Year |
Citation |
Score |
2010 |
Gill SE, Kassim SY, Birkland TP, Parks WC. Mouse models of MMP and TIMP function Methods in Molecular Biology (Clifton, N.J.). 622: 31-52. PMID 20135274 DOI: 10.1007/978-1-60327-299-5_2 |
0.564 |
|
2009 |
Vaisar T, Kassim SY, Gomez IG, Green PS, Hargarten S, Gough PJ, Parks WC, Wilson CL, Raines EW, Heinecke JW. MMP-9 sheds the beta2 integrin subunit (CD18) from macrophages. Molecular & Cellular Proteomics : McP. 8: 1044-60. PMID 19116209 DOI: 10.1074/Mcp.M800449-Mcp200 |
0.605 |
|
2007 |
Kassim SY, Gharib SA, Mecham BH, Birkland TP, Parks WC, McGuire JK. Individual matrix metalloproteinases control distinct transcriptional responses in airway epithelial cells infected with Pseudomonas aeruginosa. Infection and Immunity. 75: 5640-50. PMID 17923522 DOI: 10.1128/Iai.00799-07 |
0.479 |
|
2007 |
Vaisar T, Pennathur S, Green PS, Gharib SA, Hoofnagle AN, Cheung MC, Byun J, Vuletic S, Kassim S, Singh P, Chea H, Knopp RH, Brunzell J, Geary R, Chait A, et al. Shotgun proteomics implicates protease inhibition and complement activation in the antiinflammatory properties of HDL. The Journal of Clinical Investigation. 117: 746-56. PMID 17332893 DOI: 10.1172/Jci26206 |
0.519 |
|
2005 |
Kassim SY, Fu X, Liles WC, Shapiro SD, Parks WC, Heinecke JW. NADPH oxidase restrains the matrix metalloproteinase activity of macrophages. The Journal of Biological Chemistry. 280: 30201-5. PMID 15983040 DOI: 10.1074/Jbc.M503292200 |
0.644 |
|
2004 |
Pennathur S, Bergt C, Shao B, Byun J, Kassim SY, Singh P, Green PS, McDonald TO, Brunzell J, Chait A, Oram JF, O'brien K, Geary RL, Heinecke JW. Human atherosclerotic intima and blood of patients with established coronary artery disease contain high density lipoprotein damaged by reactive nitrogen species. The Journal of Biological Chemistry. 279: 42977-83. PMID 15292228 DOI: 10.1074/Jbc.M406762200 |
0.507 |
|
2004 |
Fu X, Kao JL, Bergt C, Kassim SY, Huq NP, d'Avignon A, Parks WC, Mecham RP, Heinecke JW. Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: specific structural motifs control protein oxidation. The Journal of Biological Chemistry. 279: 6209-12. PMID 14670964 DOI: 10.1074/Jbc.C300506200 |
0.641 |
|
2003 |
Fu X, Kassim SY, Parks WC, Heinecke JW. Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation. The Journal of Biological Chemistry. 278: 28403-9. PMID 12759346 DOI: 10.1074/Jbc.M304739200 |
0.661 |
|
2001 |
Fu X, Kassim SY, Parks WC, Heinecke JW. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. The Journal of Biological Chemistry. 276: 41279-87. PMID 11533038 DOI: 10.1074/Jbc.M106958200 |
0.668 |
|
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