The DOI matches its Crossref record; 85 of the 86 references it cites were found in a registry or an index.
Overview of the Matrisome--An Inventory of Extracellular Matrix Constituents and Functions
Open accessAbstract
Completion of genome sequences for many organisms allows a reasonably complete definition of the complement of extracellular matrix (ECM) proteins. In mammals this "core matrisome" comprises ∼300 proteins. In addition there are large numbers of ECM-modifying enzymes, ECM-binding growth factors, and other ECM-associated proteins. These different categories of ECM and ECM-associated proteins cooperate to assemble and remodel extracellular matrices and bind to cells through ECM receptors. Together with receptors for ECM-bound growth factors, they provide multiple inputs into cells to control survival, proliferation, differentiation, shape, polarity, and motility of cells. The evolution of ECM proteins was key in the transition to multicellularity, the arrangement of cells into tissue layers, and the elaboration of novel structures during vertebrate evolution. This key role of ECM is reflected in the diversity of ECM proteins and the modular domain structures of ECM proteins both allow their multiple interactions and, during evolution, development of novel protein architectures.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Hynes and Naba first presented the matrisomics concept in 2012, establishing a matrisome database (http://matrisomeproject.mit.edu/) which classifies ECM into core matrisome proteins, including collagens, proteoglycans, and glycoproteins, and matrisome‐associated proteins, encompassing secreted factors, regulators, and ECM‐affiliated proteins, thus providing a reliable reference for comprehensive”
From Bioactive scaffolds for tissue engineering: A review of decellularized extracellular matrix applications and innovations (2025) · cites this paper as [118]
Experimental — accuracy not yet measuredIn the citing paper
“Native ECM is complex; it contains over 300 different proteins, each of which has a different biological function and stiffness123.”
From Towards organoid culture without Matrigel (2021) · cites this paper as [123]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606
Self-citationMatrix Metalloproteinases: Regulators of the Tumor Microenvironment
Kessenbrock, K., Plaks, V., & Werb, Z. (2010) · Cell · doi:10.1016/j.cell.2010.03.015 · Cited by 5,151
The Extracellular Matrix: Not Just Pretty Fibrils
Hynes, R. O. (2009) · Science · doi:10.1126/science.1176009 · Cited by 3,527
Self-citationMatrix metalloproteinases and the regulation of tissue remodelling
Page-McCaw, A., Ewald, A. J., & Werb, Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2125 · Cited by 2,630
Towards a knowledge-based Human Protein Atlas
Uhlen, M., Oksvold, P., Fagerberg, L., Lundberg, E., Jonasson, K., Forsberg, M., Zwahlen, M., Kampf, C., Wester, K., Hober, S., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt1210-1248 · Cited by 2,440
Ricard-Blum, S. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004978 · Cited by 2,305
Extracellular Matrix Degradation and Remodeling in Development and Disease
Lu, P., Takai, K., Weaver, V. M., & Werb, Z. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005058 · Cited by 2,265
Humphries, J. D., Byron, A., & Humphries, M. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03098 · Cited by 1,711
Heparan sulphate proteoglycans fine-tune mammalian physiology
Bishop, J. R., Schuksz, M., & Esko, J. D. (2007) · Nature · doi:10.1038/nature05817 · Cited by 1,631
Heparan Sulfate ProteoglycansPreprint
Sarrazin, S., Lamanna, W. C., & Esko, J. D. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004952 · Cited by 1,605
Flagged first, then by citations
1 of the 86 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Hynes RO. 1990. Fibronectins. Springer-Verlag, New York.
Cited by
Sorted by citations
Items 501–600 of 999
Barqué, A., Jan, K., Fuente, E. D. L., Nicholas, C. L., Hynes, R. O., & Naba, A. (2020) · Developmental Dynamics · doi:10.1002/dvdy.258 · Cited by 24
Self-citationPijning, A. E., Blyth, M. T., Coote, M. L., Passam, F. H., Chiu, J., & Hogg, P. J. (2021) · Blood · doi:10.1182/blood.2021012441 · Cited by 25
Defining the versican interactome in lung health and disease
Tang, F., Brune, J. E., Chang, M. Y., Reeves, S. R., Altemeier, W. A., & Frevert, C. W. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00162.2022 · Cited by 25
Li, X., Li, W., Xu, L., & Song, Y. (2023) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002818 · Cited by 26
A New Chapter for Mesenchymal Stem Cells: Decellularized Extracellular Matrices
Anasiz, Y., Özgül, R. K., & Uçkan, D. (2017) · Stem Cell Reviews and Reports · doi:10.1007/s12015-017-9757-x · Cited by 25
Autophagy in the mesh of collagen VI
Castagnaro, S., Gambarotto, L., Cescon, M., & Bonaldo, P. (2020) · Matrix Biology · doi:10.1016/j.matbio.2020.12.004 · Cited by 25
Ortega, J. A., de Aguiar, G. P. S., Chandravanshi, P., Levy, N., Engel, E., & Álvarez, Z. (2024) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1962 · Cited by 27
Fetal-like reversion in the regenerating intestine is regulated by mesenchymal asporin
Iqbal, S., Andersson, S., Nesta, E., Pentinmikko, N., Kumar, A. A., Jha, S. K., Borshagovski, D., Webb, A., Gebert, N., Viitala, E. W., et al. (2025) · Cell stem cell · doi:10.1016/j.stem.2025.02.009 · Cited by 34
Three-dimensional bio-derived materials for biomedical applications: challenges and opportunities
Singaravelu, S., Abrahamse, H., & Kumar, S. S. D. (2025) · RSC Advances · doi:10.1039/d4ra07531e · Cited by 28
Extracellular Matrix Remodeling During Palate Development
Wang, X., Li, C., Zhu, Z., Yuan, L., Chan, W. Y., & Sha, O. (2020) · Organogenesis · doi:10.1080/15476278.2020.1735239 · Cited by 24
Vishwanath, N., Monis, W. J., Hoffmann, G. A., Ramachandran, B., DiGiacomo, V., Wong, J. Y., Smith, M. L., & Layne, M. D. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013902 · Cited by 25
Efthymiou, G., Radwańska, A., Grapa, A.-I., Divonne, S. B.-D. L. F., Grall, D., Schaub, S., Hattab, M., Pisano, S., Poët, M., Pisani, D. F., et al. (2021) · Journal of Cell Science · doi:10.1242/jcs.252957 · Cited by 25
Gouardères, S., Ober, C., Doumard, L., Dandurand, J., Vicendo, P., Fourquaux, I., Golberg, A., Samouillan, V., & Gibot, L. (2021) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2021.09.025 · Cited by 25
The Matrisome Is Associated with Metabolic Reprograming in Stem-like Phenotypes of Gastric Cancer
Sung, J., & Cheong, J. (2022) · Cancers · doi:10.3390/cancers14061438 · Cited by 24
Matrix proteoglycans in tumor inflammation and immunity
Deb, G., Cicala, A., Papadas, A., & Asimakopoulos, F. A. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00023.2022 · Cited by 26
The Actin Network Interfacing Diverse Integrin-Mediated Adhesions
Geiger, B., Boujemaa‐Paterski, R., Winograd-Katz, S. E., Venghateri, J. B., Chung, W.-L., & Medalia, O. (2023) · Biomolecules · doi:10.3390/biom13020294 · Cited by 23
Gao, Q., Jia, F., Li, X., Kong, Y., Tian, Z., Bi, L., & Li, L. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114655 · Cited by 23
Extracellular Matrix as a Driver of Chronic Lung Diseases
Burgess, J. K., Weiss, D. J., Westergren‐Thorsson, G., Wigén, J., Dean, C. H., Mumby, S. E., Bush, A., & Adcock, I. M. (2024) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2023-0176ps · Cited by 31
Pregnancy-Induced Dynamical and Structural Changes of Reproductive Tract Collagen
Dhital, B., Gul‐E‐Noor, F., Downing, K. T., Hirsch, S., & Boutis, G. S. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.05.049 · Cited by 24
Epithelial cell integrin β1 is required for developmental angiogenesis in the pituitary gland
Scully, K. M., Skowronska‐Krawczyk, D., Krawczyk, M., Merkurjev, D., Taylor, H., Livolsi, A., Tollkühn, J., Stan, R. V., & Rosenfeld, M. G. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614970113 · Cited by 24
Schiera, G., Liegro, C. M. D., & Liegro, I. D. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122774 · Cited by 23
Biosynthesis and assembly of the Collagen IV-like protein Pericardin inDrosophila melanogaster
Wilmes, A. C., Klinke, N., Rotstein, B., Meyer, H., & Paululat, A. (2018) · Biology Open · doi:10.1242/bio.030361 · Cited by 24
Andrews, R. N., Dugan, G. O., Peiffer, A. M., Hawkins, G. A., Hanbury, D. B., Bourland, J. D., Hampson, R. E., Deadwyler, S. A., & Cline, J. M. (2019) · Radiation Research · doi:10.1667/rr15263.1 · Cited by 24
Choudhary, S., Burns, S. C., Mirsafian, H., Li, W., Vo, D. T., Qiao, M., Lei, X., Smith, A. D., & Penalva, L. O. F. (2020) · Scientific Reports · doi:10.1038/s41598-020-65638-1 · Cited by 24
Cell-Extracellular Matrix Interactions Play Multiple Essential Roles in Aortic Arch Development
Warkala, M., Chen, D., Jubran, A., Ramirez, A., Schonning, M. J., Wang, X., Zhao, H., & Astrof, S. (2020) · Circulation Research · doi:10.1161/circresaha.120.318200 · Cited by 24
The Thermodynamics of Medial Vascular Calcification
Millán, Á., Lanzer, P., & Sorribas, V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.633465 · Cited by 23
The extracellular matrix phenome across species
Statzer, C., & Ewald, C. Y. (2020) · Matrix Biology Plus · doi:10.1016/j.mbplus.2020.100039 · Cited by 21
Senescence-Associated Alterations in Matrisome of Mesenchymal Stem Cells
Константиновна, М. Д., Kashirina, D. N., Ездакова, М. И., Larina, I., Buravkova, L. B., & Ratushnyy, A. Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25105332 · Cited by 23
Wei, J., Wang, G., Li, X., Ren, P., Yu, H., & Dong, B. (2017) · Biology Open · doi:10.1242/bio.026336 · Cited by 23
The Rapidly Evolving Concept of Whole Heart Engineering
Iop, L., Sasso, E. D., Menabò, R., Lisa, F. D., & Gerosa, G. (2017) · Stem Cells International · doi:10.1155/2017/8920940 · Cited by 23
Dermal Fibroblast SLC3A2 Deficiency Leads to Premature Aging and Loss of Epithelial Homeostasis
Tissot, F. S., Estrach, S., Boulter, E., Cailleteau, L., Tosello, L., Seguin, L., Pisano, S., Audebert, S., Croce, O., & Féral, C. C. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2018.05.026 · Cited by 26
Roles of Fibulin-2 in Carcinogenesis
Zhang, H., Hui, D., & Fu, X. (2020) · Medical Science Monitor · doi:10.12659/msm.918099 · Cited by 23
Papadimitriou, K., Kostopoulos, I. V., Tsopanidou, A., Orologas‐Stavrou, N., Kastritis, E., Tsitsilonis, O., Dimopoulos, M. A., & Terpos, E. (2020) · Cancers · doi:10.3390/cancers12082006 · Cited by 23
Bascetin, R., Laurent-Issartel, C., Blanc‐Fournier, C., Vendrely, C., Kellouche, S., Carreiras, F., Gallet, O., & Leroy‐Dudal, J. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.120610 · Cited by 23
Mass spectrometry methods for analysis of extracellular matrix components in neurological diseases
Downs, M. J., Zaia, J., & Sethi, M. K. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21792 · Cited by 23
Recent advances in lab-on-a-chip systems for breast cancer metastasis research
Yildirir, B. F., Yalcin-Ozuysal, Ö., & Nonappa, N. (2023) · Nanoscale Advances · doi:10.1039/d2na00823h · Cited by 31
3D in vitro cell culture models of tube formation
Zegers, M. M. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.02.016 · Cited by 24
Liem, D. A., Murali, S., Sigdel, D., Shi, Y., Wang, X., Shen, J., Choi, H., Caufield, J. H., Wang, W. W., Ping, P., et al. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00175.2018 · Cited by 23
Engineered basement membranes: fromin vivoconsiderations to cell-based assays
Perry, G., Xiao, W., Welsh, G. I., Perriman, A. W., & Lennon, R. (2018) · Integrative Biology · doi:10.1039/c8ib00138c · Cited by 24
Horst, E. N., Bregenzer, M. E., Mehta, P., Snyder, C. S., Repetto, T., Yang‐Hartwich, Y., & Mehta, G. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.04.041 · Cited by 25
Dose-Dependent Effects of Matrix Metalloproteinases On Ecm Hydrogel Biodegradation
Didwischus, N., Guduru, A., Badylak, S. F., & Modo, M. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.12.003 · Cited by 22
Bio Mimicking of Extracellular Matrix
Ghosh, M., Halperin‐Sternfeld, M., & Adler‐Abramovich, L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9791-2_12 · Cited by 22
Sparacio, A. P., Trojanowski, N. F., Snetselaar, K. M., Nelson, M. D., & Raizen, D. M. (2020) · PLoS ONE · doi:10.1371/journal.pone.0233059 · Cited by 20
Advances in the clinical use of collagen as biomarker of liver fibrosis
Meurer, S. K., Karsdal, M. A., & Weiskirchen, R. (2020) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2020.1814746 · Cited by 22
Werkman, I. L., Dubbelaar, M. L., van der Vlies, P., de Boer-Bergsma, J. J., Eggen, B. J. L., & Baron, W. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-02045-3 · Cited by 23
Freitas, A., Aroso, M., Rocha, S., Ferreira, R. M., Vitorino, R. M. P., & Gómez-Lázaro, M. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15316 · Cited by 21
Hindi, E. A., Williams, C. J., Zeef, L. A. H., Lopes, F. M., Newman, K., Davey, M., Hodson, N. W., Hilton, E. N., Huang, J. L., Price, K. L., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-94532-7 · Cited by 22
Tissue, age, sex, and disease patterns of matrisome expression in GTEx transcriptome data
Nieuwenhuis, T. O., Rosenberg, A. Z., McCall, M. N., & Halushka, M. K. (2021) · Scientific Reports · doi:10.1038/s41598-021-00943-x · Cited by 21
Francés‐Herrero, E., Rodríguez‐Eguren, A., Gómez‐Álvarez, M., de Miguel–Gómez, L., Ferrero, H., & Cervelló, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073765 · Cited by 23
Collagen and elastic fiber remodeling in the pregnant mouse myometrium
Ouellette, A., Mahendroo, M., & Nallasamy, S. (2022) · Biology of Reproduction · doi:10.1093/biolre/ioac102 · Cited by 22
Rao, Y., Zhu, C., Suen, H. C., Huang, S., Liao, J., Ker, D. F. E., Tuan, R. S., & Wang, D. M. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-022-03038-0 · Cited by 22
Jailkhani, N., Clauser, K. R., Mak, H. H., Rickelt, S., Tian, C., Whittaker, C. A., Tanabe, K. K., Purdy, S. R., Carr, S. A., & Hynes, R. O. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-1532 · Cited by 22
Self-citationAlveolar repair following LPS-induced injury requires cell-ECM interactions
Sucre, J. M. S., Bock, F. M., Negretti, N. M., Benjamin, J. T., Gulleman, P. M., Dong, X., Ferguson, K. T., Jetter, C. S., Han, W., Liu, Y., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.167211 · Cited by 23
Afshar, K., Sanaei, M., Ravari, M. S., Pourbagheri‐Sigaroodi, A., & Bashash, D. (2023) · Cell Biochemistry and Function · doi:10.1002/cbf.3846 · Cited by 23
Mechanism of irradiation‐induced mammary cancer metastasis: A role for SAP‐dependent Mkl1 signaling
Asparuhova, M. B., Secondini, C., Rüegg, C., & Chiquet‐Ehrismann, R. (2015) · Molecular Oncology · doi:10.1016/j.molonc.2015.04.003 · Cited by 22
Extracellular matrix constitution and function for tissue regeneration and repair
Caldeira, J., Sousa, A., Sousa, D. M., & Barros, D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-08-100803-4.00002-4 · Cited by 24
Caires‐dos‐Santos, L., da Silva, S. V., Smuczek, B., de Siqueira, A. S., Borbely, K. S. C., Barbuto, J. A. M., Augusto, T. M., Freitas, V. M., Carvalho, H. F., & Jaeger, R. G. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28997 · Cited by 21
Extracellular Matrix as an Inductive Scaffold for Functional Tissue Reconstruction
Brown, B. N., & Badylak, S. F. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800548-4.00002-4 · Cited by 21
Prospective Multicenter Evaluation of an Advanced Extracellular Matrix for Wound Management
Raizman, R., Hill, R., & Woo, K. Y. (2020) · Advances in Skin & Wound Care · doi:10.1097/01.asw.0000667052.74087.d6 · Cited by 22
Proteomic analysis of decellularized mice liver and kidney extracellular matrices
Diedrich, A.-M., Daneshgar, A., Tang, P., Klein, O., Mohr, A., Onwuegbuchulam, O. A., von Rüden, S., Menck, K., Bleckmann, A., Juratli, M. A., et al. (2024) · Journal of Biological Engineering · doi:10.1186/s13036-024-00413-8 · Cited by 23
Biomaterials‐Boosted Immunotherapy for Osteosarcoma
Sun, C., Li, S., & Ding, J. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202400864 · Cited by 25
Jiang, J., Xu, C., Han, D., Lu, Y., Yang, F., Wang, J., Yan, X., Mu, X., Zhang, J., Jia, C., et al. (2024) · Biomarker Research · doi:10.1186/s40364-024-00656-z · Cited by 24
Liu, R., Dai, M., Gong, G., Chen, M., Cao, C., Wang, T., Hou, Z., Shi, Y., Guo, J., Zhang, Y., et al. (2022) · Journal of Leather Science and Engineering · doi:10.1186/s42825-022-00087-2 · Cited by 22
Horwacik, I. (2022) · Cells · doi:10.3390/cells11193172 · Cited by 23
Fibroblasts secrete fibronectin under lamellipodia in a microtubule- and myosin II–dependent fashion
Huet-Calderwood, C., Rivera-Molina, F. E., Toomre, D. K., & Calderwood, D. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202204100 · Cited by 21
Maiti, G., Ashworth, S., Choi, T., & Chakravarti, S. (2023) · Matrix Biology · doi:10.1016/j.matbio.2023.10.001 · Cited by 23
Yao, J., Atasheva, S., Wagner, N. J., Paolo, N. C. D., Stewart, P. L., & Shayakhmetov, D. M. (2023) · Molecular Therapy · doi:10.1016/j.ymthe.2023.10.023 · Cited by 23
Matricellular proteins in cancer: a focus on secreted Frizzled-related proteins
Vincent, K. M., & Postovit, L.-M. M. (2017) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-017-0398-2 · Cited by 21
Zappia, J., Joiret, M., Sanchez, C., Lambert, C., Geris, L., Müller, M., & Henrotin, Y. E. (2020) · Biomolecules · doi:10.3390/biom10010080 · Cited by 21
A Systematic Review of Extracellular Matrix-Related Alterations in Parkinson’s Disease
Chapman, M. A., & Sorg, B. A. (2024) · Brain Sciences · doi:10.3390/brainsci14060522 · Cited by 21
Tomos, I. P., Kanellopoulou, P., Nastos, D., & Aidinis, V. (2025) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2025.2471579 · Cited by 19
Huang, J., Sun, L., Yin, Y., Yang, H., Zeng, K., Huang, P., Liang, X., Wu, J., Xiang, A. P., & Wang, J. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116207 · Cited by 20
Weng, B., Wang, Y., Zhang, Q., Jiang, Y., Shang, J., Liu, X., & Wang, F. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202507241 · Cited by 20
Jeyaraj, G., Rajendran, A. K., Sathishkumar, K., Almutairi, B. O., Vadivelu, A., Chokkakula, S., Tu, Y., & Xie, W. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1688455 · Cited by 25
Breaking down barriers: the evolution of cell invasion
Medwig-Kinney, T. N., & Matus, D. Q. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.08.003 · Cited by 20
Tumour Initiation: a Discussion on Evidence for a “Load-Trigger” Mechanism
Evans, J. J., Alkaisi, M. M., & Sykes, P. H. (2019) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-019-00888-z · Cited by 20
Zamboulis, D. E., Thorpe, C. T., Kharaz, Y. A., Birch, H. L., Screen, H. R. C., & Clegg, P. (2020) · eLife · doi:10.7554/elife.58075 · Cited by 20
Draicchio, F., Behrends, V., Tillin, N. A., Hurren, N. M., Sylow, L., & Mackenzie, R. (2022) · The Journal of Physiology · doi:10.1113/jp283039 · Cited by 23
Clinical applications of 3D normal and breast cancer organoids: A review of concepts and methods
Lewis, S. M., Callaway, M. K., & dos Santos, C. O. (2022) · Experimental Biology and Medicine · doi:10.1177/15353702221131877 · Cited by 20
Re-Sensitizing Cancer Stem Cells to Conventional Chemotherapy Agents
Kim, M., Bakyt, L., Akhmetkaliyev, A., Toktarkhanova, D., & Bulanin, D. S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032122 · Cited by 21
Tang, R.-Z., & Liu, X. (2023) · Materials Today Bio · doi:10.1016/j.mtbio.2023.100607 · Cited by 21
Matrix stiffness, endothelial dysfunction and atherosclerosis
Xu, Z., Chen, Y., Wang, Y., Han, W., Xu, W., Liao, X., Zhang, T., & Wang, G. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08502-5 · Cited by 20
Influence of Extracellular Vesicles on Lung Stromal Cells during Breast Cancer Metastasis
Patel, U., Susman, D., & Allan, A. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411801 · Cited by 20
Metalloproteinases as Biomarkers and Sociomarkers in Human Health and Disease
Costa, D., Scalise, E., Ielapi, N., Bracale, U. M., Andreucci, M., & Serra, R. (2024) · Biomolecules · doi:10.3390/biom14010096 · Cited by 23
Directionality of Macrophages Movement in Tumour Invasion: A Multiscale Moving-Boundary Approach
Suveges, S., Eftimie, R., & Trucu, D. (2020) · Bulletin of Mathematical Biology · doi:10.1007/s11538-020-00819-7 · Cited by 22
Vascularization Strategies for Tissue Engineering for Tracheal Reconstruction
Sun, F., Lü, Y., Wang, Z., & Shi, H. (2021) · Regenerative Medicine · doi:10.2217/rme-2020-0091 · Cited by 20
Feng, Y., Jiang, Y., & Hao, F. (2021) · Journal of Translational Medicine · doi:10.1186/s12967-021-03050-7 · Cited by 21
Batzios, S. P., Zafeiriou, D., & Papakonstantinou, E. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.02.035 · Cited by 20
Nossin, Y., Farrell, E., Koevoet, W. J. L. M., Somoza, R. A., Caplan, A. I., Brachvogel, B., & van Osch, G. J. V. M. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00327 · Cited by 19
Fu, H., Sun, Y., Shao, Y., Saredy, J., Cueto, R., Liu, L., Drummer, C., Johnson, C., Xu, K., Lu, Y., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.595813 · Cited by 20
Holkar, K., Kale, V. P., & Ingavle, G. C. (2022) · Biomaterials Science · doi:10.1039/d2bm00750a · Cited by 19
Degradomics technologies in matrisome exploration
Haack, A. M., Overall, C. M., & Keller, U. A. D. (2022) · Matrix Biology · doi:10.1016/j.matbio.2022.10.003 · Cited by 20
Davis, J. L., Kennedy, C., Clerkin, S., Treacy, N. J., Dodd, T., Moss, C., Murphy, A., Brazil, D. P., Cagney, G., Brougham, D. F., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-04264-1 · Cited by 22
Extracellular Matrix of Echinoderms
Dolmatov, I. Y., & Nizhnichenko, V. A. (2023) · Marine Drugs · doi:10.3390/md21070417 · Cited by 19
Effects of Hyaluronan on Breast Cancer Aggressiveness
Parnigoni, A., Moretto, P., Viola, M., Karousou, E. G., Passi, A. G., & Vigetti, D. (2023) · Cancers · doi:10.3390/cancers15153813 · Cited by 20
Pereira, M. C. A., Soares, C. O., Canuto, G. A. B., Tavares, M. F. M., Colli, W., & Alves, M. J. M. (2015) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0003683 · Cited by 19
Vascular Bed Molecular Profiling by Differential Systemic Decellularization In Vivo
Serra, A., Gallart‐Palau, X., Park, J. E., Lim, G. G. Y., Lim, K. L., Ho, H. H., Tam, J. P., & Sze, S. K. (2018) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.311552 · Cited by 19
Robert, A. W., Pereira, I. T., Dallagiovanna, B., & Stimamiglio, M. A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00049 · Cited by 19
The Good and Bad Sides of Heparanase-1 and Heparanase-2
Pinhal, M. A. D. S., Melo, C. M., & Nader, H. B. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-34521-1_36 · Cited by 19
Li, W., Wu, Y., Zhang, Y., Gao, W., Li, X., Luo, H., Lu, M., Liu, Z., & Luo, A. (2025) · Advanced Science · doi:10.1002/advs.202416523 · Cited by 22
Metadata
- Authors
- Hynes, R. O., & Naba, A.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Hynes, R. O.
- ORCID
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-09-21
- Volume
- 4
- Issue
- 1
- Pages
- a004903-a004903
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3249625
- OpenAlex
- W2119792393
- Cited by
- 1,349
- References
- 86
- Citations by year
- 2026: 94 · 2025: 137 · 2024: 129 · 2023: 143 · 2022: 142 · 2021: 146 · 2020: 136 · 2019: 85 · 2018: 93 · 2017: 61 · 2016: 46 · 2015: 37 · 2014: 46 · 2013: 37 · 2012: 12
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (U54CA163109, P30CA014051)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Keywords
- extracellular matrix, matrisome, ECM receptors, extracellular matrix remodeling, cell-matrix interactions, evolution of multicellularity, protein domain architecture, cell proliferation and differentiation
- MeSH terms
- Animals, Collagen, Glycoproteins, Humans, Proteoglycans, Integrins, Transforming Growth Factor beta, Extracellular Matrix Proteins, Evolution, Molecular
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review