Zobrazeno 1 - 10
of 17
pro vyhledávání: '"J R, Gallimore"'
Autor:
Mark B. Pepys, Winston L. Hutchinson, I. M. Collins, David R. Booth, J. R. Gallimore, Erhard Hohenester
Publikováno v:
Amyloid. 4:274-295
Autor:
G. A. Tennent, J. R. Gallimore, Philip N. Hawkins, Edwin G. Moore, M H van Rijswijk, Julie Wilkins, Mark B. Pepys, Pieter Limburg
Publikováno v:
Clinical Chemistry. 40:1284-1290
Serum amyloid A (SAA), a sensitive acute-phase protein, is the precursor of AA fibrils in reactive amyloidosis. However, SAA is poorly immunogenic, and development and standardization of immunoassays of this protein have been difficult. We establishe
Autor:
G E Noble, S. R. Nelson, Philip N. Hawkins, P Williams, Mark B. Pepys, J. R. Gallimore, T W Rademacher, Jeff Herbert, S. Amatayakul-Chantler, Winston L. Hutchinson
Publikováno v:
Proceedings of the National Academy of Sciences. 91:5602-5606
Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease. We show here that its single N-linked
Autor:
A. F. Bristow, Glenys A. Tennent, Mark B. Pepys, R. E. Gaines-Das, N. Buttress, J. R. Gallimore
Publikováno v:
Clinical Endocrinology. 38:361-366
Summary OBJECTIVE Thyroxine binding globulin is the major thyroid hormone binding and transport protein of the plasma, and its quantitative estimation is therefore of clinical importance. The objectives of the present study were to prepare and ampoul
Autor:
Müjde Soytürk, J. R. Gallimore, Helen J. Lachmann, David R. Booth, Tugba Yavuzsen, A Bybee, SE Booth, Mehmet Tunca, Servet Akar, Philip N. Hawkins, Bulent Sengul
Objective. To prospectively monitor inflammatory activity over a prolonged period in a cohort of Turkish patients with FMF, their healthy relatives and healthy controls and to relate this to their MEFV genotypes.Methods. 43 patients with FMF and 75 o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afa023a103adf8ca471b95fb43b08d0c
https://avesis.deu.edu.tr/publication/details/43c5f2e5-6f0f-40d2-92b2-f6e2b06c489b/oai
https://avesis.deu.edu.tr/publication/details/43c5f2e5-6f0f-40d2-92b2-f6e2b06c489b/oai
Autor:
M, Tunca, S, Akar, M, Soytürk, G, Kirkali, H, Resmi, H, Akhunlar, O, Gönen, J R, Gallimore, P N, Hawkins, E, Tankurt
Publikováno v:
Clinical and experimental rheumatology. 22(4 Suppl 34)
About a quarter of familial Mediterranean fever (FMF) patients are partially or totally resistant to colchicine. A previous observation reported that acute attacks may be shortened by administration of interferon alpha (IFN).We designed a double-blin
Autor:
Ken Ichi Yamamura, Sarah S. Murray, Helen J. Lachmann, Tamas Bartfai, Alexander Alanine, Simon Kolstoe, Winston L. Hutchinson, Alan Purvis, Cornelia Hertel, Roger David Norcross, Torsten Hoffmann, J. A. Kemp, D Thompson, Laurence Lovat, Philip N. Hawkins, Mark B. Pepys, Roland Jakob-Roetne, J. R. Gallimore, Graham W. Taylor, Misao Suzuki, Steve P. Wood, Glenys A. Tennent, Jeff Herbert
Publikováno v:
Nature. 417(6886)
The normal plasma protein serum amyloid P component (SAP) binds to fibrils in all types of amyloid deposits, and contributes to the pathogenesis of amyloidosis. In order to intervene in this process we have developed a drug, R-1-[6-[R-2-carboxy-pyrro
Publikováno v:
Clinical chemistry. 44(6 Pt 1)
Publikováno v:
Journal of molecular biology. 272(3)
Human serum amyloid P component (SAP) is a normal plasma glycoprotein and the precursor of amyloid P component which is a universal constituent of the abnormal tissue deposits in amyloidosis. X-ray and neutron scattering data showed that pentameric o
Autor:
Tim D. Spector, David V. Doyle, D J Hart, J. R. Gallimore, N. Mackillop, D. Nandra, Mark B. Pepys
Publikováno v:
Arthritis and rheumatism. 40(4)
Objective. To examine the role of low-grade inflammation in the etiology and progression of early osteoarthritis (OA) of the knee. Methods. We used a new, high-sensitivity, automated monoclonal antibody immunoassay for the classic acute-phase protein