Abstract
The extracellular matrix (ECM) is the complex scaffold made of hundreds of proteins that governs the organization of cells and tissues in all multicellular organisms. It provides structural and mechanical properties to tissues. It also exerts signaling roles, either directly by interacting with cell surface receptors, or by interacting with growth factors and modulating their signaling activities, and by doing so regulates a multitude of cellular functions including cell-matrix interactions, cell proliferation, survival, and differentiation. The purpose of this introductory chapter is to present resources and tools developed to facilitate the identification and analysis of ECM genes and proteins across different conditions using high-throughput methodologies (i.e., genomics, transcriptomics, proteomics, and interactomics). Databases focused on specific ECM genes and ECM-related diseases including genetic diseases are highlighted in the second part of the chapter. The accessibility and standardization of -omic data are a prerequisite for the FAIR (Findability, Accessibility, Interoperability, and Reusability) guiding principles for scientific data management.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
Notes
- 1.
We apologize to the authors of studies we were not able to cite due to space limitations.
References
We apologize to the authors of studies we were not able to cite due to space limitations.
Amberger JS, Bocchini CA, Scott AF, Hamosh A (2019) OMIM.org: leveraging knowledge across phenotype-gene relationships. Nucleic Acids Res 47:D1038–D1043. https://doi.org/10.1093/nar/gky1151
Attrill H, Gaudet P, Huntley RP, Lovering RC, Engel SR, Poux S, Van Auken KM, Georghiou G, Chibucos MC, Berardini TZ, Wood V, Drabkin H, Fey P, Garmiri P, Harris MA, Sawford T, Reiser L, Tauber R, Toro S (2019) Annotation of gene product function from high-throughput studies using the gene ontology. Database (Oxford) 2019. https://doi.org/10.1093/database/baz007
Aumailley M (2013) The laminin family. Cell Adh Migr 7:48–55. https://doi.org/10.4161/cam.22826
Bateman JF, Boot-Handford RP, Lamandé SR (2009) Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations. Nat Rev Genet 10:173–183. https://doi.org/10.1038/nrg2520
Berardi AC (ed) (2018) Extracellular matrix for tissue engineering and biomaterials. Humana Press, Totowa, NJ
Bin Lim S, Chua MLK, Yeong JPS, Tan SJ, Lim W-T, Lim CT (2019) Pan-cancer analysis connects tumor matrisome to immune response. NPJ Precis Oncol 3:15. https://doi.org/10.1038/s41698-019-0087-0
Bingham GC, Lee F, Naba A, Barker TH (2020) Spatial-omics: novel approaches to probe cell heterogeneity and ECM biology. Matrix Biol 91-92:152–166.
Brekken RA, Stupack D (eds) (2017) Extracellular matrix in tumor biology. Springer, Berlin
Burn J, Watson M (2016) The Human Variome Project. Hum Mutat 37:505–507. https://doi.org/10.1002/humu.22986
Chautard E, Ballut L, Thierry-Mieg N, Ricard-Blum S (2009) MatrixDB, a database focused on extracellular protein–protein and protein–carbohydrate interactions. Bioinformatics 25:690–691. https://doi.org/10.1093/bioinformatics/btp025
Chautard E, Fatoux-Ardore M, Ballut L, Thierry-Mieg N, Ricard-Blum S (2011) MatrixDB, the extracellular matrix interaction database. Nucleic Acids Res 39:D235–D240. https://doi.org/10.1093/nar/gkq830
Chew C, Lennon R (2018) Basement membrane defects in genetic kidney diseases. Front Pediatr 6. https://doi.org/10.3389/fped.2018.00011
Clerc O, Deniaud M, Vallet SD, Naba A, Rivet A, Perez S, Thierry-Mieg N, Ricard-Blum S (2019) MatrixDB: integration of new data with a focus on glycosaminoglycan interactions. Nucleic Acids Res 47:D376–D381. https://doi.org/10.1093/nar/gky1035
Collod-Béroud G, Le Bourdelles S, Ades L, Ala-Kokko L, Booms P, Boxer M, Child A, Comeglio P, De Paepe A, Hyland JC, Holman K, Kaitila I, Loeys B, Matyas G, Nuytinck L, Peltonen L, Rantamaki T, Robinson P, Steinmann B, Junien C, Béroud C, Boileau C (2003) Update of the UMD-FBN1 mutation database and creation of an FBN1 polymorphism database. Hum Mutat 22:199–208. https://doi.org/10.1002/humu.10249
Crockett DK, Pont-Kingdon G, Gedge F, Sumner K, Seamons R, Lyon E (2010) The Alport syndrome COL4A5 variant database. Hum Mutat 31:E1652–E1657. https://doi.org/10.1002/humu.21312
Dalgleish R (1997) The human type I collagen mutation database. Nucleic Acids Res 25:181–187. https://doi.org/10.1093/nar/25.1.181
Dalgleish R (1998) The Human Collagen Mutation Database 1998. Nucleic Acids Res 26:253–255. https://doi.org/10.1093/nar/26.1.253
DeSimone DW, Mecham R (eds) (2013) Extracellular matrix in development. Springer, Berlin
Domogatskaya A, Rodin S, Tryggvason K (2012) Functional diversity of laminins. Annu Rev Cell Dev Biol 28:523–553. https://doi.org/10.1146/annurev-cellbio-101011-155750
Dzamba BJ, DeSimone DW (2018) Extracellular matrix (ECM) and the sculpting of embryonic tissues. Curr Top Dev Biol 130:245–274. https://doi.org/10.1016/bs.ctdb.2018.03.006
Etich J, Koch M, Wagener R, Zaucke F, Fabri M, Brachvogel B (2019) Gene expression profiling of the extracellular matrix signature in macrophages of different activation status: relevance for skin wound healing. Int J Mol Sci 20. https://doi.org/10.3390/ijms20205086
Fabregat A, Jupe S, Matthews L, Sidiropoulos K, Gillespie M, Garapati P, Haw R, Jassal B, Korninger F, May B, Milacic M, Roca CD, Rothfels K, Sevilla C, Shamovsky V, Shorser S, Varusai T, Viteri G, Weiser J, Wu G, Stein L, Hermjakob H, D’Eustachio P (2018) The Reactome Pathway Knowledgebase. Nucleic Acids Res 46:D649–D655. https://doi.org/10.1093/nar/gkx1132
Fokkema IFAC, Taschner PEM, Schaafsma GCP, Celli J, Laros JFJ, den Dunnen JT (2011) LOVD v.2.0: the next generation in gene variant databases. Hum Mutat 32:557–563. https://doi.org/10.1002/humu.21438
Golbert DCF, Santana-van-Vliet E, Mundstein AS, Calfo V, Savino W, de Vasconcelos ATR (2014) Laminin-database v.2.0: an update on laminins in health and neuromuscular disorders. Nucleic Acids Res 42:D426–D429. https://doi.org/10.1093/nar/gkt901
Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C (2016) ChEBI in 2016: improved services and an expanding collection of metabolites. Nucleic Acids Res 44:D1214–D1219. https://doi.org/10.1093/nar/gkv1031
Hiebert P, Wietecha MS, Cangkrama M, Haertel E, Mavrogonatou E, Stumpe M, Steenbock H, Grossi S, Beer H-D, Angel P, Brinckmann J, Kletsas D, Dengjel J, Werner S (2018) Nrf2-mediated fibroblast reprogramming drives cellular senescence by targeting the matrisome. Dev Cell 46:145–161.e10. https://doi.org/10.1016/j.devcel.2018.06.012
Hohenester E, Yurchenco PD (2013) Laminins in basement membrane assembly. Cell Adh Migr 7:56–63. https://doi.org/10.4161/cam.21831
Horton ER, Byron A, Askari JA, Ng DHJ, Millon-Frémillon A, Robertson J, Koper EJ, Paul NR, Warwood S, Knight D, Humphries JD, Humphries MJ (2015) Definition of a consensus integrin adhesome and its dynamics during adhesion complex assembly and disassembly. Nat Cell Biol 17:1577–1587. https://doi.org/10.1038/ncb3257
Horton ER, Humphries JD, James J, Jones MC, Askari JA, Humphries MJ (2016) The integrin adhesome network at a glance. J Cell Sci 129:4159–4163. https://doi.org/10.1242/jcs.192054
Huang DW, Sherman BT, Lempicki RA (2009) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4:44–57. https://doi.org/10.1038/nprot.2008.211
Hynes RO (2009) The extracellular matrix: not just pretty fibrils. Science 326:1216–1219. https://doi.org/10.1126/science.1176009
Hynes RO, Naba A (2012) Overview of the matrisome - an inventory of extracellular matrix constituents and functions. Cold Spring Harb Perspect Biol 4:a004903–a004903. https://doi.org/10.1101/cshperspect.a004903
Hynes RO, Yamada KM (2012) Extracellular matrix biology, Cold Spring Harbor perspectives in biology. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
IMEx Consortium Curators, Del-Toro N, Duesbury M, Koch M, Perfetto L, Shrivastava A, Ochoa D, Wagih O, Piñero J, Kotlyar M, Pastrello C, Beltrao P, Furlong LI, Jurisica I, Hermjakob H, Orchard S, Porras P (2019) Capturing variation impact on molecular interactions in the IMEx Consortium mutations data set. Nat Commun 10:10. https://doi.org/10.1038/s41467-018-07709-6
Iozzo RV, Gubbiotti MA (2018) Extracellular matrix: the driving force of mammalian diseases. Matrix Biol 71–72:1–9. https://doi.org/10.1016/j.matbio.2018.03.023
Izzi V, Lakkala J, Devarajan R, Savolainen E-R, Koistinen P, Heljasvaara R, Pihlajaniemi T (2018) Expression of a specific extracellular matrix signature is a favorable prognostic factor in acute myeloid leukemia. Leuk Res Rep 9:9–13. https://doi.org/10.1016/j.lrr.2017.12.001
Izzi V, Lakkala J, Devarajan R, Kääriäinen A, Koivunen J, Heljasvaara R, Pihlajaniemi T (2019) Pan-Cancer analysis of the expression and regulation of matrisome genes across 32 tumor types. Matrix Biol Plus 1:100004. https://doi.org/10.1016/j.mbplus.2019.04.001
Jiao X, Sherman BT, Huang DW, Stephens R, Baseler MW, Lane HC, Lempicki RA (2012) DAVID-WS: a stateful web service to facilitate gene/protein list analysis. Bioinformatics 28:1805–1806. https://doi.org/10.1093/bioinformatics/bts251
Jobling R, D’Souza R, Baker N, Lara-Corrales I, Mendoza-Londono R, Dupuis L, Savarirayan R, Ala-Kokko L, Kannu P (2014) The collagenopathies: review of clinical phenotypes and molecular correlations. Curr Rheumatol Rep 16:394. https://doi.org/10.1007/s11926-013-0394-3
Kai F, Drain AP, Weaver VM (2019) The extracellular matrix modulates the metastatic journey. Dev Cell 49:332–346. https://doi.org/10.1016/j.devcel.2019.03.026
Karamanos NK, Theocharis AD, Neill T, Iozzo RV (2019) Matrix modeling and remodeling: a biological interplay regulating tissue homeostasis and diseases. Matrix Biol 75–76:1–11. https://doi.org/10.1016/j.matbio.2018.08.007
Lamandé SR, Bateman JF (2018) Collagen VI disorders: insights on form and function in the extracellular matrix and beyond. Matrix Biol 71–72:348–367. https://doi.org/10.1016/j.matbio.2017.12.008
Lamandé SR, Bateman JF (2019) Genetic disorders of the extracellular matrix. Anat Rec (Hoboken). https://doi.org/10.1002/ar.24086
Lamandé SR, Cameron TL, Savarirayan R, Bateman JF (2017) Molecular genetics of the cartilage collagenopathies. In: Grässel S, Aszódi A (eds) Cartilage, Pathophysiology, vol 2. Springer, Cham, pp 99–133
Landrum MJ, Lee JM, Riley GR, Jang W, Rubinstein WS, Church DM, Maglott DR (2014) ClinVar: public archive of relationships among sequence variation and human phenotype. Nucleic Acids Res 42:D980–D985. https://doi.org/10.1093/nar/gkt1113
Landrum MJ, Chitipiralla S, Brown GR, Chen C, Gu B, Hart J, Hoffman D, Jang W, Kaur K, Liu C, Lyoshin V, Maddipatla Z, Maiti R, Mitchell J, O’Leary N, Riley GR, Shi W, Zhou G, Schneider V, Maglott D, Holmes JB, Kattman BL (2020) ClinVar: improvements to accessing data. Nucleic Acids Res 48:D835–D844. https://doi.org/10.1093/nar/gkz972
Launay G, Salza R, Multedo D, Thierry-Mieg N, Ricard-Blum S (2015) MatrixDB, the extracellular matrix interaction database: updated content, a new navigator and expanded functionalities. Nucleic Acids Res 43:D321–D327. https://doi.org/10.1093/nar/gku1091
Liberzon A, Birger C, Thorvaldsdóttir H, Ghandi M, Mesirov JP, Tamayo P (2015) The Molecular Signatures Database hallmark gene set collection. Cell Syst 1:417–425. https://doi.org/10.1016/j.cels.2015.12.004
Lindsey ML, Jung M, Hall ME, DeLeon-Pennell KY (2018) Proteomic analysis of the cardiac extracellular matrix: clinical research applications. Expert Rev Proteomics 15:105–112. https://doi.org/10.1080/14789450.2018.1421947
Martin S, Söllner C, Charoensawan V, Adryan B, Thisse B, Thisse C, Teichmann S, Wright GJ (2010) Construction of a large extracellular protein interaction network and its resolution by spatiotemporal expression profiling. Mol Cell Proteomics 9:2654–2665. https://doi.org/10.1074/mcp.M110.004119
Mecham R (ed) (2011) The extracellular matrix: an overview. Springer, Berlin
Meester JAN, Verstraeten A, Schepers D, Alaerts M, Van Laer L, Loeys BL (2017) Differences in manifestations of Marfan syndrome, Ehlers-Danlos syndrome, and Loeys-Dietz syndrome. Ann Cardiothorac Surg 6:582–594. https://doi.org/10.21037/acs.2017.11.03
Meldal BHM, Bye-A-Jee H, Gajdoš L, Hammerová Z, Horácková A, Melicher F, Perfetto L, Pokorný D, Lopez MR, Türková A, Wong ED, Xie Z, Casanova EB, Del-Toro N, Koch M, Porras P, Hermjakob H, Orchard S (2019) Complex Portal 2018: extended content and enhanced visualization tools for macromolecular complexes. Nucleic Acids Res 47:D550–D558. https://doi.org/10.1093/nar/gky1001
Merico D, Isserlin R, Stueker O, Emili A, Bader GD (2010) Enrichment map: a network-based method for gene-set enrichment visualization and interpretation. PLoS ONE 5:e13984. https://doi.org/10.1371/journal.pone.0013984
Naba A, Clauser KR, Hoersch S, Liu H, Carr SA, Hynes RO (2012a) The matrisome: in silico definition and in vivo characterization by proteomics of normal and tumor extracellular matrices. Mol Cell Proteomics 11:M111.014647. https://doi.org/10.1074/mcp.M111.014647
Naba A, Hoersch S, Hynes RO (2012b) Towards definition of an ECM parts list: an advance on GO categories. Matrix Biol 31:371–372. https://doi.org/10.1016/j.matbio.2012.11.008
Naba A, Clauser KR, Ding H, Whittaker CA, Carr SA, Hynes RO (2016) The extracellular matrix: tools and insights for the “omics” era. Matrix Biol 49:10–24. https://doi.org/10.1016/j.matbio.2015.06.003
Nagaraj SH, Waddell N, Madugundu AK, Wood S, Jones A, Mandyam RA, Nones K, Pearson JV, Grimmond SM (2015) PGTools: a software suite for proteogenomic data analysis and visualization. J Proteome Res 14:2255–2266. https://doi.org/10.1021/acs.jproteome.5b00029
Orchard S, Kerrien S, Abbani S, Aranda B, Bhate J, Bidwell S, Bridge A, Briganti L, Brinkman FSL, Cesareni G, Chatr-aryamontri A, Chautard E, Chen C, Dumousseau M, Goll J, Hancock REW, Hannick LI, Jurisica I, Khadake J, Lynn DJ, Mahadevan U, Perfetto L, Raghunath A, Ricard-Blum S, Roechert B, Salwinski L, Stümpflen V, Tyers M, Uetz P, Xenarios I, Hermjakob H (2012) Protein interaction data curation: the International Molecular Exchange (IMEx) consortium. Nat Methods 9:345–350. https://doi.org/10.1038/nmeth.1931
Orchard S, Ammari M, Aranda B, Breuza L, Briganti L, Broackes-Carter F, Campbell NH, Chavali G, Chen C, del-Toro N, Duesbury M, Dumousseau M, Galeota E, Hinz U, Iannuccelli M, Jagannathan S, Jimenez R, Khadake J, Lagreid A, Licata L, Lovering RC, Meldal B, Melidoni AN, Milagros M, Peluso D, Perfetto L, Porras P, Raghunath A, Ricard-Blum S, Roechert B, Stutz A, Tognolli M, van Roey K, Cesareni G, Hermjakob H (2014) The MIntAct project--IntAct as a common curation platform for 11 molecular interaction databases. Nucleic Acids Res 42:D358–D363. https://doi.org/10.1093/nar/gkt1115
Parks WC, Mecham R (eds) (2011) Extracellular matrix degradation. Springer, Berlin
Pathan M, Keerthikumar S, Ang C-S, Gangoda L, Quek CYJ, Williamson NA, Mouradov D, Sieber OM, Simpson RJ, Salim A, Bacic A, Hill AF, Stroud DA, Ryan MT, Agbinya JI, Mariadason JM, Burgess AW, Mathivanan S (2015) FunRich: an open access standalone functional enrichment and interaction network analysis tool. Proteomics 15:2597–2601. https://doi.org/10.1002/pmic.201400515
Perez-Riverol Y, Bai M, da Veiga LF, Squizzato S, Park YM, Haug K, Carroll AJ, Spalding D, Paschall J, Wang M, Del-Toro N, Ternent T, Zhang P, Buso N, Bandeira N, Deutsch EW, Campbell DS, Beavis RC, Salek RM, Sarkans U, Petryszak R, Keays M, Fahy E, Sud M, Subramaniam S, Barbera A, Jiménez RC, Nesvizhskii AI, Sansone S-A, Steinbeck C, Lopez R, Vizcaíno JA, Ping P, Hermjakob H (2017) Discovering and linking public omics data sets using the Omics Discovery Index. Nat Biotechnol 35:406–409. https://doi.org/10.1038/nbt.3790
Perez-Riverol Y, Zorin A, Dass G, Vu M-T, Xu P, Glont M, Vizcaíno JA, Jarnuczak AF, Petryszak R, Ping P, Hermjakob H (2019) Quantifying the impact of public omics data. Nat Commun 10:3512. https://doi.org/10.1038/s41467-019-11461-w
Posey KL, Coustry F, Hecht JT (2018) Cartilage oligomeric matrix protein: COMPopathies and beyond. Matrix Biol 71–72:161–173. https://doi.org/10.1016/j.matbio.2018.02.023
Raghunathan R, Sethi MK, Klein JA, Zaia J (2019) Proteomics, glycomics, and glycoproteomics of matrisome molecules. Mol Cell Proteomics. https://doi.org/10.1074/mcp.R119.001543
Randles MJ, Humphries MJ, Lennon R (2017) Proteomic definitions of basement membrane composition in health and disease. Matrix Biol 57–58:12–28. https://doi.org/10.1016/j.matbio.2016.08.006
Raudvere U, Kolberg L, Kuzmin I, Arak T, Adler P, Peterson H, Vilo J (2019) g:Profiler: a web server for functional enrichment analysis and conversions of gene lists (2019 update). Nucleic Acids Res 47:W191–W198. https://doi.org/10.1093/nar/gkz369
Ricard-Blum S, Miele AE (2019) Omic approaches to decipher the molecular mechanisms of fibrosis, and design new anti-fibrotic strategies. Semin Cell Dev Biol S1084952118302635. https://doi.org/10.1016/j.semcdb.2019.12.009
Ricard-Blum S, Vallet SD (2019) Fragments generated upon extracellular matrix remodeling: biological regulators and potential drugs. Matrix Biol 75–76:170–189. https://doi.org/10.1016/j.matbio.2017.11.005
Rozario T, DeSimone DW (2010) The extracellular matrix in development and morphogenesis: a dynamic view. Dev Biol 341:126–140. https://doi.org/10.1016/j.ydbio.2009.10.026
Ruggles KV, Krug K, Wang X, Clauser KR, Wang J, Payne SH, Fenyö D, Zhang B, Mani DR (2017) Methods, tools and current perspectives in proteogenomics. Mol Cell Proteomics 16:959–981. https://doi.org/10.1074/mcp.MR117.000024
Saito R, Smoot ME, Ono K, Ruscheinski J, Wang P-L, Lotia S, Pico AR, Bader GD, Ideker T (2012) A travel guide to Cytoscape plugins. Nat Methods 9:1069–1076. https://doi.org/10.1038/nmeth.2212
Schéele S, Nyström A, Durbeej M, Talts JF, Ekblom M, Ekblom P (2007) Laminin isoforms in development and disease. J Mol Med 85:825–836. https://doi.org/10.1007/s00109-007-0182-5
Schlotter F, Halu A, Goto S, Blaser MC, Body SC, Lee LH, Higashi H, DeLaughter DM, Hutcheson JD, Vyas P, Pham T, Rogers MA, Sharma A, Seidman CE, Loscalzo J, Seidman JG, Aikawa M, Singh SA, Aikawa E (2018) Spatiotemporal multi-omics mapping generates a molecular atlas of the aortic valve and reveals networks driving disease. Circulation 138:377–393. https://doi.org/10.1161/CIRCULATIONAHA.117.032291
Scietti L, Campioni M, Forneris F (2019) SiMPLOD, a structure-integrated database of collagen lysyl hydroxylase (LH/PLOD) enzyme variants. J Bone Miner Res 34:1376–1382. https://doi.org/10.1002/jbmr.3692
Shannon P, Markiel A, Ozier O, Baliga NS, Wang JT, Ramage D, Amin N, Schwikowski B, Ideker T (2003) Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res 13:2498–2504. https://doi.org/10.1101/gr.1239303
Shao X, Taha IN, Clauser KR, Gao Y (Tom), Naba A (2019) MatrisomeDB: the ECM-protein knowledge database. Nucleic Acids Res. https://doi.org/10.1093/nar/gkz849
Socovich AM, Naba A (2019) The cancer matrisome: from comprehensive characterization to biomarker discovery. Semin Cell Dev Biol 89:157–166. https://doi.org/10.1016/j.semcdb.2018.06.005
Su G, Morris JH, Demchak B, Bader GD (2014) Biological network exploration with Cytoscape 3. Curr Protoc Bioinformatics 47:8.13.1–8.1324. https://doi.org/10.1002/0471250953.bi0813s47
Subramanian A, Tamayo P, Mootha VK, Mukherjee S, Ebert BL, Gillette MA, Paulovich A, Pomeroy SL, Golub TR, Lander ES, Mesirov JP (2005) Gene set enrichment analysis: a knowledge-based approach for interpreting genome-wide expression profiles. Proc Natl Acad Sci USA 102:15545–15550. https://doi.org/10.1073/pnas.0506580102
Subramanian A, Kuehn H, Gould J, Tamayo P, Mesirov JP (2007) GSEA-P: a desktop application for gene set enrichment analysis. Bioinformatics 23:3251–3253. https://doi.org/10.1093/bioinformatics/btm369
Subramanian I, Verma S, Kumar S, Jere A, Anamika K (2020) Multi-omics data integration, interpretation, and its application. Bioinform Biol Insights 14:117793221989905. https://doi.org/10.1177/1177932219899051
Taha IN, Naba A (2019) Exploring the extracellular matrix in health and disease using proteomics. Essays Biochem:EBC20190001. https://doi.org/10.1042/EBC20190001
The Gene Ontology Consortium (2019) The Gene Ontology Resource: 20 years and still going strong. Nucleic Acids Res 47:D330–D338. https://doi.org/10.1093/nar/gky1055
The UniProt Consortium (2019) UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res 47:D506–D515. https://doi.org/10.1093/nar/gky1049
Theocharis AD, Manou D, Karamanos NK (2019) The extracellular matrix as a multitasking player in disease. FEBS J 286:2830–2869. https://doi.org/10.1111/febs.14818
van den Akker PC, Jonkman MF, Rengaw T, Bruckner-Tuderman L, Has C, Bauer JW, Klausegger A, Zambruno G, Castiglia D, Mellerio JE, McGrath JA, van Essen AJ, Hofstra RMW, Swertz MA (2011) The international dystrophic epidermolysis bullosa patient registry: an online database of dystrophic epidermolysis bullosa patients and their COL7A1 mutations. Hum Mutat 32:1100–1107. https://doi.org/10.1002/humu.21551
Wertheim-Tysarowska K, Sobczyńska-Tomaszewska A, Kowalewski C, Skroński M, Święćkowski G, Kutkowska-Kaźmierczak A, Woźniak K, Bal J (2012) The COL7A1 mutation database. Hum Mutat 33:327–331. https://doi.org/10.1002/humu.21651
Whittaker CA, Bergeron K-F, Whittle J, Brandhorst BP, Burke RD, Hynes RO (2006) The echinoderm adhesome. Dev Biol 300:252–266. https://doi.org/10.1016/j.ydbio.2006.07.044
Wilkinson MD, Dumontier M, Aalbersberg IjJ, Appleton G, Axton M, Baak A, Blomberg N, Boiten J-W, Santos LB da S, Bourne PE, Bouwman J, Brookes AJ, Clark T, Crosas M, Dillo I, Dumon O, Edmunds S, Evelo CT, Finkers R, Gonzalez-Beltran A, Gray AJG, Groth P, Goble C, Grethe JS, Heringa J, Hoen PAC ‘t, Hooft R, Kuhn T, Kok R, Kok J, Lusher SJ, Martone ME, Mons A, Packer AL, Persson B, Rocca-Serra P, Roos M, Schaik R van, Sansone S-A, Schultes E, Sengstag T, Slater T, Strawn G, Swertz MA, Thompson M, Lei J van der, Mulligen E van, Velterop J, Waagmeester A, Wittenburg P, Wolstencroft K, Zhao J, Mons B (2016) The FAIR guiding principles for scientific data management and stewardship. Sci Data 3:1–9. https://doi.org/10.1038/sdata.2016.18
Winograd-Katz SE, Fässler R, Geiger B, Legate KR (2014) The integrin adhesome: from genes and proteins to human disease. Nat Rev Mol Cell Biol 15:273–288. https://doi.org/10.1038/nrm3769
Zaidel-Bar R, Itzkovitz S, Ma’ayan A, Iyengar R, Geiger B (2007) Functional atlas of the integrin adhesome. Nat Cell Biol 9:858–867. https://doi.org/10.1038/ncb0807-858
Zeng S, Lyu Z, Narisetti SRK, Xu D, Joshi T (2019) Knowledge Base Commons (KBCommons) v1.1: a universal framework for multi-omics data integration and biological discoveries. BMC Genomics 20:947. https://doi.org/10.1186/s12864-019-6287-8
Zhang B, Kuster B (2019) Proteomics is not an island: multi-omics integration is the key to understanding biological systems. Mol Cell Proteomics 18:S1–S4. https://doi.org/10.1074/mcp.E119.001693
Zhou Y, Horowitz JC, Naba A, Ambalavanan N, Atabai K, Balestrini J, Bitterman PB, Corley RA, Ding B-S, Engler AJ, Hansen KC, Hagood JS, Kheradmand F, Lin QS, Neptune E, Niklason L, Ortiz LA, Parks WC, Tschumperlin DJ, White ES, Chapman HA, Thannickal VJ (2018) Extracellular matrix in lung development, homeostasis and disease. Matrix Biol 73:77–104. https://doi.org/10.1016/j.matbio.2018.03.005
Acknowledgments
The authors would like to thank Martin Davis from the Naba lab for his critical reading of the manuscript.
Author information
Authors and Affiliations
Corresponding authors
Editor information
Editors and Affiliations
Ethics declarations
Funding Sources
The work of the authors reported here was supported by a start-up fund from the Department of Physiology and Biophysics to and in part by a Catalyst Award from the Chicago Biomedical Consortium with support from the Searle Funds at the Chicago Community Trust (Grant C-088) to AN, and by the “Fondation pour la Recherche Médicale, France [grant number DBI20141231336 to SRB], the Institut Français de Bioinformatique [ANR-11-INBS-0013, Glycomatrix project, call 2015 to SRB], and the Groupement de Recherche (GDR) GagoSciences [CNRS, GDR 3739, Structure, Fonction et Régulation des Glycosaminoglycanes to SRB].
Rights and permissions
Copyright information
© 2020 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Naba, A., Ricard-Blum, S. (2020). The Extracellular Matrix Goes -Omics: Resources and Tools. In: Ricard-Blum, S. (eds) Extracellular Matrix Omics. Biology of Extracellular Matrix, vol 7. Springer, Cham. https://doi.org/10.1007/978-3-030-58330-9_1
Download citation
DOI: https://doi.org/10.1007/978-3-030-58330-9_1
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-58329-3
Online ISBN: 978-3-030-58330-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)