Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Jiann-Jiu Wu"'
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e93467 (2014)
Approximately half the proline residues in fibrillar collagen are hydroxylated. The predominant form is 4-hydroxyproline, which helps fold and stabilize the triple helix. A minor form, 3-hydroxyproline, still has no clear function. Using peptide mass
Externí odkaz:
https://doaj.org/article/24d75c5e479c4ff68ecc094c702c5c4a
Publikováno v:
Spine. 36:2031-2038
Immunohistochemical analysis of type IX collagen in disc tissue from spinal fusion patients.To determine if collagen IX can be detected in adult disc tissue removed at spinal fusion surgery from patients either with or without degeneration-associated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c0adb7fbadf7938a559ca94f59c3a78
https://doi.org/10.1097/brs.0b013e3181ffdd61
https://doi.org/10.1097/brs.0b013e3181ffdd61
Publikováno v:
Journal of Biological Chemistry. 286:7732-7736
Because of its unique physical and chemical properties, rat tail tendon collagen has long been favored for crystallographic and biochemical studies of fibril structure. In studies of the distribution of 3-hydroxyproline in type I collagen of rat bone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18fa81333b7454b531b5d72f63531edf
https://doi.org/10.1074/jbc.c110.195768
https://doi.org/10.1074/jbc.c110.195768
Publikováno v:
Journal of Biological Chemistry. 285:18537-18544
The collagen framework of hyaline cartilages, including articular cartilage, consists largely of type II collagen that matures from a cross-linked heteropolymeric fibril template of types II, IX, and XI collagens. In the articular cartilages of adult
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ae7725373bb1a7a5ce60be837f8b680
https://doi.org/10.1074/jbc.m110.112904
https://doi.org/10.1074/jbc.m110.112904
Publikováno v:
European Cells & Materials, Vol 12, Pp 57-63 (2006)
Adult articular cartilage by dry weight is two-thirds collagen. The collagen has a unique molecular phenotype. The nascent type II collagen fibril is a heteropolymer, with collagen IX molecules covalently linked to the surface and collagen XI forming
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7fd0d06602b8bdb37f0a8c80e695a6c1
https://doi.org/10.22203/ecm.v012a07
https://doi.org/10.22203/ecm.v012a07
Autor:
Carlo Bellabarba, Christopher I. Shaffrey, Jiann Jiu Wu, Sohail K. Mirza, Jens R. Chapman, B. Carter, Yoshito Matsui, David R. Eyre
Publikováno v:
The Journal of Bone and Joint Surgery. British volume. :1021-1026
Two collagen type IX gene polymorphisms that introduce a tryptophan residue into the protein’s triple-helical domain have been linked to an increased risk of lumbar disc disease. To determine whether a particular subset of symptomatic lumbar diseas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5cdb248be2245811e080bf0cf0d44b0
https://doi.org/10.1302/0301-620x.86b7.14994
https://doi.org/10.1302/0301-620x.86b7.14994
Autor:
Jiann Jiu Wu, David R. Eyre
Publikováno v:
Journal of Biological Chemistry. 278:24521-24525
Nucleus pulposus, the central zone of the intervertebral disc, is gel-like and has a similar collagen phenotype to that of hyaline cartilage. Amino-terminal protein sequence analysis of the α1(IX)COL3 domain purified from bovine nucleus pulposus gav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::506cf604b20993c35e5950e3e94f43d6
https://doi.org/10.1074/jbc.m302431200
https://doi.org/10.1074/jbc.m302431200
Autor:
Desiree Engel, Gerd R. Kleemann, John R. Yates, David R. Eyre, Jiann-Jiu Wu, Doris Kleemann-Fischer
Publikováno v:
Archives of Biochemistry and Biophysics. 387:209-215
Matrilin-3 is a recently identified matrix protein of cartilage that shows sequence homology to matrilin-1 (cartilage matrix protein or CMP). Here we identify and characterize the molecular properties of matrilin-3 from human growth cartilage by immu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::beeb7db21ceec6e0053e544aaf7f5a25
https://doi.org/10.1006/abbi.2000.2256
https://doi.org/10.1006/abbi.2000.2256
Publikováno v:
Archives of Biochemistry and Biophysics. 378:33-39
Type IX collagen is a quantitatively minor component of hyaline cartilage that is essential for the normal structural integrity of the tissue. Purification and analysis are difficult because the mature protein is insoluble as a cross-linked integral
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76d4bde22ce019394ee4c554aae36038
https://doi.org/10.1006/abbi.2000.1805
https://doi.org/10.1006/abbi.2000.1805
Publikováno v:
Journal of Biological Chemistry. 272:4783-4786
Fibronectin is a highly conserved dimeric glycoprotein found in high concentrations in plasma and widely distributed in low concentrations in the extracellular matrix of tissues. The protein is the product of a single gene, but multiple splicing vari
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e959780fad65ef802fb953ace0dcd51
https://doi.org/10.1074/jbc.272.8.4783
https://doi.org/10.1074/jbc.272.8.4783