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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 .
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The ...
The procollagen complex is then modified by different enzyme proteinases which cleave N and C terminal pro-peptides that are present on either side of the molecule. This process occurs outside of the cellular membrane at which post processing, the molecules cross link and form a final type I collagen product.
The N-terminal telopeptide (NTX), also known as amino-terminal collagen crosslinks, is the N-terminal telopeptide of fibrillar collagens such as collagen type I and type II. It is used as a biomarker to measure the rate of bone turnover. NTX can be measured in the urine (uNTX) or serum (serum NTX). [1]
Group I proteins have the N terminus on the far side and C terminus on the cytosolic side. Group II proteins have the C terminus on the far side and N terminus in the cytosol. However final topology is not the only criterion for defining transmembrane protein groups, rather location of topogenic determinants and mechanism of assembly is ...
The strongest evidence was for urinary C-terminal telopeptide of type II collagen (uCTX-II) as a prognostic marker for knee osteoarthritis progression, and serum cartilage oligomeric matrix protein (COMP) levels as a prognostic marker for incidence of both knee and hip osteoarthritis.
C-terminal telopeptide, commonly known as CTX, a serum biomarker for bone turnover rate and a tool used to evaluate patient risk for complications due to BRONJ; Osteonecrosis of the jaw, see section on Bisphosphonates; Osteoradionecrosis, a term for osteonecrosis caused by radiotherapy; Phossy jaw
The original TAP method involves the fusion of the TAP tag to the C-terminus of the protein under study. The TAP tag consists of three components: a calmodulin binding peptide (CBP), TEV protease cleavage site, and two Protein A domains, which bind tightly to IgG (making a TAP tag a type of epitope tag). [1]