPR-mediated erythroblast gene editing. EMBO Mol. Med. 10 (6), e8454. https://doi.org/10.15252/emmm.201708454 (2018).

    Google Scholar 

  15. Giarratana, M. C. et al. Proof of principle for transfusion of in vitro-generated red blood cells. Blood 118 (19), 5071–5079. https://doi.org/10.1182/BLOOD-2011-06-362038 (2011).

    Google Scholar 

  16. Wilson, M. C. et al. Comparison of the proteome of adult and cord erythroid cells, and changes in the proteome following reticulocyte maturation. Mol. Cell. Proteomics. 15 (6), 1938–1946. https://doi.org/10.1074/mcp.M115.057315 (2016).

    Google Scholar 

  17. Moura, P. L. et al. Non-muscle myosin II drives vesicle loss during human reticulocyte maturation. Haematologica 103 (12), 1997–2007. https://doi.org/10.3324/HAEMATOL.2018.199083 (2018).

    Google Scholar 

  18. Bernecker, C. et al. Biomechanical properties of native and cultured red blood cells–Interplay of shape, structure and biomechanics. Front. Physiol. 13, 979298. https://doi.org/10.3389/FPHYS.2022.979298/FULL (2022).

    Google Scholar 

  19. Claessen, M. J. A. G. et al. Production and stability of cultured red blood cells depends on the concentration of cholesterol in culture medium. Sci. Rep. 2024. 14 (1), 1. https://doi.org/10.1038/s41598-024-66440-z (2024).

    Google Scholar 

  20. Satchwell, T. J. et al. Genetic manipulation of cell line derived reticulocytes enables dissection of host malaria invasion requirements. Nat. Commun. 10 (1). https://doi.org/10.1038/S41467-019-11790-W (2019).

  21. Martins Freire, C. et al. Complete absence of GLUT1 does not impair human terminal erythroid differentiation. Blood Adv. 8 (19), 5166–5178. https://doi.org/10.1182/BLOODADVANCES.2024012743/2232404/BLOODADVANCES.2024012743.PDF (2024).

    Google Scholar 

  22. Moura, P. L. et al. PIEZO1 gain-of-function mutations delay reticulocyte maturation in hereditary xerocytosis. Haematologica 105 (6), e268. https://doi.org/10.3324/HAEMATOL.2019.231159 (2020).

    Google Scholar 

  23. Bernecker, C. et al. Cholesterol deficiency causes impaired osmotic stability of cultured red blood cells. Front. Physiol. 10, 1529. https://doi.org/10.3389/fphys.2019.01529 (2019).

    Google Scholar 

  24. Zingariello, M. et al. Dexamethasone predisposes human erythroblasts toward impaired lipid metabolism and renders their ex vivo expansion highly dependent on plasma lipoproteins. Front. Physiol. 10 (APR), 281. https://doi.org/10.3389/fphys.2019.00281 (2019).

    Google Scholar 

  25. Griffiths, R. E. et al. Maturing reticulocytes internalize plasma membrane in Glycophorin A-containing vesicles that fuse with autophagosomes before exocytosis. https://doi.org/10.1182/blood-2011-09-376475.

  26. Kupzig, S., Parsons, S. F., Curnow, E., Anstee, D. J. & Blair, A. Superior survival of ex vivo cultured human reticulocytes following transfusion into mice. Haematologica 102 (3), 476–483. https://doi.org/10.3324/haematol.2016.154443 (2017).

    Google Scholar 

  27. Bruil, A., Beugeling, T., Feijen, J. & van Aken, W. G. The mechanisms of leukocyte removal by filtration. Transfus. Med. Rev. 9 (2), 145–166. https://doi.org/10.1016/S0887-7963(05)80053-7 (1995).

    Google Scholar 

  28. Malleret, B. et al. Significant Biochemical, biophysical and metabolic diversity in Circulating human cord blood reticulocytes. PLoS One. 8 (10), e76062. https://doi.org/10.1371/journal.pone.0076062 (2013).

    Google Scholar 

  29. Hu, J. et al. Isolation and functional characterization of human erythroblasts at distinct stages: implications for Understanding of normal and disordered erythropoiesis in vivo. Blood 121 (16), 3246–3253. https://doi.org/10.1182/blood-2013-01-476390 (2013).

    Google Scholar 

  30. Gautier, E. F. et al. Absolute proteome quantification of highly purified populations of Circulating reticulocytes and mature erythrocytes. Published Online. https://doi.org/10.1182/bloodadvances.2018023515 (2018).

    Google Scholar 

  31. Anderson, M. E. & Meister, A. Transport and direct utilization of gamma-glutamylcyst(e)ine for glutathione synthesis. Proc. Natl. Acad. Sci. U S A. 80 (3), 707. https://doi.org/10.1073/PNAS.80.3.707 (1983).

    Google Scholar 

  32. Maiorino, F. M. et al. Diversity of glutathione peroxidases. Methods Enzymol. 252 (C), 38–48. https://doi.org/10.1016/0076-6879(95)52007-4 (1995).

    Google Scholar 

  33. Stevens-Hernandez, C. J., Flatt, J. F., Kupzig, S. & Bruce, L. J. Reticulocyte maturation and variant red blood cells. Front. Physiol. 13 https://doi.org/10.3389/FPHYS.2022.834463/FULL (2022).

  34. Kalfa, T. A. Diagnosis and clinical management of red cell membrane disorders. Hematology 2021 (1), 331–340. https://doi.org/10.1182/HEMATOLOGY.2021000265 (2021).

    Google Scholar 

  35. Domingues, C. C. et al. Effect of cholesterol depletion and temperature on the isolation of detergent-resistant membranes from human erythrocytes. J. Membr. Biol. 234 (3), 195–205. https://doi.org/10.1007/S00232-010-9246-5/FIGURES/4 (2010).

    Google Scholar 

  36. Sagawa, S., Shirakii, K., CHANGES OF OSMOTIC FRAGILITY OF RED BLOOD CELLS & DUE TO REPLETION OR DEPLETION OF CHOLESTEROL IN HUMAN AND RAT RED CELLS IN VITRO. J. Nutr. Sci. Vitaminol ;26:161–169. (1980).

    Google Scholar 

  37. Nagasawa, T. Deformability and osmotic fragility of phenylhydrazine-injected rat erythrocytes fractionated by Percoll density-gradients. Jpn J. Physiol. 32 (2), 161–170. https://doi.org/10.2170/JJPHYSIOL.32.161 (1982).

    Google Scholar 

  38. Vasileva, V. & Chubinskiy-Nadezhdin, V. Regulation of PIEZO1 channels by lipids and the structural components of extracellular matrix/cell cytoskeleton. J. Cell. Physiol. 238 (5), 918–930. https://doi.org/10.1002/JCP.31001 (2023).

    Google Scholar 

  39. Geoghegan, N. D. et al. 4D analysis of malaria parasite invasion offers insights into erythrocyte membrane remodeling and parasitophorous vacuole formation. Nat. Commun. 2021. 12 (1), 1. https://doi.org/10.1038/s41467-021-23626-7 (2021).

    Google Scholar 

  40. Lu, Z. et al. Fine-Tuning of cholesterol homeostasis controls erythroid differentiation. Published online 2021. https://doi.org/10.1002/advs.202102669.

  41. Luo, J., Yang, H. & Song, B. L. Mechanisms and regulation of cholesterol homeostasis. https://doi.org/10.1038/s41580-019-0190-7.

  42. Duan, Y. et al. Regulation of cholesterol homeostasis in health and diseases: from mechanisms to targeted therapeutics. Signal. Transduct. Target. Therapy 2022. 7 (1), 1. https://doi.org/10.1038/s41392-022-01125-5 (2022).

    Google Scholar 

  43. Du, Q. et al. FASN promotes lymph node metastasis in cervical cancer via cholesterol reprogramming and lymphangiogenesis. Cell. Death Disease 2022. 13 (5), 5. https://doi.org/10.1038/s41419-022-04926-2 (2022).

    Google Scholar 

  44. Jin, Y. et al. SREBP1/FASN/cholesterol axis facilitates radioresistance in colorectal cancer. FEBS Open. Bio. 11 (5), 1343–1352. https://doi.org/10.1002/2211-5463.13137 (2021).

    Google Scholar 

  45. Carroll, R. G. et al. An unexpected link between fatty acid synthase and cholesterol synthesis in Proinflammatory macrophage activation. J. Biol. Chem. 293 (15), 5509–5521. https://doi.org/10.1074/jbc.RA118.001921 (2018).

    Google Scholar 

  46. Geng, F. et al. SREBP-1 upregulates lipophagy to maintain cholesterol homeostasis in brain tumor cells. Cell. Rep. 42 (7), 112790. https://doi.org/10.1016/J.CELREP.2023.112790/ATTACHMENT/7DD0985A-F539-4841-8AC1-2B1E08EA0EEF/MMC9.PDF (2023).

    Google Scholar 

  47. Brown, A. J., Coates, H. W. & Sharpe, L. J. Cholesterol synthesis. Biochemistry of Lipids, lipoproteins and membranes. Published Online January. 1, 317–355. https://doi.org/10.1016/B978-0-12-824048-9.00005-5 (2021).

    Google Scholar 

  48. Koter, M., Franiak, I., Strychalska, K., Broncel, M. & Chojnowska-Jezierska, J. Damage to the structure of erythrocyte plasma membranes in patients with type-2 hypercholesterolemia. Int. J. Biochem. Cell. Biol. 36 (2), 205–215. https://doi.org/10.1016/S1357-2725(03)00195-X (2004).

    Google Scholar 

  49. Buyan, A., Allender, D. W., Corry, B. & Schick, M. Lipid redistribution in the highly curved footprint of Piezo1. Biophys. J. 122 (11), 1900–1913. https://doi.org/10.1016/j.bpj.2022.07.022 (2023).

    Google Scholar 

  50. Beverley, K. M. & Levitan, I. Cholesterol regulation of mechanosensitive ion channels. Front. Cell. Dev. Biol. 12, 1352259. https://doi.org/10.3389/FCELL.2024.1352259/BIBTEX (2024).

    Google Scholar 

  51. Botello-Smith, W. M. et al. A mechanism for the activation of the mechanosensitive Piezo1 channel by the small molecule Yoda1. Nat. Commun. 10(1), 1–10. https://doi.org/10.1038/s41467-019-12501-1 (2019).

  52. Ridone, P. et al. Disruption of membrane cholesterol organization impairs the activity of PIEZO1 channel clusters. J. Gen. Physiol. 152 (8). https://doi.org/10.1085/JGP.201912515/VIDEO-4 (2020).

  53. Samuel, B. U. et al. The role of cholesterol and Glycosylphosphatidylinositol-anchored proteins of erythrocyte rafts in regulating raft protein content and malarial infection. J. Biol. Chem. 276 (31), 29319–29329. https://doi.org/10.1074/jbc.M101268200 (2001).

    Google Scholar 

  54. Maxfield, F. R. & Wüstner, D. Analysis of cholesterol trafficking with fluorescent probes. Methods Cell. Biol. 108, 367. https://doi.org/10.1016/B978-0-12-386487-1.00017-1 (2012).

    Google Scholar 

  55. Trager, W. & Jensen, J. B. Human malaria parasites in continuous culture. Science 193(4254), 673–675. https://doi.org/10.1126/SCIENCE.781840 (1976).

  56. King, N. R. et al. Basigin mediation of Plasmodium falciparum red blood cell invasion does not require its transmembrane domain or interaction with monocarboxylate transporter 1. PLoS Pathog. 20(2), e1011989. https://doi.org/10.1371/JOURNAL.PPAT.1011989 (2024).

  57. Nemkov, T., Reisz, J. A., Gehrke, S., Hansen, K. C. & D’Alessandro, A. High-throughput metabolomics: isocratic and gradient mass spectrometry-based methods. Methods Mol. Biol. 1978, 13–26. https://doi.org/10.1007/978-1-4939-9236-2_2/TABLES/1 (2019).

    Google Scholar 

  58. Nemkov, T., Hansen, K. C. & D’Alessandro, A. A three-minute method for high-throughput quantitative metabolomics and quantitative tracing experiments of central carbon and nitrogen pathways. Rapid Commun. Mass Spectrom. 31 (8), 663–673. https://doi.org/10.1002/RCM.7834 (2017).

    Google Scholar 

  59. Reisz, J. A., Zheng, C., D’Alessandro, A. & Nemkov, T. Untargeted and semi-targeted lipid analysis of biological samples using mass spectrometry-based metabolomics. Methods Mol. Biol. 1978, 121–135. https://doi.org/10.1007/978-1-4939-9236-2_8/FIGURES/1 (2019).

    Google Scholar 

  60. Thomas, T. et al. Evidence for structural protein damage and membrane lipid remodeling in red blood cells from COVID-19 patients. J. Proteome Res. 19 (11), 4455. https://doi.org/10.1021/ACS.JPROTEOME.0C00606 (2020).

    Google Scholar 

Download references

Funding

This study was supported through funding provided by the European Union ITN ‘EVIDENCE’ grant agreement ID 860436 for CMF, the Medical Research Council (MR/V010506/1) for TJS, NRK and infrastructure support funding from the National Institute for Health Research Blood and Transplant Research Unit (NIHR BTRU) in Red Cell Products (IS-BTU-1214-10032). AD was supported by funds from the National Heart, Lung and Blood Institutes (NHLBI) R01 HL146442, R01 HL161004, R01 HL148151, R21 HL150032. The views expressed are those of the authors and not necessarily those of the National Health Service, NIHR, or the Department of Health and Social Care.

Author information

Author notes
  1. These authors contributed equally: T. J. Satchwell and A. M. Toye.

Authors and Affiliations

  1. School of Biochemistry and Cellular Molecular Medicine, University of Bristol, Bristol, UK

    C. M. Freire, N. R. King & A. M. Toye

  2. Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, Aurora, CO, 80045, USA

    M. Dzieciatkowska, D. Stephenson & A. D’Alessandro

  3. Biomedical Engineering and Physics, Amsterdam UMC location University of Amsterdam, Meibergdreef 9, Amsterdam, The Netherlands

    J. G. G. Dobbe & G. J. Streekstra

  4. Centre for Biomedical Research, School of Applied Sciences, University of the West of England, Bristol, UK

    T. J. Satchwell

Authors
  1. C. M. Freire
    View author publications

    Search author on:PubMed Google Scholar

  2. N. R. King
    View author publications

    Search author on:PubMed Google Scholar

  3. M. Dzieciatkowska
    View author publications

    Search author on:PubMed Google Scholar

  4. D. Stephenson
    View author publications

    Search author on:PubMed Google Scholar

  5. J. G. G. Dobbe
    View author publications

    Search author on:PubMed Google Scholar

  6. G. J. Streekstra
    View author publications

    Search author on:PubMed Google Scholar

  7. A. D’Alessandro
    View author publications

    Search author on:PubMed Google Scholar

  8. T. J. Satchwell
    View author publications

    Search author on:PubMed Google Scholar

  9. A. M. Toye
    View author publications

    Search author on:PubMed Google Scholar

Contributions

CMF, AMT and TJS conceived and designed the study. CMF performed and analysed most experiments, NRK contributed to experimental work, including the planning and execution of the P. falciparum assay. JGGD and GJS developed ARCA hardware and analysis software. MD, DS, and AD conducted omics analyses and interpretation. AMT and TJS supervised the study. The manuscript was written by CMF and AMT and edited by CMF, TJS and AMT. All authors reviewed and approved the final manuscript.

Corresponding authors

Correspondence to T. J. Satchwell or A. M. Toye.

Ethics declarations

Competing interests

AMT is a co-founder, a Director and consultant to Scarlet Therapeutics Ltd. TJS is a co-founder and scientific consultant to Scarlet Therapeutics Ltd. All remaining authors declare no conflict of interest.

Additional information

Publisher’s note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Supplementary Information

Below is the link to the electronic supplementary material.

Supplementary Material 1

Rights and permissions

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Freire, C.M., King, N.R., Dzieciatkowska, M. et al. Choice of lipid supplementation for in vitro erythroid cell culture impacts reticulocyte yield and characteristics. Sci Rep (2026). https://doi.org/10.1038/s41598-026-37229-z

Download citation

  • Received: 22 July 2025

  • Accepted: 20 January 2026

  • Published: 29 January 2026

  • DOI: https://doi.org/10.1038/s41598-026-37229-z

Share this article

Anyone you share the following link with will be able to read this content:

Sorry, a shareable link is not currently available for this article.

Provided by the Springer Nature SharedIt content-sharing initiative

Download PDF

Advertisement

Explore content

  • Research articles
  • News & Comment
  • Collections
  • Subjects
  • Follow us on Facebook
  • Follow us on Twitter
  • Sign up for alerts
  • RSS feed

About the journal

  • About Scientific Reports
  • Contact
  • Journal policies
  • Guide to referees
  • Calls for Papers
  • Editor's Choice
  • Journal highlights
  • Open Access Fees and Funding

Publish with us

  • For authors
  • Language editing services
  • Open access funding
  • Submit manuscript

Search

Advanced search

Quick links

  • Explore articles by subject
  • Find a job
  • Guide to authors
  • Editorial policies

Scientific Reports (Sci Rep)

ISSN 2045-2322 (online)

nature.com sitemap

About Nature Portfolio

  • About us
  • Press releases
  • Press office
  • Contact us

Discover content

  • Journals A-Z
  • Articles by subject
  • protocols.io
  • Nature Index

Publishing policies

  • Nature portfolio policies
  • Open access

Author & Researcher services

  • Reprints & permissions
  • Research data
  • Language editing
  • Scientific editing
  • Nature Masterclasses
  • Research Solutions

Libraries & institutions

  • Librarian service & tools
  • Librarian portal
  • Open research
  • Recommend to library

Advertising & partnerships

  • Advertising
  • Partnerships & Services
  • Media kits
  • Branded content

Professional development

  • Nature Awards
  • Nature Careers
  • Nature Conferences

Regional websites

  • Nature Africa
  • Nature China
  • Nature India
  • Nature Japan
  • Nature Middle East
  • Privacy Policy
  • Use of cookies
  • Legal notice
  • Accessibility statement
  • Terms & Conditions
  • Your US state privacy rights
Springer Nature

© 2026 Springer Nature Limited

Nature Briefing: Translational Research

Sign up for the Nature Briefing: Translational Research newsletter — top stories in biotechnology, drug discovery and pharma.

Get what matters in translational research, free to your inbox weekly. Sign up for Nature Briefing: Translational Research