The DOI matches its Crossref record; 289 of the 289 references it cites were found in a registry or an index.
Mechanisms of assembly and remodelling of the extracellular matrix
Open accessAbstract
The extracellular matrix (ECM) is the complex meshwork of proteins and glycans that forms the scaffold that surrounds and supports cells. It exerts key roles in all aspects of metazoan physiology, from conferring physical and mechanical properties on tissues and organs to modulating cellular processes such as proliferation, differentiation and migration. Understanding the mechanisms that orchestrate the assembly of the ECM scaffold is thus crucial to understand ECM functions in health and disease. This Review discusses novel insights into the compositional diversity of matrisome components and the mechanisms that lead to tissue-specific assemblies and architectures tailored to support specific functions. The Review then highlights recently discovered mechanisms, including post-translational modifications and metabolic pathways such as amino acid availability and the circadian clock, that modulate ECM secretion, assembly and remodelling in homeostasis and human diseases. Last, the Review explores the potential of ‘matritherapies’, that is, strategies to normalize ECM composition and architecture to achieve a therapeutic benefit. The extracellular matrix (ECM) is a scaffold that supports cell structure and function. This Review discusses the compositional diversity, tissue-specific assembly and remodelling of the ECM in health and disease, and explores its potential for therapeutic targeting.
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Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606
The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145
Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin
Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323
UniProt: the Universal Protein Knowledgebase in 2023
The UniProt Consortium, Bateman, A., Martin, M.-J., Orchard, S., Magrane, M., Ahmad, S., Alpi, E., Bowler-Barnett, E. H., Britto, R., Bye-A-Jee, H., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkac1052 · Cited by 7,210
Collagen Structure and Stability
Shoulders, M. D., & Raines, R. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.032207.120833 · Cited by 3,923
The Extracellular Matrix: Not Just Pretty Fibrils
Hynes, R. O. (2009) · Science · doi:10.1126/science.1176009 · Cited by 3,527
Disruption of epithelial cell-matrix interactions induces apoptosis
Frisch, S., & Francis, H. (1994) · The Journal of cell biology · doi:10.1083/jcb.124.4.619 · Cited by 3,254
Fredriksson, R., Lagerström, M. C., Lundin, L.-G., & Schiöth, H. B. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.6.1256 · Cited by 2,941
Paysan-Lafosse, T., Blum, M., Chuguransky, S., Grego, T., Pinto, B. L., Salazar, G. A., Bileschi, M. L., Bork, P., Bridge, A., Colwell, L., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkac993 · Cited by 2,399
Ricard-Blum, S. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004978 · Cited by 2,305
Research works printed but not linked: 12
- Jones, M. J. & Jones, M. C. Cell cycle control by cell–matrix interactions. Curr. Opin. Cell Biol. 86, 102288 (2023). · doi:10.1016/j.ceb.2023.102288
- Merry, C. L. R. et al. in Essentials of Glycobiology 4th edn (eds Varki, A. et al.) Ch. 17 (Cold Spring Harbor Laboratory Press, 2022).
- Schwenzer, A. et al. Identification of an immunodominant peptide from citrullinated tenascin-C as a major target for autoantibodies in rheumatoid arthritis. Ann. Rheum. Dis. 75, 1876–1883 (2016). · doi:10.1136/annrheumdis-2015-208495
- Naba, A., Clauser, K. R. & Hynes, R. O. Enrichment of extracellular matrix proteins from tissues and digestion into peptides for mass spectrometry analysis. J. Vis. Exp. 101, e53057 (2015).
- Bagdonaite, I. et al. Glycoproteomics. Nat. Rev. Methods Prim. 2, 47 (2022). · doi:10.1038/s43586-022-00140-8
- Rudd, P. M. et al. in Essentials of Glycobiology 4th edn (eds Varki, A. et al.) Ch. 51 (Cold Spring Harbor Laboratory Press, 2022).
- Wilhelm, D. et al. Tissue-specific collagen hydroxylation at GEP/GDP triplets mediated by P4HA2. Matrix Biol. 119, 141–153 (2023). · doi:10.1016/j.matbio.2023.03.009
- McKee, K. K., Hohenester, E., Aleksandrova, M. & Yurchenco, P. D. Organization of the laminin polymer node. Matrix Biol. 98, 49–63 (2021). · doi:10.1016/j.matbio.2021.05.004
- Shaw, L., Sugden, C. J. & Hamill, K. J. Laminin polymerization and inherited disease: lessons from genetics. Front. Genet. 12, 707087 (2021). · doi:10.3389/fgene.2021.707087
- Lovett, B. M., Hill, K. E., Randolph, E. M., Wang, L. & Schwarzbauer, J. E. Nucleation of fibronectin fibril assembly requires binding between heparin and the 13th type III module of fibronectin. J. Biol. Chem. 299, 104622 (2023). · doi:10.1016/j.jbc.2023.104622
- Bornert, O. et al. QR-313, an antisense oligonucleotide, shows therapeutic eficacy for treatment of dominant and recessive dystrophic epidermolysis bullosa: a preclinical study. J. Invest. Dermatol. 141, 883–893.e6 (2021). · doi:10.1016/j.jid.2020.08.018
- Crockett, D. K. et al. The Alport syndrome COL4A5 variant database. Hum. Mutat. 31, E1652–E1657 (2010). · doi:10.1002/humu.21312
Cited by
Breaking Boundaries: Chronic Diseases and the Frontiers of Immune Microenvironments
Li, G., Wan, Y., Jiao, A., Jiang, K., Cui, G., Tang, J., Yu, S., Hu, Z., Zhao, S., Yi, Z., et al. (2025) · Med Research · doi:10.1002/mdr2.70007 · Cited by 63
Metadata
- Authors
- Naba, A.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2024-09-02
- Volume
- 25
- Issue
- 11
- Pages
- 865-885
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W4402126619
- Cited by
- 316
- References
- 289
- FWCI
- 20.70
- Type
- journal article
- Language
- en
- Open access
- green
- Licence
- www.springernature.com/gp/researchers/text-and-data-mining (tdm)
- www.springernature.com/gp/researchers/text-and-data-mining (vor)
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- Naba, A. (2024). Mechanisms of assembly and remodelling of the extracellular matrix. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/s41580-024-00767-3
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
