Zobrazeno 1 - 6
of 6
pro vyhledávání: '"K. L. Duffin"'
Publikováno v:
The Journal of Immunology. 155:5655-5662
Naturally processed peptides from immunoaffinity-purified HLA-DRB1*0401, -DRB1*0404 (rheumatoid arthritis (RA)-associated), and -DRB1*0402 (non-RA-associated) molecules were analyzed by capillary liquid chromatography and mass spectrometry. The molec
Autor:
M V Toth, Arthur J. Wittwer, R.C. Wiegand, Christine E. Smith, L S Carr, K L Duffin, M L Bryant, Barry C. Holwerda
Publikováno v:
Journal of Biological Chemistry. 269:25911-25915
The human cytomegalovirus UL80 protease was expressed in Escherichia coli and purified by metal-chelate chromatography using a histidine tag engineered at the amino terminus. Cleavage of the 30-kDa protease at an internal site, VEA/A144, resulted in
Autor:
T. Kita, C. E. Smith, K. F. Fok, K. L. Duffin, W. M. Moore, P. J. Karabatsos, J. F. Kachur, F. K. Hamra, N. V. Pidhorodeckyj, L. R. Forte, al. et
Publikováno v:
American Journal of Physiology-Renal Physiology. 266:F342-F348
Guanylin, a peptide homologue of the bacterial heat-stable enterotoxins (ST), is an endogenous activator of guanylate cyclase C (GC-C). We have initiated a search for other members of the guanylin peptide family and in the current study describe a "g
Publikováno v:
Inflammation. 21(2)
Gout is an acute rheumatic disorder that occurs in connection with the deposition of monosodium urate (MSU) crystals in the joints. This disease is characterized by intermittent episodes of severe pain and inflammatory joint swelling which are seemin
Autor:
D A, Kirschmann, K L, Duffin, C E, Smith, J K, Welply, S C, Howard, B D, Schwartz, S L, Woulfe
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 155(12)
Naturally processed peptides from immunoaffinity-purified HLA-DRB1*0401, -DRB1*0404 (rheumatoid arthritis (RA)-associated), and -DRB1*0402 (non-RA-associated) molecules were analyzed by capillary liquid chromatography and mass spectrometry. The molec
Publikováno v:
The Journal of biological chemistry. 270(19)
Insulin-like growth factor binding protein 4 (IGFBP-4) is a 24-kDa protein that binds insulin-like growth factor 1 (IGF-1) and IGF-2 with high affinity and inhibits IGF action in vitro. We recently described a protease produced by the B104 neuronal c