File:Collagentriplehelix.png · Wikimedia Commons · See Wikimedia Commons
collagen
Sign in to saveAlso known as GO:0005581, collogen
thumb|upright=1.5|The triple helix: three left-handed polyproline type II helices (red, green, blue) assemble by an axial hydrogen bond to form a right-handed triple helix, the tertiary structure of collagen.
Collagen is a protein made up of three intertwined strands that form a stable triple-helix structure, which gives it strength and stability. This structural arrangement is important because it allows collagen to provide support and firmness to tissues throughout the body.
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Research
297,411 papers- Type 1 collagen: Synthesis, structure and key functions in bone mineralization.ReviewDifferentiation; research in biological diversity · 2024Selvaraj V, Sekaran S, Dhanasekaran A et al.DOI: 10.1016/j.diff.2024.100757
- The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development.ReviewAdvanced materials (Deerfield Beach, Fla.) · 2019Sorushanova A, Delgado LM, Wu Z et al.DOI: 10.1002/adma.201801651
- Mechanochemistry of collagen.ReviewActa biomaterialia · 2023Siadat SM, Ruberti JWDOI: 10.1016/j.actbio.2023.01.025
- Role of Collagen Regulators in Cancer Treatment: A Comprehensive Review.ReviewAnti-cancer agents in medicinal chemistry · 2022Angre T, Kumar A, Singh AK et al.DOI: 10.2174/1871520622666220501162351
- Mechanobiology of Collagen Synthesis, Assembly, and Mineralization.ReviewJournal of dental research · 2025Wang S, Song F, Liang S et al.DOI: 10.1177/00220345251361795
- Hydrated Collagen: Where Physical Chemistry, Medical Imaging, and Bioengineering Meet.ReviewThe journal of physical chemistry. B · 2022Momot KIDOI: 10.1021/acs.jpcb.2c06217
- Collagen Mechanics.Sub-cellular biochemistry · 2026Szarek P, Ruberti JWDOI: 10.1007/978-3-032-05273-5_10
- The Multifaced Role of Collagen in Cancer Development and Progression.ReviewInternational journal of molecular sciences · 2024Lo Buglio G, Lo Cicero A, Campora S et al.DOI: 10.3390/ijms252413523
via PubMed
Wikidata facts
- Image
- Fibers of Collagen Type I - TEM .jpg
Show 3 more facts
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- purl.obolibrary.org/obo/GO_0005581
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~34 min read
Article
24 sectionsContents
- Etymology
- Types
- In humans
- Cardiac
- Bone grafts
- Tissue regeneration
- Reconstructive surgery
- Wound healing
- Use in basic research
- Biology
- Synthesis
- Amino acids
- Collagen I formation
- Molecular structure
- Associated disorders
- Diseases
- Animal harvesting
- Characteristics
- Mechanical properties
- Uses
- Cosmetics
- History
- See also
- References
thumb|upright=1.5|The triple helix: three left-handed polyproline type II helices (red, green, blue) assemble by an axial hydrogen bond to form a right-handed triple helix, the tertiary structure of collagen.
Collagen () is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, making up 25% to 35% of protein content. Amino acids are bound together to form a triple helix of elongated fibril known as a collagen helix. It is mostly found in cartilage, bones, tendons, ligaments, and skin. Vitamin C is vital for collagen synthesis.
Gallery (18)
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