{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T02:17:33Z","timestamp":1793931453808,"version":"4.8.0"},"reference-count":150,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,1,25]],"date-time":"2024-01-25T00:00:00Z","timestamp":1706140800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2024,1,25]],"date-time":"2024-01-25T00:00:00Z","timestamp":1706140800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Neurodegeneration"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The extracellular matrix is a richly bioactive composition of substrates that provides biophysical stability, facilitates intercellular signaling, and both reflects and governs the physiological status of the local microenvironment. The matrix in the central nervous system (CNS) is far from simply an inert scaffold for mechanical support, instead conducting an active role in homeostasis and providing broad capacity for adaptation and remodeling in response to stress that otherwise would challenge equilibrium between neuronal, glial, and vascular elements. A major constituent is collagen, whose characteristic triple helical structure renders mechanical and biochemical stability to enable bidirectional crosstalk between matrix and resident cells. Multiple members of the collagen superfamily are critical to neuronal maturation and circuit formation, axon guidance, and synaptogenesis in the brain. In mature tissue, collagen interacts with other fibrous proteins and glycoproteins to sustain a three-dimensional medium through which complex networks of cells can communicate. While critical for matrix scaffolding, collagen in the CNS is also highly dynamic, with multiple binding sites for partnering matrix proteins, cell-surface receptors, and other ligands. These interactions are emerging as critical mediators of CNS disease and injury, particularly regarding changes in matrix stiffness, astrocyte recruitment and reactivity, and pro-inflammatory signaling in local microenvironments. Changes in the structure and\/or deposition of collagen impact cellular signaling and tissue biomechanics in the brain, which in turn can alter cellular responses including antigenicity, angiogenesis, gliosis, and recruitment of immune-related cells. These factors, each involving matrix collagen, contribute to the limited capacity for regeneration of CNS tissue. Emerging therapeutics that attempt to rebuild the matrix using peptide fragments, including collagen-enriched scaffolds and mimetics, hold great potential to promote neural repair and regeneration. Recent evidence from our group and others indicates that repairing protease-degraded collagen helices with mimetic peptides helps restore CNS tissue and promote neuronal survival in a broad spectrum of degenerative conditions. Restoration likely involves bolstering matrix stiffness to reduce the potential for astrocyte reactivity and local inflammation as well as repairing inhibitory binding sites for immune-signaling ligands. Facilitating repair rather than endogenous replacement of collagen degraded by disease or injury may represent the next frontier in developing therapies based on protection, repair, and regeneration of neurons in the central nervous system.<\/jats:p>","DOI":"10.1186\/s13024-024-00704-0","type":"journal-article","created":{"date-parts":[[2024,1,25]],"date-time":"2024-01-25T01:01:50Z","timestamp":1706144510000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":109,"title":["Collagen in the central nervous system: contributions to neurodegeneration and promise as a therapeutic target"],"prefix":"10.1186","volume":"19","author":[{"given":"Lauren K.","family":"Wareham","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert O.","family":"Baratta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian J.","family":"Del Buono","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric","family":"Schlumpf","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8475-9959","authenticated-orcid":false,"given":"David J.","family":"Calkins","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,1,25]]},"reference":[{"issue":"1","key":"704_CR1","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1186\/s13024-022-00524-0","volume":"17","author":"LK Wareham","year":"2022","unstructured":"Wareham LK, et al. Solving neurodegeneration: common mechanisms and strategies for new treatments. Mol Neurodegener. 2022;17(1):23.","journal-title":"Mol Neurodegener"},{"issue":"Pt 24","key":"704_CR2","doi-asserted-by":"publisher","first-page":"4195","DOI":"10.1242\/jcs.023820","volume":"123","author":"C Frantz","year":"2010","unstructured":"Frantz C, Stewart KM, Weaver VM. The extracellular matrix at a glance. J Cell Sci. 2010;123(Pt 24):4195\u2013200.","journal-title":"J Cell Sci"},{"key":"704_CR3","doi-asserted-by":"crossref","unstructured":"Soles A et al. Extracellular Matrix Regulation in Physiology and in Brain Disease. Int J Mol Sci. 2023. 24(8).","DOI":"10.3390\/ijms24087049"},{"issue":"12","key":"704_CR4","doi-asserted-by":"publisher","first-page":"771","DOI":"10.1038\/nrm3902","volume":"15","author":"JK Mouw","year":"2014","unstructured":"Mouw JK, Ou G, Weaver VM. Extracellular matrix assembly: a multiscale deconstruction. Nat Rev Mol Cell Biol. 2014;15(12):771\u201385.","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"7","key":"704_CR5","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1038\/s41578-018-0023-x","volume":"3","author":"GS Hussey","year":"2018","unstructured":"Hussey GS, Dziki JL, Badylak SF. Extracellular matrix-based materials for regenerative medicine. Nat Reviews Mater. 2018;3(7):159\u201373.","journal-title":"Nat Reviews Mater"},{"issue":"24","key":"704_CR6","doi-asserted-by":"publisher","first-page":"4300","DOI":"10.1091\/mbc.e10-03-0251","volume":"21","author":"S Ozbek","year":"2010","unstructured":"Ozbek S, et al. The evolution of extracellular matrix. Mol Biol Cell. 2010;21(24):4300\u20135.","journal-title":"Mol Biol Cell"},{"issue":"1","key":"704_CR7","doi-asserted-by":"publisher","first-page":"a005108","DOI":"10.1101\/cshperspect.a005108","volume":"3","author":"CS Barros","year":"2011","unstructured":"Barros CS, Franco SJ, Muller U. Extracellular matrix: functions in the nervous system. Cold Spring Harb Perspect Biol. 2011;3(1):a005108.","journal-title":"Cold Spring Harb Perspect Biol"},{"issue":"12","key":"704_CR8","doi-asserted-by":"publisher","first-page":"786","DOI":"10.1038\/nrm3904","volume":"15","author":"C Bonnans","year":"2014","unstructured":"Bonnans C, Chou J, Werb Z. Remodelling the extracellular matrix in development and disease. Nat Rev Mol Cell Biol. 2014;15(12):786\u2013801.","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"4","key":"704_CR9","doi-asserted-by":"publisher","first-page":"427","DOI":"10.1016\/S0968-4328(00)00011-1","volume":"32","author":"N Zagris","year":"2001","unstructured":"Zagris N. Extracellular matrix in development of the early embryo. Micron. 2001;32(4):427\u201338.","journal-title":"Micron"},{"issue":"1","key":"704_CR10","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1016\/0012-1606(80)90365-6","volume":"76","author":"I Leivo","year":"1980","unstructured":"Leivo I, et al. Appearance and distribution of collagens and laminin in the early mouse embryo. Dev Biol. 1980;76(1):100\u201314.","journal-title":"Dev Biol"},{"issue":"4","key":"704_CR11","doi-asserted-by":"publisher","first-page":"1267","DOI":"10.1152\/physrev.2000.80.4.1267","volume":"80","author":"CE Bandtlow","year":"2000","unstructured":"Bandtlow CE, Zimmermann DR. Proteoglycans in the developing brain: new conceptual insights for old proteins. Physiol Rev. 2000;80(4):1267\u201390.","journal-title":"Physiol Rev"},{"key":"704_CR12","doi-asserted-by":"crossref","unstructured":"Su J et al. A cell-ECM mechanism for connecting the ipsilateral eye to the brain Proc Natl Acad Sci U S A, 2021. 118(42).","DOI":"10.1073\/pnas.2104343118"},{"issue":"16","key":"704_CR13","doi-asserted-by":"publisher","first-page":"3229","DOI":"10.1007\/s00018-019-03182-6","volume":"76","author":"VR Krishnaswamy","year":"2019","unstructured":"Krishnaswamy VR, et al. Demystifying the extracellular matrix and its proteolytic remodeling in the brain: structural and functional insights. Cell Mol Life Sci. 2019;76(16):3229\u201348.","journal-title":"Cell Mol Life Sci"},{"issue":"1","key":"704_CR14","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s40778-019-0149-9","volume":"5","author":"A Pardo-Saganta","year":"2019","unstructured":"Pardo-Saganta A, et al. Role of the Extracellular Matrix in Stem Cell maintenance. Curr Stem Cell Rep. 2019;5(1):1\u201310.","journal-title":"Curr Stem Cell Rep"},{"issue":"8","key":"704_CR15","doi-asserted-by":"publisher","first-page":"590","DOI":"10.1002\/term.200","volume":"3","author":"V Agrawal","year":"2009","unstructured":"Agrawal V, et al. Evidence of innervation following extracellular matrix scaffold-mediated remodelling of muscular tissues. J Tissue Eng Regen Med. 2009;3(8):590\u2013600.","journal-title":"J Tissue Eng Regen Med"},{"issue":"1","key":"704_CR16","first-page":"13","volume":"1654","author":"J Sottile","year":"2004","unstructured":"Sottile J. Regulation of angiogenesis by extracellular matrix. Biochim Biophys Acta. 2004;1654(1):13\u201322.","journal-title":"Biochim Biophys Acta"},{"key":"704_CR17","doi-asserted-by":"publisher","first-page":"147","DOI":"10.1016\/j.semcdb.2018.08.007","volume":"89","author":"M Marchand","year":"2019","unstructured":"Marchand M, et al. Extracellular matrix scaffolding in angiogenesis and capillary homeostasis. Semin Cell Dev Biol. 2019;89:147\u201356.","journal-title":"Semin Cell Dev Biol"},{"issue":"7","key":"704_CR18","doi-asserted-by":"publisher","first-page":"834","DOI":"10.1002\/dvdy.178","volume":"249","author":"CM Arenas G\u00f3mez","year":"2020","unstructured":"Arenas G\u00f3mez CM, Sabin KZ, Echeverri K. Wound healing across the animal kingdom: crosstalk between the immune system and the extracellular matrix. Dev Dyn. 2020;249(7):834\u201346.","journal-title":"Dev Dyn"},{"issue":"12","key":"704_CR19","doi-asserted-by":"publisher","first-page":"802","DOI":"10.1038\/nrm3896","volume":"15","author":"JD Humphrey","year":"2014","unstructured":"Humphrey JD, Dufresne ER, Schwartz MA. Mechanotransduction and extracellular matrix homeostasis. Nat Rev Mol Cell Biol. 2014;15(12):802\u201312.","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"1","key":"704_CR20","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1016\/0022-5193(82)90388-5","volume":"99","author":"MJ Bissell","year":"1982","unstructured":"Bissell MJ, Hall HG, Parry G. How does the extracellular matrix direct gene expression? J Theor Biol. 1982;99(1):31\u201368.","journal-title":"J Theor Biol"},{"issue":"2","key":"704_CR21","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1111\/j.1524-475X.2011.00673.x","volume":"19","author":"GS Schultz","year":"2011","unstructured":"Schultz GS, et al. Dynamic reciprocity in the wound microenvironment. Wound Repair Regen. 2011;19(2):134\u201348.","journal-title":"Wound Repair Regen"},{"issue":"2\u20133","key":"704_CR22","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1016\/0304-3940(79)96130-5","volume":"15","author":"B Cragg","year":"1979","unstructured":"Cragg B. Brain extracellular space fixed for electron microscopy. Neurosci Lett. 1979;15(2\u20133):301\u20136.","journal-title":"Neurosci Lett"},{"key":"704_CR23","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1016\/j.brainresbull.2017.03.003","volume":"136","author":"I Song","year":"2018","unstructured":"Song I, Dityatev A. Crosstalk between glia, extracellular matrix and neurons. Brain Res Bull. 2018;136:101\u20138.","journal-title":"Brain Res Bull"},{"issue":"Pt 3B","key":"704_CR24","doi-asserted-by":"publisher","first-page":"437","DOI":"10.1038\/eye.2000.128","volume":"14","author":"JE Morgan","year":"2000","unstructured":"Morgan JE. Optic nerve head structure in glaucoma: astrocytes as mediators of axonal damage. Eye (Lond). 2000;14(Pt 3B):437\u201344.","journal-title":"Eye (Lond)"},{"key":"704_CR25","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1007\/s00401-009-0619-8","volume":"119","author":"MV Sofroniew","year":"2010","unstructured":"Sofroniew MV, Vinters HV. Astrocytes: biology and pathology. Acta Neuropathol. 2010;119:7\u201335.","journal-title":"Acta Neuropathol"},{"issue":"2","key":"704_CR26","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1007\/s004410050944","volume":"290","author":"MT Fitch","year":"1997","unstructured":"Fitch MT, Silver J. Glial cell extracellular matrix: boundaries for axon growth in development and regeneration. Cell Tissue Res. 1997;290(2):379\u201384.","journal-title":"Cell Tissue Res"},{"issue":"6","key":"704_CR27","doi-asserted-by":"publisher","first-page":"456","DOI":"10.1038\/nrn1115","volume":"4","author":"A Dityatev","year":"2003","unstructured":"Dityatev A, Schachner M. Extracellular matrix molecules and synaptic plasticity. Nat Rev Neurosci. 2003;4(6):456\u201368.","journal-title":"Nat Rev Neurosci"},{"issue":"16","key":"704_CR28","doi-asserted-by":"publisher","first-page":"3083","DOI":"10.1007\/s00018-019-03171-9","volume":"76","author":"S Chopra","year":"2019","unstructured":"Chopra S, Overall CM, Dufour A. Matrix metalloproteinases in the CNS: interferons get nervous. Cell Mol Life Sci. 2019;76(16):3083\u201395.","journal-title":"Cell Mol Life Sci"},{"issue":"24","key":"704_CR29","doi-asserted-by":"publisher","first-page":"6850","DOI":"10.1111\/febs.15776","volume":"288","author":"NK Karamanos","year":"2021","unstructured":"Karamanos NK, et al. A guide to the composition and functions of the extracellular matrix. FEBS J. 2021;288(24):6850\u2013912.","journal-title":"FEBS J"},{"key":"704_CR30","doi-asserted-by":"crossref","unstructured":"Gregorio I, et al. Collagen VI in healthy and diseased nervous system. Volume 11. Disease Models & Mechanisms; 2018. 6.","DOI":"10.1242\/dmm.032946"},{"issue":"1","key":"704_CR31","first-page":"73","volume":"53","author":"A Suttkus","year":"2016","unstructured":"Suttkus A, Morawski M, Arendt T. Protective Prop Neural Extracell Matrix Mol Neurobiol. 2016;53(1):73\u201382.","journal-title":"Protective Prop Neural Extracell Matrix Mol Neurobiol"},{"key":"704_CR32","doi-asserted-by":"crossref","unstructured":"Ruggiero F. The collagen superfamily and collagenopathies. Springer; 2021.","DOI":"10.1007\/978-3-030-67592-9"},{"issue":"11","key":"704_CR33","doi-asserted-by":"publisher","first-page":"5583","DOI":"10.3390\/ijms22115583","volume":"22","author":"J Melrose","year":"2021","unstructured":"Melrose J, Hayes AJ, Bix G. The CNS\/PNS extracellular matrix provides instructive Guidance cues to neural cells and Neuroregulatory Proteins in neural development and repair. Int J Mol Sci. 2021;22(11):5583.","journal-title":"Int J Mol Sci"},{"key":"704_CR34","doi-asserted-by":"publisher","first-page":"101444","DOI":"10.1016\/j.tice.2020.101444","volume":"69","author":"M Su","year":"2021","unstructured":"Su M, et al. Effects of the extracellular matrix on myelin development and regeneration in the central nervous system. Tissue Cell. 2021;69:101444.","journal-title":"Tissue Cell"},{"issue":"16","key":"704_CR35","doi-asserted-by":"publisher","first-page":"3051","DOI":"10.1007\/s00018-019-03172-8","volume":"76","author":"S Rivera","year":"2019","unstructured":"Rivera S. Metalloproteinases in nervous system function and pathology: introduction. Cell Mol Life Sci. 2019;76(16):3051\u20133.","journal-title":"Cell Mol Life Sci"},{"issue":"5","key":"704_CR36","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1002\/wrna.1177","volume":"4","author":"B Stefanovic","year":"2013","unstructured":"Stefanovic B. RNA protein interactions governing expression of the most abundant protein in human body, type I collagen. Wiley Interdiscip Rev RNA. 2013;4(5):535\u201345.","journal-title":"Wiley Interdiscip Rev RNA"},{"issue":"13","key":"704_CR37","doi-asserted-by":"publisher","first-page":"2051","DOI":"10.1093\/hmg\/9.13.2051","volume":"9","author":"AL Sertie","year":"2000","unstructured":"Sertie AL, et al. Collagen XVIII, containing an endogenous inhibitor of angiogenesis and tumor growth, plays a critical role in the maintenance of retinal structure and in neural tube closure (Knobloch syndrome). Hum Mol Genet. 2000;9(13):2051\u20138.","journal-title":"Hum Mol Genet"},{"issue":"5","key":"704_CR38","doi-asserted-by":"publisher","first-page":"508","DOI":"10.1016\/j.ceb.2008.05.003","volume":"20","author":"MA Fox","year":"2008","unstructured":"Fox MA. Novel roles for collagens in wiring the vertebrate nervous system. Curr Opin Cell Biol. 2008;20(5):508\u201313.","journal-title":"Curr Opin Cell Biol"},{"issue":"7","key":"704_CR39","doi-asserted-by":"publisher","first-page":"1223","DOI":"10.1007\/s00018-008-8561-9","volume":"66","author":"T Hubert","year":"2009","unstructured":"Hubert T, et al. Collagens in the developing and diseased nervous system. Cell Mol Life Sci. 2009;66(7):1223\u201338.","journal-title":"Cell Mol Life Sci"},{"issue":"2","key":"704_CR40","first-page":"92","volume":"1","author":"I Decimo","year":"2012","unstructured":"Decimo I, et al. Meninges: from protective membrane to stem cell niche. Am J Stem Cells. 2012;1(2):92\u2013105.","journal-title":"Am J Stem Cells"},{"key":"704_CR41","doi-asserted-by":"publisher","first-page":"102676","DOI":"10.1016\/j.conb.2023.102676","volume":"79","author":"CN Como","year":"2023","unstructured":"Como CN, Kim S, Siegenthaler J. Stuck on you: meninges cellular crosstalk in development. Curr Opin Neurobiol. 2023;79:102676.","journal-title":"Curr Opin Neurobiol"},{"issue":"1","key":"704_CR42","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1186\/s13024-021-00502-y","volume":"16","author":"B Nguyen","year":"2021","unstructured":"Nguyen B, Bix G, Yao Y. Basal lamina changes in neurodegenerative disorders. Mol Neurodegener. 2021;16(1):81.","journal-title":"Mol Neurodegener"},{"issue":"12","key":"704_CR43","doi-asserted-by":"publisher","first-page":"2422","DOI":"10.1016\/j.bbagen.2015.09.007","volume":"1850","author":"A Walia","year":"2015","unstructured":"Walia A, et al. Endostatin\u2019s emerging roles in angiogenesis, lymphangiogenesis, disease, and clinical applications. Biochim et Biophys Acta (BBA)-General Subj. 2015;1850(12):2422\u201338.","journal-title":"Biochim et Biophys Acta (BBA)-General Subj"},{"issue":"7","key":"704_CR44","doi-asserted-by":"publisher","first-page":"1103","DOI":"10.1089\/neu.2006.23.1103","volume":"23","author":"MH Deininger","year":"2006","unstructured":"Deininger MH, Meyermann R, Schluesener HJ. Endostatin\/collagen XVIII accumulates in patients with traumatic brain injury. J Neurotrauma. 2006;23(7):1103\u201310.","journal-title":"J Neurotrauma"},{"issue":"1","key":"704_CR45","doi-asserted-by":"publisher","first-page":"14787","DOI":"10.1038\/ncomms14787","volume":"8","author":"E Moeendarbary","year":"2017","unstructured":"Moeendarbary E, et al. The soft mechanical signature of glial scars in the central nervous system. Nat Commun. 2017;8(1):14787.","journal-title":"Nat Commun"},{"issue":"4","key":"704_CR46","doi-asserted-by":"publisher","first-page":"1651157","DOI":"10.1080\/21688370.2019.1651157","volume":"7","author":"MJ Reed","year":"2019","unstructured":"Reed MJ, Damodarasamy M, Banks WA. The extracellular matrix of the blood\u2013brain barrier: structural and functional roles in health, aging, and Alzheimer\u2019s disease. Tissue Barriers. 2019;7(4):1651157.","journal-title":"Tissue Barriers"},{"key":"704_CR47","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1016\/j.neuroscience.2018.06.046","volume":"405","author":"H Thurgur","year":"2019","unstructured":"Thurgur H, Pinteaux E. Microglia in the neurovascular unit: blood\u2013brain barrier\u2013microglia interactions after Central Nervous System disorders. Neuroscience. 2019;405:55\u201367.","journal-title":"Neuroscience"},{"key":"704_CR48","doi-asserted-by":"publisher","first-page":"362","DOI":"10.3389\/fncel.2014.00362","volume":"8","author":"ACC da Fonseca","year":"2014","unstructured":"da Fonseca ACC, et al. The impact of microglial activation on blood-brain barrier in brain diseases. Front Cell Neurosci. 2014;8:362.","journal-title":"Front Cell Neurosci"},{"issue":"10","key":"704_CR49","doi-asserted-by":"publisher","first-page":"3300","DOI":"10.1177\/0271678X17722436","volume":"37","author":"MS Thomsen","year":"2017","unstructured":"Thomsen MS, Routhe LJ, Moos T. The vascular basement membrane in the healthy and pathological brain. J Cereb Blood Flow Metabolism. 2017;37(10):3300\u201317.","journal-title":"J Cereb Blood Flow Metabolism"},{"issue":"1","key":"704_CR50","doi-asserted-by":"publisher","first-page":"175909141668902","DOI":"10.1177\/1759091416689020","volume":"9","author":"J Su","year":"2017","unstructured":"Su J, Cole J, Fox MA. Loss of Interneuron-Derived Collagen XIX leads to a reduction in Perineuronal Nets in the mammalian Telencephalon. ASN Neuro. 2017;9(1):1759091416689020.","journal-title":"ASN Neuro"},{"issue":"6","key":"704_CR51","doi-asserted-by":"publisher","first-page":"102617","DOI":"10.1016\/j.isci.2021.102617","volume":"24","author":"V Jovasevic","year":"2021","unstructured":"Jovasevic V, et al. Primary cilia are required for the persistence of memory and stabilization of perineuronal nets. iScience. 2021;24(6):102617.","journal-title":"iScience"},{"key":"704_CR52","doi-asserted-by":"publisher","first-page":"851988","DOI":"10.3389\/fnint.2022.851988","volume":"16","author":"W Hartig","year":"2022","unstructured":"Hartig W, et al. Update on Perineuronal Net Staining with Wisteria floribunda Agglutinin (WFA). Front Integr Neurosci. 2022;16:851988.","journal-title":"Front Integr Neurosci"},{"issue":"12","key":"704_CR53","doi-asserted-by":"publisher","first-page":"3811","DOI":"10.1111\/ejn.14887","volume":"53","author":"P Ulbrich","year":"2021","unstructured":"Ulbrich P, et al. Interplay between perivascular and perineuronal extracellular matrix remodelling in neurological and psychiatric diseases. Eur J Neurosci. 2021;53(12):3811\u201330.","journal-title":"Eur J Neurosci"},{"key":"704_CR54","doi-asserted-by":"publisher","first-page":"134980","DOI":"10.1016\/j.neulet.2020.134980","volume":"729","author":"RP Gorter","year":"2020","unstructured":"Gorter RP, Baron W. Matrix metalloproteinases shape the oligodendrocyte (niche) during development and upon demyelination. Neurosci Lett. 2020;729:134980.","journal-title":"Neurosci Lett"},{"issue":"4","key":"704_CR55","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1002\/dvdy.24473","volume":"246","author":"P Mehta","year":"2017","unstructured":"Mehta P, Piao X. Adhesion G-protein coupled receptors and extracellular matrix proteins: roles in myelination and glial cell development. Dev Dyn. 2017;246(4):275\u201384.","journal-title":"Dev Dyn"},{"key":"704_CR56","doi-asserted-by":"publisher","first-page":"175909142211045","DOI":"10.1177\/17590914221104566","volume":"14","author":"AM Rodriguez","year":"2022","unstructured":"Rodriguez AM, Rodriguez J, Giambartolomei GH. Microglia at the crossroads of Pathogen-Induced Neuroinflammation. ASN Neuro. 2022;14:17590914221104566.","journal-title":"ASN Neuro"},{"key":"704_CR57","doi-asserted-by":"crossref","unstructured":"Gottschall PE, Deb S. Regulation of matrix metalloproteinase expression in astrocytes, microglia and neurons. Volume 3. NEUROIMMUNOMODULATION-BASEL-; 1996. pp. 69\u201375.","DOI":"10.1159\/000097229"},{"key":"704_CR58","doi-asserted-by":"crossref","unstructured":"Yurchenco PD. Basement membranes: cell scaffoldings and signaling platforms. Cold Spring Harb Perspect Biol, 2011. 3(2).","DOI":"10.1101\/cshperspect.a004911"},{"issue":"6","key":"704_CR59","doi-asserted-by":"publisher","first-page":"1577","DOI":"10.1096\/fasebj.4.6.2180767","volume":"4","author":"PD Yurchenco","year":"1990","unstructured":"Yurchenco PD, Schittny JC. Molecular architecture of basement membranes. FASEB J. 1990;4(6):1577\u201390.","journal-title":"FASEB J"},{"issue":"1\u20132","key":"704_CR60","first-page":"93","volume":"27","author":"M Paulsson","year":"1992","unstructured":"Paulsson M. Basement membrane proteins: structure, assembly, and cellular interactions. Crit Rev Biochem Mol Biol. 1992;27(1\u20132):93\u2013127.","journal-title":"Crit Rev Biochem Mol Biol"},{"issue":"12","key":"704_CR61","doi-asserted-by":"publisher","first-page":"1277","DOI":"10.2174\/138161209787846766","volume":"15","author":"PD Yurchenco","year":"2009","unstructured":"Yurchenco PD, Patton BL. Developmental and pathogenic mechanisms of basement membrane assembly. Curr Pharm Des. 2009;15(12):1277\u201394.","journal-title":"Curr Pharm Des"},{"key":"704_CR62","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1146\/annurev.cb.03.110187.000421","volume":"3","author":"GR Martin","year":"1987","unstructured":"Martin GR, Timpl R. Laminin and other basement membrane components. Annu Rev Cell Biol. 1987;3:57\u201385.","journal-title":"Annu Rev Cell Biol"},{"issue":"5","key":"704_CR63","doi-asserted-by":"publisher","first-page":"501","DOI":"10.1016\/j.conb.2006.08.005","volume":"16","author":"FA Court","year":"2006","unstructured":"Court FA, Wrabetz L, Feltri ML. Basal lamina: Schwann cells wrap to the rhythm of space-time. Curr Opin Neurobiol. 2006;16(5):501\u20137.","journal-title":"Curr Opin Neurobiol"},{"issue":"3","key":"704_CR64","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1016\/j.matbio.2005.11.004","volume":"25","author":"A Seppanen","year":"2006","unstructured":"Seppanen A, et al. Collagen XVII is expressed in human CNS neurons. Matrix Biol. 2006;25(3):185\u20138.","journal-title":"Matrix Biol"},{"key":"704_CR65","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1016\/j.brainres.2007.04.073","volume":"1158","author":"A Seppanen","year":"2007","unstructured":"Seppanen A, et al. Distribution of collagen XVII in the human brain. Brain Res. 2007;1158:50\u20136.","journal-title":"Brain Res"},{"issue":"1","key":"704_CR66","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1016\/j.neuron.2015.11.013","volume":"89","author":"Y Zhang","year":"2016","unstructured":"Zhang Y, et al. Purification and characterization of progenitor and mature human astrocytes reveals transcriptional and functional differences with Mouse. Neuron. 2016;89(1):37\u201353.","journal-title":"Neuron"},{"issue":"8","key":"704_CR67","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1038\/s41583-019-0196-3","volume":"20","author":"JW Fawcett","year":"2019","unstructured":"Fawcett JW, Oohashi T, Pizzorusso T. The roles of perineuronal nets and the perinodal extracellular matrix in neuronal function. Nat Rev Neurosci. 2019;20(8):451\u201365.","journal-title":"Nat Rev Neurosci"},{"key":"704_CR68","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1016\/j.addr.2015.11.013","volume":"97","author":"B An","year":"2016","unstructured":"An B, Lin YS, Brodsky B. Collagen interactions: drug design and delivery. Adv Drug Deliv Rev. 2016;97:69\u201384.","journal-title":"Adv Drug Deliv Rev"},{"issue":"1","key":"704_CR69","doi-asserted-by":"publisher","first-page":"147","DOI":"10.1016\/S0001-706X(00)00128-5","volume":"77","author":"HM Kagan","year":"2000","unstructured":"Kagan HM. Intra- and extracellular enzymes of collagen biosynthesis as biological and chemical targets in the control of fibrosis. Acta Trop. 2000;77(1):147\u201352.","journal-title":"Acta Trop"},{"issue":"6","key":"704_CR70","doi-asserted-by":"publisher","first-page":"2133","DOI":"10.1074\/jbc.TM118.002812","volume":"294","author":"S Ito","year":"2019","unstructured":"Ito S, Nagata K. Roles of the endoplasmic reticulum\u2013resident, collagen-specific molecular chaperone Hsp47 in vertebrate cells and human disease. J Biol Chem. 2019;294(6):2133\u201341.","journal-title":"J Biol Chem"},{"issue":"8","key":"704_CR71","doi-asserted-by":"publisher","first-page":"457","DOI":"10.1038\/s41580-019-0134-2","volume":"20","author":"JZ Kechagia","year":"2019","unstructured":"Kechagia JZ, Ivaska J, Roca-Cusachs P. Integrins as biomechanical sensors of the microenvironment. Nat Rev Mol Cell Biol. 2019;20(8):457\u201373.","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"5","key":"704_CR72","doi-asserted-by":"publisher","first-page":"105400","DOI":"10.1016\/j.jbspin.2022.105400","volume":"89","author":"GM Kim","year":"2022","unstructured":"Kim GM, Park H, Lee SY. Roles of osteoclast-associated receptor in rheumatoid arthritis and osteoarthritis. Joint Bone Spine. 2022;89(5):105400.","journal-title":"Joint Bone Spine"},{"key":"704_CR73","doi-asserted-by":"publisher","first-page":"765034","DOI":"10.3389\/fimmu.2021.765034","volume":"12","author":"HJ van der Zande","year":"2021","unstructured":"van der Zande HJ, et al. The mannose receptor: from endocytic receptor and biomarker to regulator of (meta) inflammation. Front Immunol. 2021;12:765034.","journal-title":"Front Immunol"},{"issue":"11","key":"704_CR74","doi-asserted-by":"publisher","first-page":"p118478","DOI":"10.1016\/j.bbamcr.2019.04.008","volume":"1866","author":"JP Orgel","year":"2019","unstructured":"Orgel JP, Madhurapantula RS. A structural prospective for collagen receptors such as DDR and their binding of the collagen fibril. Biochim et Biophys Acta (BBA)-Molecular Cell Res. 2019;1866(11):p118478.","journal-title":"Biochim et Biophys Acta (BBA)-Molecular Cell Res"},{"issue":"3","key":"704_CR75","doi-asserted-by":"publisher","first-page":"714","DOI":"10.1124\/pharmrev.121.000349","volume":"74","author":"LG de Almeida","year":"2022","unstructured":"de Almeida LG, et al. Matrix metalloproteinases: from molecular mechanisms to physiology, pathophysiology, and pharmacology. Pharmacol Rev. 2022;74(3):714\u201370.","journal-title":"Pharmacol Rev"},{"issue":"24","key":"704_CR76","doi-asserted-by":"publisher","first-page":"9739","DOI":"10.3390\/ijms21249739","volume":"21","author":"GA Cabral-Pacheco","year":"2020","unstructured":"Cabral-Pacheco GA, et al. The roles of Matrix metalloproteinases and their inhibitors in Human diseases. Int J Mol Sci. 2020;21(24):9739.","journal-title":"Int J Mol Sci"},{"issue":"19","key":"704_CR77","doi-asserted-by":"publisher","first-page":"10705","DOI":"10.1021\/acs.jmedchem.0c00352","volume":"63","author":"P Zipfel","year":"2020","unstructured":"Zipfel P, et al. Matrix metalloproteinases as new targets in Alzheimer\u2019s Disease: opportunities and challenges. J Med Chem. 2020;63(19):10705\u201325.","journal-title":"J Med Chem"},{"issue":"1","key":"704_CR78","doi-asserted-by":"publisher","first-page":"a004978","DOI":"10.1101\/cshperspect.a004978","volume":"3","author":"S Ricard-Blum","year":"2011","unstructured":"Ricard-Blum S. The collagen family. Cold Spring Harb Perspect Biol. 2011;3(1):a004978.","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"704_CR79","doi-asserted-by":"crossref","unstructured":"Boraschi-Diaz I et al. Collagen type I as a Ligand for receptor-mediated signaling. Front Phys, 2017. 5.","DOI":"10.3389\/fphy.2017.00012"},{"issue":"1","key":"704_CR80","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1016\/S0968-0004(06)80023-X","volume":"21","author":"K Nagata","year":"1996","unstructured":"Nagata K. Hsp47: a collagen-specific molecular chaperone. Trends Biochem Sci. 1996;21(1):23\u20136.","journal-title":"Trends Biochem Sci"},{"issue":"18","key":"704_CR81","doi-asserted-by":"publisher","first-page":"4168","DOI":"10.1038\/sj.emboj.7601833","volume":"26","author":"O Ichikawa","year":"2007","unstructured":"Ichikawa O, et al. Structural basis of the collagen-binding mode of discoidin domain receptor 2. EMBO J. 2007;26(18):4168\u201376.","journal-title":"EMBO J"},{"issue":"1","key":"704_CR82","doi-asserted-by":"publisher","first-page":"2","DOI":"10.3109\/03008207.2010.511353","volume":"52","author":"J Orgel","year":"2011","unstructured":"Orgel J, San Antonio J, Antipova O. Molecular and structural mapping of collagen fibril interactions. Connect Tissue Res. 2011;52(1):2\u201317.","journal-title":"Connect Tissue Res"},{"issue":"8","key":"704_CR83","doi-asserted-by":"publisher","first-page":"1108","DOI":"10.1016\/j.cellsig.2006.02.012","volume":"18","author":"WF Vogel","year":"2006","unstructured":"Vogel WF, Abdulhussein R, Ford CE. Sensing extracellular matrix: an update on discoidin domain receptor function. Cell Signal. 2006;18(8):1108\u201316.","journal-title":"Cell Signal"},{"issue":"1","key":"704_CR84","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1016\/S0092-8674(00)80622-4","volume":"101","author":"J Emsley","year":"2000","unstructured":"Emsley J, et al. Structural basis of collagen recognition by integrin \u03b12\u03b21. Cell. 2000;101(1):47\u201356.","journal-title":"Cell"},{"key":"704_CR85","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1007\/s00441-009-0834-6","volume":"339","author":"M Barczyk","year":"2010","unstructured":"Barczyk M, Carracedo S, Gullberg D. Integrins Cell and Tissue Research. 2010;339:269\u201380.","journal-title":"Integrins Cell and Tissue Research"},{"issue":"4","key":"704_CR86","doi-asserted-by":"publisher","first-page":"821","DOI":"10.1161\/01.RES.79.4.821","volume":"79","author":"JE Mogford","year":"1996","unstructured":"Mogford JE, et al. Vascular smooth muscle \u03b1v\u03b23 integrin mediates arteriolar vasodilation in response to RGD peptides. Circul Res. 1996;79(4):821\u20136.","journal-title":"Circul Res"},{"issue":"10","key":"704_CR87","doi-asserted-by":"publisher","first-page":"2827","DOI":"10.1016\/j.biomaterials.2009.12.051","volume":"31","author":"AV Taubenberger","year":"2010","unstructured":"Taubenberger AV, et al. The effect of unlocking RGD-motifs in collagen I on pre-osteoblast adhesion and differentiation. Biomaterials. 2010;31(10):2827\u201335.","journal-title":"Biomaterials"},{"issue":"7","key":"704_CR88","doi-asserted-by":"publisher","first-page":"983","DOI":"10.3390\/biom11070983","volume":"11","author":"H Cai","year":"2021","unstructured":"Cai H, et al. Identification of HSP47 binding site on native collagen and its implications for the development of HSP47 inhibitors. Biomolecules. 2021;11(7):983.","journal-title":"Biomolecules"},{"key":"704_CR89","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1016\/j.matbio.2015.01.005","volume":"44","author":"SR Van Doren","year":"2015","unstructured":"Van Doren SR. Matrix metalloproteinase interactions with collagen and elastin. Matrix Biol. 2015;44:224\u201331.","journal-title":"Matrix Biol"},{"issue":"12","key":"704_CR90","doi-asserted-by":"publisher","first-page":"4826","DOI":"10.1073\/pnas.71.12.4826","volume":"71","author":"RC Siegel","year":"1974","unstructured":"Siegel RC. Biosynthesis of collagen crosslinks: increased activity of purified lysyl oxidase with reconstituted collagen fibrils. Proc Natl Acad Sci U S A. 1974;71(12):4826\u201330.","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"704_CR91","doi-asserted-by":"publisher","first-page":"109","DOI":"10.3109\/03008208509015017","volume":"14","author":"AL Cronlund","year":"1985","unstructured":"Cronlund AL, Smith BD, Kagan HM. Binding of lysyl oxidase to fibrils of type I collagen. Connect Tissue Res. 1985;14(2):109\u201319.","journal-title":"Connect Tissue Res"},{"issue":"3","key":"704_CR92","doi-asserted-by":"publisher","first-page":"1613","DOI":"10.1074\/jbc.271.3.1613","volume":"271","author":"D Beher","year":"1996","unstructured":"Beher D, et al. Regulation of amyloid protein precursor (APP) binding to Collagen and mapping of the binding sites on APP and collagen type I (\u2217). J Biol Chem. 1996;271(3):1613\u201320.","journal-title":"J Biol Chem"},{"key":"704_CR93","volume-title":"Crumpton [and seven others]","author":"M Sela","year":"1974","unstructured":"Sela M, Crumpton MJ. The antigens. Volume II \/ edited by Michael Sela; contributors. Crumpton [and seven others]. New York, New York;: Academic Press, Inc.; 1974."},{"issue":"2","key":"704_CR94","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1002\/jbm.b.30096","volume":"71","author":"AK Lynn","year":"2004","unstructured":"Lynn AK, Yannas IV, Bonfield W. Antigenicity and immunogenicity of collagen. J Biomed Mater Res B Appl Biomater. 2004;71(2):343\u201354.","journal-title":"J Biomed Mater Res B Appl Biomater"},{"key":"704_CR95","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1016\/B978-0-12-363707-9.50008-3","volume":"7","author":"H Furthmayr","year":"1976","unstructured":"Furthmayr H, Timpl R. Immunochemistry of collagens and procollagens. Int Rev Connect Tissue Res. 1976;7:61\u201399.","journal-title":"Int Rev Connect Tissue Res"},{"key":"704_CR96","doi-asserted-by":"crossref","unstructured":"Heikkinen A, Fox MA, Pihlajaniemi T. Collagens as New Players in Nervous System Diseases, in The Collagen Superfamily and Collagenopathies, F. Ruggiero, Editor. 2021, Springer International Publishing: Cham. p. 289\u2013338.","DOI":"10.1007\/978-3-030-67592-9_8"},{"issue":"3","key":"704_CR97","doi-asserted-by":"publisher","first-page":"332","DOI":"10.1111\/j.1365-2990.2006.00732.x","volume":"32","author":"J Tian","year":"2006","unstructured":"Tian J, et al. Relationships in Alzheimer\u2019s disease between the extent of Abeta deposition in cerebral blood vessel walls, as cerebral amyloid angiopathy, and the amount of cerebrovascular smooth muscle cells and collagen. Neuropathol Appl Neurobiol. 2006;32(3):332\u201340.","journal-title":"Neuropathol Appl Neurobiol"},{"issue":"6","key":"704_CR98","doi-asserted-by":"publisher","first-page":"1985","DOI":"10.3390\/ijms21061985","volume":"21","author":"CD Morrone","year":"2020","unstructured":"Morrone CD, Bishay J, McLaurin J. Potential role of venular amyloid in Alzheimer\u2019s disease pathogenesis. Int J Mol Sci. 2020;21(6):1985.","journal-title":"Int J Mol Sci"},{"issue":"9","key":"704_CR99","doi-asserted-by":"publisher","first-page":"3005","DOI":"10.1007\/s00216-022-03929-4","volume":"414","author":"M Downs","year":"2022","unstructured":"Downs M, et al. Matrisome changes in Parkinson\u2019s disease. Anal Bioanal Chem. 2022;414(9):3005\u201315.","journal-title":"Anal Bioanal Chem"},{"issue":"1","key":"704_CR100","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1186\/s12883-021-02215-7","volume":"21","author":"C-Y Jin","year":"2021","unstructured":"Jin C-Y, et al. Study of the collagen type VI alpha 3 (COL6A3) gene in Parkinson\u2019s disease. BMC Neurol. 2021;21(1):187.","journal-title":"BMC Neurol"},{"key":"704_CR101","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1016\/j.matbio.2014.03.007","volume":"37","author":"DM Wallace","year":"2014","unstructured":"Wallace DM, et al. The role of matricellular proteins in glaucoma. Matrix Biol. 2014;37:174\u201382.","journal-title":"Matrix Biol"},{"issue":"4","key":"704_CR102","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1093\/hmg\/ddq511","volume":"20","author":"EN Vithana","year":"2011","unstructured":"Vithana EN, et al. Collagen-related genes influence the glaucoma risk factor, central corneal thickness. Hum Mol Genet. 2011;20(4):649\u201358.","journal-title":"Hum Mol Genet"},{"issue":"10","key":"704_CR103","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1002\/bip.22070","volume":"97","author":"AS Parmar","year":"2012","unstructured":"Parmar AS, et al. A peptide study of the relationship between the collagen triple-helix and amyloid. Biopolymers. 2012;97(10):795\u2013806.","journal-title":"Biopolymers"},{"issue":"3","key":"704_CR104","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1016\/j.neurobiolaging.2008.04.009","volume":"31","author":"C Forsell","year":"2010","unstructured":"Forsell C, et al. Genetic association to the amyloid plaque associated protein gene COL25A1 in Alzheimer\u2019s disease. Neurobiol Aging. 2010;31(3):409\u201315.","journal-title":"Neurobiol Aging"},{"issue":"1\u20132","key":"704_CR105","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1016\/0006-8993(95)01250-8","volume":"705","author":"RN Kalaria","year":"1995","unstructured":"Kalaria RN, Pax AB. Increased collagen content of cerebral microvessels in Alzheimer\u2019s disease. Brain Res. 1995;705(1\u20132):349\u201352.","journal-title":"Brain Res"},{"key":"704_CR106","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1186\/1742-2094-7-22","volume":"7","author":"CM Sondag","year":"2010","unstructured":"Sondag CM, Combs CK. Adhesion of monocytes to type I collagen stimulates an APP-dependent proinflammatory signaling response and release of Abeta1-40. J Neuroinflammation. 2010;7:22.","journal-title":"J Neuroinflammation"},{"issue":"2","key":"704_CR107","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1038\/nn.2240","volume":"12","author":"JS Cheng","year":"2009","unstructured":"Cheng JS, et al. Collagen VI protects neurons against Abeta toxicity. Nat Neurosci. 2009;12(2):119\u201321.","journal-title":"Nat Neurosci"},{"issue":"6","key":"704_CR108","doi-asserted-by":"publisher","first-page":"1419","DOI":"10.1084\/jem.20052554","volume":"203","author":"RJ Lebbink","year":"2006","unstructured":"Lebbink RJ, et al. Collagens are functional, high affinity ligands for the inhibitory immune receptor LAIR-1. J Exp Med. 2006;203(6):1419\u201325.","journal-title":"J Exp Med"},{"issue":"128","key":"704_CR109","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1016\/j.imlet.2009.09.014","volume":"1","author":"L Meyaard","year":"2010","unstructured":"Meyaard L. LAIR and collagens in immune regulation. Immunol Lett. 2010;1(128):26\u20138.","journal-title":"Immunol Lett"},{"issue":"11","key":"704_CR110","doi-asserted-by":"publisher","first-page":"2106","DOI":"10.1016\/j.bbadis.2014.07.008","volume":"1842","author":"J Xu","year":"2014","unstructured":"Xu J, Shi G-P. Vascular wall extracellular matrix proteins and vascular diseases. Biochim et Biophys Acta (BBA)-Molecular Basis Disease. 2014;1842(11):2106\u201319.","journal-title":"Biochim et Biophys Acta (BBA)-Molecular Basis Disease"},{"issue":"3","key":"704_CR111","doi-asserted-by":"publisher","first-page":"146","DOI":"10.1111\/j.1752-8062.2011.00304.x","volume":"4","author":"KJ Shields","year":"2011","unstructured":"Shields KJ, et al. Complement proteins C3 and C4 bind to collagen and elastin in the vascular wall: a potential role in vascular stiffness and atherosclerosis. Clin Transl Sci. 2011;4(3):146\u201352.","journal-title":"Clin Transl Sci"},{"issue":"2","key":"704_CR112","doi-asserted-by":"publisher","first-page":"337","DOI":"10.3390\/biom12020337","volume":"12","author":"Y Chen","year":"2022","unstructured":"Chen Y, et al. The complement system in the central nervous system: from neurodevelopment to neurodegeneration. Biomolecules. 2022;12(2):337.","journal-title":"Biomolecules"},{"issue":"3","key":"704_CR113","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1007\/s00401-015-1524-y","volume":"131","author":"N Dudvarski Stankovic","year":"2016","unstructured":"Dudvarski Stankovic N, et al. Microglia\u2013blood vessel interactions: a double-edged sword in brain pathologies. Acta Neuropathol. 2016;131(3):347\u201363.","journal-title":"Acta Neuropathol"},{"issue":"6286","key":"704_CR114","doi-asserted-by":"publisher","first-page":"712","DOI":"10.1126\/science.aad8373","volume":"352","author":"S Hong","year":"2016","unstructured":"Hong S, et al. Complement and microglia mediate early synapse loss in Alzheimer mouse models. Science. 2016;352(6286):712\u20136.","journal-title":"Science"},{"key":"704_CR115","doi-asserted-by":"publisher","first-page":"101612","DOI":"10.1016\/j.pneurobio.2019.04.001","volume":"178","author":"SM-T Smolders","year":"2019","unstructured":"Smolders SM-T, et al. Microglia: brain cells on the move. Prog Neurobiol. 2019;178:101612.","journal-title":"Prog Neurobiol"},{"key":"704_CR116","doi-asserted-by":"publisher","first-page":"3969","DOI":"10.1007\/s00018-014-1670-8","volume":"71","author":"A Fernandes","year":"2014","unstructured":"Fernandes A, Miller-Fleming L, Pais TF. Microglia and inflammation: conspiracy, controversy or control? Cell Mol Life Sci. 2014;71:3969\u201385.","journal-title":"Cell Mol Life Sci"},{"issue":"2","key":"704_CR117","doi-asserted-by":"publisher","first-page":"646","DOI":"10.1161\/01.STR.0000254477.34231.cb","volume":"38","author":"GJd Zoppo","year":"2007","unstructured":"Zoppo GJd, et al. Microglial activation and matrix protease generation during focal cerebral ischemia. Stroke. 2007;38(2):646\u201351.","journal-title":"Stroke"},{"issue":"1","key":"704_CR118","doi-asserted-by":"publisher","first-page":"3879","DOI":"10.1038\/s41467-019-11707-7","volume":"10","author":"EJ Bradbury","year":"2019","unstructured":"Bradbury EJ, Burnside ER. Moving beyond the glial scar for spinal cord repair. Nat Commun. 2019;10(1):3879.","journal-title":"Nat Commun"},{"issue":"2","key":"704_CR119","doi-asserted-by":"publisher","first-page":"437","DOI":"10.1016\/j.bbrc.2004.03.049","volume":"317","author":"S Hirano","year":"2004","unstructured":"Hirano S, et al. Astrocytes express type VIII collagen during the repair process of brain cold injury. Biochem Biophys Res Commun. 2004;317(2):437\u201343.","journal-title":"Biochem Biophys Res Commun"},{"issue":"3\u20134","key":"704_CR120","doi-asserted-by":"publisher","first-page":"422","DOI":"10.1089\/neu.2006.23.422","volume":"23","author":"N Klapka","year":"2006","unstructured":"Klapka N, M\u00fcller HW. Collagen matrix in spinal cord injury. J Neurotrauma. 2006;23(3\u20134):422\u201336.","journal-title":"J Neurotrauma"},{"issue":"4\u20135","key":"704_CR121","doi-asserted-by":"publisher","first-page":"306","DOI":"10.1016\/j.brainresbull.2010.06.015","volume":"84","author":"EJ Bradbury","year":"2011","unstructured":"Bradbury EJ, Carter LM. Manipulating the glial scar: chondroitinase ABC as a therapy for spinal cord injury. Brain Res Bull. 2011;84(4\u20135):306\u201316.","journal-title":"Brain Res Bull"},{"issue":"13","key":"704_CR122","doi-asserted-by":"publisher","first-page":"1968","DOI":"10.1089\/scd.2012.0282","volume":"22","author":"CM Coleman","year":"2013","unstructured":"Coleman CM, et al. Growth differentiation factor-5 enhances in vitro mesenchymal stromal cell chondrogenesis and hypertrophy. Stem Cells Dev. 2013;22(13):1968\u201376.","journal-title":"Stem Cells Dev"},{"key":"704_CR123","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1007\/s13311-018-0631-6","volume":"15","author":"MB Orr","year":"2018","unstructured":"Orr MB, Gensel JC. Spinal cord injury scarring and inflammation: therapies targeting glial and inflammatory responses. Neurotherapeutics. 2018;15:541\u201353.","journal-title":"Neurotherapeutics"},{"issue":"2","key":"704_CR124","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1080\/02713683.2022.2039204","volume":"48","author":"S Powell","year":"2023","unstructured":"Powell S, Irnaten M, O\u2019Brien C. Glaucoma - \u2018A Stiff Eye in a Stiff body\u2019. Curr Eye Res. 2023;48(2):152\u201360.","journal-title":"Curr Eye Res"},{"issue":"3","key":"704_CR125","doi-asserted-by":"publisher","first-page":"1339","DOI":"10.1111\/brv.12398","volume":"93","author":"B Nieuwenhuis","year":"2018","unstructured":"Nieuwenhuis B, et al. Integrins promote axonal regeneration after injury of the nervous system. Biol Rev. 2018;93(3):1339\u201362.","journal-title":"Biol Rev"},{"key":"704_CR126","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1016\/S0074-7742(09)87019-0","volume":"87","author":"G Koopmans","year":"2009","unstructured":"Koopmans G, Hasse B, Sinis N. Chap. 19: the role of collagen in peripheral nerve repair. Int Rev Neurobiol. 2009;87:363\u201379.","journal-title":"Int Rev Neurobiol"},{"issue":"14","key":"704_CR127","doi-asserted-by":"publisher","first-page":"1498","DOI":"10.1002\/glia.20740","volume":"56","author":"MA Chernousov","year":"2008","unstructured":"Chernousov MA, et al. Regulation of Schwann cell function by the extracellular matrix. Glia. 2008;56(14):1498\u2013507.","journal-title":"Glia"},{"issue":"1","key":"704_CR128","doi-asserted-by":"publisher","first-page":"126","DOI":"10.1038\/s41467-017-00143-0","volume":"8","author":"D Wehner","year":"2017","unstructured":"Wehner D, et al. Wnt signaling controls pro-regenerative Collagen XII in functional spinal cord regeneration in zebrafish. Nat Commun. 2017;8(1):126.","journal-title":"Nat Commun"},{"key":"704_CR129","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1016\/j.semcdb.2018.10.002","volume":"89","author":"S Bretaud","year":"2019","unstructured":"Bretaud S, et al. Fishing for collagen function: about development, regeneration and disease. Semin Cell Dev Biol. 2019;89:100\u20138.","journal-title":"Semin Cell Dev Biol"},{"issue":"2","key":"704_CR130","doi-asserted-by":"publisher","first-page":"228","DOI":"10.1016\/j.expneurol.2007.07.020","volume":"208","author":"C Mueller","year":"2007","unstructured":"Mueller C, et al. Lesional expression of the endogenous angiogenesis inhibitor endostatin\/collagen XVIII following traumatic brain injury (TBI). Exp Neurol. 2007;208(2):228\u201337.","journal-title":"Exp Neurol"},{"issue":"4","key":"704_CR131","doi-asserted-by":"publisher","first-page":"573","DOI":"10.1002\/jnr.24151","volume":"96","author":"N George","year":"2018","unstructured":"George N, Geller HM. Extracellular matrix and traumatic brain injury. J Neurosci Res. 2018;96(4):573\u201388.","journal-title":"J Neurosci Res"},{"issue":"6","key":"704_CR132","doi-asserted-by":"publisher","first-page":"061002","DOI":"10.1088\/1478-3975\/12\/6\/061002","volume":"12","author":"LA Hapach","year":"2015","unstructured":"Hapach LA, et al. Manipulation of in vitro collagen matrix architecture for scaffolds of improved physiological relevance. Phys Biol. 2015;12(6):061002.","journal-title":"Phys Biol"},{"key":"704_CR133","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/j.biomaterials.2015.01.059","volume":"50","author":"X Ren","year":"2015","unstructured":"Ren X, et al. Osteogenesis on nanoparticulate mineralized collagen scaffolds via autogenous activation of the canonical BMP receptor signaling pathway. Biomaterials. 2015;50:107\u201314.","journal-title":"Biomaterials"},{"key":"704_CR134","doi-asserted-by":"crossref","unstructured":"Estrada V, Tekinay A, M\u00fcller HW. Chap. 16 - Neural ECM mimetics, in Progress in Brain Research, A. Dityatev, B. Wehrle-Haller, and A. Pitk\u00e4nen, Editors. 2014, Elsevier. p. 391\u2013413.","DOI":"10.1016\/B978-0-444-63486-3.00016-5"},{"key":"704_CR135","doi-asserted-by":"crossref","unstructured":"Chen J-H et al. Neuroprotective effects of collagen-glycosaminoglycan matrix implantation following surgical brain injury Mediators of Inflammation, 2019. 2019.","DOI":"10.1155\/2019\/6848943"},{"issue":"12","key":"704_CR136","doi-asserted-by":"publisher","first-page":"1955","DOI":"10.1242\/jcs.03453","volume":"120","author":"KE Kadler","year":"2007","unstructured":"Kadler KE, et al. Collagens at a glance. J Cell Sci. 2007;120(12):1955\u20138.","journal-title":"J Cell Sci"},{"key":"704_CR137","doi-asserted-by":"crossref","unstructured":"Ribeiro M et al. Intraocular delivery of a Collagen Mimetic Peptide repairs retinal ganglion cell axons in chronic and Acute Injury models. Int J Mol Sci, 2022. 23(6).","DOI":"10.3390\/ijms23062911"},{"key":"704_CR138","doi-asserted-by":"publisher","first-page":"764709","DOI":"10.3389\/fphar.2021.764709","volume":"12","author":"NR McGrady","year":"2021","unstructured":"McGrady NR, et al. Restoring the Extracellular Matrix: a neuroprotective role for collagen mimetic peptides in experimental Glaucoma. Front Pharmacol. 2021;12:764709.","journal-title":"Front Pharmacol"},{"issue":"6","key":"704_CR139","doi-asserted-by":"publisher","first-page":"702","DOI":"10.1016\/j.preteyeres.2012.07.001","volume":"31","author":"DJ Calkins","year":"2012","unstructured":"Calkins DJ. Critical pathogenic events underlying progression of neurodegeneration in glaucoma. Prog Retin Eye Res. 2012;31(6):702\u201319.","journal-title":"Prog Retin Eye Res"},{"key":"704_CR140","doi-asserted-by":"crossref","unstructured":"Calkins DJ. Adaptive responses to neurodegenerative stress in glaucoma. Prog Retin Eye Res, 2021: p. 100953.","DOI":"10.1016\/j.preteyeres.2021.100953"},{"issue":"8","key":"704_CR141","doi-asserted-by":"publisher","first-page":"983","DOI":"10.1163\/156856207781494377","volume":"18","author":"C Deister","year":"2007","unstructured":"Deister C, Aljabari S, Schmidt CE. Effects of collagen 1, fibronectin, laminin and hyaluronic acid concentration in multi-component gels on neurite extension. J Biomater Sci Polym Ed. 2007;18(8):983\u201397.","journal-title":"J Biomater Sci Polym Ed"},{"issue":"22","key":"704_CR142","doi-asserted-by":"publisher","first-page":"4201","DOI":"10.1242\/jcs.00106","volume":"115","author":"N Ortega","year":"2002","unstructured":"Ortega N, Werb Z. New functional roles for non-collagenous domains of basement membrane collagens. J Cell Sci. 2002;115(22):4201\u201314.","journal-title":"J Cell Sci"},{"issue":"30","key":"704_CR143","doi-asserted-by":"publisher","first-page":"5892","DOI":"10.1039\/c2ob25190f","volume":"10","author":"S Chattopadhyay","year":"2012","unstructured":"Chattopadhyay S, et al. Peptides that anneal to natural collagen in vitro and ex vivo. Org Biomol Chem. 2012;10(30):5892\u20137.","journal-title":"Org Biomol Chem"},{"issue":"12","key":"704_CR144","doi-asserted-by":"publisher","first-page":"1012","DOI":"10.1002\/term.1886","volume":"10","author":"S Chattopadhyay","year":"2016","unstructured":"Chattopadhyay S, et al. Anchoring a cytoactive factor in a wound bed promotes healing. J Tissue Eng Regen Med. 2016;10(12):1012\u201320.","journal-title":"J Tissue Eng Regen Med"},{"issue":"17","key":"704_CR145","doi-asserted-by":"publisher","first-page":"1823","DOI":"10.1091\/mbc.E19-12-0709","volume":"31","author":"VW Tang","year":"2020","unstructured":"Tang VW. Collagen, stiffness, and adhesion: the evolutionary basis of vertebrate mechanobiology. Mol Biol Cell. 2020;31(17):1823\u201334.","journal-title":"Mol Biol Cell"},{"issue":"1","key":"704_CR146","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1038\/s41427-021-00304-0","volume":"13","author":"Y Hu","year":"2021","unstructured":"Hu Y, et al. Matrix stiffness changes affect astrocyte phenotype in an in vitro injury model. NPG Asia Materials. 2021;13(1):35.","journal-title":"NPG Asia Materials"},{"issue":"4","key":"704_CR147","doi-asserted-by":"publisher","first-page":"799","DOI":"10.1189\/jlb.0907609","volume":"83","author":"L Meyaard","year":"2008","unstructured":"Meyaard L. The inhibitory collagen receptor LAIR-1 (CD305). J Leucocyte Biology. 2008;83(4):799\u2013803.","journal-title":"J Leucocyte Biology"},{"issue":"5","key":"704_CR148","doi-asserted-by":"publisher","first-page":"567","DOI":"10.1038\/s12276-022-00774-4","volume":"54","author":"M Son","year":"2022","unstructured":"Son M. Understanding the contextual functions of C1q and LAIR-1 and their applications. Exp Mol Med. 2022;54(5):567\u201372.","journal-title":"Exp Mol Med"},{"issue":"6","key":"704_CR149","doi-asserted-by":"publisher","first-page":"1164","DOI":"10.1016\/j.cell.2007.10.036","volume":"131","author":"B Stevens","year":"2007","unstructured":"Stevens B, et al. The classical complement cascade mediates CNS synapse elimination. Cell. 2007;131(6):1164\u201378.","journal-title":"Cell"},{"issue":"3","key":"704_CR150","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1189\/jlb.0209098","volume":"87","author":"W-Y Quan","year":"2010","unstructured":"Quan W-Y, et al. Integrin-mediated inhibition of interleukin-8 secretion from human neutrophils by collagen type I. J Leukoc Biol. 2010;87(3):487\u201391.","journal-title":"J Leukoc Biol"}],"container-title":["Molecular Neurodegeneration"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s13024-024-00704-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s13024-024-00704-0\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s13024-024-00704-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,1,25]],"date-time":"2024-01-25T02:06:25Z","timestamp":1706148385000},"score":1,"resource":{"primary":{"URL":"https:\/\/molecularneurodegeneration.biomedcentral.com\/articles\/10.1186\/s13024-024-00704-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,1,25]]},"references-count":150,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["704"],"URL":"https:\/\/doi.org\/10.1186\/s13024-024-00704-0","relation":{},"ISSN":["1750-1326"],"issn-type":[{"value":"1750-1326","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,1,25]]},"assertion":[{"value":"27 September 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"10 January 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"25 January 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"Not applicable.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"11"}}