Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Karena Last"'
Autor:
Edward R. Bastow, Karena Last, Sue Golub, Jennifer L. Stow, Amanda C. Stanley, Amanda J. Fosang
Publikováno v:
Biology Open, Vol 1, Iss 4, Pp 318-328 (2012)
Summary The abundant proteoglycan, aggrecan, is resorbed from growth plate cartilage during endochondral bone ossification, yet mice with genetically-ablated aggrecan-degrading activity have no defects in bone formation. To account for this apparent
Externí odkaz:
https://doaj.org/article/95c410bda8fb4893ad4e73c80b57a423
Autor:
Fraser Rogerson, Karena Last, Suzanne Golub, Stephanie Gauci, Heather Stanton, Katrina Bell, Amanda Fosang
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 3, p 573 (2019)
International Journal of Molecular Sciences
Volume 20
Issue 3
International Journal of Molecular Sciences
Volume 20
Issue 3
A disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)-4 and ADAMTS-5 are the principal aggrecanases in mice and humans
however, mice lacking the catalytic domain of both enzymes (TS-4/5∆cat) have no skeletal phenotype, sugges
however, mice lacking the catalytic domain of both enzymes (TS-4/5∆cat) have no skeletal phenotype, sugges
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0947e18f9b1020c9f527d6dde818229f
https://www.mdpi.com/1422-0067/20/3/573
https://www.mdpi.com/1422-0067/20/3/573
Autor:
Sophie, Lees, Suzanne B, Golub, Karena, Last, Weiguang, Zeng, David C, Jackson, Philip, Sutton, Amanda J, Fosang
Publikováno v:
Arthritisrheumatology (Hoboken, N.J.). 67(5)
To determine whether an aggrecan 32-mer fragment derived from dual ADAMTS and matrix metalloproteinase (MMP) cleavage in the aggrecan interglobular domain was bioactive and, if so, to elucidate its mechanism of action.Mouse primary chondrocytes, syno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::528730915e6597bbfaada382c4add640
https://pubmed.ncbi.nlm.nih.gov/25707860
https://pubmed.ncbi.nlm.nih.gov/25707860
Publikováno v:
Journal of Biological Chemistry. 275:33038-33045
We have expressed G1-G2 mutants with amino acid changes at the DIPEN(341) downward arrow(342)FFGVG and ITEGE(373) downward arrow(374)ARGSV cleavage sites, in order to investigate the relationship between matrix metalloproteinase (MMP) and aggrecanase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f6599510add7e4ff37e6f98a3fcce769
https://doi.org/10.1074/jbc.275.42.33038
https://doi.org/10.1074/jbc.275.42.33038
Publikováno v:
Arthritis and rheumatism. 62(11)
Objective To compare the regulation of aggrecanase messenger RNA (mRNA) and enzyme activity by proinflammatory cytokines in primary mouse chondrocytes. Methods Primary chondrocytes were isolated from knee epiphyses of 6–8-day-old mice and cultured
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33ff676ba79225be4942fa5bdb5371a2
https://pubmed.ncbi.nlm.nih.gov/20662062
https://pubmed.ncbi.nlm.nih.gov/20662062
Autor:
Amanda J, Fosang, Karena, Last, Heather, Stanton, Suzanne B, Golub, Christopher B, Little, Lorena, Brown, David C, Jackson
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 622
Neoepitope antibodies recognize the newly created N or C terminus of protein degradation products but fail to recognize the same sequence of amino acids present in intact or undigested protein. Aggrecan neoepitope antibodies have been pivotal in stud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::70cdcef5e44a576c3474232cf177f4c3
https://pubmed.ncbi.nlm.nih.gov/20135291
https://pubmed.ncbi.nlm.nih.gov/20135291
Autor:
John A. Hamilton, Daisy Cheung, Enrico L. Filonzi, Diana S. Piccoli, Johann Wojta, Marisa Gallichio, Katherine McGrath, Karena Last
Publikováno v:
Scopus-Elsevier
Objective. To study the plasminogen activator inhibitor(s) (PAI) produced in vitro by human synovial fibroblast-like cells. Methods. Human synovial cell explant cultures were established using cells from nonrheumatoid donors. PAI-2 and PAI-1 antigens
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60dfca413d6ae1978e082f9892a43925
https://doi.org/10.1002/art.1780351217
https://doi.org/10.1002/art.1780351217
Autor:
Amanda J. Fosang, Karena Last, Heather Stanton, Suzanne B. Golub, Christopher B. Little, Lorena Brown, David C. Jackson
Publikováno v:
Methods in Molecular Biology ISBN: 9781603272988
Neoepitope antibodies recognize the newly created N or C terminus of protein degradation products but fail to recognize the same sequence of amino acids present in intact or undigested protein. Aggrecan neoepitope antibodies have been pivotal in stud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::773445943d37a6c45b63e8ea847e23f0
https://doi.org/10.1007/978-1-60327-299-5_19
https://doi.org/10.1007/978-1-60327-299-5_19
Autor:
Christopher J. Poon, Anna H. Plaas, Doug R. Keene, David J. McQuillan, Karena Last, Amanda J. Fosang
Publikováno v:
The Journal of biological chemistry. 280(25)
Keratan sulfate is thought to influence the cleavage of aggrecan by metalloenzymes. We have therefore produced a recombinant substrate, substituted with keratan sulfate, suitable for the study of aggrecanolysis in vitro. Recombinant human G1-G2 was p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::750e723ffcd80005a70a6d745e76344a
https://pubmed.ncbi.nlm.nih.gov/15849197
https://pubmed.ncbi.nlm.nih.gov/15849197
Autor:
Heather Stanton, Fraser M. Rogerson, Charlotte J. East, Suzanne B. Golub, Kate E. Lawlor, Clare T. Meeker, Christopher B. Little, Karena Last, Pamela J. Farmer, Ian K. Campbell, Anne M. Fourie, Amanda J. Fosang
Publikováno v:
Nature. 434(7033)
The degradation of cartilage in arthritic joints is associated with loss of aggrecan, a large aggregating proteoglycan, and for many years researchers have sought the ‘aggrecanase’ responsible. Two groups now report success: the enzyme ADAMTS5 (a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f95a5df33c7ca6c35444816fc97deb1b
https://pubmed.ncbi.nlm.nih.gov/15800625
https://pubmed.ncbi.nlm.nih.gov/15800625