PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10960024-15 2000 These effects appear to occur without altering either mRNA or protein levels for these enzymes, supporting a possible mechanism of action that involves the ability of bisphosphonates to chelate cations from the MMPs. Diphosphonates 167-182 matrix metallopeptidase 1 Homo sapiens 211-215 11984068-1 2002 Bisphosphonates (clodronate, alendronate, pamidronate and zoledronate) at therapeutically attainable non-cytotoxic concentrations inhibited MMP-3, -12, -13 and -20 as well as MMP-1, -2, -8 and -9, but not urokinase-type plasminogen activator (uPA), a serine proteinase and a pro-MMP activator. Diphosphonates 0-15 matrix metallopeptidase 1 Homo sapiens 175-195 11984068-8 2002 Bisphosphonates are broad-spectrum MMP inhibitors and this inhibition involves cation chelation. Diphosphonates 0-15 matrix metallopeptidase 1 Homo sapiens 35-38 10620064-10 1999 In conclusion, the apoptosis of myeloma cells and BMSCs and the inhibition of both IL-6 and MMP-1 production induced by bisphosphonates, mainly zoledronate, could have antitumoral effects in patients with MM. Diphosphonates 120-135 matrix metallopeptidase 1 Homo sapiens 92-97 10415748-4 1999 We have discovered that various matrix metalloproteinases (MMPs) are inhibited in vitro by several bisphosphonates. Diphosphonates 99-114 matrix metallopeptidase 1 Homo sapiens 59-63 9192515-1 1997 Interstitial collagenase present in human jaw cyst extract and purified human fibroblast-type collagenase (MMP-1) were both efficiently inhibited in vitro by clodronate, an osteoactive, antiresorptive bisphosphonate. Diphosphonates 201-215 matrix metallopeptidase 1 Homo sapiens 0-24 9192515-1 1997 Interstitial collagenase present in human jaw cyst extract and purified human fibroblast-type collagenase (MMP-1) were both efficiently inhibited in vitro by clodronate, an osteoactive, antiresorptive bisphosphonate. Diphosphonates 201-215 matrix metallopeptidase 1 Homo sapiens 107-112