CoChat
Sign Up
Cited by 22

The DOI matches its Crossref record.

Peripheral membrane associations of matrix metalloproteinases.

Van Doren, Steven R., Marcink, Tara C., Koppisetti, Rama K., Jurkevich, Alexander, Fulcher, Yan G.·2017·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
DOI 10.1016/j.bbamcr.2017.04.013PMC PMC5605405
Open this paper in CoChat — free account

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.bbamcr.2017.04.013

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.

A few free checks a day · papers already verified open instantly · results are public

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?

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

No references could be resolved yet.

Research works printed but not linked: 112

  1. Yu, 2000, Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7), J. Biol. Chem., 275, 4183, 10.1074/jbc.275.6.4183 · DOI
  2. Gadher, 1990, Degradation of cartilage collagens type II, IX, X and XI by enzymes derived from human articular chondrocytes, Matrix, 10, 154, 10.1016/S0934-8832(11)80164-2 · DOI
  3. Cha, 1996, Metal and pH dependence of heptapeptide catalysis by human matrilysin, Biochemistry, 35, 15831, 10.1021/bi962085f · DOI
  4. Sakamoto, 1975, Studies on the interaction between heparin and mouse bone collagenase, Biochim. Biophys. Acta Gen. Subj., 385, 41, 10.1016/0304-4165(75)90072-0 · DOI
  5. Crabbe, 1994, Reciprocated matrix metalloproteinase activation: a process performed by interstitial collagenase and progelatinase A, Biochemistry, 33, 14419, 10.1021/bi00252a007 · DOI
  6. Amour, 1998, TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3, FEBS Lett., 435, 39, 10.1016/S0014-5793(98)01031-X · DOI
  7. Wallon, 1997, The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding. Binding properties of recombinant gelatinase A C domain to extracellular matrix and basement membrane components, J. Biol. Chem., 272, 7473, 10.1074/jbc.272.11.7473 · DOI
  8. Theocharis, 2014, Cell–matrix interactions: focus on proteoglycan–proteinase interplay and pharmacological targeting in cancer, FEBS J., 281, 5023, 10.1111/febs.12927 · DOI
  9. Hadler-Olsen, 2011, Regulation of matrix metalloproteinase activity in health and disease, FEBS J., 278, 28, 10.1111/j.1742-4658.2010.07920.x · DOI
  10. Tocchi, 2013, Functional interactions between matrix metalloproteinases and glycosaminoglycans, FEBS J., 280, 2332, 10.1111/febs.12198 · DOI
  11. Yu, 2002, CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling, Genes Dev., 16, 307, 10.1101/gad.925702 · DOI
  12. 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
  13. Gao, 2004, J. Biol. Chem., 279, 10042, 10.1074/jbc.M312100200 · DOI
  14. Iida, 2007, Cell surface chondroitin sulfate glycosaminoglycan in melanoma: role in the activation of pro-MMP-2 (pro-gelatinase A), Biochem. J., 403, 553, 10.1042/BJ20061176 · DOI
  15. Echtermeyer, 2009, Syndecan-4 regulates ADAMTS-5 activation and cartilage breakdown in osteoarthritis, Nat. Med., 15, 1072, 10.1038/nm.1998 · DOI
  16. Ra, 2009, Control of promatrilysin (MMP7) activation and substrate-specific activity by sulfated glycosaminoglycans, J. Biol. Chem., 284, 27924, 10.1074/jbc.M109.035147 · DOI
  17. Sorensen, 2008, Heparan sulfate regulates ADAM12 through a molecular switch mechanism, J. Biol. Chem., 283, 31920, 10.1074/jbc.M804113200 · DOI
  18. Fulcher, 2014, Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery, ACS Chem. Biol., 9, 957, 10.1021/cb400898t · DOI
  19. Y.G. Fulcher, S.H. Prior, F. Zhang, R.J. Linhardt, S.R. Van Doren, Glycan Sites That Activate a Sheddase: Electrostatic Recognition Between Heparin and the MMP-7 Zymogen, (Under Review).
  20. Owen, 2003, Inducible expression of tissue inhibitor of metalloproteinases-resistant matrix metalloproteinase-9 on the cell surface of neutrophils, Am. J. Respir. Cell Mol. Biol., 29, 283, 10.1165/rcmb.2003-0034OC · DOI
  21. Owen, 2004, Membrane-bound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinase-resistant collagenase and serpinase, J. Immunol., 172, 7791, 10.4049/jimmunol.172.12.7791 · DOI
  22. Kioi, 2003, Matrilysin (MMP-7) induces homotypic adhesion of human colon cancer cells and enhances their metastatic potential in nude mouse model, Oncogene, 22, 8662, 10.1038/sj.onc.1207181 · DOI
  23. Berton, 2007, Binding of matrilysin-1 to human epithelial cells promotes its activity, Cell. Mol. Life Sci., 64, 610, 10.1007/s00018-007-6415-5 · DOI
  24. Cobos-Correa, 2009, Membrane-bound FRET probe visualizes MMP12 activity in pulmonary inflammation, Nat. Chem. Biol., 5, 628, 10.1038/nchembio.196 · DOI
  25. van Meer, 2008, Membrane lipids: where they are and how they behave, Nat. Rev. Mol. Cell Biol., 9, 112, 10.1038/nrm2330 · DOI · Paper page
  26. Kusumi, 2012, Dynamic organizing principles of the plasma membrane that regulate signal transduction: commemorating the fortieth anniversary of Singer and Nicolson's fluid-mosaic model, Annu. Rev. Cell Dev. Biol., 28, 215, 10.1146/annurev-cellbio-100809-151736 · DOI
  27. Yu, 2012, N-WASP coordinates the delivery and F-actin-mediated capture of MT1-MMP at invasive pseudopods, J. Cell Biol., 199, 527, 10.1083/jcb.201203025 · DOI
  28. El Azzouzi, 2016, Metalloproteinase MT1-MMP islets act as memory devices for podosome reemergence, J. Cell Biol., 213, 109, 10.1083/jcb.201510043 · DOI
  29. Sato, 1994, A matrix metalloproteinase expressed on the surface of invasive tumour cells, Nature, 370, 61, 10.1038/370061a0 · DOI
  30. Imai, 1996, Membrane-type matrix metalloproteinase 1 is a gelatinolytic enzyme and is secreted in a complex with tissue inhibitor of metalloproteinases 2, Cancer Res., 56, 2707
  31. Itoh, 2001, Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion, EMBO J., 20, 4782, 10.1093/emboj/20.17.4782 · DOI
  32. Zhao, 2004, Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 regulates pro-MMP-2 activation, J. Biol. Chem., 279, 8592, 10.1074/jbc.M308708200 · DOI
  33. Shiomi, 2005, Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151, Lab. Invest., 85, 1489, 10.1038/labinvest.3700351 · DOI
  34. Yu, 1999, Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion, Genes Dev., 13, 35, 10.1101/gad.13.1.35 · DOI
  35. Mori, 2002, CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain, EMBO J., 21, 3949, 10.1093/emboj/cdf411 · DOI · Paper page
  36. Suenaga, 2005, CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase, Oncogene, 24, 859, 10.1038/sj.onc.1208258 · DOI
  37. Takino, 2003, Tetraspanin CD63 promotes targeting and lysosomal proteolysis of membrane-type 1 matrix metalloproteinase, Biochem. Biophys. Res. Commun., 304, 160, 10.1016/S0006-291X(03)00544-8 · DOI
  38. Yanez-Mo, 2008, MT1-MMP collagenolytic activity is regulated through association with tetraspanin CD151 in primary endothelial cells, Blood, 112, 3217, 10.1182/blood-2008-02-139394 · DOI · Paper page
  39. Dumin, 2001, Pro-collagenase-1 (matrix metalloproteinase-1) binds the alpha(2)beta(1) integrin upon release from keratinocytes migrating on type I collagen, J. Biol. Chem., 276, 29368, 10.1074/jbc.M104179200 · DOI
  40. Stricker, 2001, Structural analysis of the alpha(2) integrin I domain/procollagenase-1 (matrix metalloproteinase-1) interaction, J. Biol. Chem., 276, 29375, 10.1074/jbc.M102217200 · DOI
  41. Stefanidakis, 2003, Identification of a negatively charged peptide motif within the catalytic domain of progelatinases that mediates binding to leukocyte beta 2 integrins, J. Biol. Chem., 278, 34674, 10.1074/jbc.M302288200 · DOI
  42. Bjorklund, 2004, Peptide inhibition of catalytic and noncatalytic activities of matrix metalloproteinase-9 blocks tumor cell migration and invasion, J. Biol. Chem., 279, 29589, 10.1074/jbc.M401601200 · DOI
  43. Redondo-Munoz, 2010, Matrix metalloproteinase-9 promotes chronic lymphocytic leukemia b cell survival through its hemopexin domain, Cancer Cell, 17, 160, 10.1016/j.ccr.2009.12.044 · DOI
  44. Emonard, 2004, Low density lipoprotein receptor-related protein mediates endocytic clearance of pro-MMP-2.TIMP-2 complex through a thrombospondin-independent mechanism, J. Biol. Chem., 279, 54944, 10.1074/jbc.M406792200 · DOI
  45. Van den Steen, 2006, The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors, J. Biol. Chem., 281, 18626, 10.1074/jbc.M512308200 · DOI
  46. Murphy, 2011, Localizing matrix metalloproteinase activities in the pericellular environment, FEBS J., 278, 2, 10.1111/j.1742-4658.2010.07918.x · DOI
  47. Piccard, 2007, Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins, J. Leukoc. Biol., 81, 870, 10.1189/jlb.1006629 · DOI
  48. Yamamoto, 2006, Binding of active matrilysin to cell surface cholesterol sulfate is essential for its membrane-associated proteolytic action and induction of homotypic cell adhesion, J. Biol. Chem., 281, 9170, 10.1074/jbc.M510377200 · DOI
  49. Ganguly, 2007, Intrinsic selectivity in binding of matrix metalloproteinase-7 to differently charged lipid membranes, FEBS Lett., 581, 5723, 10.1016/j.febslet.2007.11.042 · DOI
  50. Prior, 2015, Charge-triggered membrane insertion of matrix metalloproteinase-7, supporter of innate immunity and tumors, Structure, 23, 2099, 10.1016/j.str.2015.08.013 · DOI
  51. Yamamoto, 2010, Cholesterol sulfate alters substrate preference of matrix metalloproteinase-7 and promotes degradations of pericellular laminin-332 and fibronectin, J. Biol. Chem., 285, 28862, 10.1074/jbc.M110.136994 · DOI
  52. Yamamoto, 2014, Pericellular proteolysis by matrix metalloproteinase-7 is differentially modulated by cholesterol sulfate, sulfatide, and cardiolipin, FEBS J., 281, 3346, 10.1111/febs.12865 · DOI
  53. Hotary, 2000, Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3, J. Cell Biol., 149, 1309, 10.1083/jcb.149.6.1309 · DOI
  54. Sabeh, 2004, Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP, J. Cell Biol., 167, 769, 10.1083/jcb.200408028 · DOI
  55. Li, 2008, Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase, Mol. Biol. Cell, 19, 3221, 10.1091/mbc.e08-01-0016 · DOI
  56. Itoh, 2006, Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP, Mol. Biol. Cell, 17, 5390, 10.1091/mbc.e06-08-0740 · DOI
  57. MacKenzie, 1997, A transmembrane helix dimer: structure and implications, Science, 276, 131, 10.1126/science.276.5309.131 · DOI
  58. Bocharov, 2010, Structure elucidation of dimeric transmembrane domains of bitopic proteins, Cell Adh. Migr., 4, 284, 10.4161/cam.4.2.11930 · DOI
  59. Martfeld, 2015, Dynamic regulation of lipid–protein interactions, Biochim. Biophys. Acta, 1848, 1849, 10.1016/j.bbamem.2015.01.019 · DOI
  60. Cerofolini, 2016, Bilayer membrane modulation of membrane type 1 matrix metalloproteinase (MT1-MMP) structure and proteolytic activity, Sci. Rep., 6, 29511, 10.1038/srep29511 · DOI
  61. Durr, 2013, When detergent meets bilayer: birth and coming of age of lipid bicelles, Prog. Nucl. Magn. Reson. Spectrosc., 69, 1, 10.1016/j.pnmrs.2013.01.001 · DOI
  62. Kajita, 2001, Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration, J. Cell Biol., 153, 893, 10.1083/jcb.153.5.893 · DOI
  63. Endo, 2003, Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration, J. Biol. Chem., 278, 40764, 10.1074/jbc.M306736200 · DOI
  64. Koshikawa, 2000, Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5, J. Cell Biol., 148, 615, 10.1083/jcb.148.3.615 · DOI
  65. Koshikawa, 2005, Membrane-type matrix metalloproteinase-1 (MT1-MMP) is a processing enzyme for human laminin gamma 2 chain, J. Biol. Chem., 280, 88, 10.1074/jbc.M411824200 · DOI
  66. Udayakumar, 2003, Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 β3 chain and induces cell migration, Cancer Res., 63, 2292
  67. Koppisetti, 2014, Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12, Nat. Commun., 5, 5552, 10.1038/ncomms6552 · DOI
  68. 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
  69. Nelsestuen, 1978, Interaction of vitamin K dependent proteins with membranes, Biochemistry, 17, 2134, 10.1021/bi00604a017 · DOI
  70. Zwaal, 1998, Lipid–protein interactions in blood coagulation, Biochim. Biophys. Acta, 1376, 433, 10.1016/S0304-4157(98)00018-5 · DOI
  71. Tavoosi, 2011, Molecular determinants of phospholipid synergy in blood clotting, J. Biol. Chem., 286, 23247, 10.1074/jbc.M111.251769 · DOI
  72. Morrissey, 2010, Protein–phospholipid interactions in blood clotting, Thromb. Res., 125, S23, 10.1016/j.thromres.2010.01.027 · DOI
  73. Berg, 1985, Orientation constraints in diffusion-limited macromolecular association. The role of surface diffusion as a rate-enhancing mechanism, Biophys. J., 47, 1, 10.1016/S0006-3495(85)83870-4 · DOI
  74. von Hippel, 1989, Facilitated target location in biological systems, J. Biol. Chem., 264, 675, 10.1016/S0021-9258(19)84994-3 · DOI
  75. Berg, 1981, Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory, Biochemistry, 20, 6929, 10.1021/bi00527a028 · DOI
  76. Gorman, 2008, Visualizing one-dimensional diffusion of proteins along DNA, Nat. Struct. Mol. Biol., 15, 768, 10.1038/nsmb.1441 · DOI
  77. Gupte, 1988, Multidimensional diffusion modes and collision frequencies of cytochrome c with its redox partners, J. Biol. Chem., 263, 5241, 10.1016/S0021-9258(18)60706-9 · DOI
  78. Moravcevic, 2012, Conditional peripheral membrane proteins: facing up to limited specificity, Structure, 20, 15, 10.1016/j.str.2011.11.012 · DOI
  79. McCloskey, 1986, Rates of membrane-associated reactions: reduction of dimensionality revisited, J. Cell Biol., 102, 88, 10.1083/jcb.102.1.88 · DOI
  80. Kholodenko, 2000, Why cytoplasmic signalling proteins should be recruited to cell membranes, Trends Cell Biol., 10, 173, 10.1016/S0962-8924(00)01741-4 · DOI
  81. Marchant, 2014, A new transcriptional role for matrix metalloproteinase-12 in antiviral immunity, Nat. Med., 20, 493, 10.1038/nm.3508 · DOI
  82. Remacle, 2005, The transmembrane domain is essential for the microtubular trafficking of membrane type-1 matrix metalloproteinase (MT1-MMP), J. Cell Sci., 118, 4975, 10.1242/jcs.02610 · DOI
  83. Truong, 2016, Dynamics of internalization and recycling of the prometastatic membrane type 4 matrix metalloproteinase (MT4-MMP) in breast cancer cells, FEBS J., 283, 704, 10.1111/febs.13625 · DOI
  84. Radichev, 2010, Biochemical characterization of the cellular glycosylphosphatidylinositol-linked membrane type-6 matrix metalloproteinase, J. Biol. Chem., 285, 16076, 10.1074/jbc.M110.107094 · DOI
  85. Remacle, 2003, Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface, J. Cell Sci., 116, 3905, 10.1242/jcs.00710 · DOI
  86. Yamamoto, 2016, MMP-13 is constitutively produced in human chondrocytes and co-endocytosed with ADAMTS-5 and TIMP-3 by the endocytic receptor LRP1, Matrix Biol., 56, 57, 10.1016/j.matbio.2016.03.007 · DOI
  87. Cauwe, 2010, Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases, Crit. Rev. Biochem. Mol. Biol., 45, 351, 10.3109/10409238.2010.501783 · DOI
  88. Si-Tayeb, 2006, Matrix metalloproteinase 3 is present in the cell nucleus and is involved in apoptosis, Am. J. Pathol., 169, 1390, 10.2353/ajpath.2006.060005 · DOI
  89. Eguchi, 2008, Novel transcription factor-like function of human matrix metalloproteinase 3 regulating the CTGF/CCN2 gene, Mol. Cell. Biol., 28, 2391, 10.1128/MCB.01288-07 · DOI
  90. Shimizu-Hirota, 2012, MT1-MMP regulates the PI3Kδ·Mi-2/NuRD-dependent control of macrophage immune function, Genes Dev., 26, 395, 10.1101/gad.178749.111 · DOI
  91. Higashi, 2008, Identification of amino acid residues of matrix metalloproteinase-7 essential for binding to cholesterol sulfate, J. Biol. Chem., 283, 35735, 10.1074/jbc.M806285200 · DOI
  92. Elias, 2014, Role of cholesterol sulfate in epidermal structure and function: lessons from X-linked ichthyosis, Biochim. Biophys. Acta, Mol. Cell. Biol. Lipids, 1841, 353, 10.1016/j.bbalip.2013.11.009 · DOI
  93. Eberlin, 2010, Cholesterol sulfate imaging in human prostate cancer tissue by desorption electrospray ionization mass spectrometry, Anal. Chem., 82, 3430, 10.1021/ac9029482 · DOI
  94. Kiguchi, 1998, Coexpression of cholesterol sulfate and cytokeratin as tumor markers in well-differentiated squamous cell carcinoma of the human uterine cervix, Clin. Cancer Res., 4, 2985
  95. van den Eijnde, 1998, Cell surface exposure of phosphatidylserine during apoptosis is phylogenetically conserved, Apoptosis, 3, 9, 10.1023/A:1009650917818 · DOI
  96. 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
  97. Lomize, 2012, OPM database and PPM web server: resources for positioning of proteins in membranes, Nucleic Acids Res., 40, D370, 10.1093/nar/gkr703 · DOI
  98. Lomize, 2006, OPM: orientations of proteins in membranes database, Bioinformatics, 22, 623, 10.1093/bioinformatics/btk023 · DOI
  99. Lomize, 2007, The role of hydrophobic interactions in positioning of peripheral proteins in membranes, BMC Struct. Biol., 7, 44, 10.1186/1472-6807-7-44 · DOI
  100. Lomize, 2006, Positioning of proteins in membranes: a computational approach, Protein Sci., 15, 1318, 10.1110/ps.062126106 · DOI
  101. Kufareva, 2014, Discovery of novel membrane binding structures and functions, Biochem. Cell Biol., 92, 555, 10.1139/bcb-2014-0074 · DOI
  102. Marcink, 2017, Mapping Lipid Bilayer Recognition Sites of Metalloproteinases and Other Prospective Peripheral Membrane Proteins, Methods Mol. Biol., 1579, 61, 10.1007/978-1-4939-6863-3_5 · DOI
  103. Houghton, 2009, Macrophage elastase kills bacteria within murine macrophages, Nature, 460, 637, 10.1038/nature08181 · DOI
  104. Geisow, 1981, Temporal changes of lysosome and phagosome pH during phagolysosome formation in macrophages: studies by fluorescence spectroscopy, J. Cell Biol., 89, 645, 10.1083/jcb.89.3.645 · DOI
  105. Denisov, 2004, Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size, J. Am. Chem. Soc., 126, 3477, 10.1021/ja0393574 · DOI
  106. Denisov, 2016, Nanodiscs for structural and functional studies of membrane proteins, Nat. Struct. Mol. Biol., 23, 481, 10.1038/nsmb.3195 · DOI
  107. Schuler, 2013, Nanodiscs as a new tool to examine lipid–protein interactions, Methods Mol. Biol., 974, 415, 10.1007/978-1-62703-275-9_18 · DOI
  108. Nasr, 2017, Covalently circularized nanodiscs for studying membrane proteins and viral entry, Nat. Methods, 14, 49, 10.1038/nmeth.4079 · DOI · Paper page
  109. Bayburt, 2002, Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins, Nano Lett., 2, 853, 10.1021/nl025623k · DOI
  110. Tatulian, 2017, Membrane Binding, Orientation, Membrane Insertion, and Activity, Methods Enzymol., 583, 197, 10.1016/bs.mie.2016.09.009 · DOI
  111. Bertini, 2008, Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12, J. Am. Chem. Soc., 130, 7011, 10.1021/ja710491y · DOI
  112. Zhao, 2015, Transient collagen triple helix binding to a key metalloproteinase in invasion and development, Structure, 23, 257, 10.1016/j.str.2014.11.021 · DOI

Cited by

Sorted by citations

Metadata

Authors
Van Doren, S. R., Marcink, T. C., Koppisetti, R. K., Jurkevich, A., & Fulcher, Y. G.
ORCID
Van Doren, Steven R.
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
2017-11
Volume
1864
Issue
11
Pages
1964-1973
ISSN
0167-4889
DOI
10.1016/j.bbamcr.2017.04.013
PMC
PMC5605405
Cited by
22
References
0
Language
en
Licence
Funders
NIH (R01GM057289, R01CA098799, S10RR022341)

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