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Volumn 6, Issue 11, 2011, Pages 1232-1243

Targeting multiple conformations leads to small molecule inhibitors of the uPAR•uPA protein-protein interaction that block cancer cell invasion

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACID DERIVATIVE; UROKINASE; UROKINASE RECEPTOR;

EID: 81555208984     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb200180m     Document Type: Article
Times cited : (52)

References (52)
  • 1
    • 0031031050 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator-deficient mice are predisposed to staphylococcal botryomycosis, pleuritis, and effacement of lymphoid follicles
    • Shapiro, R. L., Duquette, J. G., Nunes, I., Roses, D. F., Harris, M. N., Wilson, E. L., and Rifkin, D. B. (1997) Urokinase-type plasminogen activator-deficient mice are predisposed to staphylococcal botryomycosis, pleuritis, and effacement of lymphoid follicles Am. J. Pathol. 150, 359-369 (Pubitemid 27027125)
    • (1997) American Journal of Pathology , vol.150 , Issue.1 , pp. 359-369
    • Shapiro, R.L.1    Duquette, J.G.2    Nunes, I.3    Roses, D.F.4    Harris, M.N.5    Lynette Wilson, E.6    Rifkin, D.B.7
  • 2
    • 33747098638 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator induces proliferation in breast cancer cells
    • Gandhari, M., Arens, N., Majety, M., Dorn-Beineke, A., and Hildenbrand, R. (2006) Urokinase-type plasminogen activator induces proliferation in breast cancer cells Int. J. Oncol. 28, 1463-1470
    • (2006) Int. J. Oncol. , vol.28 , pp. 1463-1470
    • Gandhari, M.1    Arens, N.2    Majety, M.3    Dorn-Beineke, A.4    Hildenbrand, R.5
  • 3
    • 56249141793 scopus 로고    scopus 로고
    • RNAi-mediated downregulation of urokinase plasminogen activator receptor inhibits proliferation, adhesion, migration and invasion in oral cancer cells
    • Liang, X., Yang, X., Tang, Y., Zhou, H., Liu, X., Xiao, L., Gao, J., and Mao, Z. (2008) RNAi-mediated downregulation of urokinase plasminogen activator receptor inhibits proliferation, adhesion, migration and invasion in oral cancer cells Oral Oncol. 44, 1172-1180
    • (2008) Oral Oncol. , vol.44 , pp. 1172-1180
    • Liang, X.1    Yang, X.2    Tang, Y.3    Zhou, H.4    Liu, X.5    Xiao, L.6    Gao, J.7    Mao, Z.8
  • 4
    • 33747137698 scopus 로고    scopus 로고
    • RNAi-mediated downregulation of urokinase plasminogen activator and its receptor in human meningioma cells inhibits tumor invasion and growth
    • Kondraganti, S., Gondi, C. S., McCutcheon, I., Dinh, D. H., Gujrati, M., Rao, J. S., and Olivero, W. C. (2006) RNAi-mediated downregulation of urokinase plasminogen activator and its receptor in human meningioma cells inhibits tumor invasion and growth Int. J. Oncol. 28, 1353-1360
    • (2006) Int. J. Oncol. , vol.28 , pp. 1353-1360
    • Kondraganti, S.1    Gondi, C.S.2    McCutcheon, I.3    Dinh, D.H.4    Gujrati, M.5    Rao, J.S.6    Olivero, W.C.7
  • 5
    • 3042784666 scopus 로고    scopus 로고
    • Vascular endothelial growth factor receptor-2-induced initial endothelial cell migration depends on the presence of the urokinase receptor
    • DOI 10.1161/01.RES.0000131498.36194.6b
    • Prager, G. W., Breuss, J. M., Steurer, S., Olcaydu, D., Mihaly, J., Brunner, P. M., Stockinger, H., and Binder, B. R. (2004) Vascular endothelial growth factor receptor-2-induced initial endothelial cell migration depends on the presence of the urokinase receptor Circ. Res. 94, 1562-1570 (Pubitemid 38856963)
    • (2004) Circulation Research , vol.94 , Issue.12 , pp. 1562-1570
    • Prager, G.W.1    Breuss, J.M.2    Steurer, S.3    Olcaydu, D.4    Mihaly, J.5    Brunner, P.M.6    Stockinger, H.7    Binder, B.R.8
  • 6
    • 64049103845 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor 2 receptor limits cell invasion by controlling alphaVbeta3 integrin expression and proteolytic processing of urokinase-type plasminogen activator receptor
    • Schiller, H. B., Szekeres, A., Binder, B. R., Stockinger, H., and Leksa, V. (2009) Mannose 6-phosphate/insulin-like growth factor 2 receptor limits cell invasion by controlling alphaVbeta3 integrin expression and proteolytic processing of urokinase-type plasminogen activator receptor Mol. Biol. Cell 20, 745-756
    • (2009) Mol. Biol. Cell , vol.20 , pp. 745-756
    • Schiller, H.B.1    Szekeres, A.2    Binder, B.R.3    Stockinger, H.4    Leksa, V.5
  • 7
    • 0030788411 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator system in cancer metastasis: A review
    • DOI 10.1002/(SICI)1097-0215(19970703)72:1<1::AID-IJC1>3.0.CO;2-Z
    • Andreasen, P. A., Kjoller, L., Christensen, L., and Duffy, M. J. (1997) The urokinase-type plasminogen activator system in cancer metastasis: A review Int. J. Cancer 72, 1-22 (Pubitemid 27314632)
    • (1997) International Journal of Cancer , vol.72 , Issue.1 , pp. 1-22
    • Andreasen, P.A.1    Kjoller, L.2    Christensen, L.3    Duffy, M.J.4
  • 8
    • 0029943568 scopus 로고    scopus 로고
    • Plasminogen activators and matrix metalloproteinases in angiogenesis
    • Mignatti, P. and Rifkin, D. B. (1996) Plasminogen activators and matrix metalloproteinases in angiogenesis Enzyme Protein 49, 117-137 (Pubitemid 26181742)
    • (1996) Enzyme and Protein , vol.49 , Issue.1-3 , pp. 117-137
    • Mignatti, P.1    Rifkin, D.B.2
  • 9
    • 0034996039 scopus 로고    scopus 로고
    • The role of the plasminogen activation system in angiogenesis and metastasis
    • Rabbani, S. A. and Mazar, A. P. (2001) The role of the plasminogen activation system in angiogenesis and metastasis Surg. Oncol. Clin. N. Am. 10, 393-415 (Pubitemid 32472537)
    • (2001) Surgical Oncology Clinics of North America , vol.10 , Issue.2 , pp. 393-415
    • Rabbani, S.A.1    Mazar, A.P.2
  • 10
    • 33744725239 scopus 로고    scopus 로고
    • SiRNA-mediated simultaneous downregulation of uPA and its receptor inhibits angiogenesis and invasiveness triggering apoptosis in breast cancer cells
    • Subramanian, R., Gondi, C. S., Lakka, S. S., Jutla, A., and Rao, J. S. (2006) siRNA-mediated simultaneous downregulation of uPA and its receptor inhibits angiogenesis and invasiveness triggering apoptosis in breast cancer cells Int. J. Oncol. 28, 831-839
    • (2006) Int. J. Oncol. , vol.28 , pp. 831-839
    • Subramanian, R.1    Gondi, C.S.2    Lakka, S.S.3    Jutla, A.4    Rao, J.S.5
  • 11
    • 35348905119 scopus 로고    scopus 로고
    • RNAi-mediated downregulation of urokinase plasminogen activator receptor and matrix metalloprotease-9 in human breast cancer cells results in decreased tumor invasion, angiogenesis and growth
    • DOI 10.1002/ijc.22962
    • Kunigal, S., Lakka, S. S., Gondi, C. S., Estes, N., and Rao, J. S. (2007) RNAi-mediated downregulation of urokinase plasminogen activator receptor and matrix metalloprotease-9 in human breast cancer cells results in decreased tumor invasion, angiogenesis and growth Int. J. Cancer 121, 2307-2316 (Pubitemid 47585614)
    • (2007) International Journal of Cancer , vol.121 , Issue.10 , pp. 2307-2316
    • Kunigal, S.1    Lakka, S.S.2    Gondi, C.S.3    Estes, N.4    Rao, J.S.5
  • 13
    • 20044363847 scopus 로고    scopus 로고
    • Urokinase-induced signaling in human vascular smooth muscle cells is mediated by PDGFR-β
    • DOI 10.1038/sj.emboj.7600669
    • Kiyan, J., Kiyan, R., Haller, H., and Dumler, I. (2005) Urokinase-induced signaling in human vascular smooth muscle cells is mediated by PDGFR-beta EMBO J. 24, 1787-1797 (Pubitemid 40769498)
    • (2005) EMBO Journal , vol.24 , Issue.10 , pp. 1787-1797
    • Kiyan, J.1    Kiyan, R.2    Haller, H.3    Dumler, I.4
  • 14
    • 0036596352 scopus 로고    scopus 로고
    • EGFR is a transducer of the urokinase receptor initiated signal that is required for in vivo growth of a human carcinoma
    • DOI 10.1016/S1535-6108(02)00072-7
    • Liu, D., Aguirre Ghiso, J., Estrada, Y., and Ossowski, L. (2002) EGFR is a transducer of the urokinase receptor initiated signal that is required for in vivo growth of a human carcinoma Cancer Cell 1, 445-457 (Pubitemid 41039125)
    • (2002) Cancer Cell , vol.1 , Issue.5 , pp. 445-457
    • Liu, D.1    Aguirre Ghiso, J.A.2    Estrada, Y.3    Ossowski, L.4
  • 16
    • 53249122047 scopus 로고    scopus 로고
    • Urokinase plasminogen activator receptor choreographs multiple ligand interactions: Implications for tumor progression and therapy
    • Mazar, A. P. (2008) Urokinase plasminogen activator receptor choreographs multiple ligand interactions: implications for tumor progression and therapy Clin. Cancer Res. 14, 5649-5655
    • (2008) Clin. Cancer Res. , vol.14 , pp. 5649-5655
    • Mazar, A.P.1
  • 17
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin, M. R. and Wells, J. A. (2004) Small-molecule inhibitors of protein-protein interactions: progressing towards the dream Nature Rev. 3, 301-317 (Pubitemid 38499758)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.4 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 18
    • 0028064814 scopus 로고
    • Structure-function relationships in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom alpha-neurotoxins
    • Ploug, M. and Ellis, V. (1994) Structure-function relationships in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom alpha-neurotoxins FEBS Lett. 349, 163-168
    • (1994) FEBS Lett. , vol.349 , pp. 163-168
    • Ploug, M.1    Ellis, V.2
  • 19
    • 33745808779 scopus 로고    scopus 로고
    • Characterization of the functional epitope on the urokinase receptor: Complete alanine scanning mutagenesis supplemented by chemical cross-linking
    • DOI 10.1074/jbc.M513583200
    • Gardsvoll, H., Gilquin, B., Le Du, M. H., Menez, A., Jorgensen, T. J., and Ploug, M. (2006) Characterization of the functional epitope on the urokinase receptor. Complete alanine scanning mutagenesis supplemented by chemical cross-linking J. Biol. Chem. 281, 19260-19272 (Pubitemid 44035430)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.28 , pp. 19260-19272
    • Gardsvoll, H.1    Gilquin, B.2    Le Du, M.H.3    Menez, A.4    Jorgensen, T.J.D.5    Ploug, M.6
  • 21
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells, J. A. and McClendon, C. L. (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces Nature 450, 1001-1009 (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 28
    • 43149092276 scopus 로고    scopus 로고
    • Principles of protein-protein interactions: What are the preferred ways for proteins to interact?
    • DOI 10.1021/cr040409x
    • Keskin, Z., Gursoy, A., Ma, B., and Nussinov, R. (2008) Principles of protein-protein interactions: What are the preferred ways for proteins to interact? Chem. Rev. 108, 1225-1244 (Pubitemid 351638814)
    • (2008) Chemical Reviews , vol.108 , Issue.4 , pp. 1225-1244
    • Keskin, O.1    Gursoy, A.2    Ma, B.3    Nussinov, R.4
  • 30
    • 41949132916 scopus 로고    scopus 로고
    • Flexible ligand docking to multiple receptor conformations: A practical alternative
    • Totrov, M. and Abagyan, R. (2008) Flexible ligand docking to multiple receptor conformations: a practical alternative Curr. Opin. Struct. Biol. 18, 178-184
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 178-184
    • Totrov, M.1    Abagyan, R.2
  • 31
    • 33846419101 scopus 로고    scopus 로고
    • A new tagging system for production of recombinant proteins in Drosophila S2 cells using the third domain of the urokinase receptor
    • DOI 10.1016/j.pep.2006.11.013, PII S1046592806003883
    • Gardsvoll, H., Hansen, L. V., Jorgensen, T. J., and Ploug, M. (2007) A new tagging system for production of recombinant proteins in Drosophila S2 cells using the third domain of the urokinase receptor Protein Expression Purif. 52, 384-394 (Pubitemid 46150136)
    • (2007) Protein Expression and Purification , vol.52 , Issue.2 , pp. 384-394
    • Gardsvoll, H.1    Hansen, L.V.2    Jorgensen, T.J.D.3    Ploug, M.4
  • 32
    • 0038678483 scopus 로고    scopus 로고
    • Suppression of the cell proliferation and invasion phenotypes in glioma cells by the LGI1 gene
    • DOI 10.1038/sj.onc.1206584
    • Kunapuli, P., Chitta, K. S., and Cowell, J. K. (2003) Suppression of the cell proliferation and invasion phenotypes in glioma cells by the LGI1 gene Oncogene 22, 3985-3991 (Pubitemid 36819638)
    • (2003) Oncogene , vol.22 , Issue.26 , pp. 3985-3991
    • Kunapuli, P.1    Chitta, K.S.2    Cowell, J.K.3
  • 33
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • DOI 10.1006/jmbi.1998.2401
    • Word, J. M., Lovell, S. C., Richardson, J. S., and Richardson, D. C. (1999) Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation J. Mol. Biol. 285, 1735-1747 (Pubitemid 29060467)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 34
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner, M. F. (1999) Python: A programming language for software integration and development J. Mol. Graphics Modell. 17, 57-61 (Pubitemid 30029318)
    • (1999) Journal of Molecular Graphics and Modelling , vol.17 , Issue.1 , pp. 57-61
    • Sanner, M.F.1
  • 36
    • 13844312649 scopus 로고    scopus 로고
    • ZINC - A free database of commercially available compounds for virtual screening
    • DOI 10.1021/ci049714+
    • Irwin, J. J. and Shoichet, B. K. (2005) ZINC-A free database of commercially available compounds for virtual screening J. Chem. Inf. Model. 45, 177-182 (Pubitemid 40736970)
    • (2005) Journal of Chemical Information and Modeling , vol.45 , Issue.1 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 39
    • 38049089909 scopus 로고    scopus 로고
    • A computational investigation of allostery in the catabolite activator protein
    • Li, L., Uversky, V. N., Dunker, A. K., and Meroueh, S. O. (2007) A computational investigation of allostery in the catabolite activator protein J. Am. Chem. Soc. 129, 15668-15676
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15668-15676
    • Li, L.1    Uversky, V.N.2    Dunker, A.K.3    Meroueh, S.O.4
  • 40
    • 0031891022 scopus 로고    scopus 로고
    • Computation of electrostatic complements to proteins: A case of charge stabilized binding
    • Chong, L. T., Dempster, S. E., Hendsch, Z. S., Lee, L. P., and Tidor, B. (1998) Computation of electrostatic complements to proteins: a case of charge stabilized binding Protein Sci. 7, 206-210 (Pubitemid 28133762)
    • (1998) Protein Science , vol.7 , Issue.1 , pp. 206-210
    • Chong, L.T.1    Dempster, S.E.2    Hendsch, Z.S.3    Lee, L.-P.4    Tidor, B.5
  • 41
    • 0036890178 scopus 로고    scopus 로고
    • Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and Validation
    • Jakalian, A., Jack, D. B., and Bayly, B. I. (2002) Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and Validation J. Comput. Chem. 23, 18
    • (2002) J. Comput. Chem. , vol.23 , pp. 18
    • Jakalian, A.1    Jack, D.B.2    Bayly, B.I.3
  • 42
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • Gohlke, H., Kiel, C., and Case, D. A. (2003) Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes J. Mol. Biol. 330, 891-913
    • (2003) J. Mol. Biol. , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 43
    • 33750013699 scopus 로고    scopus 로고
    • Synthesis of 3-alkyl-5-arylamino-6,11-dihydro-3 H -anthra[1,2- d ]-[1,2,3]triazole-6,11-dione 2-oxides by nitrosation of 3-alkyl-amino-5- arylamino-6 H -anthra[1,9- cd ]isoxazol-6-ones
    • Gornostaev, L. A., DoIgushina, L. V., Titova, N. G., Arnol'd, E. V., and Lavrikova, T. I. (2006) Synthesis of 3-alkyl-5-arylamino-6,11-dihydro-3 H -anthra[1,2- d ]-[1,2,3]triazole-6,11-dione 2-oxides by nitrosation of 3-alkyl-amino-5-arylamino-6 H -anthra[1,9- cd ]isoxazol-6-ones Russ. J. Org. Chem. 42, 1364-1367
    • (2006) Russ. J. Org. Chem. , vol.42 , pp. 1364-1367
    • Gornostaev, L.A.1    Doigushina, L.V.2    Titova, N.G.3    Arnol'D, E.V.4    Lavrikova, T.I.5
  • 44
    • 70849088180 scopus 로고    scopus 로고
    • An atypical role for collapsin response mediator protein 2 (CRMP-2) in neurotransmitter release via interaction with presynaptic voltage-gated calcium channels
    • Brittain, J. M., Piekarz, A. D., Wang, Y., Kondo, T., Cummins, T. R., and Khanna, R. (2009) An atypical role for collapsin response mediator protein 2 (CRMP-2) in neurotransmitter release via interaction with presynaptic voltage-gated calcium channels J. Biol. Chem. 284, 31375-31390
    • (2009) J. Biol. Chem. , vol.284 , pp. 31375-31390
    • Brittain, J.M.1    Piekarz, A.D.2    Wang, Y.3    Kondo, T.4    Cummins, T.R.5    Khanna, R.6
  • 45
    • 33751321865 scopus 로고    scopus 로고
    • A detergent-based assay for the detection of promiscuous inhibitors
    • Feng, B. Y. and Shoichet, B. K. (2006) A detergent-based assay for the detection of promiscuous inhibitors Nat. Protoc. 1, 550-553
    • (2006) Nat. Protoc. , vol.1 , pp. 550-553
    • Feng, B.Y.1    Shoichet, B.K.2
  • 46
    • 59849095562 scopus 로고    scopus 로고
    • Exploring the molecular design of protein interaction sites with molecular dynamics simulations and free energy calculations
    • Liang, S., Li, L., Hsu, W. L., Pilcher, M. N., Uversky, V., Zhou, Y., Dunker, A. K., and Meroueh, S. O. (2009) Exploring the molecular design of protein interaction sites with molecular dynamics simulations and free energy calculations Biochemistry 48, 399-414
    • (2009) Biochemistry , vol.48 , pp. 399-414
    • Liang, S.1    Li, L.2    Hsu, W.L.3    Pilcher, M.N.4    Uversky, V.5    Zhou, Y.6    Dunker, A.K.7    Meroueh, S.O.8
  • 47
    • 75849162018 scopus 로고    scopus 로고
    • Incorporating receptor flexibility in the molecular design of protein interfaces
    • Li, L., Liang, S., Pilcher, M. M., and Meroueh, S. O. (2009) Incorporating receptor flexibility in the molecular design of protein interfaces Protein Eng., Des. Sel. 22, 575-586
    • (2009) Protein Eng., Des. Sel. , vol.22 , pp. 575-586
    • Li, L.1    Liang, S.2    Pilcher, M.M.3    Meroueh, S.O.4
  • 48
    • 77951216201 scopus 로고    scopus 로고
    • Structure-based engineering of species selectivity in the interaction between urokinase and its receptor: Implication for preclinical cancer therapy
    • Lin, L., Gardsvoll, H., Huai, Q., Huang, M., and Ploug, M. (2010) Structure-based engineering of species selectivity in the interaction between urokinase and its receptor: implication for preclinical cancer therapy J. Biol. Chem. 285, 10982-10992
    • (2010) J. Biol. Chem. , vol.285 , pp. 10982-10992
    • Lin, L.1    Gardsvoll, H.2    Huai, Q.3    Huang, M.4    Ploug, M.5
  • 49
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr, D. D., Nussinov, R., and Wright, P. E. (2009) The role of dynamic conformational ensembles in biomolecular recognition Nat. Chem. Biol. 5, 789-796
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 51
    • 0035158527 scopus 로고    scopus 로고
    • Urokinase receptors promote β1 integrin function through interactions with integrin α3β1
    • Wei, Y., Eble, J. A., Wang, Z. M., Kreidberg, J. A., and Chapman, H. A. (2001) Urokinase receptors promote beta 1 integrin function through interactions with integrin alpha 3 beta 1 Mol. Biol. Cell 12, 2975-2986 (Pubitemid 33062955)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.10 , pp. 2975-2986
    • Wei, Y.1    Eble, J.A.2    Wang, Z.3    Kreidberg, J.A.4    Chapman, H.A.5
  • 52
    • 34250318934 scopus 로고    scopus 로고
    • Mapping of the vitronectin-binding site on the urokinase receptor involvement of a coherent receptor: Interface consisting of residues from both domain I and the flanking interdomain linker region
    • DOI 10.1074/jbc.M610184200
    • Gardsvoll, H. and Ploug, M. (2007) Mapping of the vitronectin-binding site on the urokinase receptor: involvement of a coherent receptor interface consisting of residues from both domain I and the flanking interdomain linker region J. Biol. Chem. 282, 13561-13572 (Pubitemid 47100512)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.18 , pp. 13561-13572
    • Gardsvoll, H.1    Ploug, M.2


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