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Volumn 27, Issue , 2011, Pages 265-290

Transmembrane collagen receptors

Author keywords

Cell adhesion; Cell collagen interaction; Hemostasis; Integrin; Receptor tyrosine kinase; Triple helix

Indexed keywords

ALPHA10BETA1 INTEGRIN; ALPHA11BETA1 INTEGRIN; ALPHA1BETA 1 INTEGRIN; COLLAGEN BINDING PROTEIN; COLLAGEN RECEPTOR; COLLAGEN TYPE 1; COLLAGEN TYPE 2; COLLAGEN TYPE 3; DISCOIDIN DOMAIN RECEPTOR; GLYCOPROTEIN VI; INTEGRIN; LEUKOCYTE ASSOCIATED IMMUNOGLOBULIN LIKE RECEPTOR 1; MEMBRANE RECEPTOR; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 2;

EID: 80054036560     PISSN: 10810706     EISSN: 15308995     Source Type: Book Series    
DOI: 10.1146/annurev-cellbio-092910-154013     Document Type: Article
Times cited : (276)

References (159)
  • 1
    • 45549088677 scopus 로고    scopus 로고
    • Identification of disulfide-linked dimers of the receptor tyrosine kinase DDR1
    • Abdulhussein R, Koo DH, VogelWF. 2008. Identification of disulfide-linked dimers of the receptor tyrosine kinase DDR1. J. Biol. Chem. 283:12026-33
    • (2008) J. Biol. Chem. , vol.283 , pp. 12026-12033
    • Abdulhussein, R.1    Koo, D.H.2    Vogel, W.F.3
  • 2
    • 73549103105 scopus 로고    scopus 로고
    • Discoidin domain receptor-1 deficiency attenuates atherosclerotic calcification and smoothmuscle cell-mediated mineralization
    • Ahmad PJ, Trcka D, Xue S, Franco C, Speer MY, et al. 2009. Discoidin domain receptor-1 deficiency attenuates atherosclerotic calcification and smoothmuscle cell-mediated mineralization. Am. J. Pathol. 175:2686-96
    • (2009) Am. J. Pathol. , vol.175 , pp. 2686-2696
    • Ahmad, P.J.1    Trcka, D.2    Xue, S.3    Franco, C.4    Speer, M.Y.5
  • 3
    • 77953514278 scopus 로고    scopus 로고
    • Trafficking defects and loss of ligand binding are the underlying causes of all reported DDR2 missense mutations found in SMED-SL patients
    • Ali BR, Xu H, Akawi NA, John A, Karuvantevida NS, et al. 2010. Trafficking defects and loss of ligand binding are the underlying causes of all reported DDR2 missense mutations found in SMED-SL patients. Hum. Mol. Genet. 19:2239-50
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2239-2250
    • Ali, B.R.1    Xu, H.2    Akawi, N.A.3    John, A.4    Karuvantevida, N.S.5
  • 4
    • 0028799694 scopus 로고
    • Distinct structural characteristics of discoidin i subfamily receptor tyrosine kinases and complementary expression in human cancer
    • Alves F, Vogel W, Mossie K, Millauer B, Hofler H, Ullrich A. 1995. Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer. Oncogene 10:609-18
    • (1995) Oncogene , vol.10 , pp. 609-618
    • Alves, F.1    Vogel, W.2    Mossie, K.3    Millauer, B.4    Hofler, H.5    Ullrich, A.6
  • 5
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • DOI 10.1016/j.ceb.2007.08.002, PII S0955067407001196, Cell to Cell Contact and Extracellular Matrix
    • Arnaout MA, Goodman SL, Xiong JP. 2007. Structure and mechanics of integrin-based cell adhesion. Curr. Opin. Cell Biol. 19:495-507 (Pubitemid 350019555)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.5 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.-P.3
  • 6
    • 35649019167 scopus 로고    scopus 로고
    • Ligand binding rapidly induces disulfide-dependent dimerization of glycoprotein VI on the platelet plasma membrane
    • DOI 10.1074/jbc.M701330200
    • Arthur JF, Shen Y, Kahn ML, Berndt MC, Andrews RK, Gardiner EE. 2007. Ligand binding rapidly induces disulfide-dependent dimerization of glycoprotein VI on the platelet plasma membrane. J. Biol. Chem. 282:30434-41 (Pubitemid 350035211)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.42 , pp. 30434-30441
    • Arthur, J.F.1    Shen, Y.2    Kahn, M.L.3    Berndt, M.C.4    Andrews, R.K.5    Gardiner, E.E.6
  • 8
    • 0141483387 scopus 로고    scopus 로고
    • β1 integrins regulate chondrocyte rotation, G1 progression, and cytokinesis
    • DOI 10.1101/gad.277003
    • Aszodi A, Hunziker EB, Brakebusch C, Fassler R. 2003. β1 integrins regulate chondrocyte rotation, G1 progression, and cytokinesis. Genes Dev. 17:2465-79 (Pubitemid 37214793)
    • (2003) Genes and Development , vol.17 , Issue.19 , pp. 2465-2479
    • Aszodi, A.1    Hunziker, E.B.2    Brakebusch, C.3    Fassler, R.4
  • 9
    • 18144381003 scopus 로고    scopus 로고
    • Adhesion of human and mouse platelets to collagen under shear: A unifying model
    • DOI 10.1096/fj.04-1940fje
    • Auger JM, Kuijpers MJ, Senis YA, Watson SP, Heemskerk JW. 2005. Adhesion of human and mouse platelets to collagen under shear: a unifying model. FASEB J. 19:825-27 (Pubitemid 40617397)
    • (2005) FASEB Journal , vol.19 , Issue.7 , pp. 825-827
    • Auger, J.M.1    Kuijpers, M.J.E.2    Senis, Y.A.3    Watson, S.P.4    Heemskerk, J.W.M.5
  • 12
    • 0031826798 scopus 로고    scopus 로고
    • The discoidin domain family revisited: New members from prokaryotes and a homology-based fold prediction
    • Baumgartner S, Hofmann K, Chiquet-Ehrismann R, Bucher P. 1998. The discoidin domain family revisited: new members from prokaryotes and a homology-based fold prediction. Protein Sci. 7:1626-31 (Pubitemid 28331283)
    • (1998) Protein Science , vol.7 , Issue.7 , pp. 1626-1631
    • Baumgartner, S.1    Hofmann, K.2    Chiquet-Ehrismann, R.3    Bucher, P.4
  • 13
    • 4644370369 scopus 로고    scopus 로고
    • The role of very late antigen-1 in immune-mediated inflammation
    • DOI 10.1016/j.clim.2004.06.007, PII S1521661604002037
    • Ben-Horin S, Bank I. 2004. The role of very late antigen-1 in immune-mediated inflammation. Clin. Immunol. 113:119-29 (Pubitemid 39296842)
    • (2004) Clinical Immunology , vol.113 , Issue.2 , pp. 119-129
    • Ben-Horin, S.1    Bank, I.2
  • 16
    • 70349859994 scopus 로고    scopus 로고
    • The relative roles of collagen adhesive receptor DDR2 activation and matrix stiffness on the downregulation of focal adhesion kinase in vascular smooth muscle cells
    • Bhadriraju K, Chung KH, Spurlin TA, Haynes RJ, Elliott JT, Plant AL. 2009. The relative roles of collagen adhesive receptor DDR2 activation and matrix stiffness on the downregulation of focal adhesion kinase in vascular smooth muscle cells. Biomaterials 30:6687-94
    • (2009) Biomaterials , vol.30 , pp. 6687-6694
    • Bhadriraju, K.1    Chung, K.H.2    Spurlin, T.A.3    Haynes, R.J.4    Elliott, J.T.5    Plant, A.L.6
  • 17
    • 0027476350 scopus 로고
    • Spondylo-meta-epiphyseal dysplasia (SMED), short limb-hand type: A congenital familial skeletal dysplasia with distinctive features and histopathology
    • DOI 10.1002/ajmg.1320450308
    • Borochowitz Z, Langer LO Jr, Gruber HE, Lachman R, Katznelson MB, Rimoin DL. 1993. Spondylometa-epiphyseal dysplasia (SMED), short limb-hand type: a congenital familial skeletal dysplasia with distinctive features and histopathology. Am. J. Med. Genet. 45:320-26 (Pubitemid 23033147)
    • (1993) American Journal of Medical Genetics , vol.45 , Issue.3 , pp. 320-326
    • Borochowitz, Z.1    Langer Jr., L.O.2    Gruber, H.E.3    Lachman, R.4    Katznelson -, M.B.M.5    Rimoin, D.L.6
  • 18
    • 17444415358 scopus 로고    scopus 로고
    • Molecular structure of the collagen triple helix
    • DOI 10.1016/S0065-3233(05)70009-7, Fibrous Proteins Coiled-Coils, Collagen and Elastomers
    • Brodsky B, Persikov AV. 2005. Molecular structure of the collagen triple helix. Adv. Protein Chem. 70:301-39 (Pubitemid 40544786)
    • (2005) Advances in Protein Chemistry , vol.70 , pp. 301-339
    • Brodsky, B.1    Persikov, A.V.2
  • 19
    • 77949887189 scopus 로고    scopus 로고
    • Crystal structure and collagenbinding site of immune inhibitory receptor LAIR-1: Unexpected implications for collagen binding by platelet receptor GPVI
    • Brondijk TH, de Ruiter T, Ballering J, Wienk H, Lebbink RJ, et al. 2010. Crystal structure and collagenbinding site of immune inhibitory receptor LAIR-1: unexpected implications for collagen binding by platelet receptor GPVI. Blood 115:1364-73
    • (2010) Blood , vol.115 , pp. 1364-1373
    • Brondijk, T.H.1    De Ruiter, T.2    Ballering, J.3    Wienk, H.4    Lebbink, R.J.5
  • 20
    • 71049118163 scopus 로고    scopus 로고
    • Crystallographic insight into collagen recognition by discoidin domain receptor 2
    • Carafoli F, Bihan D, Stathopoulos S, Konitsiotis AD, Kvansakul M, et al. 2009. Crystallographic insight into collagen recognition by discoidin domain receptor 2. Structure 17:1573-81
    • (2009) Structure , vol.17 , pp. 1573-1581
    • Carafoli, F.1    Bihan, D.2    Stathopoulos, S.3    Konitsiotis, A.D.4    Kvansakul, M.5
  • 21
    • 0038112077 scopus 로고    scopus 로고
    • Reciprocal signaling by integrin and nonintegrin receptors during collagen activation of platelets
    • DOI 10.1128/MCB.23.14.4764-4777.2003
    • Chen H, KahnML. 2003. Reciprocal signaling by integrin and nonintegrin receptors during collagen activation of platelets. Mol. Cell. Biol. 23:4764-77 (Pubitemid 36793324)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.14 , pp. 4764-4777
    • Chen, H.1    Kahn, M.L.2
  • 22
    • 0036314793 scopus 로고    scopus 로고
    • 2 integrin subunit-deficient mouse: A multifaceted phenotype including defects of branching morphogenesis and hemostasis
    • Chen J, Diacovo TG, Grenache DG, Santoro SA, Zutter MM. 2002. The α 2 integrin subunit-deficient mouse: a multifaceted phenotype including defects of branching morphogenesis and hemostasis. Am. J. Pathol. 161:337-44 (Pubitemid 34760799)
    • (2002) American Journal of Pathology , vol.161 , Issue.1 , pp. 337-344
    • Chen, J.1    Diacovo, T.G.2    Grenache, D.G.3    Santoro, S.A.4    Zutter, M.M.5
  • 23
    • 0141756154 scopus 로고    scopus 로고
    • Interactions between growth factor receptors and adhesion molecules: Breaking the rules
    • DOI 10.1016/S0955-0674(03)00096-6
    • Comoglio PM, Boccaccio C, Trusolino L. 2003. Interactions between growth factor receptors and adhesion molecules: breaking the rules. Curr. Opin. Cell Biol. 15:565-71 (Pubitemid 37176965)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.5 , pp. 565-571
    • Comoglio, P.M.1    Boccaccio, C.2    Trusolino, L.3
  • 24
    • 0033623532 scopus 로고    scopus 로고
    • Integrin α1β1 and transforming growth factor-β1 play distinct roles in Alport glomerular pathogenesis and serve as dual targets for metabolic therapy
    • Cosgrove D, Rodgers K, Meehan D, Miller C, Bovard K, et al. 2000. Integrin α1β1 and transforming growth factor-β1 play distinct roles in Alport glomerular pathogenesis and serve as dual targets for metabolic therapy. Am. J. Pathol. 157:1649-59
    • (2000) Am. J. Pathol. , vol.157 , pp. 1649-1659
    • Cosgrove, D.1    Rodgers, K.2    Meehan, D.3    Miller, C.4    Bovard, K.5
  • 25
    • 0036840511 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 controls growth and adhesion of mesangial cells
    • DOI 10.1097/01.ASN.0000032419.13208.0C
    • Curat CA, Vogel WF. 2002. Discoidin domain receptor 1 controls growth and adhesion of mesangial cells. J. Am. Soc. Nephrol. 13:2648-56 (Pubitemid 35216033)
    • (2002) Journal of the American Society of Nephrology , vol.13 , Issue.11 , pp. 2648-2656
    • Curat, C.A.1    Vogel, W.F.2
  • 28
    • 0027378858 scopus 로고
    • 2α2(IV)
    • Eble JA, Golbik R, Mann K, Kuhn K. 1993. The α1β1 integrin recognition site of the basement membrane collagen molecule [α1(IV)]2 α2(IV). EMBO J. 12:4795-802 (Pubitemid 23330285)
    • (1993) EMBO Journal , vol.12 , Issue.12 , pp. 4795-4802
    • Eble, J.A.1    Golbik, E.2    Mann, K.3    Kuhn, K.4
  • 30
    • 77957221459 scopus 로고    scopus 로고
    • Dynamic interplay between the collagen scaffold and tumor evolution
    • Egeblad M, Rasch MG, Weaver VM. 2010. Dynamic interplay between the collagen scaffold and tumor evolution. Curr. Opin. Cell Biol. 22:697-706
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 697-706
    • Egeblad, M.1    Rasch, M.G.2    Weaver, V.M.3
  • 35
    • 77955795080 scopus 로고    scopus 로고
    • Synthetic collagen mimics: Self-assembly of homotrimers, heterotrimers and higher order structures
    • Fallas JA, O'Leary LE, Hartgerink JD. 2010. Synthetic collagen mimics: self-assembly of homotrimers, heterotrimers and higher order structures. Chem. Soc. Rev. 39:3510-27
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 3510-3527
    • Fallas, J.A.1    O'Leary, L.E.2    Hartgerink, J.D.3
  • 36
    • 30044438639 scopus 로고    scopus 로고
    • DDR1 signaling is essential to sustain Stat5 function during lactogenesis
    • DOI 10.1002/jcb.20618
    • Faraci-Orf E, McFadden C, Vogel WF. 2006. DDR1 signaling is essential to sustain Stat5 function during lactogenesis. J. Cell. Biochem. 97:109-21 (Pubitemid 43050183)
    • (2006) Journal of Cellular Biochemistry , vol.97 , Issue.1 , pp. 109-121
    • Faraci-Orf, E.1    McFadden, C.2    Vogel, W.F.3
  • 39
    • 34250730360 scopus 로고    scopus 로고
    • Platelet receptor recognition and cross-talk in collagen-induced activation of platelets
    • DOI 10.1111/j.1538-7836.2007.02521.x, State of the Art 2007: XXI Congress of the International Society on Thrombosis and Haemostasis
    • Farndale RW, Slatter DA, Siljander PR, Jarvis GE. 2007. Platelet receptor recognition and cross-talk in collagen-induced activation of platelets. J. Thromb. Haemost. 5(Suppl. 1):220-29 (Pubitemid 46958837)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.SUPPL. 1 , pp. 220-229
    • Farndale, R.W.1    Slatter, D.A.2    Siljander, P.R.-M.3    Jarvis, G.E.4
  • 40
    • 1942469341 scopus 로고    scopus 로고
    • Role of discoidin domain receptors 1 and 2 in human smooth muscle cell-mediated collagen remodeling: Potential implications in atherosclerosis and lymphangioleiomyomatosis
    • Ferri N, Carragher NO, Raines EW. 2004. Role of discoidin domain receptors 1 and 2 in human smoothmuscle cell-mediated collagen remodeling: potential implications in atherosclerosis and lymphangioleiomyomatosis. Am. J. Pathol. 164:1575-85 (Pubitemid 38529760)
    • (2004) American Journal of Pathology , vol.164 , Issue.5 , pp. 1575-1585
    • Ferri, N.1    Carragher, N.O.2    Raines, E.W.3
  • 41
    • 77749265074 scopus 로고    scopus 로고
    • Synthesis and biological applications of collagen-model triple-helical peptides
    • Fields GB. 2010. Synthesis and biological applications of collagen-model triple-helical peptides. Org. Biomol. Chem. 8:1237-58
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 1237-1258
    • Fields, G.B.1
  • 43
    • 73349088747 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 on bone marrowderived cells promotes macrophage accumulation during atherogenesis
    • Franco C, Britto K, Wong E, Hou G, Zhu SN, et al. 2009. Discoidin domain receptor 1 on bone marrowderived cells promotes macrophage accumulation during atherogenesis. Circ. Res. 105:1141-48
    • (2009) Circ. Res. , vol.105 , pp. 1141-1148
    • Franco, C.1    Britto, K.2    Wong, E.3    Hou, G.4    Zhu, S.N.5
  • 44
    • 45149117999 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 (Ddr1) deletion decreases atherosclerosis by accelerating matrix accumulation and reducing inflammation in low-density lipoprotein receptor-deficient mice
    • Franco C, Hou G, Ahmad PJ, Fu EY, Koh L, et al. 2008. Discoidin domain receptor 1 (Ddr1) deletion decreases atherosclerosis by accelerating matrix accumulation and reducing inflammation in low-density lipoprotein receptor-deficient mice. Circ. Res. 102:1202-11
    • (2008) Circ. Res. , vol.102 , pp. 1202-1211
    • Franco, C.1    Hou, G.2    Ahmad, P.J.3    Fu, E.Y.4    Koh, L.5
  • 45
    • 0029894277 scopus 로고    scopus 로고
    • Deletion of integrin α1 by homologous recombination permits normal murine development but gives rise to a specific deficit in cell adhesion
    • DOI 10.1006/dbio.1996.0116
    • Gardner H, Kreidberg J, Koteliansky V, Jaenisch R. 1996. Deletion of integrin α1 by homologous recombination permits normal murine development but gives rise to a specific deficit in cell adhesion. Dev. Biol. 175:301-13 (Pubitemid 26160758)
    • (1996) Developmental Biology , vol.175 , Issue.2 , pp. 301-313
    • Gardner, H.1    Kreidberg, J.2    Koteliansky, V.3    Jaenisch, R.4
  • 48
    • 79959426876 scopus 로고    scopus 로고
    • Integrin α2-deficient mice provide insights into specific functions of collagen receptors in the kidney
    • Girgert R, Martin M, Kruegel J, Miosge N, Temme J, et al. 2010. Integrin α2-deficient mice provide insights into specific functions of collagen receptors in the kidney. Fibrogenesis Tissue Repair 3:19
    • (2010) Fibrogenesis Tissue Repair , vol.3 , pp. 19
    • Girgert, R.1    Martin, M.2    Kruegel, J.3    Miosge, N.4    Temme, J.5
  • 49
    • 50349096759 scopus 로고    scopus 로고
    • Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens
    • Giudici C, Raynal N, Wiedemann H, Cabral WA, Marini JC, et al. 2008. Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens. J. Biol. Chem. 283:19551-60
    • (2008) J. Biol. Chem. , vol.283 , pp. 19551-19560
    • Giudici, C.1    Raynal, N.2    Wiedemann, H.3    Cabral, W.A.4    Marini, J.C.5
  • 50
    • 0034708331 scopus 로고    scopus 로고
    • The spatial orientation of the essential amino acid residues arginine and aspartate within theα1β1 integrin recognition site of collagen IV has been resolved using fluorescence resonance energy transfer
    • Golbik R, Eble JA, Ries A, Kuhn K. 2000. The spatial orientation of the essential amino acid residues arginine and aspartate within theα1β1 integrin recognition site of collagen IV has been resolved using fluorescence resonance energy transfer. J. Mol. Biol. 297:501-9
    • (2000) J. Mol. Biol. , vol.297 , pp. 501-509
    • Golbik, R.1    Eble, J.A.2    Ries, A.3    Kuhn, K.4
  • 52
    • 77954458648 scopus 로고    scopus 로고
    • Loss of collagen-receptor DDR1 delays renal fibrosis in hereditary type IV collagen disease
    • Gross O, Girgert R, Beirowski B, Kretzler M, Kang HG, et al. 2010. Loss of collagen-receptor DDR1 delays renal fibrosis in hereditary type IV collagen disease. Matrix Biol. 29:346-56
    • (2010) Matrix Biol. , vol.29 , pp. 346-356
    • Gross, O.1    Girgert, R.2    Beirowski, B.3    Kretzler, M.4    Kang, H.G.5
  • 53
    • 34948867738 scopus 로고    scopus 로고
    • The collagen family members as cell adhesion proteins
    • DOI 10.1002/bies.20636
    • Heino J. 2007. The collagen family members as cell adhesion proteins. BioEssays 29:1001-10 (Pubitemid 47522840)
    • (2007) BioEssays , vol.29 , Issue.10 , pp. 1001-1010
    • Heino, J.1
  • 54
    • 67749124481 scopus 로고    scopus 로고
    • Structural insights into the interactions between platelet receptors and fibrillar collagen
    • Herr AB, Farndale RW. 2009. Structural insights into the interactions between platelet receptors and fibrillar collagen. J. Biol. Chem. 284:19781-85
    • (2009) J. Biol. Chem. , vol.284 , pp. 19781-19785
    • Herr, A.B.1    Farndale, R.W.2
  • 55
    • 78650512223 scopus 로고    scopus 로고
    • Collective cell migration requires suppression of actomyosin at cell-cell contacts mediated by DDR1 and the cell polarity regulators Par3 and Par6
    • Hidalgo-Carcedo C, Hooper S, Chaudhry SI, Williamson P, Harrington K, et al. 2011. Collective cell migration requires suppression of actomyosin at cell-cell contacts mediated by DDR1 and the cell polarity regulators Par3 and Par6. Nat. Cell Biol. 13:49-58
    • (2011) Nat. Cell Biol. , vol.13 , pp. 49-58
    • Hidalgo-Carcedo, C.1    Hooper, S.2    Chaudhry, S.I.3    Williamson, P.4    Harrington, K.5
  • 56
    • 39149127944 scopus 로고    scopus 로고
    • KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling
    • Hilton HN, Stanford PM, Harris J, Oakes SR, Kaplan W, et al. 2008. KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling. Biochim. Biophys. Acta 1783:383-93
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 383-393
    • Hilton, H.N.1    Stanford, P.M.2    Harris, J.3    Oakes, S.R.4    Kaplan, W.5
  • 58
    • 33746658013 scopus 로고    scopus 로고
    • Structural basis for platelet collagen responses by the immune-type receptor glycoprotein VI
    • DOI 10.1182/blood-2006-01-010215
    • Horii K, Kahn ML, Herr AB. 2006. Structural basis for platelet collagen responses by the immune-type receptor glycoprotein VI. Blood 108:936-42 (Pubitemid 44154628)
    • (2006) Blood , vol.108 , Issue.3 , pp. 936-942
    • Horii, K.1    Kahn, M.L.2    Herr, A.B.3
  • 59
    • 0035107205 scopus 로고    scopus 로고
    • The discoidin domain receptor tyrosine kinase DDR1 in arterial wound repair
    • HouG, Vogel W, Bendeck MP. 2001. The discoidin domain receptor tyrosine kinase DDR1 in arterial wound repair. J. Clin. Investig. 107:727-35. (Pubitemid 32225358)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.6 , pp. 727-735
    • Hou, G.1    Vogel, W.2    Bendeck, M.P.3
  • 61
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • Hynes R. 2002. Integrins. Bidirectional, allosteric signaling machines. Cell 110:673-87 (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 62
    • 34648819975 scopus 로고    scopus 로고
    • Structural basis of the collagen-binding mode of discoidin domain receptor 2
    • DOI 10.1038/sj.emboj.7601833, PII 7601833
    • Ichikawa O, Osawa M, Nishida N, Goshima N, Nomura N, Shimada I. 2007. Structural basis of the collagenbinding mode of discoidin domain receptor 2. EMBO J. 26:4168-76 (Pubitemid 47462092)
    • (2007) EMBO Journal , vol.26 , Issue.18 , pp. 4168-4176
    • Ichikawa, O.1    Osawa, M.2    Nishida, N.3    Goshima, N.4    Nomura, N.5    Shimada, I.6
  • 65
    • 46749100659 scopus 로고    scopus 로고
    • Identification of a major GpVI-binding locus in human type III collagen
    • Jarvis GE, Raynal N, Langford JP, Onley DJ, Andrews A, et al. 2008. Identification of a major GpVI-binding locus in human type III collagen. Blood 111:4986-96
    • (2008) Blood , vol.111 , pp. 4986-4996
    • Jarvis, G.E.1    Raynal, N.2    Langford, J.P.3    Onley, D.J.4    Andrews, A.5
  • 68
    • 67949089731 scopus 로고    scopus 로고
    • Glycoprotein (GP) VI dimer as a major collagen-binding site of native platelets: Direct evidence obtained with dimeric GPVI-specific Fabs
    • Jung SM, Tsuji K, Moroi M. 2009. Glycoprotein (GP) VI dimer as a major collagen-binding site of native platelets: direct evidence obtained with dimeric GPVI-specific Fabs. J. Thromb. Haemost. 7:1347-55
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 1347-1355
    • Jung, S.M.1    Tsuji, K.2    Moroi, M.3
  • 69
    • 0035653635 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 isoform-A (DDR1a) promotes migration of leukocytes in three-dimensional collagen lattices
    • Kamohara H, Yamashiro S, Galligan C, Yoshimura T. 2001. Discoidin domain receptor 1 isoform-a (DDR1a) promotes migration of leukocytes in three-dimensional collagen lattices. FASEB J. 15:2724-26
    • (2001) FASEB J. , vol.15 , pp. 2724-2726
    • Kamohara, H.1    Yamashiro, S.2    Galligan, C.3    Yoshimura, T.4
  • 70
    • 48249091732 scopus 로고    scopus 로고
    • A novel dwarfism with gonadal dysfunction due to loss-of-function allele of the collagen receptor gene, Ddr2, in themouse
    • Kano K, Marin de Evsikova C, Young J, Wnek C, Maddatu TP, et al. 2008. A novel dwarfism with gonadal dysfunction due to loss-of-function allele of the collagen receptor gene, Ddr2, in themouse. Mol. Endocrinol. 22:1866-80
    • (2008) Mol. Endocrinol. , vol.22 , pp. 1866-1880
    • Kano, K.1    Marin De Evsikova, C.2    Young, J.3    Wnek, C.4    Maddatu, T.P.5
  • 72
    • 0031973037 scopus 로고    scopus 로고
    • Glycoprotein VI is a major collagen receptor for platelet activation: It recognizes the platelet-activating quaternary structure of collagen, whereas CD36, glycoprotein IIb/IIIa, and von Willebrand factor do not
    • Kehrel B, Wierwille S, Clemetson KJ, Anders O, Steiner M, et al. 1998. Glycoprotein VI is a major collagen receptor for platelet activation: It recognizes the platelet-activating quaternary structure of collagen, whereas CD36, glycoprotein IIb/IIIa, and vonWillebrand factor do not. Blood 91:491-99 (Pubitemid 28053371)
    • (1998) Blood , vol.91 , Issue.2 , pp. 491-499
    • Kehrel, B.1    Wierwille, S.2    Clemetson, K.J.3    Anders, O.4    Steiner, M.5    Knight, C.G.6    Farndale, R.W.7    Okuma, M.8    Barnes, M.J.9
  • 73
    • 0027268377 scopus 로고
    • Interaction of type IV collagen with the isolated integrins α1β1 and α2β1
    • Kern A, Eble J, Golbik R, Kuhn K. 1993. Interaction of type IV collagen with the isolated integrins α1β1 and α2β1. Eur. J. Biochem. 215:151-59 (Pubitemid 23211136)
    • (1993) European Journal of Biochemistry , vol.215 , Issue.1 , pp. 151-159
    • Kern, A.1    Eble, J.2    Golbik, R.3    Kuhn, K.4
  • 74
    • 25444479366 scopus 로고    scopus 로고
    • A novel binding site in collagen type III for integrins α1β1 and α2β1
    • Kim JK, Xu Y, Xu X, Keene DR, Gurusiddappa S, et al. 2005. A novel binding site in collagen type III for integrins α1β1 and α2β1. J. Biol. Chem. 280:32512-20
    • (2005) J. Biol. Chem. , vol.280 , pp. 32512-32520
    • Kim, J.K.1    Xu, Y.2    Xu, X.3    Keene, D.R.4    Gurusiddappa, S.5
  • 75
    • 0032509342 scopus 로고    scopus 로고
    • Identification in collagen type i of an integrin α2β1-binding site containing an essential GER sequence
    • Knight CG, Morton LF, Onley DJ, Peachey AR, Messent AJ, et al. 1998. Identification in collagen type I of an integrin α2β1-binding site containing an essential GER sequence. J. Biol. Chem. 273:33287-94
    • (1998) J. Biol. Chem. , vol.273 , pp. 33287-33294
    • Knight, C.G.1    Morton, L.F.2    Onley, D.J.3    Peachey, A.R.4    Messent, A.J.5
  • 76
    • 0034614620 scopus 로고    scopus 로고
    • 1 recognize the same specific amino acid sequence, GFOGER, in native (triple- helical) collagens
    • DOI 10.1074/jbc.275.1.35
    • Knight CG, Morton LF, Peachey AR, Tuckwell DS, Farndale RW, Barnes MJ. 2000. The collagen-binding A-domains of integrins α1β1 and α2β1 recognize the same specific amino acid sequence, GFOGE R, in native (triple-helical) collagens. J. Biol. Chem. 275:35-40 (Pubitemid 30038949)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.1 , pp. 35-40
    • Knight, C.G.1    Morton, L.F.2    Peachey, A.R.3    Tuckwell, D.S.4    Farndale, R.W.5    Barnes, M.J.6
  • 78
    • 29344437297 scopus 로고    scopus 로고
    • Pinpointing phosphotyrosine-dependent interactions downstream of the collagen receptor DDR1
    • DOI 10.1016/j.febslet.2005.11.035, PII S0014579305013980
    • Koo DH, McFadden C, Huang Y, Abdulhussein R, Friese-Hamim M, Vogel WF. 2006. Pinpointing phosphotyrosine-dependent interactions downstream of the collagen receptor DDR1. FEBS Lett. 580:15-22 (Pubitemid 43005305)
    • (2006) FEBS Letters , vol.580 , Issue.1 , pp. 15-22
    • Koo, D.H.H.1    McFadden, C.2    Huang, Y.3    Abdulhussein, R.4    Friese-Hamim, M.5    Vogel, W.F.6
  • 79
    • 0037389469 scopus 로고    scopus 로고
    • Complementary roles of glycoprotein VI and α2β1 integrin in collagen-induced thrombus formation in flowing whole blood ex vivo
    • Kuijpers MJ, Schulte V, Bergmeier W, Lindhout T, Brakebusch C, et al. 2003. Complementary roles of glycoprotein VI and α2β1 integrin in collagen-induced thrombus formation in flowing whole blood ex vivo. FASEB J. 17:685-87
    • (2003) FASEB J. , vol.17 , pp. 685-687
    • Kuijpers, M.J.1    Schulte, V.2    Bergmeier, W.3    Lindhout, T.4    Brakebusch, C.5
  • 82
    • 67349140403 scopus 로고    scopus 로고
    • Identification of multiple potent binding sites for human leukocyte associated Ig-like receptor LAIR on collagens II and III
    • Lebbink RJ, Raynal N, de Ruiter T, Bihan DG, Farndale RW, Meyaard L. 2009. Identification of multiple potent binding sites for human leukocyte associated Ig-like receptor LAIR on collagens II and III. Matrix Biol. 28:202-10
    • (2009) Matrix Biol. , vol.28 , pp. 202-210
    • Lebbink, R.J.1    Raynal, N.2    De Ruiter, T.3    Bihan, D.G.4    Farndale, R.W.5    Meyaard, L.6
  • 83
    • 40749153495 scopus 로고    scopus 로고
    • The soluble leukocyteassociated Ig-like receptor (LAIR)-2 antagonizes the collagen/LAIR-1 inhibitory immune interaction
    • Lebbink RJ, Van Den Berg MC, de Ruiter T, Raynal N, Van Roon JA, et al. 2008. The soluble leukocyteassociated Ig-like receptor (LAIR)-2 antagonizes the collagen/LAIR-1 inhibitory immune interaction. J. Immunol. 180:1662-69
    • (2008) J. Immunol. , vol.180 , pp. 1662-1669
    • Lebbink, R.J.1    Van Den Berg, M.C.2    De Ruiter, T.3    Raynal, N.4    Van Roon, J.A.5
  • 85
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (I-domain): A pathway for activation?
    • DOI 10.1016/S0969-2126(01)00271-4
    • Lee J-O, Bankston LA, Arnaout MA, Liddington RC. 1995. Two conformations of the integrin A-domain (I-domain): a pathway for activation? Structure 3:1333-40 (Pubitemid 3012265)
    • (1995) Structure , vol.3 , Issue.12 , pp. 1333-1340
    • Lee, J.-O.1    Bankston, L.A.2    Arnaout, M.A.3    Liddington, R.C.4
  • 86
    • 0038607924 scopus 로고    scopus 로고
    • Molecular analysis of collagen binding by the human discoidin domain receptors, DDR1 and DDR2. Identification of collagen binding sites in DDR2
    • DOI 10.1074/jbc.M301370200
    • Leitinger B. 2003. Molecular analysis of collagen binding by the human discoidin domain receptors, DDR1 and DDR2. Identification of collagen binding sites in DDR2. J. Biol. Chem. 278:16761-69 (Pubitemid 36799543)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16761-16769
    • Leitinger, B.1
  • 87
    • 33746831573 scopus 로고    scopus 로고
    • The discoidin domain receptor DDR2 is a receptor for type X collagen
    • DOI 10.1016/j.matbio.2006.05.006, PII S0945053X06000588
    • Leitinger B, Kwan AP. 2006. The discoidin domain receptor DDR2 is a receptor for type X collagen. Matrix Biol. 25:355-64 (Pubitemid 44175833)
    • (2006) Matrix Biology , vol.25 , Issue.6 , pp. 355-364
    • Leitinger, B.1    Kwan, A.P.L.2
  • 88
    • 8544270883 scopus 로고    scopus 로고
    • The D2 period of collagen II contains a specific binding site for the human discoidin domain receptor, DDR2
    • DOI 10.1016/j.jmb.2004.09.089, PII S0022283604012604
    • Leitinger B, Steplewski A, Fertala A. 2004. The D2 period of collagen II contains a specific binding site for the human discoidin domain receptor, DDR2. J. Mol. Biol. 344:993-1003 (Pubitemid 39491245)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.4 , pp. 993-1003
    • Leitinger, B.1    Steplewski, A.2    Fertala, A.3
  • 89
    • 78349240652 scopus 로고    scopus 로고
    • Transcriptional upregulation of DDR2 by ATF4 facilitates osteoblastic differentiation through p38 MAPK-mediated Runx2 activation
    • Lin KL, Chou CH, Hsieh SC, Hwa SY, Lee MT, Wang FF. 2010. Transcriptional upregulation of DDR2 by ATF4 facilitates osteoblastic differentiation through p38 MAPK-mediated Runx2 activation. J. Bone Miner. Res. 25:2489-503
    • (2010) J. Bone Miner. Res. , vol.25 , pp. 2489-2503
    • Lin, K.L.1    Chou, C.H.2    Hsieh, S.C.3    Hwa, S.Y.4    Lee, M.T.5    Wang, F.F.6
  • 90
    • 33845268866 scopus 로고    scopus 로고
    • A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides
    • DOI 10.1182/blood-2006-03-011965
    • Lisman T, Raynal N, Groeneveld D, Maddox B, Peachey AR, et al. 2006. A single high-affinity binding site for vonWillebrand factor in collagen II I, identified using synthetic triple-helical peptides. Blood 108:3753-56 (Pubitemid 44864555)
    • (2006) Blood , vol.108 , Issue.12 , pp. 3753-3756
    • Lisman, T.1    Raynal, N.2    Groeneveld, D.3    Maddox, B.4    Peachey, A.R.5    Huizinga, E.G.6    De Groot, P.G.7    Farndale, R.W.8
  • 91
    • 78149346947 scopus 로고    scopus 로고
    • Expression of integrin β1 by fibroblasts is required for tissue repair in vivo
    • Liu S, Xu SW, Blumbach K, Eastwood M, Denton CP, et al. 2010. Expression of integrin β1 by fibroblasts is required for tissue repair in vivo. J. Cell Sci. 123:3674-82
    • (2010) J. Cell Sci. , vol.123 , pp. 3674-3682
    • Liu, S.1    Xu, S.W.2    Blumbach, K.3    Eastwood, M.4    Denton, C.P.5
  • 92
    • 79551610201 scopus 로고    scopus 로고
    • Collagen stimulates discoidin domain receptor 1-mediated migration of smooth muscle cells through Src
    • Lu KK, Trcka D, Bendeck MP. 2011. Collagen stimulates discoidin domain receptor 1-mediated migration of smooth muscle cells through Src. Cardiovasc. Pathol. 20:71-76
    • (2011) Cardiovasc. Pathol. , vol.20 , pp. 71-76
    • Lu, K.K.1    Trcka, D.2    Bendeck, M.P.3
  • 93
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • DOI 10.1146/annurev.immunol.25.022106.141618
    • Luo BH, Carman CV, Springer TA. 2007. Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 25:619-47 (Pubitemid 46697919)
    • (2007) Annual Review of Immunology , vol.25 , pp. 619-647
    • Luo, B.-H.1    Carman, C.V.2    Springer, T.A.3
  • 94
    • 51049098142 scopus 로고    scopus 로고
    • Loss of integrinα1β1 amelioratesKras-induced lung cancer
    • Macias-Perez I, Borza C, Chen X, Yan X, Ibanez R, et al. 2008. Loss of integrinα1β1 amelioratesKras-induced lung cancer. Cancer Res. 68:6127-35
    • (2008) Cancer Res. , vol.68 , pp. 6127-6135
    • MacIas-Perez, I.1    Borza, C.2    Chen, X.3    Yan, X.4    Ibanez, R.5
  • 95
    • 70350494479 scopus 로고    scopus 로고
    • Distinct spatio-temporal Ca2+ signaling elicited by integrin α2β1 and glycoprotein VI under flow
    • Mazzucato M, Cozzi MR, Battiston M, Jandrot-Perrus M, Mongiat M, et al. 2009. Distinct spatio-temporal Ca2+ signaling elicited by integrin α2β1 and glycoprotein VI under flow. Blood 114:2793-801
    • (2009) Blood , vol.114 , pp. 2793-2801
    • Mazzucato, M.1    Cozzi, M.R.2    Battiston, M.3    Jandrot-Perrus, M.4    Mongiat, M.5
  • 96
    • 44449101289 scopus 로고    scopus 로고
    • The inhibitory collagen receptor LAIR-1 (CD305)
    • DOI 10.1189/jlb.0907609
    • Meyaard L. 2008. The inhibitory collagen receptor LAIR-1 (CD305). J. Leukoc. Biol. 83:799-803 (Pubitemid 351959858)
    • (2008) Journal of Leukocyte Biology , vol.83 , Issue.4 , pp. 799-803
    • Meyaard, L.1
  • 98
    • 58149096469 scopus 로고    scopus 로고
    • Mapping of DDR1 distribution and oligomerization on the cell surface by FRET microscopy
    • Mihai C, Chotani M, Elton TS, Agarwal G. 2009. Mapping of DDR1 distribution and oligomerization on the cell surface by FRET microscopy. J. Mol. Biol. 385:432-45
    • (2009) J. Mol. Biol. , vol.385 , pp. 432-445
    • Mihai, C.1    Chotani, M.2    Elton, T.S.3    Agarwal, G.4
  • 99
    • 2242455042 scopus 로고    scopus 로고
    • Analysis of the interaction of platelet collagen receptor glycoprotein VI (GPVI) with collagen: A dimeric form of GPVI, but not the monomeric form, shows affinity to fibrous collagen
    • DOI 10.1074/jbc.M204029200
    • Miura Y, Takahashi T, Jung SM, Moroi M. 2002. Analysis of the interaction of platelet collagen receptor glycoprotein VI (GPVI) with collagen. A dimeric form of GPV I, but not the monomeric form, shows affinity to fibrous collagen. J. Biol. Chem. 277:46197-204 (Pubitemid 35417611)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46197-46204
    • Miura, Y.1    Takahashi, T.2    Jung, S.M.3    Moroi, M.4
  • 100
    • 4644262225 scopus 로고    scopus 로고
    • Platelet glycoprotein VI: Its structure and function
    • DOI 10.1016/j.thromres.2004.06.046, PII S0049384804003780
    • Moroi M, Jung SM. 2004. Platelet glycoprotein VI: its structure and function. Thromb. Res. 114:221-33 (Pubitemid 39286008)
    • (2004) Thrombosis Research , vol.114 , Issue.4 , pp. 221-233
    • Moroi, M.1    Jung, S.M.2
  • 101
    • 0028986390 scopus 로고
    • Integrin α2β1-independent activation of platelets by simple collagen-like peptides: Collagen tertiary (triple-helical) and quaternary (polymeric) structures are sufficient alone for α2β1-independent platelet reactivity
    • Morton LF, Hargreaves PG, Farndale RW, Young RD, Barnes MJ. 1995. Integrin α2β1-independent activation of platelets by simple collagen-like peptides: collagen tertiary (triple-helical) and quaternary (polymeric) structures are sufficient alone for α2β1-independent platelet reactivity. Biochem. J. 306:337-44
    • (1995) Biochem. J. , vol.306 , pp. 337-344
    • Morton, L.F.1    Hargreaves, P.G.2    Farndale, R.W.3    Young, R.D.4    Barnes, M.J.5
  • 102
    • 0028351682 scopus 로고
    • Conformation-dependent platelet adhesion to collagen involving integrin α2β1-mediated and other mechanisms: Multiple α2β1- recognition sites in collagen type I
    • Morton LF, Peachey AR, Zijenah LS, Goodall AH, Humphries MJ, Barnes MJ. 1994. Conformationdependent platelet adhesion to collagen involving integrin α2β1-mediated and other mechanisms: multiple α2β1- recognition sites in collagen type I. Biochem. J. 299:791-97 (Pubitemid 24138550)
    • (1994) Biochemical Journal , vol.299 , Issue.3 , pp. 791-797
    • Morton, L.F.1    Peachey, A.R.2    Zijenah, L.S.3    Goodall, A.H.4    Humphries, M.J.5    Barnes, M.J.6
  • 103
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • DOI 10.1016/j.tig.2003.11.004
    • Myllyharju J, Kivirikko KI. 2004. Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet. 20:33-43 (Pubitemid 38032818)
    • (2004) Trends in Genetics , vol.20 , Issue.1 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 104
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: Is GPVI the central receptor?
    • DOI 10.1182/blood-2002-12-3882
    • Nieswandt B, Watson SP. 2003. Platelet-collagen interaction: Is GPVI the central receptor? Blood 102:449-61 (Pubitemid 36841960)
    • (2003) Blood , vol.102 , Issue.2 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 105
    • 33747330131 scopus 로고    scopus 로고
    • A transmembrane leucine zipper is required for activation of the dimeric receptor tyrosine kinase DDR1
    • Noordeen NA, Carafoli F, Hohenester E, Horton MA, Leitinger B. 2006. A transmembrane leucine zipper is required for activation of the dimeric receptor tyrosine kinase DDR1. J. Biol. Chem. 281:22744-51
    • (2006) J. Biol. Chem. , vol.281 , pp. 22744-22751
    • Noordeen, N.A.1    Carafoli, F.2    Hohenester, E.3    Horton, M.A.4    Leitinger, B.5
  • 106
    • 67749109933 scopus 로고    scopus 로고
    • High-resolution structures of collagenlike peptides [(Pro-Pro-Gly) 4-Xaa-Yaa-Gly-(Pro-Pro-Gly)4]: Implications for triple-helix hydration and Hyp(X) puckering
    • Okuyama K, Hongo C, Wu G, Mizuno K, Noguchi K, et al. 2009. High-resolution structures of collagenlike peptides [(Pro-Pro-Gly)4-Xaa-Yaa-Gly- (Pro-Pro-Gly)4]: implications for triple-helix hydration and Hyp(X) puckering. Biopolymers 91:361-72
    • (2009) Biopolymers , vol.91 , pp. 361-372
    • Okuyama, K.1    Hongo, C.2    Wu, G.3    Mizuno, K.4    Noguchi, K.5
  • 108
    • 0036479206 scopus 로고    scopus 로고
    • Discoidin domain receptor 2 regulates fibroblast proliferation and migration through the extracellular matrix in association with transcriptional activation of matrix metalloproteinase-2
    • DOI 10.1074/jbc.M107571200
    • Olaso E, Labrador JP, Wang L, Ikeda K, Eng FJ, et al. 2002. Discoidin domain receptor 2 regulates fibroblast proliferation and migration through the extracellular matrix in association with transcriptional activation of matrix metalloproteinase-2. J. Biol. Chem. 277:3606-13 (Pubitemid 34953233)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3606-3613
    • Olaso, E.1    Labrador, J.-P.2    Wang, L.3    Ikeda, K.4    Eng, F.J.5    Klein, R.6    Lovett, D.H.7    Lin, H.C.8    Friedman, S.L.9
  • 112
    • 0030953664 scopus 로고    scopus 로고
    • Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (Tropical rattlesnake) venom via the p62/GPVI collagen receptor
    • DOI 10.1074/jbc.272.21.13576
    • Polgar J, Clemetson JM, Kehrel BE, Wiedemann M, Magnenat EM, et al. 1997. Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor. J. Biol. Chem. 272:13576-83 (Pubitemid 27224788)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.21 , pp. 13576-13583
    • Polgar, J.1    Clemetson, J.M.2    Kehrel, B.E.3    Wiedemann, M.4    Magnenat, E.M.5    Wells, T.N.C.6    Clemetson, K.J.7
  • 114
    • 34250643243 scopus 로고    scopus 로고
    • Physiology and pathology of collagen receptors
    • DOI 10.1111/j.1748-1716.2007.01718.x
    • Popova SN, Lundgren-Akerlund E, Wiig H, Gullberg D. 2007b. Physiology and pathology of collagen receptors. Acta Physiol. 190:179-87 (Pubitemid 46934663)
    • (2007) Acta Physiologica , vol.190 , Issue.3 , pp. 179-187
    • Popova, S.N.1    Lundgren-Akerlund, E.2    Wiig, H.3    Gullberg, D.4
  • 116
    • 0032572410 scopus 로고    scopus 로고
    • Integrin α1β1 mediates a unique collagen-dependent proliferation pathway in vivo
    • DOI 10.1083/jcb.142.2.587
    • Pozzi A, Wary KK, Giancotti FG, Gardner HA. 1998. Integrin α1β1 mediates a unique collagen-dependent proliferation pathway in vivo. J. Cell Biol. 142:587-94 (Pubitemid 28361562)
    • (1998) Journal of Cell Biology , vol.142 , Issue.2 , pp. 587-594
    • Pozzi, A.1    Wary, K.K.2    Giancotti, F.G.3    Gardner, H.A.4
  • 117
    • 77953922179 scopus 로고    scopus 로고
    • Synergism between platelet collagen receptors defined using receptor-specific collagen-mimetic peptide substrata in flowing blood
    • Pugh N, Simpson AM, Smethurst PA, de Groot PG, Raynal N, Farndale RW. 2010. Synergism between platelet collagen receptors defined using receptor-specific collagen-mimetic peptide substrata in flowing blood. Blood 115:5069-79
    • (2010) Blood , vol.115 , pp. 5069-5079
    • Pugh, N.1    Simpson, A.M.2    Smethurst, P.A.3    De Groot, P.G.4    Raynal, N.5    Farndale, R.W.6
  • 118
    • 0028822128 scopus 로고
    • Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αlβ2) integrin
    • Qu A, Leahy DJ. 1995. Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αLβ2) integrin. Proc. Natl. Acad. Sci. USA 92:10277-81
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10277-10281
    • Qu, A.1    Leahy, D.J.2
  • 119
    • 33645320530 scopus 로고    scopus 로고
    • Discoidin domain receptor-1a (DDR1a) promotes glioma cell invasion and adhesion in association with matrix metalloproteinase-2
    • Ram R, Lorente G, Nikolich K, Urfer R, Foehr E, Nagavarapu U. 2006. Discoidin domain receptor-1a (DDR1a) promotes glioma cell invasion and adhesion in association with matrix metalloproteinase-2. J. Neurooncol. 76:239-48
    • (2006) J. Neurooncol. , vol.76 , pp. 239-248
    • Ram, R.1    Lorente, G.2    Nikolich, K.3    Urfer, R.4    Foehr, E.5    Nagavarapu, U.6
  • 121
    • 34250818668 scopus 로고    scopus 로고
    • Adhesion mechanisms in platelet function
    • DOI 10.1161/01.RES.0000267878.97021.ab, PII 0000301220070622000003
    • Ruggeri ZM, Mendolicchio GL. 2007. Adhesion mechanisms in platelet function. Circ. Res. 100:1673-85 (Pubitemid 46987859)
    • (2007) Circulation Research , vol.100 , Issue.12 , pp. 1673-1685
    • Ruggeri, Z.M.1    Mendolicchio, G.L.2
  • 122
    • 23744472080 scopus 로고    scopus 로고
    • 1 play independent critical roles during platelet adhesion and aggregate formation to collagen under flow
    • DOI 10.1182/blood-2004-11-4434
    • Sarratt KL, Chen H, Zutter MM, Santoro SA, Hammer DA, Kahn ML. 2005. GPVI and α2β1 play independent critical roles during platelet adhesion and aggregate formation to collagen under flow. Blood 106:1268-77 (Pubitemid 41129590)
    • (2005) Blood , vol.106 , Issue.4 , pp. 1268-1277
    • Sarratt, K.L.1    Chen, H.2    Zutter, M.M.3    Santoro, S.A.4    Hammer, D.A.5    Kahn, M.L.6
  • 123
    • 41549155540 scopus 로고    scopus 로고
    • Collagen I-mediated up-regulation of N-cadherin requires cooperative signals from integrins and discoidin domain receptor
    • DOI 10.1083/jcb.200708137
    • Shintani Y, Fukumoto Y, Chaika N, Svoboda R, Wheelock MJ, Johnson KR. 2008. Collagen I-mediated up-regulation of N-cadherin requires cooperative signals from integrins and discoidin domain receptor 1. J. Cell Biol. 180:1277-89 (Pubitemid 351468480)
    • (2008) Journal of Cell Biology , vol.180 , Issue.6 , pp. 1277-1289
    • Shintani, Y.1    Fukumoto, Y.2    Chaika, N.3    Svoboda, R.4    Wheelock, M.J.5    Johnson, K.R.6
  • 128
    • 33847736329 scopus 로고    scopus 로고
    • Structural basis for the platelet-collagen interaction: The smallest motif within collagen that recognizes and activates platelet Glycoprotein VI contains two glycine-proline-hydroxyproline triplets
    • DOI 10.1074/jbc.M606479200
    • Smethurst PA, Onley DJ, Jarvis GE, O'Connor MN, Knight CG, et al. 2007. Structural basis for the plateletcollagen interaction: the smallest motifwithin collagen that recognizes and activates platelet Glycoprotein VI contains two glycine-proline-hydroxyproline triplets. J. Biol. Chem. 282:1296-304 (Pubitemid 47076576)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.2 , pp. 1296-1304
    • Smethurst, P.A.1    Onley, D.J.2    Jarvis, G.E.3    O'Connor, M.N.4    Graham Knight, C.5    Herr, A.B.6    Ouwehand, W.H.7    Farndale, R.W.8
  • 129
    • 73349114585 scopus 로고    scopus 로고
    • Discoidin domain receptor 2 is associated with the increased expression of matrix metalloproteinase-13 in synovial fibroblasts of rheumatoid arthritis
    • Su J, Yu J, Ren T, Zhang W, Zhang Y, et al. 2009. Discoidin domain receptor 2 is associated with the increased expression of matrix metalloproteinase-13 in synovial fibroblasts of rheumatoid arthritis. Mol. Cell. Biochem. 330:141-52
    • (2009) Mol. Cell. Biochem. , vol.330 , pp. 141-152
    • Su, J.1    Yu, J.2    Ren, T.3    Zhang, W.4    Zhang, Y.5
  • 130
    • 66949165900 scopus 로고    scopus 로고
    • A single residue, arginine 65, is critical for the functional interaction of leukocyte-associated inhibitory receptor-1 with collagens
    • Tang X, Narayanan S, Peruzzi G, Apara A, Natarajan K, et al. 2009. A single residue, arginine 65, is critical for the functional interaction of leukocyte-associated inhibitory receptor-1 with collagens. J. Immunol. 182:5446-52
    • (2009) J. Immunol. , vol.182 , pp. 5446-5452
    • Tang, X.1    Narayanan, S.2    Peruzzi, G.3    Apara, A.4    Natarajan, K.5
  • 131
    • 0035437863 scopus 로고    scopus 로고
    • α11β1 integrin is a receptor for interstitial collagens involved in cell migration and collagen reorganization on mesenchymal nonmuscle cells
    • DOI 10.1006/dbio.2001.0363
    • Tiger CF, Fougerousse F, Grundstrom G, Velling T, Gullberg D. 2001. α11β1 integrin is a receptor for interstitial collagens involved in cell migration and collagen reorganization on mesenchymal nonmuscle cells. Dev. Biol. 237:116-29 (Pubitemid 32844310)
    • (2001) Developmental Biology , vol.237 , Issue.1 , pp. 116-129
    • Tiger, C.-F.1    Fougerousse, F.2    Grundstrom, G.3    Velling, T.4    Gullberg, D.5
  • 133
    • 0035930611 scopus 로고    scopus 로고
    • Selective binding of collagen subtypes by integrin α1I, α2I, and α10I domains
    • Tulla M, Pentikainen OT, Viitasalo T, Kapyla J, Impola U, et al. 2001. Selective binding of collagen subtypes by integrin α1I, α2I, and α10I domains. J. Biol. Chem. 276:48206-12
    • (2001) J. Biol. Chem. , vol.276 , pp. 48206-48212
    • Tulla, M.1    Pentikainen, O.T.2    Viitasalo, T.3    Kapyla, J.4    Impola, U.5
  • 135
    • 30944456522 scopus 로고    scopus 로고
    • Leukocyte-associated Ig-like receptor-1 SH2 domain-containing phosphatase-independent function and recruits C-terminal Src kinase
    • DOI 10.1002/eji.200535226
    • Verbrugge A, Rijkers ES, de Ruiter T, Meyaard L. 2006. Leukocyte-associated Ig-like receptor-1 has SH2 domain-containing phosphatase-independent function and recruits C-terminal Src kinase. Eur. J. Immunol. 36:190-98 (Pubitemid 43116405)
    • (2006) European Journal of Immunology , vol.36 , Issue.1 , pp. 190-198
    • Verbrugge, A.1    Rijkers, E.S.K.2    De Ruiter, T.3    Meyaard, L.4
  • 137
    • 0031309902 scopus 로고    scopus 로고
    • The discoidin domain receptor tyrosine kinases are activated by collagen
    • Vogel W, Gish GD, Alves F, Pawson T. 1997. The discoidin domain receptor tyrosine kinases are activated by collagen. Mol. Cell 1:13-23 (Pubitemid 127376389)
    • (1997) Molecular Cell , vol.1 , Issue.1 , pp. 13-23
    • Vogel, W.1    Gish, G.D.2    Alves, F.3    Pawson, T.4
  • 138
    • 33646341752 scopus 로고    scopus 로고
    • Sensing extracellular matrix: An update on discoidin domain receptor function
    • DOI 10.1016/j.cellsig.2006.02.012, PII S0898656806000477
    • Vogel WF, Abdulhussein R, Ford CE. 2006. Sensing extracellular matrix: an update on discoidin domain receptor function. Cell. Signal. 18:1108-16 (Pubitemid 43674043)
    • (2006) Cellular Signalling , vol.18 , Issue.8 , pp. 1108-1116
    • Vogel, W.F.1    Abdulhussein, R.2    Ford, C.E.3
  • 139
    • 0035085253 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 tyrosine kinase has an essential role in mammary gland development
    • DOI 10.1128/MCB.21.8.2906-2917.2001
    • Vogel WF, Aszodi A, Alves F, Pawson T. 2001. Discoidin domain receptor 1 tyrosine kinase has an essential role in mammary gland development. Mol. Cell. Biol. 21:2906-17 (Pubitemid 32244933)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.8 , pp. 2906-2917
    • Vogel, W.F.1    Aszodi, A.2    Alves, F.3    Pawson, T.4
  • 140
    • 28844477778 scopus 로고    scopus 로고
    • Discoidin domain receptor 2 mediates tumor cell cycle arrest induced by fibrillar collagen
    • DOI 10.1074/jbc.M508226200
    • Wall SJ, Werner E, Werb Z, DeClerck YA. 2005. Discoidin domain receptor 2 mediates tumor cell cycle arrest induced by fibrillar collagen. J. Biol. Chem. 280:40187-94 (Pubitemid 41779155)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 40187-40194
    • Wall, S.J.1    Werner, E.2    Werb, Z.3    DeClerck, Y.A.4
  • 141
    • 14744272604 scopus 로고    scopus 로고
    • Function of discoidin domain receptor i in HGF-induced branching tubulogenesis of MDCK cells in collagen gel
    • Wang CZ, Hsu YM, Tang MJ. 2005. Function of discoidin domain receptor I in HGF-induced branching tubulogenesis of MDCK cells in collagen gel. J. Cell. Physiol. 203:295-304
    • (2005) J. Cell. Physiol. , vol.203 , pp. 295-304
    • Wang, C.Z.1    Hsu, Y.M.2    Tang, M.J.3
  • 142
    • 33744764925 scopus 로고    scopus 로고
    • A discoidin domain receptor 1/SHP-2 signaling complex inhibitsα2β1-integrin-mediated signal transducers and activators of transcription 1/3 activation and cell migration
    • Wang CZ, Su HW, Hsu YC, Shen MR, Tang MJ. 2006. A discoidin domain receptor 1/SHP-2 signaling complex inhibitsα2β1-integrin-mediated signal transducers and activators of transcription 1/3 activation and cell migration. Mol. Biol. Cell 17:2839-52
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2839-2852
    • Wang, C.Z.1    Su, H.W.2    Hsu, Y.C.3    Shen, M.R.4    Tang, M.J.5
  • 143
    • 68849099260 scopus 로고    scopus 로고
    • DDR1/E-cadherin complex regulates the activation of DDR1 and cell spreading
    • Wang CZ, Yeh YC, Tang MJ. 2009. DDR1/E-cadherin complex regulates the activation of DDR1 and cell spreading. Am. J. Physiol. Cell Physiol. 297:C419-29
    • (2009) Am. J. Physiol. Cell Physiol. , vol.297
    • Wang, C.Z.1    Yeh, Y.C.2    Tang, M.J.3
  • 146
    • 38349140682 scopus 로고    scopus 로고
    • Integrin α2β1 is the required receptor for endorepellin angiostatic activity
    • Woodall BP, Nystrom A, Iozzo RA, Eble JA, Niland S, et al. 2008. Integrin α2β1 is the required receptor for endorepellin angiostatic activity. J. Biol. Chem. 283:2335-43
    • (2008) J. Biol. Chem. , vol.283 , pp. 2335-2343
    • Woodall, B.P.1    Nystrom, A.2    Iozzo, R.A.3    Eble, J.A.4    Niland, S.5
  • 147
    • 78951473449 scopus 로고    scopus 로고
    • Collagen binding specificity of the discoidin domain receptors: Binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1
    • Xu H, Raynal N, Stathopoulos S, Myllyharju J, Farndale RW, Leitinger B. 2011. Collagen binding specificity of the discoidin domain receptors: binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1. Matrix Biol. 30:16-26
    • (2011) Matrix Biol. , vol.30 , pp. 16-26
    • Xu, H.1    Raynal, N.2    Stathopoulos, S.3    Myllyharju, J.4    Farndale, R.W.5    Leitinger, B.6
  • 148
    • 34547783916 scopus 로고    scopus 로고
    • Increased expression of the collagen receptor discoidin domain receptor 2 in articular cartilage as a key event in the pathogenesis of osteoarthritis
    • DOI 10.1002/art.22761
    • Xu L, Peng H, Glasson S, Lee PL, Hu K, et al. 2007. Increased expression of the collagen receptor discoidin domain receptor 2 in articular cartilage as a key event in the pathogenesis of osteoarthritis. Arthritis Rheum. 56:2663-73 (Pubitemid 47237284)
    • (2007) Arthritis and Rheumatism , vol.56 , Issue.8 , pp. 2663-2673
    • Xu, L.1    Peng, H.2    Glasson, S.3    Lee, P.L.4    Hu, K.5    Ijiri, K.6    Olsen, B.R.7    Goldring, M.B.8    Li, Y.9
  • 149
    • 77956369628 scopus 로고    scopus 로고
    • Attenuation of osteoarthritis progression by reduction of discoidin domain receptor 2 in mice
    • Xu L, Servais J, Polur I, Kim D, Lee PL, et al. 2010. Attenuation of osteoarthritis progression by reduction of discoidin domain receptor 2 in mice. Arthritis Rheum. 62:2736-44
    • (2010) Arthritis Rheum. , vol.62 , pp. 2736-2744
    • Xu, L.1    Servais, J.2    Polur, I.3    Kim, D.4    Lee, P.L.5
  • 150
    • 0034671734 scopus 로고    scopus 로고
    • Multiple binding sites in collagen type i for the integrins α1β1 and α2β1
    • Xu Y, Gurusiddappa S, Rich RL, Owens RT, Keene DR, et al. 2000. Multiple binding sites in collagen type I for the integrins α1β1 and α2β1. J. Biol. Chem. 275:38981-89
    • (2000) J. Biol. Chem. , vol.275 , pp. 38981-38989
    • Xu, Y.1    Gurusiddappa, S.2    Rich, R.L.3    Owens, R.T.4    Keene, D.R.5
  • 151
    • 28244437005 scopus 로고    scopus 로고
    • Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src stimulates intramolecular autophosphorylation and Shc signaling complex formation
    • DOI 10.1074/jbc.M506921200
    • Yang K, Kim JH, Kim HJ, Park IS, Kim IY, Yang BS. 2005. Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src stimulates intramolecular autophosphorylation and Shc signaling complex formation. J. Biol. Chem. 280:39058-66 (Pubitemid 41713856)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39058-39066
    • Yang, K.1    Kim, J.H.2    Kim, H.J.3    Park, I.-S.4    Kim, I.Y.5    Yang, B.-S.6
  • 152
    • 58149142702 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 activation suppresses α2β1 integrindependent cell spreading through inhibition of Cdc42 activity
    • Yeh YC, Wang CZ, Tang MJ. 2009. Discoidin domain receptor 1 activation suppresses α2β1 integrindependent cell spreading through inhibition of Cdc42 activity. J. Cell. Physiol. 218:146-56
    • (2009) J. Cell. Physiol. , vol.218 , pp. 146-156
    • Yeh, Y.C.1    Wang, C.Z.2    Tang, M.J.3
  • 153
    • 33846990969 scopus 로고    scopus 로고
    • Enhancement of pituitary adenoma cell invasion and adhesion is mediated by discoidin domain receptor-1
    • Yoshida D, Teramoto A. 2007. Enhancement of pituitary adenoma cell invasion and adhesion is mediated by discoidin domain receptor-1. J. Neurooncol. 82:29-40
    • (2007) J. Neurooncol. , vol.82 , pp. 29-40
    • Yoshida, D.1    Teramoto, A.2
  • 154
    • 0142072319 scopus 로고    scopus 로고
    • Accelerated, Aging-Dependent Development of Osteoarthritis in α1 Integrin-Deficient Mice
    • DOI 10.1002/art.11246
    • Zemmyo M, Meharra EJ, Kuhn K, Creighton-Achermann L, Lotz M. 2003. Accelerated, aging-dependent development of osteoarthritis in α1 integrin-deficient mice. Arthritis Rheum. 48:2873-80 (Pubitemid 37280616)
    • (2003) Arthritis and Rheumatism , vol.48 , Issue.10 , pp. 2873-2880
    • Zemmyo, M.1    Meharra, E.J.2    Kuhn, K.3    Creighton-Achermann, L.4    Lotz, M.5
  • 156
    • 79951847897 scopus 로고    scopus 로고
    • An essential role of discoidin domain receptor 2 (DDR2) in osteoblast differentiation and chondrocyte maturation via modulation of Runx2 activation
    • Zhang Y, Su J, Yu J, Bu X, Ren T, et al. 2011. An essential role of discoidin domain receptor 2 (DDR2) in osteoblast differentiation and chondrocyte maturation via modulation of Runx2 activation. J. Bone Miner. Res. 26:604-17
    • (2011) J. Bone Miner. Res. , vol.26 , pp. 604-617
    • Zhang, Y.1    Su, J.2    Yu, J.3    Bu, X.4    Ren, T.5
  • 157
    • 41349111883 scopus 로고    scopus 로고
    • α2β1 integrin expression in the tumor microenvironment enhances tumor angiogenesis in a tumor cell-specific manner
    • DOI 10.1182/blood-2007-06-094680
    • Zhang Z, Ramirez NE, Yankeelov TE, Li Z, Ford LE, et al. 2008. α2β1 integrin expression in the tumor microenvironment enhances tumor angiogenesis in a tumor cell-specific manner. Blood 111:1980-88 (Pubitemid 351451508)
    • (2008) Blood , vol.111 , Issue.4 , pp. 1980-1988
    • Zhang, Z.1    Ramirez, N.E.2    Yankeelov, T.E.3    Li, Z.4    Ford, L.E.5    Qi, Y.6    Pozzi, A.7    Zutter, M.M.8
  • 159
    • 34249752194 scopus 로고    scopus 로고
    • The α2β1 integrin: A novel collectin/C1q receptor
    • DOI 10.1016/j.imbio.2006.11.013, PII S0171298506001483
    • Zutter MM, Edelson BT. 2007. Theα2β1 integrin: a novel collectin/C1q receptor. Immunobiology 212:343-53 (Pubitemid 46825240)
    • (2007) Immunobiology , vol.212 , Issue.4-5 , pp. 343-353
    • Zutter, M.M.1    Edelson, B.T.2


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