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1277 12842 Ensembl ENSG00000108821 ENSMUSG00000001506 UniProt P02452 P11087 RefSeq (mRNA) NM_000088 NM_007742 RefSeq (protein) NP_000079 NP_031768 Location (UCSC) Chr 17: 50.18 – 50.2 Mb Chr 11: 94.83 – 94.84 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the COL1A1 gene ...
Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large, eosinophilic fibers known as collagen fibers, which make up most of the rope-like dense connective tissue in ...
1281 12825 Ensembl ENSG00000168542 ENSMUSG00000026043 UniProt P02461 P08121 RefSeq (mRNA) NM_000090 NM_001376916 NM_009930 RefSeq (protein) NP_000081 NP_034060 Location (UCSC) Chr 2: 188.97 – 189.01 Mb Chr 1: 45.35 – 45.39 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Type III Collagen is a homotrimer, or a protein composed of three identical peptide chains (monomers), each ...
The ratio and the proportion of collagen play an important role in the tensile and compressive strength, as well as the elasticity of the tissue. The content of collagen in cartilage is different between joints and soft tissue structures. [3] For example, cartilage in the knee has a different structure to the ankle. Cartilage, skin, and spinal ...
The C-terminal telopeptide (CTX), also known as carboxy-terminal collagen crosslinks, is the C-terminal telopeptide of fibrillar collagens such as collagen type I and type II. It is used as a biomarker in the serum to measure the rate of bone turnover .
In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.
The alpha chains may be identical or different, depending on the type of collagen. Type II collagen is made by combining three copies of the alpha chain made by the COL2A1 gene. Type XI collagen, on the other hand, is composed of three different alpha chains: the products of the COL2A1, COL11A1, and COL11A2 genes.
In vitro tests yield evidence that suggest tenascin X accelerates collagen fibril formation through an additive mechanism when collagen VI is present. [1] In addition to tenascin X, multiple proteins, glycoconjugates, and small molecules have shown to influence not only the rate of collagen fibrillogenesis, but also the structure of collagen ...
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