PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25564338-7 2015 Both MMP-2 and MMP-9 required divalent ions Ca and Zn for its activity and MMP-9 was more active at higher Ca/Zn ratio. Zinc 51-53 matrix metallopeptidase 2 Homo sapiens 5-10 34162214-6 2021 MFRMs redistribute zinc from neurotoxic amyloid beta zinc (Abeta:Zn) complexes to the cytoplasm facilitating the degradation of Abeta plaques by MMP-2. Zinc 65-67 matrix metallopeptidase 2 Homo sapiens 145-150 35574354-11 2022 Molecular docking studies showed that Zn2+ and the His201, His205, His211, Glu202, and Ala165 residues of MMP2 contributed to its high affinity for GA-Me. Zinc 38-42 matrix metallopeptidase 2 Homo sapiens 106-110 31860849-14 2019 CONCLUSION: Conclusions: Taking into account the fact that MMPs belong to Zn- and Ca-dependent proteolytic enzymes, it can be assumed that microelementosis and changes in the level of MMP-2 found in women are interrelated, they are complex and contribute to the creation of favorable conditions for the risk of development of PIs and other complications of the fetus. Zinc 74-76 matrix metallopeptidase 2 Homo sapiens 59-63 31860849-14 2019 CONCLUSION: Conclusions: Taking into account the fact that MMPs belong to Zn- and Ca-dependent proteolytic enzymes, it can be assumed that microelementosis and changes in the level of MMP-2 found in women are interrelated, they are complex and contribute to the creation of favorable conditions for the risk of development of PIs and other complications of the fetus. Zinc 74-76 matrix metallopeptidase 2 Homo sapiens 184-189 28190830-0 2017 Forster Resonance Energy Transfer Mediated Photoluminescence Quenching in Stoichiometrically Assembled CdSe/ZnS Quantum Dot-Peptide Labeled Black Hole Quencher Conjugates for Matrix Metalloproteinase-2 Sensing. Zinc 108-111 matrix metallopeptidase 2 Homo sapiens 175-201 31461891-0 2019 Conformation and Domain Movement Analysis of Human Matrix Metalloproteinase-2: Role of Associated Zn2+ and Ca2+ Ions. Zinc 98-102 matrix metallopeptidase 2 Homo sapiens 51-77 25564338-7 2015 Both MMP-2 and MMP-9 required divalent ions Ca and Zn for its activity and MMP-9 was more active at higher Ca/Zn ratio. Zinc 110-112 matrix metallopeptidase 2 Homo sapiens 5-10 24333596-8 2014 ZnT2-mediated lysosomal Zn sequestration was associated with reduced matrix metalloproteinase 2 (MMP-2) activity and decreased invasion. Zinc 0-2 matrix metallopeptidase 2 Homo sapiens 69-95 25227315-6 2015 MFAO effects on Abeta:Zn complex formation were evaluated with Zinquin staining and the ability of the Abeta:Zn complex to be degraded by matrix metalloproteinase-2 (MMP-2). Zinc 109-111 matrix metallopeptidase 2 Homo sapiens 138-164 25227315-11 2015 MFAOs also removed zinc from the Abeta:Zn complex so that Abeta plaque could be degraded by MMP-2. Zinc 39-41 matrix metallopeptidase 2 Homo sapiens 92-97 24758941-7 2014 Toward MMP-2, Gd@C82(OH)22 could block either the Zn(2+)-catalylitic site directly or the S1" loop indirectly. Zinc 50-56 matrix metallopeptidase 2 Homo sapiens 7-12 24333596-8 2014 ZnT2-mediated lysosomal Zn sequestration was associated with reduced matrix metalloproteinase 2 (MMP-2) activity and decreased invasion. Zinc 0-2 matrix metallopeptidase 2 Homo sapiens 97-102 24701473-3 2014 Matrix metalloproteinases (MMPs), a class of Zn containing enzymes, are involved in the erosion of the fibrous cap and rupture of the plaque which leads to AMI. Zinc 45-47 matrix metallopeptidase 2 Homo sapiens 27-31 14727091-6 2004 The Zn(2+)-chelating activity of these siderophores correlated with the inhibition of MMP-2 activity. Zinc 4-10 matrix metallopeptidase 2 Homo sapiens 86-91 21934214-4 2011 Matrix metalloproteinases (MMPs) are the members of the family of zinc (Zn)- and calcium-dependent endopeptidases that degrade the extracellular matrix. Zinc 72-74 matrix metallopeptidase 2 Homo sapiens 27-31 19542470-9 2009 By chelating Zn(2+), S100A12 significantly inhibited MMP-2, MMP-9, and MMP-3, and the Zn(2+)-induced S100A12 complex colocalized with these in foam cells in human atheroma. Zinc 13-15 matrix metallopeptidase 2 Homo sapiens 53-58 19542470-9 2009 By chelating Zn(2+), S100A12 significantly inhibited MMP-2, MMP-9, and MMP-3, and the Zn(2+)-induced S100A12 complex colocalized with these in foam cells in human atheroma. Zinc 86-88 matrix metallopeptidase 2 Homo sapiens 53-58 24489995-2 2014 Matrix metalloproteinases (MMPs) comprise a family of over two dozen Zn-dependent endopeptidases thought to be primary effectors of extracellular tissue renewal and remodeling processes. Zinc 69-71 matrix metallopeptidase 2 Homo sapiens 27-31 23755195-8 2013 However, application of the Zn(II) complexes noticeably changed the pro-MMP-2/MMP-2 ratio towards a higher amount of maturated MMP-2, when they induced a 4-times higher production of maturated MMP-2 in comparison with the vehicle-treated cells under LPS stimulation. Zinc 28-34 matrix metallopeptidase 2 Homo sapiens 72-77 23755195-8 2013 However, application of the Zn(II) complexes noticeably changed the pro-MMP-2/MMP-2 ratio towards a higher amount of maturated MMP-2, when they induced a 4-times higher production of maturated MMP-2 in comparison with the vehicle-treated cells under LPS stimulation. Zinc 28-34 matrix metallopeptidase 2 Homo sapiens 78-83 23755195-8 2013 However, application of the Zn(II) complexes noticeably changed the pro-MMP-2/MMP-2 ratio towards a higher amount of maturated MMP-2, when they induced a 4-times higher production of maturated MMP-2 in comparison with the vehicle-treated cells under LPS stimulation. Zinc 28-34 matrix metallopeptidase 2 Homo sapiens 78-83 23755195-8 2013 However, application of the Zn(II) complexes noticeably changed the pro-MMP-2/MMP-2 ratio towards a higher amount of maturated MMP-2, when they induced a 4-times higher production of maturated MMP-2 in comparison with the vehicle-treated cells under LPS stimulation. Zinc 28-34 matrix metallopeptidase 2 Homo sapiens 78-83 22411188-2 2012 Adapting findings from the literature of Zn(II) ion sensors, we previously reported chelating sulfonamide inhibitors of MMP-2, some of which showed excellent selectivity over other gelatinases (MMP-9). Zinc 41-47 matrix metallopeptidase 2 Homo sapiens 120-125 20356629-10 2010 Cd(II) and Zn(II) complexes and cisplatin increased MMP-2 activity in supernatants of tested cells, while Ni(II) complex with the same ligand decreased the activity, implying a possible activity in preventing tumor invasion and metastasis processes. Zinc 11-17 matrix metallopeptidase 2 Homo sapiens 52-57 17901898-8 2007 While addition of Fe2+ did not reverse inhibition, the addition of Zn2+ resulted in a recovery of MMP-2 activity, and furthermore, zinc-saturated LTF did not inhibit MMP-2. Zinc 67-71 matrix metallopeptidase 2 Homo sapiens 98-103 15841324-2 2005 The matrix metalloproteinases (MMPs) are a family of Zn(++) and Ca(++) dependent endopeptidases, which are key mediators of ECM remodelling. Zinc 53-59 matrix metallopeptidase 2 Homo sapiens 31-35 15781326-2 2005 The majority of MMP-2 inhibitor candidate drugs block the active site of MMP-2 by binding to its catalytic Zn2+ ion through a chelating (hydroxamate, sulphonate etc.) Zinc 107-111 matrix metallopeptidase 2 Homo sapiens 16-21 15781326-2 2005 The majority of MMP-2 inhibitor candidate drugs block the active site of MMP-2 by binding to its catalytic Zn2+ ion through a chelating (hydroxamate, sulphonate etc.) Zinc 107-111 matrix metallopeptidase 2 Homo sapiens 73-78 14727091-7 2004 Therefore, it is considered that siderophores such as pyoverdines inhibit MMP-2 activity by chelating Zn(2+) on the active site of MMP-2. Zinc 102-108 matrix metallopeptidase 2 Homo sapiens 74-79 14727091-7 2004 Therefore, it is considered that siderophores such as pyoverdines inhibit MMP-2 activity by chelating Zn(2+) on the active site of MMP-2. Zinc 102-108 matrix metallopeptidase 2 Homo sapiens 131-136 11203530-3 2000 The aim of this work was to test the effect of Zn, Cu, Sn and Hg ions on the activity of the major gingival gelatinolytic MMPs. Zinc 47-49 matrix metallopeptidase 2 Homo sapiens 122-126 15036267-4 2004 We propose second generation selective MMPs, directed toward gelatinase A (MMP-2), based on a non-hydroxamate Zn-ligand grafted on the galardin (ilomastat) skeleton. Zinc 110-112 matrix metallopeptidase 2 Homo sapiens 39-43 15036267-4 2004 We propose second generation selective MMPs, directed toward gelatinase A (MMP-2), based on a non-hydroxamate Zn-ligand grafted on the galardin (ilomastat) skeleton. Zinc 110-112 matrix metallopeptidase 2 Homo sapiens 75-80 15832497-2 2004 Matrix metalloproteinases-2 and -9 (MMP-2 and -9, respectively) are cell-surface Zn-dependent endoproteases associated with diverse processes throughout tumor formation and progression. Zinc 81-83 matrix metallopeptidase 2 Homo sapiens 0-34 15832497-2 2004 Matrix metalloproteinases-2 and -9 (MMP-2 and -9, respectively) are cell-surface Zn-dependent endoproteases associated with diverse processes throughout tumor formation and progression. Zinc 81-83 matrix metallopeptidase 2 Homo sapiens 36-48 10574817-9 1999 Although the in vitro activity of MMP-2 was inhibited by both Cu(2+) and Zn(2+), Cu(2+) apparently induced the keratocytes to produce activated enzyme and Zn(2+) irreversibly inhibited their production of MMP-2. Zinc 73-75 matrix metallopeptidase 2 Homo sapiens 34-39 10574817-9 1999 Although the in vitro activity of MMP-2 was inhibited by both Cu(2+) and Zn(2+), Cu(2+) apparently induced the keratocytes to produce activated enzyme and Zn(2+) irreversibly inhibited their production of MMP-2. Zinc 155-157 matrix metallopeptidase 2 Homo sapiens 34-39 10574817-12 1999 Zn(2+) on the other hand inhibited both MMP-2 production and MMP-2 activity and may, therefore, be of therapeutic value if suitably formulated and used in conjunction with systemic steroid treatment. Zinc 0-2 matrix metallopeptidase 2 Homo sapiens 40-45 10574817-12 1999 Zn(2+) on the other hand inhibited both MMP-2 production and MMP-2 activity and may, therefore, be of therapeutic value if suitably formulated and used in conjunction with systemic steroid treatment. Zinc 0-2 matrix metallopeptidase 2 Homo sapiens 61-66 10551873-1 1999 Membrane type (MT) matrix metalloproteinases (MMPs) are recently recognized members of the family of Zn(2+)- and Ca(2+)-dependent MMPs. Zinc 101-107 matrix metallopeptidase 2 Homo sapiens 46-50 10551873-1 1999 Membrane type (MT) matrix metalloproteinases (MMPs) are recently recognized members of the family of Zn(2+)- and Ca(2+)-dependent MMPs. Zinc 101-107 matrix metallopeptidase 2 Homo sapiens 130-134 10551873-9 1999 MT4-MMP is, therefore, a competent Zn(2+)-dependent MMP with unique specificity among synthetic substrates and the capability to both degrade gelatin and activate progelatinase A. Zinc 35-37 matrix metallopeptidase 2 Homo sapiens 163-178