메뉴 건너뛰기




Volumn 46, Issue , 2015, Pages 105-116

Bioactive TTR105-115-based amyloid fibrils reduce the viability of mammalian cells

Author keywords

Apoptosis; Biocompatibility; Cell adhesion; MTT assay; RGD peptide

Indexed keywords

BIOCOMPATIBILITY; CELL ADHESION; CELL DEATH; MAMMALS; PROTEINS;

EID: 84922782113     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2014.12.039     Document Type: Article
Times cited : (8)

References (67)
  • 1
    • 79955119650 scopus 로고    scopus 로고
    • Transplantation of nanostructured composite scaffolds results in the regeneration of chronically injured spinal cords
    • Gelain F., Panseri S., Antonini S., Cunha C., Donega M., Lowery J., et al. Transplantation of nanostructured composite scaffolds results in the regeneration of chronically injured spinal cords. ACS Nano 2011, 5:227-236.
    • (2011) ACS Nano , vol.5 , pp. 227-236
    • Gelain, F.1    Panseri, S.2    Antonini, S.3    Cunha, C.4    Donega, M.5    Lowery, J.6
  • 4
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
    • Holmes T.C., Sd Lacalle, Su X., Liu G., Rich A., Zhang S. Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds. Proc Natl Acad Sci U S A 2000, 97:6728-6733.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6728-6733
    • Holmes, T.C.1    Sd, L.2    Su, X.3    Liu, G.4    Rich, A.5    Zhang, S.6
  • 5
    • 84896765770 scopus 로고    scopus 로고
    • Engineered lysozyme amyloid fibril networks support cellular growth and spreading
    • Reynolds N.P., Charnley M., Mezzenga R., Hartley P.G. Engineered lysozyme amyloid fibril networks support cellular growth and spreading. Biomacromolecules 2014, 15:599-608.
    • (2014) Biomacromolecules , vol.15 , pp. 599-608
    • Reynolds, N.P.1    Charnley, M.2    Mezzenga, R.3    Hartley, P.G.4
  • 6
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: not only pathological agents but also ordered nanomaterials
    • Cherny I., Gazit E. Amyloids: not only pathological agents but also ordered nanomaterials. Angew Chem Int Ed 2008, 47:4062-4069.
    • (2008) Angew Chem Int Ed , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 9
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M., Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv Protein Chem 1997, 50:123-159.
    • (1997) Adv Protein Chem , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 10
    • 1042267371 scopus 로고    scopus 로고
    • Amyloid fibrillogenesis of silkmoth chorion protein peptide-analogues via a liquid-crystalline intermediate phase
    • Hamodrakas S.J., Hoenger A., Iconomidou V.A. Amyloid fibrillogenesis of silkmoth chorion protein peptide-analogues via a liquid-crystalline intermediate phase. JStruct Biol 2004, 145:226-235.
    • (2004) JStruct Biol , vol.145 , pp. 226-235
    • Hamodrakas, S.J.1    Hoenger, A.2    Iconomidou, V.A.3
  • 11
    • 77951684919 scopus 로고    scopus 로고
    • Characterization of the adhesive plaque of the barnacle Balanus amphitrite: amyloid-like nanofibrils are a major component
    • Barlow D.E., Dickinson G.H., Orihuela B., Kulp J.L., Rittschof D., Wahl K.J. Characterization of the adhesive plaque of the barnacle Balanus amphitrite: amyloid-like nanofibrils are a major component. Langmuir 2010, 26:6549-6556.
    • (2010) Langmuir , vol.26 , pp. 6549-6556
    • Barlow, D.E.1    Dickinson, G.H.2    Orihuela, B.3    Kulp, J.L.4    Rittschof, D.5    Wahl, K.J.6
  • 12
  • 13
    • 67650809307 scopus 로고    scopus 로고
    • Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
    • Maji S.K., Perrin M.H., Sawaya M.R., Jessberger S., Vadodaria K., Rissman R.A., et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 2009, 325:328-332.
    • (2009) Science , vol.325 , pp. 328-332
    • Maji, S.K.1    Perrin, M.H.2    Sawaya, M.R.3    Jessberger, S.4    Vadodaria, K.5    Rissman, R.A.6
  • 14
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 2003, 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 15
    • 84885176987 scopus 로고    scopus 로고
    • The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity
    • Cecchi C., Stefani M. The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity. Biophys Chem 2013, 182:30-43.
    • (2013) Biophys Chem , vol.182 , pp. 30-43
    • Cecchi, C.1    Stefani, M.2
  • 17
    • 84904307757 scopus 로고    scopus 로고
    • Amyloid fibrils enhance transport of metal nanoparticles in living cells and induced cytotoxicity
    • Bolisetty S., Boddupalli C.S., Handschin S., Chaitanya K., Adamcik J., Saito Y., et al. Amyloid fibrils enhance transport of metal nanoparticles in living cells and induced cytotoxicity. Biomacromolecules 2014, 15:2793-2799.
    • (2014) Biomacromolecules , vol.15 , pp. 2793-2799
    • Bolisetty, S.1    Boddupalli, C.S.2    Handschin, S.3    Chaitanya, K.4    Adamcik, J.5    Saito, Y.6
  • 19
    • 79959875103 scopus 로고    scopus 로고
    • Functional fibrils derived from the peptide TTR1-cycloRGDfK that target cell adhesion and spreading
    • Bongiovanni M.N., Scanlon D.B., Gras S.L. Functional fibrils derived from the peptide TTR1-cycloRGDfK that target cell adhesion and spreading. Biomaterials 2011, 32:6099-6110.
    • (2011) Biomaterials , vol.32 , pp. 6099-6110
    • Bongiovanni, M.N.1    Scanlon, D.B.2    Gras, S.L.3
  • 21
    • 84899948888 scopus 로고    scopus 로고
    • Complex interfaces in food: structure and mechanical properties.
    • Sagis LMC, Scholten E. Complex interfaces in food: structure and mechanical properties. Trends Food Sci Technol 37:59-71.
    • Trends Food Sci Technol , vol.37 , pp. 59-71
    • Sagis, L.M.C.1    Scholten, E.2
  • 22
    • 12544259221 scopus 로고    scopus 로고
    • Reversal of protein aggregation provides evidence for multiple aggregated states
    • Calamai M., Canale C., Relini A., Stefani M., Chiti F., Dobson C.M. Reversal of protein aggregation provides evidence for multiple aggregated states. JMol Biol 2005, 346:603-616.
    • (2005) JMol Biol , vol.346 , pp. 603-616
    • Calamai, M.1    Canale, C.2    Relini, A.3    Stefani, M.4    Chiti, F.5    Dobson, C.M.6
  • 23
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of α-synuclein
    • Cremades N., Cohen S.I.A., Deas E., Abramov A.Y., Chen A.Y., Orte A., et al. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 2012, 149:1048-1059.
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1    Cohen, S.I.A.2    Deas, E.3    Abramov, A.Y.4    Chen, A.Y.5    Orte, A.6
  • 24
    • 0034646573 scopus 로고    scopus 로고
    • Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin
    • MacPhee C.E., Dobson C.M. Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin. JMol Biol 2000, 297:1203-1215.
    • (2000) JMol Biol , vol.297 , pp. 1203-1215
    • MacPhee, C.E.1    Dobson, C.M.2
  • 26
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002, 416:507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 28
    • 63249103989 scopus 로고    scopus 로고
    • Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer
    • Kayed R., Pensalfini A., Margol L., Sokolov Y., Sarsoza F., Head E., et al. Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer. JBiol Chem 2009, 284:4230-4237.
    • (2009) JBiol Chem , vol.284 , pp. 4230-4237
    • Kayed, R.1    Pensalfini, A.2    Margol, L.3    Sokolov, Y.4    Sarsoza, F.5    Head, E.6
  • 29
    • 84856545963 scopus 로고    scopus 로고
    • Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1
    • Bucciantini M., Nosi D., Forzan M., Russo E., Calamai M., Pieri L., et al. Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1. FASEB J 2012, 26:818-831.
    • (2012) FASEB J , vol.26 , pp. 818-831
    • Bucciantini, M.1    Nosi, D.2    Forzan, M.3    Russo, E.4    Calamai, M.5    Pieri, L.6
  • 30
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya V., Bocharova O.V., Bronstein I., Baskakov I.V. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. JBiol Chem 2006, 281:13828-13836.
    • (2006) JBiol Chem , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 31
    • 84874407281 scopus 로고    scopus 로고
    • Lysine functionalised amyloid fibrils: the design and assembly of a TTR1-based peptide
    • Bongiovanni M., Caruso F., Gras S.L. Lysine functionalised amyloid fibrils: the design and assembly of a TTR1-based peptide. Soft Matter 2013, 9:3315-3330.
    • (2013) Soft Matter , vol.9 , pp. 3315-3330
    • Bongiovanni, M.1    Caruso, F.2    Gras, S.L.3
  • 35
    • 0036798144 scopus 로고    scopus 로고
    • Staurosporine induces endothelial cell apoptosis via focal adhesion kinase dephosphorylation and focal adhesion disassembly independent of focal adhesion kinase proteolysis
    • Kabir J., Lobo M., Zachary I. Staurosporine induces endothelial cell apoptosis via focal adhesion kinase dephosphorylation and focal adhesion disassembly independent of focal adhesion kinase proteolysis. Biochem J 2002, 367:145-155.
    • (2002) Biochem J , vol.367 , pp. 145-155
    • Kabir, J.1    Lobo, M.2    Zachary, I.3
  • 36
    • 0023738916 scopus 로고
    • Aquick and simple method for the quantitation of lactate dehydrogenase release in measurements of cellular cytotoxicity and tumor necrosis factor (TNF) activity
    • Decker T., Lohmann-Matthes M.-L. Aquick and simple method for the quantitation of lactate dehydrogenase release in measurements of cellular cytotoxicity and tumor necrosis factor (TNF) activity. JImmunol Methods 1988, 115:61-69.
    • (1988) JImmunol Methods , vol.115 , pp. 61-69
    • Decker, T.1    Lohmann-Matthes, M.-L.2
  • 37
    • 0030883765 scopus 로고    scopus 로고
    • Early detection of apoptosis using a fluorescent conjugate of annexin V
    • Zhang G., Gurtu V., Kain S.R., Yan G. Early detection of apoptosis using a fluorescent conjugate of annexin V. BioTechniques 1997, 23:525-531.
    • (1997) BioTechniques , vol.23 , pp. 525-531
    • Zhang, G.1    Gurtu, V.2    Kain, S.R.3    Yan, G.4
  • 38
    • 4444372444 scopus 로고    scopus 로고
    • Staurosporine induces apoptosis of melanoma by both caspase-dependent and -independent apoptotic pathways
    • Zhang X.D., Gillespie S.K., Hersey P. Staurosporine induces apoptosis of melanoma by both caspase-dependent and -independent apoptotic pathways. Mol Cancer Ther 2004, 3:187-197.
    • (2004) Mol Cancer Ther , vol.3 , pp. 187-197
    • Zhang, X.D.1    Gillespie, S.K.2    Hersey, P.3
  • 39
    • 62749187796 scopus 로고    scopus 로고
    • Peptide-functionalized, low-biofouling click multilayers for promoting cell adhesion and growth
    • Kinnane C.R., Wark K., Such G.K., Johnston A.P.R., Caruso F. Peptide-functionalized, low-biofouling click multilayers for promoting cell adhesion and growth. Small 2009, 5:444-448.
    • (2009) Small , vol.5 , pp. 444-448
    • Kinnane, C.R.1    Wark, K.2    Such, G.K.3    Johnston, A.P.R.4    Caruso, F.5
  • 41
    • 78149466716 scopus 로고    scopus 로고
    • αB-crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide
    • Dehle F.C., Ecroyd H., Musgrave I.F., Carver J.A. αB-crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide. Cell Stress Chaperones 2010, 15:1013-1026.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 1013-1026
    • Dehle, F.C.1    Ecroyd, H.2    Musgrave, I.F.3    Carver, J.A.4
  • 42
    • 67649397928 scopus 로고    scopus 로고
    • Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils
    • Zako T., Sakono M., Hashimoto N., Ihara M., Maeda M. Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils. Biophys J 2009, 96:3331-3340.
    • (2009) Biophys J , vol.96 , pp. 3331-3340
    • Zako, T.1    Sakono, M.2    Hashimoto, N.3    Ihara, M.4    Maeda, M.5
  • 43
    • 33746128413 scopus 로고    scopus 로고
    • The aggregation potential of human amylin determines its cytotoxicity towards islet β-cells
    • Konarkowska B., Aitken J.F., Kistler J., Zhang S., Cooper G.J.S. The aggregation potential of human amylin determines its cytotoxicity towards islet β-cells. FEBS J 2006, 273:3614-3624.
    • (2006) FEBS J , vol.273 , pp. 3614-3624
    • Konarkowska, B.1    Aitken, J.F.2    Kistler, J.3    Zhang, S.4    Cooper, G.J.S.5
  • 44
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth A. Infrared spectroscopy of proteins. Biochim Biophys Acta 2007, 1767:1073-1101.
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 46
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • Cardamone M., Puri N.K. Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem J 1992, 282:589.
    • (1992) Biochem J , vol.282 , pp. 589
    • Cardamone, M.1    Puri, N.K.2
  • 47
    • 0037852937 scopus 로고    scopus 로고
    • Areview of modified DLC coatings for biological applications
    • Hauert R. Areview of modified DLC coatings for biological applications. Diam Relat Mater 2003, 12:583-589.
    • (2003) Diam Relat Mater , vol.12 , pp. 583-589
    • Hauert, R.1
  • 49
  • 50
    • 0034902905 scopus 로고    scopus 로고
    • Integrins and cell proliferation regulation of cyclin-dependent kinases via cytoplasmic signaling pathways
    • Schwartz M.A., Assoian R.K. Integrins and cell proliferation regulation of cyclin-dependent kinases via cytoplasmic signaling pathways. JCell Sci 2001, 114:2553-2560.
    • (2001) JCell Sci , vol.114 , pp. 2553-2560
    • Schwartz, M.A.1    Assoian, R.K.2
  • 52
    • 33846799471 scopus 로고    scopus 로고
    • Systematic study of osteoblast and fibroblast response to roughness by means of surface-morphology gradients
    • Kunzler T.P., Drobek T., Schuler M., Spencer N.D. Systematic study of osteoblast and fibroblast response to roughness by means of surface-morphology gradients. Biomaterials 2007, 28:2175-2182.
    • (2007) Biomaterials , vol.28 , pp. 2175-2182
    • Kunzler, T.P.1    Drobek, T.2    Schuler, M.3    Spencer, N.D.4
  • 53
    • 77952346781 scopus 로고    scopus 로고
    • EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity
    • Bieschke J., Russ J., Friedrich R.P., Ehrnhoefer D.E., Wobst H., Neugebauer K., et al. EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity. PNAS 2010, 107:7710-7715.
    • (2010) PNAS , vol.107 , pp. 7710-7715
    • Bieschke, J.1    Russ, J.2    Friedrich, R.P.3    Ehrnhoefer, D.E.4    Wobst, H.5    Neugebauer, K.6
  • 54
    • 33845480548 scopus 로고    scopus 로고
    • Caspase function in programmed cell death
    • Kumar S. Caspase function in programmed cell death. Cell Death Differ 2007, 14:32-43.
    • (2007) Cell Death Differ , vol.14 , pp. 32-43
    • Kumar, S.1
  • 55
    • 32444434664 scopus 로고    scopus 로고
    • Caspases 3 and 7: key mediators of mitochondrial events of apoptosis
    • Lakhani S.A., Masud A., Kuida K., Porter G.A., Booth C.J., Mehal W.Z., et al. Caspases 3 and 7: key mediators of mitochondrial events of apoptosis. Science 2006, 311:847-851.
    • (2006) Science , vol.311 , pp. 847-851
    • Lakhani, S.A.1    Masud, A.2    Kuida, K.3    Porter, G.A.4    Booth, C.J.5    Mehal, W.Z.6
  • 56
  • 57
    • 0035478618 scopus 로고    scopus 로고
    • β-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand
    • Morishima Y., Gotoh Y., Zieg J., Barrett T., Takano H., Flavell R., et al. β-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand. JNeurosci: Off J Soc Neurosci 2001, 21:7551-7560.
    • (2001) JNeurosci: Off J Soc Neurosci , vol.21 , pp. 7551-7560
    • Morishima, Y.1    Gotoh, Y.2    Zieg, J.3    Barrett, T.4    Takano, H.5    Flavell, R.6
  • 58
    • 0028171547 scopus 로고
    • Ultrastructural analysis of β-amyloid-induced apoptosis in cultured hippocampal neurons
    • Watt J.A., Pike C.J., Walencewicz-Wasserman A.J., Cotman C.W. Ultrastructural analysis of β-amyloid-induced apoptosis in cultured hippocampal neurons. Brain Res 1994, 661:147-156.
    • (1994) Brain Res , vol.661 , pp. 147-156
    • Watt, J.A.1    Pike, C.J.2    Walencewicz-Wasserman, A.J.3    Cotman, C.W.4
  • 59
    • 34250857530 scopus 로고    scopus 로고
    • Three-dimensional cell culture of chondrocytes on modified di-phenylalanine scaffolds
    • Jayawarna V., Smith A., Gough J.E., Ulijn R.V. Three-dimensional cell culture of chondrocytes on modified di-phenylalanine scaffolds. Biochem Soc Trans 2007, 35:535-537.
    • (2007) Biochem Soc Trans , vol.35 , pp. 535-537
    • Jayawarna, V.1    Smith, A.2    Gough, J.E.3    Ulijn, R.V.4
  • 60
    • 84863694111 scopus 로고    scopus 로고
    • Interactions of cells with silk surfaces
    • Leal-Egaña A., Scheibel T. Interactions of cells with silk surfaces. JMater Chem 2012, 22.
    • (2012) JMater Chem , vol.22
    • Leal-Egaña, A.1    Scheibel, T.2
  • 61
    • 0025801516 scopus 로고
    • Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils invitro
    • Gustavsson A., Engström U., Westermark P. Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils invitro. Biochem Biophys Res Commun 1991, 175:1159-1164.
    • (1991) Biochem Biophys Res Commun , vol.175 , pp. 1159-1164
    • Gustavsson, A.1    Engström, U.2    Westermark, P.3
  • 62
    • 0242634332 scopus 로고    scopus 로고
    • Transthyretin (TTR)-derived amyloid fibrils: immunoelectron microscopy of fibrils formed invivo and invitro from synthetic peptides and normal transthyretin
    • Gustavsson Å., Engström U., Westermark P. Transthyretin (TTR)-derived amyloid fibrils: immunoelectron microscopy of fibrils formed invivo and invitro from synthetic peptides and normal transthyretin. Amyloid 1997, 4:1-12.
    • (1997) Amyloid , vol.4 , pp. 1-12
    • Gustavsson, Å.1    Engström, U.2    Westermark, P.3
  • 63
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • Reixach N., Deechongkit S., Jiang X., Kelly J.W., Buxbaum J.N. Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc Natl Acad Sci U S A 2004, 101:2817-2822.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 64
    • 56349095198 scopus 로고    scopus 로고
    • Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture
    • Sörgjerd K., Klingstedt T., Lindgren M., Kågedal K., Hammarström P. Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture. Biochem Biophys Res Commun 2008, 377:1072-1078.
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 1072-1078
    • Sörgjerd, K.1    Klingstedt, T.2    Lindgren, M.3    Kågedal, K.4    Hammarström, P.5
  • 65
    • 0041559949 scopus 로고    scopus 로고
    • RGD modified polymers: biomaterials for stimulated cell adhesion and beyond
    • Hersel U., Dahmen C., Kessler H. RGD modified polymers: biomaterials for stimulated cell adhesion and beyond. Biomaterials 2003, 24:4385-4415.
    • (2003) Biomaterials , vol.24 , pp. 4385-4415
    • Hersel, U.1    Dahmen, C.2    Kessler, H.3
  • 66
    • 0026503815 scopus 로고
    • Immobilized Arg-Gly-Asp (RGD) peptides of varying lengths as structural probes of the platelet glycoprotein-IIβ/IIIα receptor
    • Beer J.H., Springer K.T., Coller B.S. Immobilized Arg-Gly-Asp (RGD) peptides of varying lengths as structural probes of the platelet glycoprotein-IIβ/IIIα receptor. Blood 1992, 79:117-128.
    • (1992) Blood , vol.79 , pp. 117-128
    • Beer, J.H.1    Springer, K.T.2    Coller, B.S.3
  • 67
    • 84880050720 scopus 로고    scopus 로고
    • Nanotopographic surfaces with defined surface chemistries from amyloid fibril networks can control cell attachment
    • Reynolds N.P., Styan K.E., Easton C.D., Li Y., Waddington L., Lara C., et al. Nanotopographic surfaces with defined surface chemistries from amyloid fibril networks can control cell attachment. Biomacromolecules 2013, 14:2305-2316.
    • (2013) Biomacromolecules , vol.14 , pp. 2305-2316
    • Reynolds, N.P.1    Styan, K.E.2    Easton, C.D.3    Li, Y.4    Waddington, L.5    Lara, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.