The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Active site specificity profiling of the matrix metalloproteinase family: Proteomic identification of 4300 cleavage sites by nine MMPs explored with structural and synthetic peptide cleavage analyses.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“While no consensus cleavage site for MMPs has been identified, it is believed that MMPs preferentially cleave specific substrates at certain locations containing specific amino acid residues (53).”
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 [53]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Overview of the CCP 4 suite and current developments
Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353
Extracellular Matrix Degradation and Remodeling in Development and Disease
Lu, P., Takai, K., Weaver, V. M., & Werb, Z. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005058 · Cited by 2,265
Van Wart, H. E., & Birkedal-Hansen, H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.14.5578 · Cited by 1,475
Overview of the Matrisome--An Inventory of Extracellular Matrix Constituents and Functions
Hynes, R. O., & Naba, A. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004903 · Cited by 1,349
Regulation of matrix biology by matrix metalloproteinases
Mott, J. D., & Werb, Z. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.07.010 · Cited by 1,104 · cited 2×
“Thus, these high throughput analyses have revealed that ECM components make up just 18% of MMP substrate repertoires, with signalingmolecules, receptors and other bioactive mediators in the matrix being more highly represented substrates [6,20–23,26], a big departure from when MMPs were considered mere matrix remodele…”
BackgroundSchenk, S., Hintermann, E., Bilban, M., Koshikawa, N., Hojilla, C., Khokha, R., & Quaranta, V. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200208145 · Cited by 309
Wells, J. M., Gaggar, A., & Blalock, J. E. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.016 · Cited by 263
Matricryptins and matrikines: biologically active fragments of the extracellular matrix
Ricard‐Blum, S., & Salza, R. (2014) · Experimental Dermatology · doi:10.1111/exd.12435 · Cited by 224
Flagged first, then by citations
Research works printed but not linked: 101
- Tallant, 2010, Matrix metalloproteinases: fold and function of their catalytic domains, Biochim. Biophys. Acta, 1803, 20-8
- Maskos, 2003, Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases, Mol. Biotechnol., 25, 241, 10.1385/MB:25:3:241 · DOI
- Murphy, 2008, Progress in matrix metalloproteinase research, Mol. Asp. Med., 29, 290, 10.1016/j.mam.2008.05.002 · DOI
- Nagase, 2006, Structure and function of matrix metalloproteinases and TIMPs, Cardiovasc. Res., 69, 562, 10.1016/j.cardiores.2005.12.002 · DOI
- Butler, 2009, Updated biological roles for matrix metalloproteinases and new “intracellular” substrates revealed by degradomics, Biochemistry (Mosc), 48, 10830, 10.1021/bi901656f · DOI
- Chen, 2007, Expression of extracellular matrix metalloproteinase inducer and matrix metalloproteinases during mouse embryonic development, Reprod. Camb. Engl., 133, 405, 10.1530/rep.1.01020 · DOI
- Deryugina, 2015, Tumor angiogenesis: MMP-mediated induction of intravasation- and metastasis-sustaining neovasculature, Matrix Biol. J. Int. Soc. Matrix Biol., 44–46, 94, 10.1016/j.matbio.2015.04.004 · DOI
- Itoh, 2006, MT1-MMP: a key regulator of cell migration in tissue, IUBMB Life, 58, 589, 10.1080/15216540600962818 · DOI
- Aiken, 2010, Unraveling metalloproteinase function in skeletal biology and disease using genetically altered mice, Biochim. Biophys. Acta, 1803, 121, 10.1016/j.bbamcr.2009.07.002 · DOI
- Giannelli, 1997, Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5, Science, 277, 225, 10.1126/science.277.5323.225 · DOI · Paper page
- Xu, 2001, Proteolytic exposure of a cryptic site within collagen type IV is required for angiogenesis and tumor growth in vivo, J. Cell Biol., 154, 1069, 10.1083/jcb.200103111 · DOI
- Agnihotri, 2001, Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin), J. Biol. Chem, 276, 28261, 10.1074/jbc.M103608200 · DOI
- Sage, 2003, Cleavage of the matricellular protein SPARC by matrix metalloproteinase 3 produces polypeptides that influence angiogenesis, J. Biol. Chem, 278, 37849, 10.1074/jbc.M302946200 · DOI
- Monboisse, 1840, Matrikines from basement membrane collagens: a new anti-cancer strategy, Biochim. Biophys. Acta, 2014, 2589
- Butler, 2013, Matrix metalloproteinase processing of signaling molecules to regulate inflammation, Periodontol., 63, 123, 10.1111/prd.12035 · DOI
- Morrison, 2009, Matrix metalloproteinase proteomics: substrates, targets, and therapy, Curr. Opin. Cell Biol., 21, 645, 10.1016/j.ceb.2009.06.006 · DOI
- Schlage, 2015, Proteomic approaches to uncover MMP function, Matrix Biol. J. Int. Soc. Matrix Biol., 44–46, 232, 10.1016/j.matbio.2015.01.003 · DOI
- Fortelny, 2014, Network analyses reveal pervasive functional regulation between proteases in the human protease web, PLoS Biol., 12, 10.1371/journal.pbio.1001869 · DOI
- Sturrock, 2014, Highlight: the protease web, Biol. Chem., 395, 1133, 10.1515/hsz-2014-0237 · DOI
- Auf dem Keller, 2013, Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation, Sci. Signal., 6, 10.1126/scisignal.2003512 · DOI
- Bellac, 2014, Macrophage matrix metalloproteinase-12 dampens inflammation and neutrophil influx in arthritis, Cell Rep., 9, 618, 10.1016/j.celrep.2014.09.006 · DOI
- Haro, 2000, Matrix metalloproteinase-7-dependent release of tumor necrosis factor-alpha in a model of herniated disc resorption, J. Clin. Invest., 105, 143, 10.1172/JCI7091 · DOI
- Suzuki, 1997, Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site, J. Biol. Chem., 272, 31730, 10.1074/jbc.272.50.31730 · DOI
- Zhang, 2003, HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration, Nat. Neurosci., 6, 1064, 10.1038/nn1127 · DOI
- McQuibban, 2000, Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3, Science, 289, 1202, 10.1126/science.289.5482.1202 · DOI
- Wilson, 1999, Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense, Science, 286, 113, 10.1126/science.286.5437.113 · DOI
- Poulalhon, 2006, Modulation of collagen and MMP-1 gene expression in fibroblasts by the immunosuppressive drug rapamycin. A direct role as an antifibrotic agent?, J. Biol. Chem., 281, 33045, 10.1074/jbc.M606366200 · DOI
- Dufour, 2013, Missing the target: matrix metalloproteinase antitargets in inflammation and cancer, Trends Pharmacol. Sci., 34, 233, 10.1016/j.tips.2013.02.004 · DOI
- Shay, 2015, Moving targets: emerging roles for MMPs in cancer progression and metastasis, Matrix Biol. J. Int. Soc. Matrix Biol., 44–46, 200, 10.1016/j.matbio.2015.01.019 · DOI
- Bonnans, 2014, Remodelling the extracellular matrix in development and disease, Nat. Rev. Mol. Cell Biol., 15, 786, 10.1038/nrm3904 · DOI · Paper page
- Cox, 2011, Remodeling and homeostasis of the extracellular matrix: implications for fibrotic diseases and cancer, Dis. Model. Mech., 4, 165, 10.1242/dmm.004077 · DOI · Paper page
- Kessenbrock, 2015, Matrix metalloproteinases in stem cell regulation and cancer, Matrix Biol. J. Int. Soc. Matrix Biol., 44–46, 184, 10.1016/j.matbio.2015.01.022 · DOI
- Itoh, 2015, Membrane-type matrix metalloproteinases: their functions and regulations, Matrix Biol. J. Int. Soc. Matrix Biol., 44–46, 207, 10.1016/j.matbio.2015.03.004 · DOI · Paper page
- Overall, 2002, Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites, Mol. Biotechnol., 22, 51, 10.1385/MB:22:1:051 · DOI
- Patterson, 2001, Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain, FEBS Lett., 503, 158, 10.1016/S0014-5793(01)02723-5 · DOI
- Steffensen, 1995, Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen, J. Biol. Chem., 270, 11555, 10.1074/jbc.270.19.11555 · DOI
- Gomis-Rüth, 1824, A standard orientation for metallopeptidases, Biochim. Biophys. Acta, 2012, 157
- Harris, 2000, Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries, Proc. Natl. Acad. Sci., 97, 7754, 10.1073/pnas.140132697 · DOI
- Kasperkiewicz, 2012, Current and prospective applications of non-proteinogenic amino acids in profiling of proteases substrate specificity, Biol. Chem., 393, 843, 10.1515/hsz-2012-0167 · DOI
- Schilling, 2007, Proteomic discovery of protease substrates, Curr. Opin. Chem. Biol., 11, 36, 10.1016/j.cbpa.2006.11.037 · DOI
- Schilling, 2008, Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites, Nat. Biotechnol., 26, 685, 10.1038/nbt1408 · DOI
- Schilling, 2011, Characterization of the prime and non-prime active site specificities of proteases by proteome-derived peptide libraries and tandem mass spectrometry, Nat. Protoc., 6, 111, 10.1038/nprot.2010.178 · DOI
- Barré, 2014, Cleavage specificity analysis of six type II transmembrane serine proteases (TTSPs) using PICS with proteome-derived peptide libraries, PLoS One, 9, 10.1371/journal.pone.0105984 · DOI
- Becker-Pauly, 2011, Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates, Mol. Cell Proteomics, 10, 10.1074/mcp.M111.009233 · DOI
- Cruz, 2014, RC1339/APRc from Rickettsia conorii is a novel aspartic protease with properties of retropepsin-like enzymes, PLoS Pathog., 10, 10.1371/journal.ppat.1004324 · DOI
- Eckhard, 2014, Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen, J. Proteome, 100, 102, 10.1016/j.jprot.2013.10.004 · DOI
- Marino, 2014, Family-wide characterization of matrix metalloproteinases from Arabidopsis thaliana reveals their distinct proteolytic activity and cleavage site specificity, Biochem. J., 457, 335, 10.1042/BJ20130196 · DOI
- Turk, 2001, Determination of protease cleavage site motifs using mixture-based oriented peptide libraries, Nat. Biotechnol., 19, 661, 10.1038/90273 · DOI
- Chen, 2003, A residue in the S2 subsite controls substrate selectivity of matrix metalloproteinase-2 and matrix metalloproteinase-9, J. Biol. Chem, 278, 17158, 10.1074/jbc.M210324200 · DOI
- Kridel, 2001, Substrate hydrolysis by matrix metalloproteinase-9, J. Biol. Chem, 276, 20572, 10.1074/jbc.M100900200 · DOI
- Reiter, 1999, Inhibition of MMP-1 and MMP-13 with phosphinic acids that exploit binding in the S2 pocket, Bioorg. Med. Chem. Lett., 9, 127, 10.1016/S0960-894X(98)00729-X · DOI
- Deng, 2000, Substrate specificity of human collagenase 3 assessed using a phage-displayed peptide library, J. Biol. Chem., 275, 31422, 10.1074/jbc.M004538200 · DOI
- McGeehan, 1994, Characterization of the peptide substrate specificities of interstitial collagenase and 92-kDa gelatinase. Implications for substrate optimization, J. Biol. Chem., 269, 32814, 10.1016/S0021-9258(20)30064-8 · DOI
- Smith, 1995, Rapid identification of highly active and selective substrates for stromelysin and matrilysin using bacteriophage peptide display libraries, J. Biol. Chem., 270, 6440, 10.1074/jbc.270.12.6440 · DOI
- Nagase, 1994, Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloproteinase-3), J. Biol. Chem., 269, 20952, 10.1016/S0021-9258(17)31914-2 · DOI
- Nagase, 1996, Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides, Biopolymers, 40, 399, 10.1002/(SICI)1097-0282(1996)40:4<399::AID-BIP5>3.0.CO;2-R · DOI
- Netzel-Arnett, 1993, Comparative sequence specificities of human 72- and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin), Biochemistry (Mosc), 32, 6427, 10.1021/bi00076a016 · DOI
- Bode, 1999, Structural properties of matrix metalloproteinases, Cell Mol. Life Sci., 55, 639, 10.1007/s000180050320 · DOI
- Ratnikov, 2014, Basis for substrate recognition and distinction by matrix metalloproteinases, Proc. Natl. Acad. Sci. U. S. A., 111, E4148, 10.1073/pnas.1406134111 · DOI
- Dean, 2008, Macrophage-specific metalloelastase (MMP-12) truncates and inactivates ELR+ CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: potential role of the macrophage in terminating polymorphonuclear leukocyte influx, Blood, 112, 3455, 10.1182/blood-2007-12-129080 · DOI
- Rawlings, 2014, MEROPS: the database of proteolytic enzymes, their substrates and inhibitors, Nucleic Acids Res., 42, D503, 10.1093/nar/gkt953 · DOI
- Overall, 2002, Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: a new tool for degradomics, Biol. Chem., 383, 1059, 10.1515/BC.2002.114 · DOI
- Li, 2002, Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury, Cell, 111, 635, 10.1016/S0092-8674(02)01079-6 · DOI
- Knight, 1992, A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases, FEBS Lett., 296, 263, 10.1016/0014-5793(92)80300-6 · DOI
- London, 2011, Rosetta FlexPepDock web server—high resolution modeling of peptide–protein interactions, Nucleic Acids Res., 39, W249, 10.1093/nar/gkr431 · DOI
- Kukreja, 2015, High-throughput multiplexed peptide-centric profiling illustrates both substrate cleavage redundancy and specificity in the MMP family, Chem. Biol., 22, 1122, 10.1016/j.chembiol.2015.07.008 · DOI
- Prudova, 2010, Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics, Mol. Cell Proteomics, 9, 894, 10.1074/mcp.M000050-MCP201 · DOI
- Kohno, 2006, Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453, Biochem. Biophys. Res. Commun., 344, 315, 10.1016/j.bbrc.2006.03.098 · DOI
- Kleifeld, 2010, Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products, Nat. Biotechnol., 28, 281, 10.1038/nbt.1611 · DOI
- Kleifeld, 2011, Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates, Nat. Protoc., 6, 1578, 10.1038/nprot.2011.382 · DOI
- Fields, 2015, New strategies for targeting matrix metalloproteinases, Matrix Biol. J. Int. Soc. Matrix Biol., 44–46, 239, 10.1016/j.matbio.2015.01.002 · DOI · Paper page
- Sela-Passwell, 2011, New opportunities in drug design of metalloproteinase inhibitors: combination between structure–function experimental approaches and systems biology, Expert Opin. Drug Discov., 6, 527, 10.1517/17460441.2011.560936 · DOI
- Morrison, 2006, TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains, J. Biol. Chem., 281, 26528, 10.1074/jbc.M603331200 · DOI
- Butler, 2004, The canonical methionine 392 of matrix metalloproteinase 2 (gelatinase A) is not required for catalytic efficiency or structural integrity: probing the role of the methionine-turn in the metzincin metalloprotease superfamily, J. Biol. Chem., 279, 15615, 10.1074/jbc.M312727200 · DOI
- Rozanov, 2003, Membrane type-1 matrix metalloproteinase functions as a proprotein self-convertase. Expression of the latent zymogen in Pichia pastoris, autolytic activation, and the peptide sequence of the cleavage forms, J. Biol. Chem, 278, 8257, 10.1074/jbc.M213246200 · DOI · Paper page
- The UniProt Consortium, 2014, Activities at the Universal Protein Resource (UniProt), Nucleic Acids Res., 42, D191, 10.1093/nar/gku469 · DOI
- Craig R, Beavis RC. TANDEM: matching proteins with tandem mass spectra. Bioinforma Oxf. Engl. 2004;20:1466–7. doi:http://dx.doi.org/10.1093/bioinformatics/bth092. · DOI
- Keller, 2002, Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search, Anal. Chem., 74, 5383, 10.1021/ac025747h · DOI
- Keller, 2005, A uniform proteomics MS/MS analysis platform utilizing open XML file formats, Mol. Syst. Biol., 1, 2005.0017, 10.1038/msb4100024 · DOI
- Schilling, 2011, Factor Xa subsite mapping by proteome-derived peptide libraries improved using WebPICS, a resource for proteomic identification of cleavage sites, Biol. Chem., 392, 1031, 10.1515/BC.2011.158 · DOI
- Kersey, 2004, The International Protein Index: an integrated database for proteomics experiments, Proteomics, 4, 1985, 10.1002/pmic.200300721 · DOI
- Colaert, 2009, Improved visualization of protein consensus sequences by iceLogo, Nat. Methods, 6, 786, 10.1038/nmeth1109-786 · DOI
- Vizcaíno, 2013, The PRoteomics IDEntifications (PRIDE) database and associated tools: status in 2013, Nucleic Acids Res., 41, D1063, 10.1093/nar/gks1262 · DOI · Paper page
- Abel, 2003, Pre-steady-state kinetics of Bacillus licheniformis 1,3–1,4-beta-glucanase: evidence for a regulatory binding site, Biochem. J., 371, 997, 10.1042/bj20021504 · DOI
- Antoni, 2013, Crystallization of bi-functional ligand protein complexes, J. Struct. Biol., 182, 246, 10.1016/j.jsb.2013.03.015 · DOI
- Browner, 1995, Matrilysin-inhibitor complexes: common themes among metalloproteases, Biochemistry (Mosc), 34, 6602, 10.1021/bi00020a004 · DOI
- Fernandez-Catalan, 1998, Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor, EMBO J., 17, 5238, 10.1093/emboj/17.17.5238 · DOI · Paper page
- Hashimoto, 2011, Structural basis for matrix metalloproteinase-2 (MMP-2)-selective inhibitory action of β-amyloid precursor protein-derived inhibitor, J. Biol. Chem., 286, 33236, 10.1074/jbc.M111.264176 · DOI
- Iyer, 2006, Crystal structure of an active form of human MMP-1, J. Mol. Biol., 362, 78, 10.1016/j.jmb.2006.06.079 · DOI
- Matter, 1999, Quantitative structure–activity relationship of human neutrophil collagenase (MMP-8) inhibitors using comparative molecular field analysis and X-ray structure analysis, J. Med. Chem., 42, 1908, 10.1021/jm980631s · DOI
- Nar, 2001, Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor, J. Mol. Biol., 312, 743, 10.1006/jmbi.2001.4953 · DOI
- Steele, 2000, Expression, characterization and structure determination of an active site mutant (Glu202-Gln) of mini-stromelysin-1, Protein Eng., 13, 397, 10.1093/protein/13.6.397 · DOI
- Bordoli, 2012, Automated protein structure modeling with SWISS-MODEL Workspace and the Protein Model Portal, Methods Mol. Biol., 857, 107, 10.1007/978-1-61779-588-6_5 · DOI
- DeLano, 2005, The case for open-source software in drug discovery, Drug Discov. Today, 10, 213, 10.1016/S1359-6446(04)03363-X · DOI
- Yang, 2012, UCSF chimera, MODELLER, and IMP: an integrated modeling system, J. Struct. Biol., 179, 269, 10.1016/j.jsb.2011.09.006 · DOI
- Dolinsky, 2004, PDB2PQR: an automated pipeline for the setup of Poisson–Boltzmann electrostatics calculations, Nucleic Acids Res., 32, W665, 10.1093/nar/gkh381 · DOI
- Olsson, 2011, PROPKA3: consistent treatment of internal and surface residues in empirical pKa predictions, J. Chem. Theory Comput., 7, 525, 10.1021/ct100578z · DOI
- Baker, 2001, Electrostatics of nanosystems: application to microtubules and the ribosome, Proc. Natl. Acad. Sci. U. S. A., 98, 10037, 10.1073/pnas.181342398 · DOI
- Bond, 2003, TopDraw: a sketchpad for protein structure topology cartoons, Bioinforma Oxf. Engl., 19, 311, 10.1093/bioinformatics/19.2.311 · DOI
- Wessel, 1984, A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids, Anal. Biochem., 138, 141, 10.1016/0003-2697(84)90782-6 · DOI
- Marchant, 2014, A new transcriptional role for matrix metalloproteinase-12 in antiviral immunity, Nat. Med., 20, 493, 10.1038/nm.3508 · DOI
Cited by
Sorted by citations
Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331
The impact of aging on cardiac extracellular matrix
Meschiari, C. A., Ero, O. K., Pan, H., Finkel, T., & Lindsey, M. L. (2017) · GeroScience · doi:10.1007/s11357-017-9959-9 · Cited by 237
Extracellular Matrix‐Based Strategies for Immunomodulatory Biomaterials Engineering
Rowley, A. T., Nagalla, R. R., Wang, S., & Liu, W. F. (2019) · Advanced Healthcare Materials · doi:10.1002/adhm.201801578 · Cited by 193
Pentz, R., Iulita, M. F., Mikutra-Cencora, M., Ducatenzeiler, A., Bennett, D. A., & Cuello, A. C. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105150 · Cited by 31
Wang, M., Alabi, A., Gu, H.-M., Gill, G., Zhang, Z., Jarad, S., Xia, X.-D., Shen, Y., Wang, G.-Q., & Zhang, D.-W. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.917238 · Cited by 13
Metadata
- Authors
- Eckhard, U., Huesgen, P. F., Schilling, O., Bellac, C. L., Butler, G. S., Cox, J. H., Dufour, A., Goebeler, V., Kappelhoff, R., Keller, U. A. D., Klein, T., Lange, P. F., Marino, G., Morrison, C. J., Prudova, A., Rodriguez, D., Starr, A. E., Wang, Y., & Overall, C. M.
- Venue
- Matrix Biology
- Publisher
- Elsevier BV
- Published
- 2016-01
- Volume
- 49
- Pages
- 37-60
- ISSN
- 0945-053X
- Cited by
- 212
- References
- 9
- Language
- en
- Funders
- Canada Research Chair in Metalloproteinase Proteomics and Systems Biology
- Canadian Institutes of Health Research (MOP-11433, MOP-37937, MOP-111055)
- Michael Smith Research Foundation for Health Research (MSFHR)
- Canada Foundations for Innovation (CFI)
- post-doctoral fellowships from MSFHR
- German Academic Exchange Service (DAAD)
- MSFHR
- fellowships from the German Research Foundation (DFG)
- postdoctoral fellowships of the Swiss National Science Foundation
- Novartis Jubilee Foundation
- Feodor Lynen Research Fellowship of the Alexander von Humboldt Foundation
- UBC Centre for Blood Research Strategic Training Program in Transfusion Science
- CBR Internal Collaborative Training Award
- Natural Sciences and Engineering Research Council of Canada Graduate Scholarships
- CIHR Strategic Training Fellowships
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review