Zobrazeno 1 - 10
of 166
pro vyhledávání: '"John S Mort"'
Autor:
Peter J Roughley, John S Mort
Publikováno v:
Journal of Experimental Orthopaedics, Vol 1, Iss 1, Pp n/a-n/a (2014)
Abstract Aggrecan is a large proteoglycan bearing numerous chondroitin sulfate and keratan sulfate chains that endow articular cartilage with its ability to withstand compressive loads. It is present in the extracellular matrix in the form of proteog
Externí odkaz:
https://doaj.org/article/4074f6aa7b024f39a85be7a2e4f491ee
Publikováno v:
Frontiers in Physics, Vol 5 (2017)
Collagens form the fibrous component of the extracellular matrix in all multi-cellular animals. Collagen type I is the most abundant collagen present in skin, tendons, vasculature, as well as the organic portion of the calcified tissue of bone and te
Externí odkaz:
https://doaj.org/article/03334fee3f6a4d8abf2f56603ab8f0b3
Autor:
Iris Boraschi-Diaz, Dieter Brömme, Yotis A. Senis, Svetlana V. Komarova, Alexandra Mazharian, John S. Mort
Publikováno v:
Bone. 117
The major organic component of bone is collagen type I. Osteoclasts are terminally differentiated multinucleated cells of hematopoietic origin that are essential for physiological development of bone and teeth. We examined if osteoclast differentiati
Publikováno v:
Arthritis & Rheumatology. 67:2691-2701
Objective Transforming growth factor α (TGFα) is increased in osteoarthritic (OA) cartilage in rats and humans and modifies chondrocyte phenotype. CCL2 is increased in OA cartilage and stimulates proteoglycan loss. This study was undertaken to test
Autor:
Matthew R. McCann, Kim L. Beaucage, M.A. Pest, Meg P. Kamphuis, Frank Beier, A. Ratneswaran, Cheryle A. Séguin, Gurkeet Lalli, Garth B. Backler, Jimin Lee, Ziana Esmail, David W. Holdsworth, John S. Mort, Priya Patel, Michael Barbalinardo, S. Jeffrey Dixon
Publikováno v:
Arthritis & Rheumatology. 67:2164-2175
Objective High-frequency, low-amplitude whole-body vibration (WBV) is being used to treat a range of musculoskeletal disorders; however, there is surprisingly limited knowledge regarding its effect(s) on joint tissues. This study was undertaken to ex
Publikováno v:
Frontiers in Physics, Vol 5 (2017)
Collagens form the fibrous component of the extracellular matrix in all multi-cellular animals. Collagen type I is the most abundant collagen present in skin, tendons, vasculature, as well as the organic portion of the calcified tissue of bone and te
Publikováno v:
Osteoarthritis and cartilage. 25(12)
Develop a species-specific ELISA for a neo-epitope generated by cathepsin K cleavage of equine type II collagen to: (1) measure cartilage type II collagen degradation by cathepsin K in vitro, (2) identify cytokines that upregulate cathepsin K express
Autor:
Somayyeh Fahiminiya, Francis H. Glorieux, John S. Mort, Jacek Majewski, Frank Rauch, Pierre Moffatt, Klaus Klaushofer, Hadil Al-Jallad, Paul Roschger
Publikováno v:
Journal of Bone and Mineral Research. 29:1805-1814
Mutations in PLS3 have been identified as a cause of bone fragility in children, but the bone phenotype associated with PLS3 mutations has not been reported in detail. PLS3 is located on the X chromosome and encodes the actin-binding protein plastin
Publikováno v:
BBA Clinical
Background The chitinase-like protein, Chi3L1, is associated with increased fibrotic activity as well as inflammatory processes. The capacity of skin cells from systemic sclerosis (SSc) patients to produce Chi3L1, and the stimulation of its synthesis
Autor:
John S. Mort, Alexander Emmott
Publikováno v:
Protein Expression and Purification. 91:37-41
The proteolysis of collagen fibrils by cathepsin K is a hallmark of bone catabolism and tissue degeneration. The production of active recombinant cathepsin K is central for our ability to study the mechanisms by which these processes occur. Here we r