Výsledky vyhledávání - "C. A. Saphos"

Orally active inhibitors of stromelysin-1 (MMP-3)

Autor: Charles G. Caldwell, Vernon L. Moore, Richard K. Harrison, Kevin T. Chapman, C. A. Saphos, Philippe L. Durette, Lisa M. Niedzwiecki, Malcolm MacCoss, William K. Hagmann, Julie M. Olszewski, Kelly M. Sperow, Amy J. Christen

Publikováno v: Bioorganic & Medicinal Chemistry Letters. 6:803-806

Further development of N-carboxyalkyl dipeptide inhibitors of stromelysin-1 (MMP-3) led to the discovery of C-carboxyalkyl dipeptide analogs with improved oral bioavailability. An in vivo assay of human MMP-3 mediated degradation of a macromolecular

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bef71cac736912d1ab04e2a2720a41c3
https://doi.org/10.1016/0960-894x(96)00109-6

Zobrazit plný text záznamu

Studies on the quantification of proteoglycans by the dimethylmethylene blue dye-Binding method specificity, quantitation in synovial lavage fluid, and automation

Autor: C. A. Saphos, Vernon L. Moore, Joseph McDonnell, P. Dey

Publikováno v: Connective Tissue Research. 28:317-324

The dimethylmethylene blue (DMMB) dye-binding technique is widely used for the quantification of sulfated glycosaminoglycans (sGAG) and proteoglycans. We conducted further studies on this technique in our laboratory and found that concentrations of D

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf33262d659bcff9fa029f351aa1a257
https://doi.org/10.3109/03008209209016823

Zobrazit plný text záznamu

In vivo activity of human recombinant tissue inhibitor of metalloproteinases (TIMP)

Autor: Michael W. Lark, Lori A. Walakovits, Vernon L. Moore, C. A. Saphos

Publikováno v: Biochemical Pharmacology. 39:2041-2049

Recombinant human tissue inhibitor of metalloproteinase (rhTIMP) suppressed the ability of native human stromelysin to degrade [ 3 H]transferrin in vitro . Maximum inhibition occurred at molar ratios (TIMP : stromelysin) of 2:1 and 1:1. Reduced and a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4c7fbfbd4ebfdf8b45a83cbb7f1bfc32
https://doi.org/10.1016/0006-2952(90)90627-w

Zobrazit plný text záznamu

Inhibition of stromelysin-1 (MMP-3) by P1'-biphenylylethyl carboxyalkyl dipeptides

Publikováno v: Journal of medicinal chemistry. 40(6)

Carboxyalkyl peptides containing a biphenylylethyl group at the P1' position were found to be potent inhibitors of stromelysin-1 (MMP-3) and gelatinase A (MMP-2), in the range of 10-50 nM, but poor inhibitors of collagenase (MMP-1). Combination of a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c225eff03f14dd3bda887be16d0152aa
https://pubmed.ncbi.nlm.nih.gov/9083493

Zobrazit plný text záznamu

Proteoglycan-degrading activity of human stromelysin-1 and leukocyte elastase in rabbit joints. Quantitation of proteoglycan and a stromelysin-induced HABR fragment of aggrecan in synovial fluid and cartilage

Autor: Vernon L. Moore, Kevin T. Chapman, Conrad P. Dorn, Hollis R. Williams, William K. Hagmann, Barbara G. Green, Julie M. Olszewski, C. A. Saphos, Jeffrey J. Hale, Joseph McDonnell, W. B. Knight, Richard A. Mumford

Publikováno v: Connective tissue research. 33(4)

The objective of this study was to compare the specificity and potency of recombinant human SLN-1 (rhSLN) and human leukocyte elastase (HLE) as proteoglycan (PG)-degrading enzymes after intraarticular injection into rabbits. Another objective was to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcb9bb8ae1d9e9d4c7803cb8fcb09914
https://pubmed.ncbi.nlm.nih.gov/8834447

Zobrazit plný text záznamu

Induction of increased levels of proteoglycan fragments in synovial fluid (SF) and increased levels of stromelysin in cartilage, synovium and SF by intraarticular injection of canine monocyte conditioned medium into dogs

Autor: M W, Lark, K A, MacNaul, S, Donatelli, J, McDonnell, L A, Hoerrner, K A, Stevens, C A, Saphos, E K, Bayne, N I, Hutchinson, V L, Moore

Publikováno v: The Journal of rheumatology. 21(9)

To study the effects of the intraarticular injection of canine monocyte conditioned medium (cMCM) into dogs on proteoglycan fragment and stromelysin levels in the joint.cMCM was injected intraarticularly into dogs, and the levels of proteoglycan frag

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e71a1d6afb9804496e6996c1c40c6edf
https://pubmed.ncbi.nlm.nih.gov/7799356

Zobrazit plný text záznamu

Sensitivity of monoclonal antibody, 5-D-4, for the detection of aggrecan, aggrecan fragments, and keratan sulfate

Autor: Michael W. Lark, C. A. Saphos, Vernon L. Moore, P. Dey

Publikováno v: Agents and actions.

Bovine nasal septum aggrecan and selected proteinase-digested products of aggrecan were evaluated in an inhibition ELISA using the anti-keratan sulfate (KS) monoclonal antibody 5-D-4 (5D4). Undegraded aggrecan was recognized with an IC50 of 0.27 micr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4184cd21d391c48c129cb84f63d4bb80
https://pubmed.ncbi.nlm.nih.gov/7506001

Zobrazit plný text záznamu

In vivo activity of human recombinant tissue inhibitor of metalloproteinases (TIMP). Activity against human stromelysin in vitro and in the rat pleural cavity

Autor: M W, Lark, C A, Saphos, L A, Walakovits, V L, Moore

Publikováno v: Biochemical pharmacology. 39(12)

Recombinant human tissue inhibitor of metalloproteinase (rhTIMP) suppressed the ability of native human stromelysin to degrade [3H]transferrin in vitro. Maximum inhibition occurred at molar ratios (TIMP: stromelysin) of 2:1 and 1:1. Reduced and alkyl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4398a1878d8d0d7cc3400a77a36923ec
https://pubmed.ncbi.nlm.nih.gov/2353943

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání