Cited by 139

The DOI matches its Crossref record.

BMP-1/tolloid-like proteinases synchronize matrix assembly with growth factor activation to promote morphogenesis and tissue remodeling

Vadon-Le Goff, Sandrine, Hulmes, David J.S., Moali, Catherine·2015·Matrix Biology

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.matbio.2015.02.006

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: 108

  1. Wozney, 1988, Novel regulators of bone formation: molecular clones and activities, Science, 242, 1528, 10.1126/science.3201241 · DOI
  2. Sterchi, 2008, Meprins, membrane-bound and secreted astacin metalloproteinases, Mol Aspects Med, 29, 309, 10.1016/j.mam.2008.08.002 · DOI
  3. Shimell, 1991, The Drosophila dorsal–ventral patterning gene tolloid is related to human bone morphogenetic protein 1, Cell, 67, 469, 10.1016/0092-8674(91)90522-Z · DOI
  4. Takahara, 1994, Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues, J Biol Chem, 269, 32572, 10.1016/S0021-9258(18)31672-7 · DOI
  5. Muir, 2011, Metalloproteinases in Drosophila to humans that are central players in developmental processes, J Biol Chem, 286, 41905, 10.1074/jbc.R111.299768 · DOI
  6. Suzuki, 1996, Failure of ventral body wall closure in mouse embryos lacking a procollagen C-proteinase encoded by Bmp1, a mammalian gene related to Drosophila tolloid, Development, 122, 3587, 10.1242/dev.122.11.3587 · DOI
  7. Clark, 1999, The mammalian tolloid-like 1 gene, Tll1, is necessary for normal septation and positioning of the heart, Development, 126, 2631, 10.1242/dev.126.12.2631 · DOI
  8. Wermter, 2007, The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains, Biol Chem, 388, 513, 10.1515/BC.2007.054 · DOI
  9. MacSweeney, 2008, Structural basis for the substrate specificity of bone morphogenetic protein 1/tolloid-like metalloproteases, J Mol Biol, 384, 228, 10.1016/j.jmb.2008.09.029 · DOI
  10. Berry, 2009, Role of dimerization and substrate exclusion in the regulation of bone morphogenetic protein-1 and mammalian tolloid, Proc Natl Acad Sci U S A, 106, 8561, 10.1073/pnas.0812178106 · DOI
  11. Berry, 2010, Structural and functional evidence for a substrate exclusion mechanism in mammalian tolloid like-1 (TLL-1) proteinase, FEBS Lett, 584, 657, 10.1016/j.febslet.2009.12.050 · DOI
  12. Kessler, 1996, Bone morphogenetic protein-1: the type I procollagen C-proteinase, Science, 271, 360, 10.1126/science.271.5247.360 · DOI
  13. Li, 1996, The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1, Proc Natl Acad Sci U S A, 93, 5127, 10.1073/pnas.93.10.5127 · DOI
  14. Hojima, 1994, Cleavage of type I procollagen by C- and N-proteinases is more rapid if the substrate is aggregated with dextran sulfate or polyethylene glycol, Anal Biochem, 223, 173, 10.1006/abio.1994.1569 · DOI
  15. Hojima, 1985, Type I procollagen carboxyl-terminal proteinase from chick embryo tendons, J Biol Chem, 260, 15996, 10.1016/S0021-9258(17)36357-3 · DOI
  16. Broder, 2013, Metalloproteases meprin alpha and meprin beta are C- and N-procollagen proteinases important for collagen assembly and tensile strength, Proc Natl Acad Sci U S A, 110, 14219, 10.1073/pnas.1305464110 · DOI
  17. Kronenberg, 2010, Processing of procollagen III by meprins: new players in extracellular matrix assembly?, J Invest Dermatol, 130, 2727, 10.1038/jid.2010.202 · DOI
  18. Steiglitz, 2006, Procollagen C proteinase enhancer 1 genes are important determinants of the mechanical properties and geometry of bone and the ultrastructure of connective tissues, Mol Cell Biol, 26, 238, 10.1128/MCB.26.1.238-249.2006 · DOI
  19. Gopalakrishnan, 2004, Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) procollagen heterotrimer, J Biol Chem, 279, 30904, 10.1074/jbc.M402252200 · DOI
  20. Imamura, 1998, Bone morphogenetic protein-1 processes the NH2-terminal propeptide, and a furin-like proprotein convertase processes the COOH-terminal propeptide of pro-alpha1(V) collagen, J Biol Chem, 273, 27511, 10.1074/jbc.273.42.27511 · DOI
  21. Kessler, 2001, Bone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer, J Biol Chem, 276, 27051, 10.1074/jbc.M102921200 · DOI
  22. Pappano, 2003, Use of Bmp1/Tll1 doubly homozygous null mice and proteomics to identify and validate in vivo substrates of bone morphogenetic protein 1/tolloid-like metalloproteinases, Mol Cell Biol, 23, 4428, 10.1128/MCB.23.13.4428-4438.2003 · DOI
  23. Linsenmayer, 1993, Type V collagen: molecular structure and fibrillar organization of the chicken alpha 1(V) NH2-terminal domain, a putative regulator of corneal fibrillogenesis, J Cell Biol, 121, 1181, 10.1083/jcb.121.5.1181 · DOI
  24. Ge, 2004, Bone morphogenetic protein-1/tolloid-related metalloproteinases process osteoglycin and enhance its ability to regulate collagen fibrillogenesis, J Biol Chem, 279, 41626, 10.1074/jbc.M406630200 · DOI
  25. Scott, 2000, Bone morphogenetic protein-1 processes probiglycan, J Biol Chem, 275, 30504, 10.1074/jbc.M004846200 · DOI
  26. von Marschall, 2010, Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1), Biochem Biophys Res Commun, 391, 1374, 10.1016/j.bbrc.2009.12.067 · DOI
  27. Rattenholl, 2002, Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen, J Biol Chem, 277, 26372, 10.1074/jbc.M203247200 · DOI
  28. Amano, 2000, Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma2 chain, J Biol Chem, 275, 22728, 10.1074/jbc.M002345200 · DOI
  29. Veitch, 2003, Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane type 1 metalloprotease, processes laminin-5 in keratinocytes and skin, J Biol Chem, 278, 15661, 10.1074/jbc.M210588200 · DOI
  30. Bachy, 2008, Syndecan-1 interaction with the LG4/5 domain in laminin-332 is essential for keratinocyte migration, J Cell Physiol, 214, 238, 10.1002/jcp.21184 · DOI
  31. Kagan, 2003, Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell, J Cell Biochem, 88, 660, 10.1002/jcb.10413 · DOI · Paper page
  32. Borel, 2001, Lysyl oxidase-like protein from bovine aorta. Isolation and maturation to an active form by bone morphogenetic protein-1, J Biol Chem, 276, 48944, 10.1074/jbc.M109499200 · DOI
  33. Cronshaw, 1995, The proteolytic processing site of the precursor of lysyl oxidase, Biochem J, 306, 279, 10.1042/bj3060279 · DOI
  34. Panchenko, 1996, Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase—potential role of procollagen C- proteinase, J Biol Chem, 271, 7113, 10.1074/jbc.271.12.7113 · DOI
  35. Baker, 2013, Lysyl oxidase enzymatic function increases stiffness to drive colorectal cancer progression through FAK, Oncogene, 32, 1863, 10.1038/onc.2012.202 · DOI
  36. Steiglitz, 2004, Bone morphogenetic protein-1/Tolloid-like proteinases process dentin matrix protein-1, J Biol Chem, 279, 980, 10.1074/jbc.M310179200 · DOI
  37. Tsuchiya, 2011, Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp), J Bone Miner Res, 26, 220, 10.1002/jbmr.202 · DOI
  38. von Marschall, 2010, Dentin sialophosphoprotein (DSPP) is cleaved into its two natural dentin matrix products by three isoforms of bone morphogenetic protein-1 (BMP1), Matrix Biol, 29, 295, 10.1016/j.matbio.2010.01.002 · DOI
  39. Lee, 1997, Transforming growth factor-beta regulation of bone morphogenetic protein-1 procollagen C-proteinase and related proteins in fibrogenic cells and keratinocytes, J Biol Chem, 272, 19059, 10.1074/jbc.272.30.19059 · DOI
  40. Tovar-Vidales, 2013, Transforming growth factor-beta2 induces expression of biologically active bone morphogenetic protein-1 in human trabecular meshwork cells, Invest Ophthalmol Vis Sci, 54, 4741, 10.1167/iovs.13-12203 · DOI
  41. Moustakas, 2012, Induction of epithelial–mesenchymal transition by transforming growth factor beta, Semin Cancer Biol, 22, 446, 10.1016/j.semcancer.2012.04.002 · DOI
  42. Ge, 2006, BMP1 controls TGFbeta1 activation via cleavage of latent TGFbeta-binding protein, J Cell Biol, 175, 111, 10.1083/jcb.200606058 · DOI
  43. Delolme, 2015, Proteolytic control of TGF-beta co-receptor activity by BMP-1/tolloid-like proteases revealed by quantitative iTRAQ proteomics, Cell Mol Life Sci, 72, 1009, 10.1007/s00018-014-1733-x · DOI
  44. Ge, 2005, GDF11 forms a bone morphogenetic protein 1-activated latent complex that can modulate nerve growth factor-induced differentiation of PC12 cells, Mol Cell Biol, 25, 5846, 10.1128/MCB.25.14.5846-5858.2005 · DOI
  45. Wolfman, 2003, Activation of latent myostatin by the BMP-1/tolloid family of metalloproteinases, Proc Natl Acad Sci U S A, 100, 15842, 10.1073/pnas.2534946100 · DOI · Paper page
  46. Marques, 1997, Production of a DPP activity gradient in the early drosophila embryo through the opposing actions of the SOG and TLD proteins, Cell, 91, 417, 10.1016/S0092-8674(00)80425-0 · DOI
  47. Piccolo, 1997, Cleavage of chordin by xolloid metalloproteinase suggests a role for proteolytic processing in the regulation of Spemann organizer activity, Cell, 91, 407, 10.1016/S0092-8674(00)80424-9 · DOI
  48. Kim, 2011, Bone morphogenetic protein-1 processes insulin-like growth factor-binding protein 3, J Biol Chem, 286, 29014, 10.1074/jbc.M111.252585 · DOI
  49. Gonzalez, 2005, BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan, J Biol Chem, 280, 7080, 10.1074/jbc.M409841200 · DOI
  50. Ge, 2007, Bone morphogenetic protein 1 processes prolactin to a 17-kDa antiangiogenic factor, Proc Natl Acad Sci U S A, 104, 10010, 10.1073/pnas.0704179104 · DOI
  51. Nguyen, 2006, Prolactin/growth hormone-derived antiangiogenic peptides highlight a potential role of tilted peptides in angiogenesis, Proc Natl Acad Sci U S A, 103, 14319, 10.1073/pnas.0606638103 · DOI
  52. Odagiri, 2014, The secreted protein ANGPTL2 promotes metastasis of osteosarcoma cells through integrin alpha5beta1, p38 MAPK, and matrix metalloproteinases, Sci Signal, 7, ra7, 10.1126/scisignal.2004612 · DOI
  53. Maertens, 2007, Cleavage and oligomerization of gliomedin, a transmembrane collagen required for node of ranvier formation, J Biol Chem, 282, 10647, 10.1074/jbc.M611339200 · DOI
  54. Chau, 2007, Bone morphogenetic protein-1 (BMP-1) cleaves human proapolipoprotein A1 and regulates its activation for lipid binding, Biochemistry, 46, 8445, 10.1021/bi700028u · DOI
  55. Adar, 1986, Evidence for a protein that enhances the activity of type I procollagen C-proteinase, Coll Relat Res, 6, 267, 10.1016/S0174-173X(86)80011-5 · DOI
  56. Kessler, 1989, Type I procollagen C-proteinase from mouse fibroblasts, Eur J Biochem, 186, 115, 10.1111/j.1432-1033.1989.tb15184.x · DOI
  57. Bourhis, 2013, Procollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation, Proc Natl Acad Sci U S A, 110, 6394, 10.1073/pnas.1300480110 · DOI
  58. Hulmes, 1997, The CUB domains of procollagen C-proteinase enhancer control collagen assembly solely by their effect on procollagen C- proteinase/bone morphogenetic protein-1, Matrix Biol, 16, 41, 10.1016/S0945-053X(97)90115-3 · DOI
  59. Kronenberg, 2009, Strong cooperativity and loose geometry between CUB domains are the basis for procollagen c-proteinase enhancer activity, J Biol Chem, 284, 33437, 10.1074/jbc.M109.046128 · DOI
  60. Takahara, 1994, Type I procollagen COOH-terminal proteinase enhancer protein: Identification, primary structure, and chromosomal localization of the cognate human gene (PCOLCE), J Biol Chem, 269, 26280, 10.1016/S0021-9258(18)47191-8 · DOI
  61. Bekhouche, 2010, Role of the NTR domain of procollagen C-proteinaser enhancer-1 in the control of metalloproteinase activity, J Biol Chem, 285, 15950, 10.1074/jbc.M109.086447 · DOI
  62. Weiss, 2010, Binding of procollagen C-proteinase enhancer-1 (PCPE-1) to heparin/heparan sulfate: properties and role in PCPE-1 interaction with cells, J Biol Chem, 285, 33867, 10.1074/jbc.M110.141366 · DOI
  63. Vadon-Le Goff, 2011, Procollagen C-proteinase enhancer stimulates procollagen processing by binding to the C-propeptide only, J Biol Chem, 286, 38932, 10.1074/jbc.M111.274944 · DOI
  64. Moali, 2005, Substrate-specific modulation of a multisubstrate proteinase. C-terminal processing of fibrillar procollagens is the only BMP-1-dependent activity to be enhanced by PCPE-1, J Biol Chem, 280, 24188, 10.1074/jbc.M501486200 · DOI
  65. Petropoulou, 2005, Identification of the minimal domain structure of bone morphogenetic protein-1 (BMP-1) for chordinase activity: chordinase activity is not enhanced by procollagen C-proteinase enhancer-1 (PCPE-1), J Biol Chem, 280, 22616, 10.1074/jbc.M413468200 · DOI
  66. Symoens, 2011, Identification of binding partners interacting with the alpha1-N-propeptide of type V collagen, Biochem J, 433, 371, 10.1042/BJ20101061 · DOI
  67. Xu, 2000, Identification and expression of a novel type I procollagen C- proteinase enhancer protein gene from the glaucoma candidate region on 3q21–q24, Genomics, 66, 264, 10.1006/geno.2000.6229 · DOI
  68. Steiglitz, 2002, PCOLCE2 encodes a functional procollagen C-proteinase enhancer (PCPE2) that is a collagen-binding protein differing in distribution of expression and post-translational modification from the previously described PCPE1, J Biol Chem, 277, 49820, 10.1074/jbc.M209891200 · DOI
  69. Zhu, 2009, Regulation of apoAI processing by procollagen C-proteinase enhancer-2 and bone morphogenetic protein-1, J Lipid Res, 50, 1330, 10.1194/jlr.M900034-JLR200 · DOI
  70. Francone, 2011, Disruption of the murine procollagen C-proteinase enhancer 2 causes accumulation of pro-apolipoprotein A-I and increased HDL levels, J Lipid Res, 52, 1974, 10.1194/jlr.M016527 · DOI
  71. Yamaguchi, 2014, Periostin in skin tissue and skin-related diseases, Allergol Int, 63, 161, 10.2332/allergolint.13-RAI-0685 · DOI
  72. Liu, 2014, Periostin, a multifunctional matricellular protein in inflammatory and tumor microenvironments, Matrix Biol, 37, 150, 10.1016/j.matbio.2014.04.007 · DOI
  73. Norris, 2007, Periostin regulates collagen fibrillogenesis and the biomechanical properties of connective tissues, J Cell Biochem, 101, 695, 10.1002/jcb.21224 · DOI
  74. Maruhashi, 2010, Interaction between periostin and BMP-1 promotes proteolytic activation of lysyl oxidase, J Biol Chem, 285, 13294, 10.1074/jbc.M109.088864 · DOI
  75. Fogelgren, 2005, Cellular fibronectin binds to lysyl oxidase with high affinity and is critical for its proteolytic activation, J Biol Chem, 280, 24690, 10.1074/jbc.M412979200 · DOI
  76. Huang, 2009, Fibronectin binds and enhances the activity of bone morphogenetic protein 1, J Biol Chem, 284, 25879, 10.1074/jbc.M109.024125 · DOI
  77. Inomata, 2008, Robust stability of the embryonic axial pattern requires a secreted scaffold for chordin degradation, Cell, 134, 854, 10.1016/j.cell.2008.07.008 · DOI
  78. Scott, 2001, Homologues of twisted gastrulation are extracellular cofactors in antagonism of BMP signalling, Nature, 410, 475, 10.1038/35068572 · DOI
  79. Sun, 2010, The expression of twisted gastrulation in postnatal mouse brain and functional implications, Neuroscience, 169, 920, 10.1016/j.neuroscience.2010.05.026 · DOI
  80. Miljkovic-Licina, 2012, Targeting olfactomedin-like 3 inhibits tumor growth by impairing angiogenesis and pericyte coverage, Mol Cancer Ther, 11, 2588, 10.1158/1535-7163.MCT-12-0245 · DOI
  81. Zhang, 2006, Inhibition of bone morphogenetic protein 1 by native and altered forms of alpha2-macroglobulin, J Biol Chem, 281, 39096, 10.1074/jbc.M601362200 · DOI
  82. Grgurevic, 2011, Circulating bone morphogenetic protein 1–3 isoform increases renal fibrosis, J Am Soc Nephrol, 22, 681, 10.1681/ASN.2010070722 · DOI
  83. Lee, 2006, Embryonic dorsal–ventral signaling: secreted frizzled-related proteins as inhibitors of tolloid proteinases, Cell, 124, 147, 10.1016/j.cell.2005.12.018 · DOI
  84. Muraoka, 2006, Sizzled controls dorso-ventral polarity by repressing cleavage of the Chordin protein, Nat Cell Biol, 8, 329, 10.1038/ncb1379 · DOI
  85. Ploper, 2011, Dorsal-ventral patterning: crescent is a dorsally secreted Frizzled-related protein that competitively inhibits Tolloid proteases, Dev Biol, 352, 317, 10.1016/j.ydbio.2011.01.029 · DOI
  86. He, 2010, Exogenously administered secreted frizzled related protein 2 (Sfrp2) reduces fibrosis and improves cardiac function in a rat model of myocardial infarction, Proc Natl Acad Sci U S A, 107, 21110, 10.1073/pnas.1004708107 · DOI
  87. Kobayashi, 2009, Secreted Frizzled-related protein 2 is a procollagen C proteinase enhancer with a role in fibrosis associated with myocardial infarction, Nat Cell Biol, 11, 46, 10.1038/ncb1811 · DOI
  88. Bijakowski, 2012, Sizzled is unique among secreted Frizzled-related proteins for its ability to specifically inhibit bone morphogenetic protein-1 (BMP-1)/Tolloid-like proteinases, J Biol Chem, 287, 33581, 10.1074/jbc.M112.380816 · DOI
  89. Lee, 2009, Enzymatic regulation of pattern: BMP4 binds CUB domains of Tolloids and inhibits proteinase activity, Genes Dev, 23, 2551, 10.1101/gad.1839309 · DOI
  90. Jasuja, 2007, Bone morphogenetic protein 1 prodomain specifically binds and regulates signaling by bone morphogenetic proteins 2 and 4, J Biol Chem, 282, 9053, 10.1074/jbc.M610929200 · DOI
  91. Reid, 2006, Inhibition of procollagen C-proteinase reduces scar hypertrophy in a rabbit model of cutaneous scarring, Wound Repair Regen, 14, 138, 10.1111/j.1743-6109.2006.00103.x · DOI
  92. Wong, 2014, Transcriptional profiling of rapamycin-treated fibroblasts from hypertrophic and keloid scars, Ann Plast Surg, 72, 711, 10.1097/SAP.0b013e31826956f6 · DOI
  93. Malecaze, 2014, Upregulation of bone morphogenetic protein-1/mammalian tolloid and procollagen C-proteinase enhancer-1 in corneal scarring, Invest Ophthalmol Vis Sci, 55, 6712, 10.1167/iovs.13-13800 · DOI
  94. Ogata, 1997, Up-regulation of type I procollagen C-proteinase enhancer protein messenger RNA in rats with CCl4-induced liver fibrosis, Hepatology, 26, 611, 10.1002/hep.510260312 · DOI
  95. Kessler-Icekson, 2006, Expression of procollagen C-proteinase enhancer-1 in the remodeling rat heart is stimulated by aldosterone, Int J Biochem Cell Biol, 38, 358, 10.1016/j.biocel.2005.10.007 · DOI
  96. Baicu, 2012, Effects of the absence of procollagen C-endopeptidase enhancer-2 on myocardial collagen accumulation in chronic pressure overload, Am J Physiol Heart Circ Physiol, 303, H234, 10.1152/ajpheart.00227.2012 · DOI
  97. Beaumont, 2014, microRNA-122 down-regulation may play a role in severe myocardial fibrosis in human aortic stenosis through TGF-beta1 up-regulation, Clin Sci (Lond), 126, 497, 10.1042/CS20130538 · DOI
  98. Lindahl, 2011, COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta, Hum Mutat, 32, 598, 10.1002/humu.21475 · DOI
  99. Asharani, 2012, Attenuated BMP1 function compromises osteogenesis, leading to bone fragility in humans and zebrafish, Am J Hum Genet, 90, 661, 10.1016/j.ajhg.2012.02.026 · DOI
  100. Martinez-Glez, 2012, Identification of a mutation causing deficient BMP1/mTLD proteolytic activity in autosomal recessive osteogenesis imperfecta, Hum Mutat, 33, 343, 10.1002/humu.21647 · DOI
  101. Valencia, 2014, Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects, Am J Med Genet A, 164A, 1143, 10.1002/ajmg.a.36427 · DOI
  102. Hoyer-Kuhn, 2013, Hyperosteoidosis and hypermineralization in the same bone: bone tissue analyses in a boy with a homozygous BMP1 mutation, Calcif Tissue Int, 93, 565, 10.1007/s00223-013-9799-2 · DOI
  103. Muir, 2014, Induced ablation of Bmp1 and Tll1 produces osteogenesis imperfecta in mice, Hum Mol Genet, 23, 3085, 10.1093/hmg/ddu013 · DOI
  104. Naba, 2014, Extracellular matrix signatures of human mammary carcinoma identify novel metastasis promoters, Elife, 3, e01308, 10.7554/eLife.01308 · DOI
  105. Torres, 2013, Proteome profiling of cancer-associated fibroblasts identifies novel proinflammatory signatures and prognostic markers for colorectal cancer, Clin Cancer Res, 19, 6006, 10.1158/1078-0432.CCR-13-1130 · DOI
  106. Wu, 2014, miR-194 suppresses metastasis of non-small cell lung cancer through regulating expression of BMP1 and p27(kip1), Oncogene, 33, 1506, 10.1038/onc.2013.108 · DOI
  107. Newman, 2011, The requirement for fibroblasts in angiogenesis: fibroblast-derived matrix proteins are essential for endothelial cell lumen formation, Mol Biol Cell, 22, 3791, 10.1091/mbc.E11-05-0393 · DOI
  108. Syx, 2015, Defective proteolytic processing of fibrillar procollagens and prodecorin due to bi-allelic BMP-1 mutations results in a severe, progressive form of osteogenesis imperfecta., J Bone Miner Res, 10.1002/jbmr.2473 · DOI

Cited by

Sorted by citations

See all 139

Metadata

Authors
Vadon-Le Goff, S., Hulmes, D. J. S., & Moali, C.
Venue
Matrix Biology
Publisher
Elsevier BV
Published
2015-05
Volume
44-46
Pages
14-23
ISSN
0945-053X
Cited by
139
References
0
Language
en

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