No retraction, correction or concern found when last checked on Nov 5, 2026.
Current Insights into Collagen Type I
Ruth Naomi, Pauzi Muhd Ridzuan, Hasnah Bahari
Polymers · 2021 · Review · CC BY
Abstract
Collagen type I (Col-I) is unique due to its high biocompatibility in human tissue. Despite its availability from various sources, Col-I naturally mimics the extracellular matrix (ECM) and generally makes up the larger protein component (90%) in vasculature, skin, tendon bone, and other tissue. The acceptable physicochemical properties of native Col-I further enhance the incorporation of Col-I in various fields, including pharmaceutical, cosmeceutical, regenerative medicine, and clinical. This review aims to discuss Col-I, covering the structure, various sources of availability, native collagen synthesis, current extraction methods, physicochemical characteristics, applications in various fields, and biomarkers. The review is intended to provide specific information on Col-I currently available, going back five years. This is expected to provide a helping hand for researchers who are concerned about any development on collagen-based products particularly for therapeutic fields.
References 122
- 1.
Holmes D.F., Lu Y., Starborg T., Kadler K.E., Litscher E.S., Wassarman P.M. Collagen fibril assembly and function. Current Topics in Developmental Biology. 2018;Volume 130:107-142.
Not in our library10.1016/bs.ctdb.2018.02.004
- 2.
Luomala T., Pihlman M., Stecco L., Stecco C., Hammer W. Anatomy of the fascia from the clinical point of view. A Practical Guide to Fascial Manipulation. 2016;19-59.
Not in our library
- 3.
Chowdhury S.R., Busra M.F., Lokanathan Y., Ng M.H., Law J.X., Cletus U.C., Haji Idrus R.B., Chun H.J. Collagen type I: A versatile biomaterial. Novel Biomaterials for Regenerative Medicine, Advances in Experimental Medicine and Biology. 2018;Volume 1077:389-414.
Not in our library10.1007/978-981-13-0947-2_21
- 4.
Chicatun F., Griffanti G., McKee M., Nazhat S., Ambrosio L. Collagen/chitosan composite scaffolds for bone and cartilage tissue engineering. Biomedical Composites. 2017;163-198.
Not in our library
- 5.
Petty R.E., Petty R.E., Laxer R.M., Lindsley C.B., Wedderburn L.R. Structure and function. Textbook of Pediatric Rheumatology. 2016;Volume 2:5-13.
Not in our library
- 6.
Sheehy E.J., Cunniffe G.M., O’Brien F.J., Barbosa M.A., Martins M.C.L. Collagen-based biomaterials for tissue regeneration and repair. Peptides and Proteins as Biomaterials for Tissue Regeneration and Repair. 2018;127-150.
Not in our library
- 7.
Pavlovic S., Ugrin M., Micic S., Gasic V., Dimitrijevic J., Barteczko U., Hostiuc S. Using genetics for enhancement (liberal eugenics). Clinical Ethics at the Crossroads of Genetic and Reproductive Technologies. 2018;335-366.
Not in our library
- 8.
Bou-Gharios G., Abraham D., Crombrugghe B. Type I collagen structure, synthesis, and regulation. Principles of Bone Biology. 2020;295-337.
Not in our library
- 9.
Naomi R., Fauzi M.B. Cellulose/collagen dressings for diabetic foot ulcer: A review. Pharmaceutics. 2020;12:881.
Not in our library10.3390/pharmaceutics12090881
- 10.
Henriksen K., Karsdal M.A., Karsdal M.A. Type I collagen. Biochemistry of Collagens, Laminins and Elastin: Structure, Function and Biomarkers. 2016;1-11.
Not in our library
- 11.
Boraschi-Diaz I., Wang J., Mort J.S., Komarova S.V. Collagen type I as a ligand for receptor-mediated signaling. Front. Phys. 2017;5.
Not in our library10.3389/fphy.2017.00012
- 12.
- 13.
Theocharis A.D., Skandalis S.S., Gialeli C., Karamanos N.K. Extracellular matrix structure. Adv. Drug Deliv. Rev. 2016;97:4-27.
Not in our library10.1016/j.addr.2015.11.001
- 14.
Naomi R., Ratanavaraporn J., Fauzi M.B. Comprehensive review of hybrid collagen and silk fibroin for cutaneous wound healing. Materials. 2020;13:3097.
Not in our library10.3390/ma13143097
- 15.
Kubyshkin V. Stabilization of the triple helix in collagen mimicking peptides. Org. Biomol. Chem. 2019;17:8031-8047.
Not in our library10.1039/c9ob01646e
- 16.
Badnjevic A., Škrbić P., Pokvić L.G., Magjarevic R. Recent advancements and implications in the delivery of collagen. IFMBE Proceedings Book Series. 2019;250-257.
Not in our library
- 17.
Sorushanova A., Delgado L.M., Wu Z., Shologu N., Kshirsagar A., Raghunath R., Mullen A.M., Bayon Y., Pandit A., Raghunath M., et al. The collagen suprafamily: From biosynthesis to advanced biomaterial development. Adv. Mater. 2018;31:e1801651.
Not in our library10.1002/adma.201801651
- 18.
Silvipriya K., Kumar K., Bhat A., Kumar B., John A., Lakshmanan P. Collagen: Animal sources and biomedical application. J. Appl. Pharm. Sci. 2015;123-127.
Not in our library10.7324/japs.2015.50322
- 19.
- 20.
Jeng W.M. Preparation of Biomaterials using Fish Collagen and Seaweed Alginate to Promote In Vivo Cell Growth and Proliferation Activity. Ph.D. Thesis. 2019.
Not in our library
- 21.
Yamada S., Yamamoto K., Ikeda T., Yanagiguchi K., Hayashi Y. Potency of fish collagen as a scaffold for regenerative medicine. BioMed Res. Int. 2014;2014:1-8.
Not in our library10.1155/2014/302932
- 22.
Eckelkamp S., Singh M. Bovine collagen: Benefits and the importance of grass-fed. Funct. Food. 2020.
Not in our library
- 23.
Cheng X., Shao Z., Li C., Yu L., Raja M.A., Liu C. Isolation, characterization and evaluation of collagen from jellyfish Rhopilema esculentum Kishinouye for use in hemostatic applications. PLoS ONE. 2017;12:e0169731.
Not in our library10.1371/journal.pone.0169731
- 24.
Raman M., Gopakumar K. Fish collagen and its applications in food and pharmaceutical industry: A review. EC Nutr. 2018;13:752-767.
Not in our library
- 25.
Rittié L. Type I Collagen Purification from Rat Tail Tendons. 2017;Volume 1627:287-308.
Not in our library10.1007/978-1-4939-7113-8_19
- 26.
He L., Lan W., Wang Y., Ahmed S., Liu Y. Extraction and characterization of self-assembled collagen isolated from grass carp and crucian carp. Foods. 2019;8:396.
Not in our library10.3390/foods8090396
- 27.
Green J., Bryan K. Collagen Business Case Report. 2018.
Not in our library
- 28.
Wu M., Cronin K., Crane J.S. Collagen synthesis. Biochemistry. 2018.
Not in our library
- 29.
Shi J., Ren M., Jia J., Tang M., Guo Y., Ni X., Shi T. Genotype-phenotype association analysis reveals new pathogenic factors for osteogenesis imperfecta disease. Front. Pharmacol. 2019;10:1200.
Not in our library10.3389/fphar.2019.01200
- 30.
Jürg C. Biomedical Significance of Collagen Glycosylation-with Focus on the Collagen Glucosyltransferase. Ph.D. Thesis. 2015.
Not in our library
- 31.
Gistelinck C., Gioia R., Gagliardi A., Tonelli F., Marchese L., Bianchi L., Landi C., Bini L., Huysseune A., Witten P.E., et al. Zebrafish collagen type I: Molecular and biochemical characterization of the major structural protein in bone and skin. Sci. Rep. 2016;6:21540.
Not in our library10.1038/srep21540
- 32.
Di Jeso B., Arvan P. Thyroglobulin from molecular and cellular biology to clinical endocrinology. Endocr. Rev. 2015;37:2-36.
Not in our library10.1210/er.2015-1090
- 33.
Rodriguez-Pascual F., Slatter D.A. Collagen cross-linking: Insights on the evolution of metazoan extracellular matrix. Sci. Rep. 2016;6:37374.
Not in our library10.1038/srep37374
- 34.
Naomi R., Ardhani R., Hafiyyah O.A., Fauzi M.B. Current insight of collagen biomatrix for gingival recession: An evidence-based systematic review. Polymers. 2020;12:2081.
Not in our library10.3390/polym12092081
- 35.
Malhotra V., Erlmann P. The pathway of collagen secretion. Annu. Rev. Cell Dev. Biol. 2015;31:109-124.
Not in our library10.1146/annurev-cellbio-100913-013002
- 36.
Fauzi M.B., Lokanathan Y., Aminuddin B., Ruszymah B., Chowdhury S. Ovine tendon collagen: Extraction, characterisation and fabrication of thin films for tissue engineering applications. Mater. Sci. Eng. C. 2016;68:163-171.
Not in our library10.1016/j.msec.2016.05.109
- 37.
Schmidt M.M., Dornelles R.C.P., Mello R.O., Kubota E.H., Mazutti M.A., Kempka A.P., Demiate I.M. Collagen extraction process. Int. Food Res. J. 2016;23:913-922.
Not in our library
- 38.
Lin X., Chen Y., Jin H., Zhao Q., Liu C., Li R., Yu F., Chen Y., Huang F., Yang Z., et al. Collagen extracted from bigeye tuna (Thunnus obesus) skin by isoelectric precipitation: Physicochemical properties, proliferation, and migration activities. Mar. Drugs. 2019;17:261.
Not in our library10.3390/md17050261
- 39.
Wang J., Pei X., Liu H., Zhou D. Extraction and characterization of acid-soluble and pepsin-soluble collagen from skin of loach (Misgurnus anguillicaudatus). Int. J. Biol. Macromol. 2018;106:544-550.
Not in our library10.1016/j.ijbiomac.2017.08.046
- 40.
Yang H., Shu Z. The extraction of collagen protein from pig skin. J. Chem. Pharm. Res. 2014;6:683-687.
Not in our library
- 41.
Munasinghe K.A., Schwarz J.G., Nyame A.K. Chicken collagen from law market value by-products as an alternate source. J. Food Process. 2014;2014:1-6.
Not in our library10.1155/2014/298295
- 42.
Morimura S., Nagata H., Uemura Y., Fahmi A., Shigematsu T., Kida K. Development of an effective process for utilization of collagen from livestock and fish waste. Process. Biochem. 2002;37:1403-1412.
Not in our library10.1016/s0032-9592(02)00024-9
- 43.
Yamamoto K., Yoshizawa Y., Yanagiguchi K., Ikeda T., Yamada S., Hayashi Y. The characterization of fish (Tilapia) collagen sponge as a biomaterial. Int. J. Polym. Sci. 2015;2015:1-5.
Not in our library10.1155/2015/957385
- 44.
- 45.
- 46.
Gorgieva S., Kokol V., Pignatello R. Collagen vs. gelatine-based biomaterials and their biocompatibility: Review and perspectives. Biomaterials Applications for Nanomedicine. 2011;17-52.
Not in our library
- 47.
Lee C., Lee Y. Collagen-based formulations for wound healing applications. Wound Heal. Biomater. 2016;135-149.
Not in our library10.1016/b978-1-78242-456-7.00007-6
- 48.
Zeng Q., Macri L.K., Prasad A., Clark R.A.F., Zeugolis D.I., Hanley C., Garcia Y., Pandit A., Ducheyne P. Skin tissue engineering. Comprehensive Biomaterials. 2011;467-499.
Not in our library
- 49.
Durham E.L., Howie R.N., Hall S., Larson N., Oakes B., Houck R., Grey Z., Steed M., LaRue A.C., Muise-Helmericks R., et al. Optimizing bone wound healing using BMP2 with absorbable collagen sponge and Talymed nanofiber scaffold. J. Transl. Med. 2018;16:321.
Not in our library10.1186/s12967-018-1697-y
- 50.
Dill V., Mörgelin M. Biological dermal templates with native collagen scaffolds provide guiding ridges for invading cells and may promote structured dermal wound healing. Int. Wound J. 2020;17:618-630.
Not in our library10.1111/iwj.13314
- 51.
Singla R., Soni S., Patial V., Kulurkar P.M., Kumari A., Padwad Y.S., Yadav S.K. In vivo diabetic wound healing potential of nanobiocomposites containing bamboo cellulose nanocrystals impregnated with silver nanoparticles. Int. J. Biol. Macromol. 2017;105:45-55.
Not in our library10.1016/j.ijbiomac.2017.06.109
- 52.
Kanta J. Collagen matrix as a tool in studying fibroblastic cell behavior. Cell Adhes. Migr. 2015;9:308-316.
Not in our library10.1080/19336918.2015.1005469
- 53.
Law J.X., Liau L.L., Bin Saim A., Yang Y., Idrus R. Electrospun collagen nanofibers and their applications in skin tissue engineering. Tissue Eng. Regen. Med. 2017;14:699-718.
Not in our library10.1007/s13770-017-0075-9
- 54.
Teo W.-E. Electrospinning collagen. Adv. Mater. 2017;9:40.
Not in our library
- 55.
Nair H.K., Chong S.S., Isa N.A.B., Khamis S.A.B. Efficacy of collagen-based wound dressings in wound healing. Wounds Asia. 2020;3:42-47.
Not in our library
- 56.
Jain S., Tote D., Kolte G., Jajoo S., Tote S. Effect of moist dressing, collagen sheet dressing and epidermal growth factor in healing of chronic wounds. Int. Surg. J. 2017;4:2594-2599.
Not in our library10.18203/2349-2902.isj20173395
- 57.
Glattauer V., Tsai W.-B., White J.F., Nigro J., Tebb T.A., Jerome A., Ramshaw J.A.M., Eberli D. Direct use of resorbable collagen-based beads for cell delivery in tissue engineering and cell therapy applications. Cells and Biomaterials. 2011.
Not in our library
- 58.
Kaufmann R., Jairam A.P., Mulder I.M., Wu Z., Verhelst J., Vennix S., Giesen L.J.X., Groningen M.C.C.-V., Jeekel J., Lange J.F. Non-cross-linked collagen mesh performs best in a physiologic, noncontaminated rat model. Surg. Innov. 2019;26:302-311.
Not in our library10.1177/1553350619833291
- 59.
Antoine E.E., Vlachos P.P., Rylander M.N. Review of collagen I hydrogels for bioengineered tissue microenvironments: Characterization of mechanics, structure, and transport. Tissue Eng. Part B Rev. 2014;20:683-696.
Not in our library10.1089/ten.teb.2014.0086
- 60.
Pawelec K.M., White A.A., Best S.M., Pawelec K.M., Planell J.A. Properties and characterization of bone repair materials. Bone Repair Biomaterials. 2019;65-102.
Not in our library
- 61.
Chattopadhyay S., Raines R.T. Collagen-based biomaterials for wound healing. Biopolymers. 2014;101:821-833.
Not in our library10.1002/bip.22486
- 62.
Yao L., Phan F., Li Y. Collagen microsphere serving as a cell carrier supports oligodendrocyte progenitor cell growth and differentiation for neurite myelination in vitro. Stem Cell Res. Ther. 2013;4:109.
Not in our library10.1186/scrt320
- 63.
- 64.
- 65.
Busra M.F.M. Recent development in the fabrication of collagen scaffolds for tissue engineering applications: A review. Curr. Pharm. Biotechnol. 2019;20:992-1003.
Not in our library10.2174/1389201020666190731121016
- 66.
Ghodbane S.A., Dunn M. Physical and mechanical properties of cross-linked type I collagen scaffolds derived from bovine, porcine, and ovine tendons. J. Biomed. Mater. Res. Part A. 2016;104:2685-2692.
Not in our library10.1002/jbm.a.35813
- 67.
Panwar P., Lamour G., Mackenzie N.C.W., Yang H., Ko F., Li H., Brömme D. Changes in structural-mechanical properties and degradability of collagen during aging-associated modifications. J. Biol. Chem. 2015;290:23291-23306.
Not in our library10.1074/jbc.m115.644310
- 68.
Sotelo C.G., Comesaña M.B., Ariza P.R., Perez-Martin R. Characterization of collagen from different discarded fish species of the west coast of the Iberian Peninsula. J. Aquat. Food Prod. Technol. 2015;25:388-399.
Not in our library10.1080/10498850.2013.865283
- 69.
Subhan F., Ikram M., Shehzad A., Ghafoor A. Marine collagen: An emerging player in biomedical applications. J. Food Sci. Technol. 2014;52:4703-4707.
Not in our library10.1007/s13197-014-1652-8
- 70.
Valenzuela-Rojo D.R., López-Cervantes J., Sánchez-Machado D.I., Maiti S., Laha B. Tilapia (Oreochromis aureus) collagen for medical biomaterials. Seaweed Biomaterials. 2018;47-52.
Not in our library
- 71.
Nikolova M.P., Chavali M.S. Recent advances in biomaterials for 3D scaffolds: A review. Bioact. Mater. 2019;4:271-292.
Not in our library10.1016/j.bioactmat.2019.10.005
- 72.
Turnbull G., Clarke J., Picard F., Riches P., Jia L., Han F., Li B., Shu W. 3D bioactive composite scaffolds for bone tissue engineering. Bioact. Mater. 2018;3:278-314.
Not in our library10.1016/j.bioactmat.2017.10.001
- 73.
Abbasi N., Hamlet S., Love R.M., Nguyen N.-T. Porous scaffolds for bone regeneration. J. Sci. Adv. Mater. Devices. 2020;5:1-9.
Not in our library10.1016/j.jsamd.2020.01.007
- 74.
Ashworth J.C., Mehr M., Buxton P.G., Best S.M., Cameron R. Optimising collagen scaffold architecture for enhanced periodontal ligament fibroblast migration. J. Mater. Sci. Mater. Med. 2018;29:1-11.
Not in our library10.1007/s10856-018-6175-9
- 75.
Song X., Zhu C., Fan D., Mi Y., Li X., Fu R.Z., Duan Z., Wang Y., Feng R.R. A novel human-like collagen hydrogel scaffold with porous structure and sponge-like properties. Polymers. 2017;9:638.
Not in our library10.3390/polym9120638
- 76.
Takallu S., Mirzaei E., Azadi A., Karimizade A., Tavakol S. Plate-shape carbonated hydroxyapatite/collagen nanocomposite hydrogel via in situ mineralization of hydroxyapatite concurrent with gelation of collagen at pH = 7.4 and 37 °C. J. Biomed. Mater. Res. Part B Appl. Biomater. 2018;107:1920-1929.
Not in our library10.1002/jbm.b.34284
- 77.
Ghica M.V., Kaya M.G.A., Dinu-Pîrvu C.-E., Lupuleasa D., Udeanu D.I. Development, optimization and in vitro/in vivo characterization of collagen-dextran spongious wound dressings loaded with flufenamic acid. Molecules. 2017;22:1552.
Not in our library10.3390/molecules22091552
- 78.
Shi Y., Zhang H., Zhang X., Chen Z., Zhao D., Ma J. A comparative study of two porous sponge scaffolds prepared by collagen derived from porcine skin and fish scales as burn wound dressings in a rabbit model. Regen. Biomater. 2019;7:63-70.
Not in our library10.1093/rb/rbz036
- 79.
- 80.
Bružauskaitė I., Bironaitė D., Bagdonas E., Bernotienė E. Scaffolds and cells for tissue regeneration: Different scaffold pore sizes—Different cell effects. Cytotechnology. 2015;68:355-369.
Not in our library10.1007/s10616-015-9895-4
- 81.
Rahul V.G., Nair P.D., Sethuraman S., Krishnan U.M., Subramanian A. Biomaterials and designs supporting cartilage regeneration. Biomaterials and Nanotechnology for Tissue Engineering. 2016;93-103.
Not in our library
- 82.
Marín-Pareja N., Cantini M., González-García C., Salvagni E., Salmeron-Sanchez M., Ginebra M.-P. Different organization of type I collagen immobilized on silanized and nonsilanized titanium surfaces affects fibroblast adhesion and fibronectin secretion. ACS Appl. Mater. Interfaces. 2015;7:20667-20677.
Not in our library10.1021/acsami.5b05420
- 83.
Kasalkova N.S., Slepicka P., Kolska Z., Svorcik Z.K.A.V. Wettability and other surface properties of modified polymers. Wetting Wettability. 2015;12:323-356.
Not in our library10.5772/60824
- 84.
Chen J., Li J., Li Z., Yi R., Shi S., Wu K., Li Y., Wu S. Physicochemical and functional properties of type I collagens in red stingray (Dasyatis akajei) skin. Mar. Drugs. 2019;17:558.
Not in our library10.3390/md17100558
- 85.
Stylianou A., Yova D., Politopoulos K. Atomic force microscopy quantitative and qualitative nanoscale characterization of collagen thin films. Proceedings of the 5th Conference on Emerging Technologies in Non-Destructive Testing. 2012;415-420.
Not in our library
- 86.
Stylianou A. Atomic force microscopy for collagen-based nanobiomaterials. J. Nanomater. 2017;2017:1-14.
Not in our library10.1155/2017/9234627
- 87.
Scarano A., Lorusso F., Orsini T., Morra M., Iviglia G., Valbonetti L. Biomimetic surfaces coated with covalently immobilized collagen type I: An X-ray photoelectron spectroscopy, atomic force microscopy, micro-CT and histomorphometrical study in rabbits. Int. J. Mol. Sci. 2019;20:724.
Not in our library10.3390/ijms20030724
- 88.
Baer D.R., Artyushkova K., Brundle C.R., Castle J.E., Engelhard M.H., Gaskell K.J., Grant J.T., Haasch R.T., Linford M.R., Powell C.J., et al. Practical guides for x-ray photoelectron spectroscopy: First steps in planning, conducting, and reporting XPS measurements. J. Vac. Sci. Technol. A. 2019;37:031401.
Not in our library10.1116/1.5065501
- 89.
Onnainty R., Granero G., Grumezescu A.M. Chitosan-based nanocomposites: Promising materials for drug delivery applications. Biomedical Applications of Nanoparticles. 2019;375-407.
Not in our library
- 90.
Riaz T., Zeeshan R., Zarif F., Ilyas K., Muhammad N., Safi S.Z., Rahim A., Rizvi S.A.A., Rehman I.U. FTIR analysis of natural and synthetic collagen. Appl. Spectrosc. Rev. 2018;53:703-746.
Not in our library10.1080/05704928.2018.1426595
- 91.
Rey C., Combes C., Aparicio C., Ginebra M.P. Physical chemistry of biological apatites. Biomineralization and Biomaterials: Fundamentals and Applications. 2015;95-127.
Not in our library
- 92.
Sanjurjo-Rodríguez C., Viñuelas R.C., Gómez T.H., Fernández-Vázquez T., Fuentes-Boquete I.M., De Toro-Santos F.J., Díaz-Prado S.M., Blanco-García F.J. Ovine mesenchymal stromal cells: Morphologic, phenotypic and functional characterization for osteochondral tissue engineering. PLoS ONE. 2017;12:e0171231.
Not in our library10.1371/journal.pone.0171231
- 93.
León-Mancilla B., Araiza-Téllez M., Flores-Flores J., Piña-Barba M. Physico-chemical characterization of collagen scaffolds for tissue engineering. J. Appl. Res. Technol. 2016;14:77-85.
Not in our library10.1016/j.jart.2016.01.001
- 94.
Morozova S., Muthukumar M. Electrostatic effects in collagen fibril formation. J. Chem. Phys. 2018;149:163333.
Not in our library10.1063/1.5036526
- 95.
Nishiyama N., Suzuki K., Nagatsuka A., Yokota I., Nemoto K. Dissociation states of collagen functional groups and their effects on the priming efficacy of HEMA bonded to collagen. J. Dent. Res. 2003;82:257-261.
Not in our library10.1177/154405910308200403
- 96.
Marini J.C., Cabral W.A., Thakker R.V., Whyte M.P., Eisman J.A., Igarashi T. Osteogenesis imperfecta. Genetics of Bone Biology and Skeletal Disease. 2018;397-420.
Not in our library
- 97.
Wu Q., Zhang B., Sun Y., Xu R., Hu X., Ren S., Ma Q., Chen C., Shu J., Qi F., et al. Identification of novel biomarkers and candidate small molecule drugs in non-small-cell lung cancer by integrated microarray analysis. OncoTargets Ther. 2019;12:3545-3563.
Not in our library10.2147/ott.s198621
- 98.
Nicol L., Morar P., Wang Y., Henriksen K., Sun S., Karsdal M., Smith R., Nagamani S.C., Shapiro J., Lee B., et al. Alterations in non-type I collagen biomarkers in osteogenesis imperfecta. Bone. 2019;120:70-74.
Not in our library10.1016/j.bone.2018.09.024
- 99.
Munir N., Callanan A. Novel phase separated polycaprolactone/collagen scaffolds for cartilage tissue engineering. Biomed. Mater. 2018;13:051001.
Not in our library10.1088/1748-605x/aac91f
- 100.
Klein S., Vykoukal J., Felthaus O., Dienstknecht T., Prantl L. Collagen type I conduits for the regeneration of nerve defects. Materials. 2016;9:219.
Not in our library10.3390/ma9040219
- 101.
Chen G., Yang L., Lv Y. Cell-free scaffolds with different stiffness but same microstructure promote bone regeneration in rabbit large bone defect model. J. Biomed. Mater. Res. Part A. 2015;104:833-841.
Not in our library10.1002/jbm.a.35622
- 102.
Irawan V., Sung T.-C., Higuchi A., Ikoma T. Collagen scaffolds in cartilage tissue engineering and relevant approaches for future development. Tissue Eng. Regen. Med. 2018;15:673-697.
Not in our library10.1007/s13770-018-0135-9
- 103.
- 104.
De Angelis B., Orlandi F., D’Autilio M.F.L.M., Scioli M.G., Orlandi A., Cervelli V., Gentile P. Long-term follow-up comparison of two different bi-layer dermal substitutes in tissue regeneration: Clinical outcomes and histological findings. Int. Wound J. 2018;15:695-706.
Not in our library10.1111/iwj.12912
- 105.
Samadian H., Vaez A., Ehterami A., Salehi M., Farzamfar S., Sahrapeyma H., Norouzi P. Sciatic nerve regeneration by using collagen type I hydrogel containing naringin. J. Mater. Sci. Mater. Med. 2019;30:107.
Not in our library10.1007/s10856-019-6309-8
- 106.
Zhang D., Wu X., Chen J., Lin K. The development of collagen based composite scaffolds for bone regeneration. Bioact. Mater. 2018;3:129-138.
Not in our library10.1016/j.bioactmat.2017.08.004
- 107.
Kumar V., Caves J.M., Haller C.A., Dai E., Liu L., Grainger S., Chaikof E.L. Acellular vascular grafts generated from collagen and elastin analogs. Acta Biomater. 2013;9:8067-8074.
Not in our library10.1016/j.actbio.2013.05.024
- 108.
Koens M.J.W., Krasznai A.G., Hanssen A.E.J., Hendriks T., Praster R., Daamen W.F., Van Der Vliet J.A., Van Kuppevelt T.H. Vascular replacement using a layered elastin-collagen vascular graft in a porcine model: One week patency versus one month occlusion. Organogenesis. 2015;11:105-121.
Not in our library10.1080/15476278.2015.1038448
- 109.
Osidak E.O., Kozhukhov V.I., Osidak M.S., Domogatskiy S.P. Collagen as bioink for bioprinting: A comprehensive review. Int. J. Bioprint. 2020;6.
Not in our library10.18063/ijb.v6i3.270
- 110.
Lee A., Hudson A.R., Shiwarski D.J., Tashman J.W., Hinton T.J., Yerneni S., Bliley J.M., Campbell P.G., Feinberg A.W. 3D bioprinting of collagen to rebuild components of the human heart. Science. 2019;365:482-487.
Not in our library10.1126/science.aav9051
- 111.
- 112.
Potti R.B., Fahad M. Extraction and characterization of collagen from broiler chicken feet (Gallus gallus domesticus)—Biomolecules from poultry waste. J. Pure Appl. Microbiol. 2017;11:315-322.
Not in our library10.22207/jpam.11.1.39
- 113.
Pahuja M.P., Arora S., Pawar P. Ocular drug delivery system: A reference to natural polymers. Expert Opin. Drug Deliv. 2012;9:837-861.
Not in our library10.1517/17425247.2012.690733
- 114.
Kumar D. A review on collagen-based drug delivery systems. Int. J. Pharm. Teach. Pract. 2013;4:811-820.
Not in our library
- 115.
Khan R., Khan M.H. Use of collagen as a biomaterial: An update. J. Indian Soc. Periodontol. 2013;17:539-542.
Not in our library10.4103/0972-124x.118333
- 116.
Rodríguez M.I.A., Barroso L.G.R., Sánchez M.L. Collagen: A review on its sources and potential cosmetic applications. J. Cosmet. Dermatol. 2017;17:20-26.
Not in our library10.1111/jocd.12450
- 117.
Samad N.A.B.A., Sikarwar A.S. Collagen: New dimension in cosmetic and healthcare. Int. J. Biochem. Res. Rev. 2016;14:1-8.
Not in our library10.9734/ijbcrr/2016/27271
- 118.
Depalle B., McGilvery C.M., Nobakhti S., Aldegaither N., Shefelbine S.J., Porter A.E. Osteopontin regulates type I collagen fibril formation in bone tissue. Acta Biomater. 2021;120:194-202.
Not in our library10.1016/j.actbio.2020.04.040
- 119.
Liu X., Zheng C., Luo X., Wang X., Jiang H. Recent advances of collagen-based biomaterials: Multi-hierarchical structure, modification and biomedical applications. Mater. Sci. Eng. C. 2019;99:1509-1522.
Not in our library10.1016/j.msec.2019.02.070
- 120.
Jongprasitkul H., Turunen S., Parihar V.S., Annurakshita S., Kellomäki M. Photocross-linkable methacrylated polypeptides and polysaccharides for casting, injecting, and 3D fabrication. Biomacromolecules. 2020;22:481-493.
Not in our library10.1021/acs.biomac.0c01322
- 121.
Rupani A., Balint R., Cartmell S. Osteoblasts and their applications in bone tissue engineering. Cell Health Cytoskelet. 2012;49.
Not in our library10.2147/chc.s21845
- 122.
Cited by papers we hold 4
- Red yeast rice expedites wound healing in diabetic rats: emphasis on its pro-collagen and angiogenic activities · 2025Not checked
- Matrix viscoelasticity promotes liver cancer progression in the pre-cirrhotic liver · 2024Corrected
- Nanoparticle protein corona: from structure and function to therapeutic targeting · 2023No notice
- Advanced Surface Modification for 3D-Printed Titanium Alloy Implant Interface Functionalization · 2022Not checked
Reads
Read by people on this page
None yet.
Checked or read by AI through naulon
None yet.
A person counts once a day per paper. We keep no cookie and no address: a reader is a hash that changes every day. Any month under five reads shows no number.
Are you an author?
Is this your paper?
Claim it to add your note and be paid when agents cite it. Free.