Zobrazeno 1 - 10
of 39
pro vyhledávání: '"M. T. BAYLISS"'
Autor:
Sally Roberts, S. Griffin, M. T. Bayliss, Helena Evans, Caroline M. Milner, Anthony J. Day, Stephen M. Eisenstein, Jill P. G. Urban, J. Menage, Marilyn S. Rugg
Publikováno v:
European Spine Journal. 14:36-42
Inflammation and irritation of the nerve roots has been indicated as an important factor in the pain associated with symptomatic disc herniations. Tumour necrosis factor alpha (TNFalpha) is now believed to be involved in this pathway. TNFalpha causes
Autor:
S Y, Ali, M T, Bayliss
Publikováno v:
Annals of the rheumatic diseases. 34
Publikováno v:
Pferdeheilkunde Equine Medicine. 26:588-590
Publikováno v:
Journal of Anatomy. 190:623-627
Publikováno v:
Arthritis & Rheumatism. 40:562-569
Objective. To evaluate the anabolic activity of osteoarthritic chondrocytes in situ by investigating the messenger RNA (mRNA) expression of 3 major cartilage components, type II collagen, aggrecan, and link protein. Methods. In situ hybridization exp
Publikováno v:
Biochemical Journal. 302:49-56
Recent studies have shown that mesangial cells derived from human adult glomeruli synthesize a number of 35S-labelled proteoglycans including a large chondroitin sulphate proteoglycan (CSPG), two dermatan sulphate proteoglycans (biglycan and decorin)
Publikováno v:
Arthritis and rheumatism. 44(8)
To investigate the differences between chondrocytes of the superficial and underlying zones of articular cartilage at the level of gene expression.Messenger RNA (mRNA) was isolated from chondrocytes harvested from the superficial and deep zones of im
Publikováno v:
Arthritis and rheumatism. 44(6)
To map aggrecan cleavage by matrix metalloproteinases (MMPs) and aggrecanases in normal murine tibial articular cartilage (CBA strain) and in the development of spontaneous osteoarthritis (OA) in the STR/ort mouse and to assess the influence of sex h
Publikováno v:
The Journal of biological chemistry. 276(15)
Asporin, a novel member of the leucine-rich repeat family of proteins, was partially purified from human articular cartilage and meniscus. Cloning of human and mouse asporin cDNAs revealed that the protein is closely related to decorin and biglycan.
Autor:
N, Verzijl, J, DeGroot, E, Oldehinkel, R A, Bank, S R, Thorpe, J W, Baynes, M T, Bayliss, J W, Bijlsma, F P, Lafeber, J M, Tekoppele
Publikováno v:
The Biochemical journal.
Non-enzymic modification of tissue proteins by reducing sugars, the so-called Maillard reaction, is a prominent feature of aging. In articular cartilage, relatively high levels of the advanced glycation end product (AGE) pentosidine accumulate with a