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New strategies for targeting matrix metalloproteinases.
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Targeting HPX with a small inhibitor can selectively inhibit MT1-MMP activity and suppress cancer cell growth.
“Targeting HPX with a small inhibitor can selectively inhibit MT1-MMP activity and suppress cancer cell growth (58).”
From Identification of amino acid residues in the MT-loop of MT1-MMP critical for its ability to cleave low-density lipoprotein receptor (2022) · cites this paper as [58]
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Cites
Strategies for MMP inhibition in cancer: innovations for the post-trial era
Overall, C. M., & López-Otín, C. (2002) · Nature Reviews Cancer · doi:10.1038/nrc884 · Cited by 1,349
Matrix metalloproteinases and their multiple roles in neurodegenerative diseases
Rosenberg, G. A. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70016-x · Cited by 594
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Research works printed but not linked: 67
- Hu, 2007, Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases, Nat Rev Drug Discov, 6, 480, 10.1038/nrd2308 · DOI
- Rivera, 2010, Metzincin proteases and their inhibitors: foes or friends in nervous system physiology?, J Neurosci, 30, 15337, 10.1523/JNEUROSCI.3467-10.2010 · DOI · Paper page
- Troeberg, 2012, Proteases involved in cartilage matrix degradation in osteoarthritis, Biochim Biophys Acta, 1824, 133, 10.1016/j.bbapap.2011.06.020 · DOI
- Sbardella, 2012, Human matrix metalloproteinases: an ubiquitarian class of enzymes involved in several pathological processes, Mol Aspects Med, 33, 119, 10.1016/j.mam.2011.10.015 · DOI
- Newby, 2012, Matrix metalloproteinase inhibition therapy for vascular diseases, Vascul Pharmacol, 56, 232, 10.1016/j.vph.2012.01.007 · DOI
- Lindsey, 2012, Temporal and spatial expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases following myocardial infarction, Cardiovasc Ther, 30, 31, 10.1111/j.1755-5922.2010.00207.x · DOI
- Whittaker, 1999, Design and therapeutic application of matrix metalloproteinase inhibitors, Chem Rev, 99, 2735, 10.1021/cr9804543 · DOI
- Jacobsen, 2010, To bind zinc or not to bind zinc: an examination of innovative approaches to improved metalloproteinase inhibition, Biochim Biophys Acta, 1803, 72, 10.1016/j.bbamcr.2009.08.006 · DOI
- Saghatelian, 2004, Activity-based probes for the proteomic profiling of metalloproteases, Proc Natl Acad Sci U S A, 101, 10000, 10.1073/pnas.0402784101 · DOI
- Peterson, 2006, The importance of estimating the therapeutic index in the development of matrix metalloproteinase inhibitors, Cardiovasc Res, 69, 677, 10.1016/j.cardiores.2005.11.032 · DOI
- Becker, 2010, Orally active MMP-1 sparing α-tetrahydropyranyl and α-piperidinyl sulfone matrix metalloproteinase (MMP) inhibitors with efficacy in cancer, arthritis, and cardiovascular disease, J Med Chem, 53, 6653, 10.1021/jm100669j · DOI
- Devy, 2011, New strategies for the next generation of matrix-metalloproteinase inhibitors: selectively targeting membrane-anchored MMPs with therapeutic antibodies, Biochem Res Int, 2011, 191670, 10.1155/2011/191670 · DOI
- Baragi, 2009, A new class of potent matrix metalloproteinase 13 inhibitors for potential treatment of osteoarthritis: evidence of histologic and clinical efficacy without musculoskeletal toxicity in rat models, Arthritis Rheum, 60, 2008, 10.1002/art.24629 · DOI
- Lauer-Fields, 2007, Triple-helical transition-state analogs: a new class of selective matrix metalloproteinase inhibitors, J Am Chem Soc, 129, 10408, 10.1021/ja0715849 · DOI
- Morrison, 2009, Matrix metalloproteinase proteomics: substrates, targets, and therapy, Curr Opin Cell Biol, 21, 645, 10.1016/j.ceb.2009.06.006 · DOI
- Sela-Passwell, 2011, New opportunities in drug design of metalloproteinase inhibitors: combination between structure–function experimental approaches and systems biology, Expert Opin Drug Discovery, 6, 527, 10.1517/17460441.2011.560936 · DOI
- Sela-Passwell, 2010, Structural and functional bases for allosteric control of MMP activities: can it pave the path for selective inhibition?, Biochim Biophys Acta, 1803, 29, 10.1016/j.bbamcr.2009.04.010 · DOI
- Udi, 2013, Unraveling hidden regulatory sites in structurally homologous metalloproteases, J Mol Biol, 425, 2330, 10.1016/j.jmb.2013.04.009 · DOI
- Ndinguri, 2012, Peptide-based selective inhibitors of matrix metalloproteinase-mediated activities, Molecules, 17, 14230, 10.3390/molecules171214230 · DOI
- Engel, 2005, Structural basis for the highly selective inhibition of MMP-13, Chem Biol, 12, 181, 10.1016/j.chembiol.2004.11.014 · DOI
- Gooljarsingh, 2008, Characterization of an exosite binding inhibitor of matrix metalloprotease 13, Protein Sci, 17, 66, 10.1110/ps.073130208 · DOI
- Johnson, 2007, Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects, J Biol Chem, 282, 27781, 10.1074/jbc.M703286200 · DOI
- Li, 2008, Quinazolinones and pyrido[3,4-d]pyrimidin-4-ones as orally active and specific matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis, J Med Chem, 51, 835, 10.1021/jm701274v · DOI
- Settle, 2010, Arthritis Rheum, 62, 3006, 10.1002/art.27596 · DOI
- Jüngel, 2010, Effect of the oral application of a highly selective MMP-13 inhibitor in three different animal models of rheumatoid arthritis, Ann Rheum Dis, 69, 898, 10.1136/ard.2008.106021 · DOI
- Piecha, 2010, Novel selective MMP-13 inhibitors reduce collagen degradation in bovine articular and human osteoarthritis cartilage explants, Inflamm Res, 59, 379, 10.1007/s00011-009-0112-9 · DOI
- Gege, 2012, Discovery and evaluation of a non-Zn chelating, selective matrix metalloproteinase 13 (MMP-13) inhibitor for potential intra-articular treatment of osteoarthritis, J Med Chem, 55, 709, 10.1021/jm201152u · DOI
- Chen, 2000, Structure-based design of a novel, potent, and selective inhibitor for MMP-13 utilizing NMR spectroscopy and computer-aided molecular design, J Am Chem Soc, 122, 9648, 10.1021/ja001547g · DOI
- Blagg, 2005, Potent pyrimidinetrione-based inhibitors of MMP-13 with enhanced selectivity over MMP-14, Bioorg Med Chem Lett, 15, 1807, 10.1016/j.bmcl.2005.02.038 · DOI
- Reiter, 2006, Potent, selective pyrimidinetrione-based inhibitors of MMP-13, Bioorg Med Chem Lett, 16, 5822, 10.1016/j.bmcl.2006.08.066 · DOI
- Shah, 2012, An MMP13-selective inhibitor delays primary tumor growth and the onset of tumor-associated osteolytic lesions in experimental models of breast cancer, PLoS One, 7, e29615, 10.1371/journal.pone.0029615 · DOI
- Heim-Riether, 2009, Improving potency and selectivity of a new class of non-Zn-chelating MMP-13 inhibitors, Bioorg Med Chem Lett, 19, 5321, 10.1016/j.bmcl.2009.07.151 · DOI
- Gao, 2010, SAR studies of non-zinc-chelating MMP-13 inhibitors: improving selectivity and metabolic stability, Bioorg Med Chem Lett, 20, 5039, 10.1016/j.bmcl.2010.07.036 · DOI
- Spicer, 2014, Characterization of selective exosite-binding inhibitors of matrix metalloproteinase 13 that prevent articular cartilage degradation in vitro, J Med Chem, 57, 9598, 10.1021/jm501284e · DOI
- Lauer-Fields, 2009, High throughput screening of potentially selective MMP-13 exosite inhibitors utilizing a triple-helical FRET substrate, Bioorg Med Chem, 17, 990, 10.1016/j.bmc.2008.03.004 · DOI
- Roth, 2011, Identification of novel, exosite-binding matrix metalloproteinase-13 inhibitor scaffolds, Bioorg Med Chem Lett, 21, 7180, 10.1016/j.bmcl.2011.09.077 · DOI
- Nara, 2014, Thieno[2,3-d]pyrimidine-2-carboxamides bearing a carboxybenzene group at 5-position: highly potent, selective, and orally available MMP-13 inhibitors interacting with the S1″ binding site, Bioorg Med Chem, 22, 5487, 10.1016/j.bmc.2014.07.025 · DOI
- Fischer, 2013, Strategic targeting of multiple water-mediated interactions: a concise and rational structure-based design approach to potent and selective MMP-13 inhibitors, ChemMedChem, 8, 1457, 10.1002/cmdc.201300278 · DOI
- Woskowicz, 2013, MT-LOOP-dependent localization of membrane type I matrix metalloproteinase (MT1-MMP) to the cell adhesion complexes promotes cancer cell invasion, J Biol Chem, 288, 35126, 10.1074/jbc.M113.496067 · DOI
- Ingvarsen, 2013, Targeting a single function of the multifunctional matrix metalloproteinase MT1-MMP: impact on lymphangiogenesis, J Biol Chem, 288, 10195, 10.1074/jbc.M112.447169 · DOI
- Shiryaev, 2013, A monoclonal antibody interferes with TIMP-2 binding and incapacitates the MMP-2-activating function of multifunctional, pro-tumorigenic MMP-14/MT1-MMP, Oncog, 2, e80, 10.1038/oncsis.2013.44 · DOI · Paper page
- Zhu, 2011, High-affinity peptide against MT1-MMP for in vivo tumor imaging, J Control Release, 150, 248, 10.1016/j.jconrel.2011.01.032 · DOI
- Remacle, 2012, Novel MT1-MMP small-molecule inhibitors based on insights into hemopexin domain function in tumor growth, Cancer Res, 72, 2339, 10.1158/0008-5472.CAN-11-4149 · DOI
- Xu, 2007, Inhibition of MMP-2 gelatinolysis by targeting exodomain–substrate interactions, Biochem J, 406, 147, 10.1042/BJ20070591 · DOI
- Lauer-Fields, 2008, Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition, J Biol Chem, 283, 20087, 10.1074/jbc.M801438200 · DOI
- Gall, 2001, Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state, J Mol Biol, 307, 577, 10.1006/jmbi.2001.4493 · DOI
- Babine, 1997, Molecular recognition of protein–ligand complexes: applications to drug design, Chem Rev, 97, 1359, 10.1021/cr960370z · DOI
- Lauer-Fields, 2009, Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity, J Biol Chem, 284, 24017, 10.1074/jbc.M109.016873 · DOI
- Bertini, 2012, Structural basis for matrix metalloproteinase 1 catalyzed collagenolysis, J Am Chem Soc, 134, 2100, 10.1021/ja208338j · DOI
- Manka, 2012, Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1, Proc Natl Acad Sci U S A, 109, 12461, 10.1073/pnas.1204991109 · DOI
- Lauer-Fields, 2002, Matrix metalloproteinases and collagen catabolism, Biopolymers (Pept. Sci), 66, 19, 10.1002/bip.10201 · DOI
- Fan, 2008, Production of multivalent protein binders using a self-trimerizing collagen-like peptide scaffold, FASEB J, 22, 3795, 10.1096/fj.08-111484 · DOI
- Ndinguri, 2012, Application of collagen-model triple-helical peptide-amphiphiles for CD44 targeted drug delivery systems, J Drug Deliv, 2012, 592602, 10.1155/2012/592602 · DOI
- Yasui, 2013, Potential of collagen-like triple helical peptides as drug carriers: their in vivo distribution, metabolism, and excretion profiles in rodents, Biopolymers (Pept Sci), 100, 705, 10.1002/bip.22234 · DOI
- Bhowmick, 2011, Efficient synthesis of fmoc-protected phosphinic pseudodipeptides: building blocks for the synthesis of matrix metalloproteinase inhibitors (MMPIs), Biopolymers (Pept Sci), 96, 1, 10.1002/bip.21425 · DOI
- Bhowmick, 2012, Synthesis of Fmoc-Gly-Ile phosphinic pseudodipeptide: residue specific conditions for construction of matrix metalloproteinase inhibitor building blocks, Int J Peptide Res & Ther, 18, 335, 10.1007/s10989-012-9307-y · DOI
- de Castro Brás, 2014, Citrate synthase is a novel in vivo matrix metalloproteinase-9 substrate that regulates mitochondrial function in the post-myocardial infarction left ventricle, Antioxid Redox Signal, 21, 1974, 10.1089/ars.2013.5411 · DOI
- Uttamchandani, 2007, Inhibitor fingerprinting of matrix metalloproteases using a combinatorial peptide hydroxamate library, J Am Chem Soc, 129, 7848, 10.1021/ja070870h · DOI
- Minond, 2007, Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences, Biochemistry, 46, 3724, 10.1021/bi062199j · DOI
- Paemen, 1995, Monoclonal antibodies specific for natural human neutrophil gelatinase B used for affinity purification, quantitation by two-site ELISA and inhibition of enzymatic activity, Eur J Biochem, 234, 759, 10.1111/j.1432-1033.1995.759_a.x · DOI
- Martens, 2007, A monoclonal antibody inhibits gelatinase B/MMP-9 by selective binding to part of the catalytic domain and not to the fibronectin or zinc binding domains, Biochim Biophys Acta, 1770, 178, 10.1016/j.bbagen.2006.10.012 · DOI
- Hu, 2004, Inhibitors of gelatinase B/matrix metalloproteinase-9 activity comparison of a peptidomimetic and polyhistidine with single-chain derivatives of a neutralizing monoclonal antibody, Biochem Pharmacol, 67, 1001, 10.1016/j.bcp.2003.10.030 · DOI
- Pruijt, 1999, Prevention of interleukin-8-induced mobilization of hematopoietic progenitor cells in rhesus monkeys by inhibitory antibodies against the metalloproteinase gelatinase B (MMP-9), Proc Natl Acad Sci U S A, 96, 10863, 10.1073/pnas.96.19.10863 · DOI
- Devy, 2009, Selective inhibition of matrix metalloproteinase-14 blocks tumor growth, invasion, and angiogenesis, Cancer Res, 69, 1517, 10.1158/0008-5472.CAN-08-3255 · DOI
- Zucker, 2009, Selective matrix metalloproteinase (MMP) inhibitors in cancer therapy: ready for prime time?, Cancer Biol Ther, 8, 1, 10.4161/cbt.8.24.10353 · DOI
- Sela-Passwell, 2011, Antibodies targeting the catalytic zinc complex of activated matrix metalloproteinases show therapeutic potential, Nat Med, 18, 143, 10.1038/nm.2582 · DOI
- Fields, 2014, Biophysical studies of matrix metalloproteinase (MMP)/triple-helix complexes, vol. 97, 37, 10.1016/bs.apcsb.2014.09.001 · DOI
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Metadata
- Authors
- Fields, G. B.
- Venue
- Matrix Biology
- Publisher
- Elsevier BV
- Published
- 2015-05
- Volume
- 44-46
- Pages
- 239-246
- ISSN
- 0945-053X
- PMC
- PMC4466128
- Cited by
- 98
- References
- 2
- Language
- en
- Funders
- NIH (CA98799, AR063795, GM106469)
- NHLBI (268201000036C))
- Multiple Sclerosis National Research Institute
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