메뉴 건너뛰기




Volumn 288, Issue 17, 2013, Pages 12114-12129

Shedding of discoidin domain receptor 1 by membrane-type matrix metalloproteinases

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL FRAGMENTS; MATRIX METALLOPROTEINASES; METALLOPROTEINASE INHIBITORS; MUTATIONAL ANALYSIS; N-TERMINAL SEQUENCING; PROTEOLYTIC ACTIVITIES; RECEPTOR TYROSINE KINASE; SIGNAL TRANSDUCTION PATHWAYS;

EID: 84876922252     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.409599     Document Type: Article
Times cited : (73)

References (54)
  • 1
    • 80054036560 scopus 로고    scopus 로고
    • Transmembrane collagen receptors
    • Leitinger, B. (2011) Transmembrane collagen receptors. Annu. Rev. Cell Dev. Biol. 27, 265-290
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 265-290
    • Leitinger, B.1
  • 3
    • 33646341752 scopus 로고    scopus 로고
    • Sensing extracellular matrix: An update on discoidin domain receptor function
    • Vogel, W. F., Abdulhussein, R., and Ford, C. E. (2006) Sensing extracellular matrix: an update on discoidin domain receptor function. Cell. Signal. 18, 1108-1116
    • (2006) Cell. Signal. , vol.18 , pp. 1108-1116
    • Vogel, W.F.1    Abdulhussein, R.2    Ford, C.E.3
  • 4
    • 0031309902 scopus 로고    scopus 로고
    • The discoidin domain receptor tyrosine kinases are activated by collagen
    • Vogel, W., Gish, G. D., Alves, F., and Pawson, T. (1997) The discoidin domain receptor tyrosine kinases are activated by collagen. Mol. Cell 1, 13-23
    • (1997) Mol. Cell , vol.1 , pp. 13-23
    • Vogel, W.1    Gish, G.D.2    Alves, F.3    Pawson, T.4
  • 6
    • 8544270883 scopus 로고    scopus 로고
    • The D2 period of collagen II contains a specific binding site for the human discoidin domain receptor, DDR2
    • Leitinger, B., Steplewski, A., and 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
    • (2004) J. Mol. Biol. , vol.344 , pp. 993-1003
    • Leitinger, B.1    Steplewski, A.2    Fertala, A.3
  • 7
    • 33746831573 scopus 로고    scopus 로고
    • The discoidin domain receptor DDR2 is a receptor for type X collagen
    • Leitinger, B., and Kwan, A. P. (2006) The discoidin domain receptor DDR2 is a receptor for type X collagen. Matrix Biol. 25, 355-364
    • (2006) Matrix Biol. , vol.25 , pp. 355-364
    • Leitinger, B.1    Kwan, A.P.2
  • 8
    • 0035107205 scopus 로고    scopus 로고
    • The discoidin domain receptor tyrosine kinase DDR1 in arterial wound repair
    • Hou, G., Vogel, W., and Bendeck, M. P. (2001) The discoidin domain receptor tyrosine kinase DDR1 in arterial wound repair. J. Clin. Invest. 107, 727-735
    • (2001) J. Clin. Invest. , vol.107 , pp. 727-735
    • Hou, G.1    Vogel, W.2    Bendeck, M.P.3
  • 9
    • 0038607924 scopus 로고    scopus 로고
    • Molecular analysis of collagen binding by the human discoidin domain receptors, DDR1 and DDR2. Identification of collagenbinding sites in DDR2
    • Leitinger, B. (2003) Molecular analysis of collagen binding by the human discoidin domain receptors, DDR1 and DDR2. Identification of collagenbinding sites in DDR2. J. Biol. Chem. 278, 16761-16769
    • (2003) J. Biol. Chem. , vol.278 , pp. 16761-16769
    • Leitinger, B.1
  • 10
    • 42449119742 scopus 로고    scopus 로고
    • Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen
    • Konitsiotis, A. D., Raynal, N., Bihan, D., Hohenester, E., Farndale, R. W., and Leitinger, B. (2008) Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen. J. Biol. Chem. 283, 6861-6868
    • (2008) J. Biol. Chem. , vol.283 , pp. 6861-6868
    • Konitsiotis, A.D.1    Raynal, N.2    Bihan, D.3    Hohenester, E.4    Farndale, R.W.5    Leitinger, B.6
  • 11
    • 78951473449 scopus 로고    scopus 로고
    • Collagen binding specificity of the discoidin domain receptors: Binding sitesoncollagens II and III and molecular determinants for collagen IV recognition by DDR1
    • Xu, H., Raynal, N., Stathopoulos, S., Myllyharju, J., Farndale, R. W., and Leitinger, B. (2011) Collagen binding specificity of the discoidin domain receptors: binding sitesoncollagens 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
  • 13
    • 84859414321 scopus 로고    scopus 로고
    • Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory Fab fragment reveals features important for signaling
    • Carafoli, F., Mayer, M. C., Shiraishi, K., Pecheva, M. A., Chan, L. Y., Nan, R., Leitinger, B., and Hohenester, E. (2012) Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory Fab fragment reveals features important for signaling. Structure 20, 688-697
    • (2012) Structure , vol.20 , pp. 688-697
    • Carafoli, F.1    Mayer, M.C.2    Shiraishi, K.3    Pecheva, M.A.4    Chan, L.Y.5    Nan, R.6    Leitinger, B.7    Hohenester, E.8
  • 14
    • 3843108034 scopus 로고    scopus 로고
    • Exploring the collagen-binding site of the DDR1 tyrosine kinase receptor
    • Abdulhussein, R., McFadden, C., Fuentes-Prior, P., and Vogel, W. F. (2004) Exploring the collagen-binding site of the DDR1 tyrosine kinase receptor. J. Biol. Chem. 279, 31462-31470
    • (2004) J. Biol. Chem. , vol.279 , pp. 31462-31470
    • Abdulhussein, R.1    McFadden, C.2    Fuentes-Prior, P.3    Vogel, W.F.4
  • 15
    • 45549088677 scopus 로고    scopus 로고
    • Identification of disulfide-linked dimers of the receptor tyrosine kinase DDR1
    • Abdulhussein, R., Koo, D. H., and Vogel, W. F. (2008) Identification of disulfide-linked dimers of the receptor tyrosine kinase DDR1. J. Biol. Chem. 283, 12026-12033
    • (2008) J. Biol. Chem. , vol.283 , pp. 12026-12033
    • Abdulhussein, R.1    Koo, D.H.2    Vogel, W.F.3
  • 16
    • 0036391436 scopus 로고    scopus 로고
    • Matrix metalloproteinases and collagen catabolism
    • Lauer-Fields, J. L., Juska, D., and Fields, G. B. (2002) Matrix metalloproteinases and collagen catabolism. Biopolymers 66, 19-32
    • (2002) Biopolymers , vol.66 , pp. 19-32
    • Lauer-Fields, J.L.1    Juska, D.2    Fields, G.B.3
  • 18
    • 0038784546 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix
    • Hotary, K. B., Allen, E. D., Brooks, P. C., Datta, N. S., Long, M. W., and Weiss, S. J. (2003) Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix. Cell 114, 33-45
    • (2003) Cell , vol.114 , pp. 33-45
    • Hotary, K.B.1    Allen, E.D.2    Brooks, P.C.3    Datta, N.S.4    Long, M.W.5    Weiss, S.J.6
  • 19
    • 70350233406 scopus 로고    scopus 로고
    • Navigating ECM barriers at the invasive front: The cancer cell-stroma interface
    • Rowe, R. G., and Weiss, S. J. (2009) Navigating ECM barriers at the invasive front: the cancer cell-stroma interface. Annu. Rev. Cell Dev. Biol. 25, 567-595
    • (2009) Annu. Rev. Cell Dev. Biol. , vol.25 , pp. 567-595
    • Rowe, R.G.1    Weiss, S.J.2
  • 20
    • 47749156773 scopus 로고    scopus 로고
    • The inactive 44-kDa processed form of membrane type 1 matrix metalloproteinase (MT1-MMP) enhances proteolytic activity via regulation of endocytosis of active MT1-MMP
    • Cho, J. A., Osenkowski, P., Zhao, H., Kim, S., Toth, M., Cole, K., Aboukameel, A., Saliganan, A., Schuger, L., Bonfil, R. D., and Fridman, R. (2008) The inactive 44-kDa processed form of membrane type 1 matrix metalloproteinase (MT1-MMP) enhances proteolytic activity via regulation of endocytosis of active MT1-MMP. J. Biol. Chem. 283, 17391-17405
    • (2008) J. Biol. Chem. , vol.283 , pp. 17391-17405
    • Cho, J.A.1    Osenkowski, P.2    Zhao, H.3    Kim, S.4    Toth, M.5    Cole, K.6    Aboukameel, A.7    Saliganan, A.8    Schuger, L.9    Bonfil, R.D.10    Fridman, R.11
  • 21
    • 0034697144 scopus 로고    scopus 로고
    • Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation
    • Hernandez-Barrantes, S., Toth, M., Bernardo, M. M., Yurkova, M., Gervasi, D. C., Raz, Y., Sang, Q. A., and Fridman, R. (2000) Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation. J. Biol. Chem. 275, 12080-12089
    • (2000) J. Biol. Chem. , vol.275 , pp. 12080-12089
    • Hernandez-Barrantes, S.1    Toth, M.2    Bernardo, M.M.3    Yurkova, M.4    Gervasi, D.C.5    Raz, Y.6    Sang, Q.A.7    Fridman, R.8
  • 23
    • 0034607873 scopus 로고    scopus 로고
    • Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases
    • Lauer-Fields, J. L., Tuzinski, K. A., Shimokawa Ki, Nagase, H., and Fields, G. B. (2000) Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases. J. Biol. Chem. 275, 13282-13290
    • (2000) J. Biol. Chem. , vol.275 , pp. 13282-13290
    • Lauer-Fields, J.L.1    Tuzinski, K.A.2    Ki, S.3    Nagase, H.4    Fields, G.B.5
  • 24
    • 0030669224 scopus 로고    scopus 로고
    • Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2
    • Olson, M. W., Gervasi, D. C., Mobashery, S., and Fridman, R. (1997) Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2. J. Biol. Chem. 272, 29975-29983
    • (1997) J. Biol. Chem. , vol.272 , pp. 29975-29983
    • Olson, M.W.1    Gervasi, D.C.2    Mobashery, S.3    Fridman, R.4
  • 25
    • 17644390235 scopus 로고    scopus 로고
    • Cleavage at the stem region releases an active ectodomain of the membrane type 1 matrix metalloproteinase
    • Toth, M., Osenkowski, P., Hesek, D., Brown, S., Meroueh, S., Sakr, W., Mobashery, S., and Fridman, R. (2005) Cleavage at the stem region releases an active ectodomain of the membrane type 1 matrix metalloproteinase. Biochem. J. 387, 497-506
    • (2005) Biochem. J. , vol.387 , pp. 497-506
    • Toth, M.1    Osenkowski, P.2    Hesek, D.3    Brown, S.4    Meroueh, S.5    Sakr, W.6    Mobashery, S.7    Fridman, R.8
  • 27
    • 33749350351 scopus 로고    scopus 로고
    • A cancer cell metalloprotease triad regulates the basement membrane transmigration program
    • Hotary, K., Li, X. Y., Allen, E., Stevens, S. L., and Weiss, S. J. (2006) A cancer cell metalloprotease triad regulates the basement membrane transmigration program. Genes Dev. 20, 2673-2686
    • (2006) Genes Dev. , vol.20 , pp. 2673-2686
    • Hotary, K.1    Li, X.Y.2    Allen, E.3    Stevens, S.L.4    Weiss, S.J.5
  • 28
    • 0031189711 scopus 로고    scopus 로고
    • Molecular recognition of proteinligand complexes: Applications to drug design
    • Babine, R. E., and Bender, S. L. (1997) Molecular recognition of proteinligand complexes: applications to drug design. Chem. Rev. 97, 1359-1472
    • (1997) Chem. Rev. , vol.97 , pp. 1359-1472
    • Babine, R.E.1    Bender, S.L.2
  • 29
    • 77149154385 scopus 로고    scopus 로고
    • Matrixmetalloproteinases: Fold and function of their catalytic domains
    • Tallant, C., Marrero, A., and Gomis-Rüth, F. X. (2010) Matrixmetalloproteinases: fold and function of their catalytic domains. Biochim. Biophys. Acta 1803, 20-28
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 20-28
    • Tallant, C.1    Marrero, A.2    Gomis-Rüth, F.X.3
  • 30
    • 0036480050 scopus 로고    scopus 로고
    • Functional analysis of discoidin domain receptor 1: Effect of adhesion on DDR1 phosphorylation
    • L'Hôte, C. G., Thomas, P. H., and Ganesan, T. S. (2002) Functional analysis of discoidin domain receptor 1: effect of adhesion on DDR1 phosphorylation. FASEBJ. 16, 234-236
    • (2002) FASEBJ. , vol.16 , pp. 234-236
    • L'Hôte, C.G.1    Thomas, P.H.2    Ganesan, T.S.3
  • 32
    • 0028838862 scopus 로고
    • Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor
    • Grams, F., Crimmin, M., Hinnes, L., Huxley, P., Pieper, M., Tschesche, H., and Bode, W. (1995) Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor. Biochemistry 34, 14012-14020
    • (1995) Biochemistry , vol.34 , pp. 14012-14020
    • Grams, F.1    Crimmin, M.2    Hinnes, L.3    Huxley, P.4    Pieper, M.5    Tschesche, H.6    Bode, W.7
  • 34
    • 63649141727 scopus 로고    scopus 로고
    • The "a disintegrin and metalloprotease" (ADAM) family of sheddases: Physiological and cellular functions
    • Reiss, K., and Saftig, P. (2009) The "a disintegrin and metalloprotease" (ADAM) family of sheddases: physiological and cellular functions. Semin. Cell Dev. Biol. 20, 126-137
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 126-137
    • Reiss, K.1    Saftig, P.2
  • 35
    • 33646581410 scopus 로고    scopus 로고
    • Collagen type I selectively activates ectodomain shedding of the discoidin domain receptor 1: Involvement of Src tyrosine kinase
    • Slack, B. E., Siniaia, M. S., and Blusztajn, J. K. (2006) Collagen type I selectively activates ectodomain shedding of the discoidin domain receptor 1: involvement of Src tyrosine kinase. J. Cell. Biochem. 98, 672-684
    • (2006) J. Cell. Biochem. , vol.98 , pp. 672-684
    • Slack, B.E.1    Siniaia, M.S.2    Blusztajn, J.K.3
  • 36
    • 81255188391 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases
    • Murphy, G. (2011) Tissue inhibitors of metalloproteinases. Genome Biol. 12, 233
    • (2011) Genome Biol. , vol.12 , pp. 233
    • Murphy, G.1
  • 37
    • 65549120390 scopus 로고    scopus 로고
    • ADAM-10-mediated N-cadherin cleavage is protein kinase C-alpha dependent and promotes glioblastoma cell migration
    • Kohutek, Z. A., diPierro, C. G., Redpath, G. T., and Hussaini, I. M. (2009) ADAM-10-mediated N-cadherin cleavage is protein kinase C-alpha dependent and promotes glioblastoma cell migration. J. Neurosci. 29, 4605-4615
    • (2009) J. Neurosci. , vol.29 , pp. 4605-4615
    • Kohutek, Z.A.1    DiPierro, C.G.2    Redpath, G.T.3    Hussaini, I.M.4
  • 38
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • Arribas, J., and Borroto, A. (2002) Protein ectodomain shedding. Chem. Rev. 102, 4627-4638
    • (2002) Chem. Rev. , vol.102 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 40
    • 79960102280 scopus 로고    scopus 로고
    • Ectodomain shedding and remnant peptide signalling of EGFRs and their ligands
    • Higashiyama, S., Nanba, D., Nakayama, H., Inoue, H., and Fukuda, S. (2011) Ectodomain shedding and remnant peptide signalling of EGFRs and their ligands. J. Biochem. 150, 15-22
    • (2011) J. Biochem. , vol.150 , pp. 15-22
    • Higashiyama, S.1    Nanba, D.2    Nakayama, H.3    Inoue, H.4    Fukuda, S.5
  • 41
    • 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., Höfler, H., and Ullrich, A. (1995) Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer. Oncogene 10, 609-618
    • (1995) Oncogene , vol.10 , pp. 609-618
    • Alves, F.1    Vogel, W.2    Mossie, K.3    Millauer, B.4    Höfler, H.5    Ullrich, A.6
  • 42
    • 0037070593 scopus 로고    scopus 로고
    • Ligand-induced shedding of discoidin domain receptor 1
    • Vogel, W. F. (2002) Ligand-induced shedding of discoidin domain receptor 1. FEBS Lett. 514, 175-180
    • (2002) FEBS Lett. , vol.514 , pp. 175-180
    • Vogel, W.F.1
  • 43
    • 0038771156 scopus 로고    scopus 로고
    • Tales from the crypt[ic] sites of the extracellular matrix
    • Schenk, S., and Quaranta, V. (2003) Tales from the crypt[ic] sites of the extracellular matrix. Trends Cell Biol. 13, 366-375
    • (2003) Trends Cell Biol. , vol.13 , pp. 366-375
    • Schenk, S.1    Quaranta, V.2
  • 44
    • 80054799662 scopus 로고    scopus 로고
    • Exosite interactions impact matrix metalloproteinase collagen specificities
    • Robichaud, T. K., Steffensen, B., and Fields, G. B. (2011) Exosite interactions impact matrix metalloproteinase collagen specificities. J. Biol. Chem. 286, 37535-37542
    • (2011) J. Biol. Chem. , vol.286 , pp. 37535-37542
    • Robichaud, T.K.1    Steffensen, B.2    Fields, G.B.3
  • 45
    • 0037189494 scopus 로고    scopus 로고
    • A unique substrate binding mode discriminates membrane type-1 matrix metalloproteinase from other matrix metalloproteinases
    • Kridel, S. J., Sawai, H., Ratnikov, B. I., Chen, E. I., Li, W., Godzik, A., Strongin, A. Y., and Smith, J. W. (2002) A unique substrate binding mode discriminates membrane type-1 matrix metalloproteinase from other matrix metalloproteinases. J. Biol. Chem. 277, 23788-23793
    • (2002) J. Biol. Chem. , vol.277 , pp. 23788-23793
    • Kridel, S.J.1    Sawai, H.2    Ratnikov, B.I.3    Chen, E.I.4    Li, W.5    Godzik, A.6    Strongin, A.Y.7    Smith, J.W.8
  • 46
    • 0033590212 scopus 로고    scopus 로고
    • Identification of substrate sequences for membrane type-1 matrix metalloproteinase using bacteriophage peptide display library
    • Ohkubo, S., Miyadera, K., Sugimoto, Y., Matsuo, K., Wierzba, K., and Yamada, Y. (1999) Identification of substrate sequences for membrane type-1 matrix metalloproteinase using bacteriophage peptide display library. Biochem. Biophys. Res. Commun. 266, 308-313
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 308-313
    • Ohkubo, S.1    Miyadera, K.2    Sugimoto, Y.3    Matsuo, K.4    Wierzba, K.5    Yamada, Y.6
  • 47
    • 47949123468 scopus 로고    scopus 로고
    • Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: Dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding
    • Butler, G. S., Dean, R. A., Tam, E. M., and Overall, C. M. (2008) Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding. Mol. Cell. Biol. 28, 4896-4914
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4896-4914
    • Butler, G.S.1    Dean, R.A.2    Tam, E.M.3    Overall, C.M.4
  • 48
    • 2342460878 scopus 로고    scopus 로고
    • Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates
    • Tam, E. M., Morrison, C. J., Wu, Y. I., Stack, M. S., and Overall, C. M. (2004) Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl. Acad. Sci. U. S. A. 101, 6917-6922
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6917-6922
    • Tam, E.M.1    Morrison, C.J.2    Wu, Y.I.3    Stack, M.S.4    Overall, C.M.5
  • 49
    • 67449104704 scopus 로고    scopus 로고
    • High throughput analysis of proteins associating with a proinvasive MT1-MMP in human malignant melanoma A375 cells
    • Tomari, T., Koshikawa, N., Uematsu, T., Shinkawa, T., Hoshino, D., Egawa, N., Isobe, T., and Seiki, M. (2009) High throughput analysis of proteins associating with a proinvasive MT1-MMP in human malignant melanoma A375 cells. Cancer Sci. 100, 1284-1290
    • (2009) Cancer Sci. , vol.100 , pp. 1284-1290
    • Tomari, T.1    Koshikawa, N.2    Uematsu, T.3    Shinkawa, T.4    Hoshino, D.5    Egawa, N.6    Isobe, T.7    Seiki, M.8
  • 50
    • 77953151717 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of ectodomain shedding
    • Hayashida, K., Bartlett, A. H., Chen, Y., and Park, P. W. (2010) Molecular and cellular mechanisms of ectodomain shedding. Anat. Rec. 293, 925-937
    • (2010) Anat. Rec. , vol.293 , pp. 925-937
    • Hayashida, K.1    Bartlett, A.H.2    Chen, Y.3    Park, P.W.4
  • 51
    • 33847122893 scopus 로고    scopus 로고
    • Interaction of discoidin domain receptor 1 with collagen type 1
    • Agarwal, G., Mihai, C., and Iscru, D. F. (2007) Interaction of discoidin domain receptor 1 with collagen type 1. J. Mol. Biol. 367, 443-455
    • (2007) J. Mol. Biol. , vol.367 , pp. 443-455
    • Agarwal, G.1    Mihai, C.2    Iscru, D.F.3
  • 52
    • 73249126900 scopus 로고    scopus 로고
    • Inhibition of collagen fibrillogenesis by cells expressing soluble extracellular domains of DDR1 and DDR2
    • Flynn, L. A., Blissett, A. R., Calomeni, E. P., and Agarwal, G. (2010) Inhibition of collagen fibrillogenesis by cells expressing soluble extracellular domains of DDR1 and DDR2. J. Mol. Biol. 395, 533-543
    • (2010) J. Mol. Biol. , vol.395 , pp. 533-543
    • Flynn, L.A.1    Blissett, A.R.2    Calomeni, E.P.3    Agarwal, G.4
  • 53
    • 77952322732 scopus 로고    scopus 로고
    • Implication of discoidin domain receptor 1 in T cell migration in three-dimensional collagen
    • Hachehouche, L. N., Chetoui, N., and Aoudjit, F. (2010) Implication of discoidin domain receptor 1 in T cell migration in three-dimensional collagen. Mol. Immunol. 47, 1866-1869
    • (2010) Mol. Immunol. , vol.47 , pp. 1866-1869
    • Hachehouche, L.N.1    Chetoui, N.2    Aoudjit, F.3
  • 54
    • 67349106681 scopus 로고    scopus 로고
    • Proteolytic cleavages give receptor tyrosine kinases the gift of ubiquity
    • Ancot, F., Foveau, B., Lefebvre, J., Leroy, C., and Tulasne, D. (2009) Proteolytic cleavages give receptor tyrosine kinases the gift of ubiquity. Oncogene 28, 2185-2195
    • (2009) Oncogene , vol.28 , pp. 2185-2195
    • Ancot, F.1    Foveau, B.2    Lefebvre, J.3    Leroy, C.4    Tulasne, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.