메뉴 건너뛰기




Volumn 321, Issue 2, 2008, Pages 250-263

Optimizing collagen transport through track-etched nanopores

Author keywords

Collagen solution; Collagen transport; Macromolecular solute transport; Nanoporous membrane transport; Semi dilute solution transport

Indexed keywords

BIOTECHNOLOGY; CELL MEMBRANES; CHEMICALS; COLLAGEN; MEMBRANES; MOLECULES; MONOMERS; NANOPORES; SEPARATION; TECHNOLOGY;

EID: 46349105148     PISSN: 03767388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.memsci.2008.04.066     Document Type: Article
Times cited : (6)

References (91)
  • 1
    • 34047242582 scopus 로고    scopus 로고
    • Quality control and advanced characterization of membranes
    • Kilz P., and Viktorin M. Quality control and advanced characterization of membranes. LC-GC Europe 20 (2007) 224
    • (2007) LC-GC Europe , vol.20 , pp. 224
    • Kilz, P.1    Viktorin, M.2
  • 2
    • 12444304404 scopus 로고    scopus 로고
    • Simulation of GPC-distribution coefficients of linear and star-shaped molecules in spherical pores: comparison of simulation and experiment
    • Gerber J., Radke W., and Wittmann G. Simulation of GPC-distribution coefficients of linear and star-shaped molecules in spherical pores: comparison of simulation and experiment. International Journal of Polymer Analysis and Characterization 9 (2004) 39
    • (2004) International Journal of Polymer Analysis and Characterization , vol.9 , pp. 39
    • Gerber, J.1    Radke, W.2    Wittmann, G.3
  • 3
    • 0035526798 scopus 로고    scopus 로고
    • Simulation of GPC-distribution coefficients of linear and star-shaped molecules in spherical pores
    • Radke W. Simulation of GPC-distribution coefficients of linear and star-shaped molecules in spherical pores. Macromolecular Theory and Simulations 10 (2001) 668
    • (2001) Macromolecular Theory and Simulations , vol.10 , pp. 668
    • Radke, W.1
  • 4
    • 0035871935 scopus 로고    scopus 로고
    • Protein determination by high-performance gel-permeation chromatography: applications to human pancreatic juice, human bile and tissue homogenate
    • Hayakawa K., et al. Protein determination by high-performance gel-permeation chromatography: applications to human pancreatic juice, human bile and tissue homogenate. Journal of Chromatography B: Biomedical Sciences and Applications 754 (2001) 65
    • (2001) Journal of Chromatography B: Biomedical Sciences and Applications , vol.754 , pp. 65
    • Hayakawa, K.1
  • 5
    • 0033936826 scopus 로고    scopus 로고
    • Analysis of linear macromolecule transport through aluminum anodic oxide membranes by pore model
    • Ichimura S., et al. Analysis of linear macromolecule transport through aluminum anodic oxide membranes by pore model. Journal of Chemical Engineering of Japan 33 (2000) 141
    • (2000) Journal of Chemical Engineering of Japan , vol.33 , pp. 141
    • Ichimura, S.1
  • 6
    • 0018677009 scopus 로고
    • Characterization of ultrafiltration membranes by polymer transport measurements
    • Cooper A.R., and Van Derveer D.S. Characterization of ultrafiltration membranes by polymer transport measurements. Separation Science and Technology 14 (1979) 551
    • (1979) Separation Science and Technology , vol.14 , pp. 551
    • Cooper, A.R.1    Van Derveer, D.S.2
  • 7
    • 4143112232 scopus 로고    scopus 로고
    • Structure of peptides investigated by nanopore analysis
    • Sutherland T.C., et al. Structure of peptides investigated by nanopore analysis. Nano Letters 4 (2004) 1273
    • (2004) Nano Letters , vol.4 , pp. 1273
    • Sutherland, T.C.1
  • 8
    • 33746590221 scopus 로고    scopus 로고
    • Transport of alpha-helical peptides through alpha-hemolysin and aerolysin pores
    • Stefureac R., et al. Transport of alpha-helical peptides through alpha-hemolysin and aerolysin pores. Biochemistry 45 (2006) 9172
    • (2006) Biochemistry , vol.45 , pp. 9172
    • Stefureac, R.1
  • 9
    • 33745224788 scopus 로고    scopus 로고
    • Plasmid size up to 20 kbp does not limit effective in vivo lung gene transfer using compacted DNA nanoparticles
    • Fink T.L., et al. Plasmid size up to 20 kbp does not limit effective in vivo lung gene transfer using compacted DNA nanoparticles. Gene Therapy 13 (2006) 1048
    • (2006) Gene Therapy , vol.13 , pp. 1048
    • Fink, T.L.1
  • 10
    • 33745774997 scopus 로고    scopus 로고
    • Direct force measurements on DNA in a solid-state nanopore
    • Keyser U.F., et al. Direct force measurements on DNA in a solid-state nanopore. Nature Physics 2 (2006) 473
    • (2006) Nature Physics , vol.2 , pp. 473
    • Keyser, U.F.1
  • 11
    • 0037855911 scopus 로고    scopus 로고
    • Dynamics of polynucleotide transport through nanometre-scale pores
    • Meller A. Dynamics of polynucleotide transport through nanometre-scale pores. Journal of Physics: Condensed Matter 15 (2003) R581
    • (2003) Journal of Physics: Condensed Matter , vol.15
    • Meller, A.1
  • 12
    • 14544294874 scopus 로고    scopus 로고
    • The nanopore connection to cell membrane unitary permeability
    • Peters R. The nanopore connection to cell membrane unitary permeability. Traffic (Oxford, United Kingdom) 6 (2005) 199
    • (2005) Traffic (Oxford, United Kingdom) , vol.6 , pp. 199
    • Peters, R.1
  • 13
    • 33745617227 scopus 로고    scopus 로고
    • The discovery of the molecular mechanism of cellular secretion
    • Zhvania M. The discovery of the molecular mechanism of cellular secretion. Journal of Biological Physics and Chemistry 4 (2004) 43
    • (2004) Journal of Biological Physics and Chemistry , vol.4 , pp. 43
    • Zhvania, M.1
  • 14
    • 2542439729 scopus 로고    scopus 로고
    • Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon
    • Canty E.G., et al. Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon. Journal of Cell Biology 165 (2004) 553
    • (2004) Journal of Cell Biology , vol.165 , pp. 553
    • Canty, E.G.1
  • 15
    • 33845966742 scopus 로고    scopus 로고
    • Actin filaments are required for fibripositor-mediated collagen fibril alignment in tendon
    • Canty E.G., et al. Actin filaments are required for fibripositor-mediated collagen fibril alignment in tendon. Journal of Biological Chemistry 281 (2006) 38592
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 38592
    • Canty, E.G.1
  • 16
    • 0022271435 scopus 로고
    • Fibroblasts create compartments in the extracellular space where collagen polymerizes into fibrils and fibrils associate into bundles
    • Birk D.E., and Trelstad R.L. Fibroblasts create compartments in the extracellular space where collagen polymerizes into fibrils and fibrils associate into bundles. Annals of the New York Academy of Sciences 460 (1985) 258
    • (1985) Annals of the New York Academy of Sciences , vol.460 , pp. 258
    • Birk, D.E.1    Trelstad, R.L.2
  • 18
    • 0029176870 scopus 로고
    • Extracellular matrix 1: fibril-forming collagens
    • Kadler K. Extracellular matrix 1: fibril-forming collagens. Protein Profile 2 (1995) 491
    • (1995) Protein Profile , vol.2 , pp. 491
    • Kadler, K.1
  • 20
    • 17844373840 scopus 로고    scopus 로고
    • Procollagen trafficking, processing and fibrillogenesis
    • Canty E.G., and Kadler K.E. Procollagen trafficking, processing and fibrillogenesis. Journal of Cell Science 118 (2005) 1341
    • (2005) Journal of Cell Science , vol.118 , pp. 1341
    • Canty, E.G.1    Kadler, K.E.2
  • 22
    • 0015892994 scopus 로고
    • Analysis of the primary structure of collagen for the origins of molecular packing
    • Hulmes D.J.S., et al. Analysis of the primary structure of collagen for the origins of molecular packing. Journal of Molecular Biology 79 (1973) 137
    • (1973) Journal of Molecular Biology , vol.79 , pp. 137
    • Hulmes, D.J.S.1
  • 25
    • 0015847573 scopus 로고
    • The self-assembly of collagen molecules
    • Yuan L., and Veis A. The self-assembly of collagen molecules. Biopolymers 12 (1973) 1437
    • (1973) Biopolymers , vol.12 , pp. 1437
    • Yuan, L.1    Veis, A.2
  • 26
    • 0002740030 scopus 로고
    • Recent studies with the electron microscope on ordered aggregates of the tropocollagen molecule
    • Madras
    • Hodge A.J., and Petruska J.A. Recent studies with the electron microscope on ordered aggregates of the tropocollagen molecule. Aspects Protein Structures, Proceedings Symposium. Madras (1963) 289
    • (1963) Aspects Protein Structures, Proceedings Symposium , pp. 289
    • Hodge, A.J.1    Petruska, J.A.2
  • 27
    • 0018354864 scopus 로고
    • Dynamic light scattering from collagen solutions. II. Photon correlation study of the depolarized light
    • Thomas J.C., and Fletcher G.C. Dynamic light scattering from collagen solutions. II. Photon correlation study of the depolarized light. Biopolymers 18 (1979) 1333
    • (1979) Biopolymers , vol.18 , pp. 1333
    • Thomas, J.C.1    Fletcher, G.C.2
  • 28
    • 0013865091 scopus 로고
    • The physical characterization of monomeric tropocollagen
    • Davison P.F., and Drake M.P. The physical characterization of monomeric tropocollagen. Biochemistry 5 (1966) 313
    • (1966) Biochemistry , vol.5 , pp. 313
    • Davison, P.F.1    Drake, M.P.2
  • 29
    • 0019158774 scopus 로고
    • Type I collagen in solution. Structure and properties of fibril fragments
    • Silver F.H., and Trelstad R.L. Type I collagen in solution. Structure and properties of fibril fragments. Journal of Biological Chemistry 255 (1980) 9427
    • (1980) Journal of Biological Chemistry , vol.255 , pp. 9427
    • Silver, F.H.1    Trelstad, R.L.2
  • 30
    • 0015299229 scopus 로고
    • Non-aggregated tropocollagen at physiological pH and ionic strength. A chemical and physico-chemical characterization of tropocollagen isolated from the skin of lathyritic rats
    • Obrink B. Non-aggregated tropocollagen at physiological pH and ionic strength. A chemical and physico-chemical characterization of tropocollagen isolated from the skin of lathyritic rats. European Journal of Biochemistry 25 (1972) 563
    • (1972) European Journal of Biochemistry , vol.25 , pp. 563
    • Obrink, B.1
  • 31
    • 0017145522 scopus 로고
    • Dynamic light scattering from collagen solutions. I. Translational diffusion coefficient and aggregation effects
    • Fletcher G.C. Dynamic light scattering from collagen solutions. I. Translational diffusion coefficient and aggregation effects. Biopolymers 15 (1976) 2201
    • (1976) Biopolymers , vol.15 , pp. 2201
    • Fletcher, G.C.1
  • 32
    • 0021126710 scopus 로고
    • Molecular structure of collagen in solution: comparison of types I, II, III and V
    • Silver F.H., and Birk D.E. Molecular structure of collagen in solution: comparison of types I, II, III and V. International Journal of Biological Macromolecules 6 (1984) 125
    • (1984) International Journal of Biological Macromolecules , vol.6 , pp. 125
    • Silver, F.H.1    Birk, D.E.2
  • 33
    • 0018568324 scopus 로고
    • Type I collagen fibrillogenesis: initiation via reversible linear and lateral growth steps
    • Silver F.H., Langley K.H., and Trelstad R.L. Type I collagen fibrillogenesis: initiation via reversible linear and lateral growth steps. Biopolymers 18 (1979) 2523
    • (1979) Biopolymers , vol.18 , pp. 2523
    • Silver, F.H.1    Langley, K.H.2    Trelstad, R.L.3
  • 34
    • 0020602711 scopus 로고
    • Corneal and scleral type I collagens: analyses of physical properties and molecular flexibility
    • Birk D.E., and Silver F.H. Corneal and scleral type I collagens: analyses of physical properties and molecular flexibility. International Journal of Biological Macromolecules 5 (1983) 209
    • (1983) International Journal of Biological Macromolecules , vol.5 , pp. 209
    • Birk, D.E.1    Silver, F.H.2
  • 35
    • 0342439682 scopus 로고
    • On the length and molecular weight of tropocollagen from calf skin
    • Rice R.V., et al. On the length and molecular weight of tropocollagen from calf skin. Archives of Biochemistry and Biophysics 105 (1964) 409
    • (1964) Archives of Biochemistry and Biophysics , vol.105 , pp. 409
    • Rice, R.V.1
  • 36
    • 0020684149 scopus 로고
    • A hydrodynamic study of collagen fibrillogenesis by electric birefringence and quasielastic light scattering
    • Bernengo J.C., et al. A hydrodynamic study of collagen fibrillogenesis by electric birefringence and quasielastic light scattering. Journal of Biological Chemistry 258 (1983) 1001
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 1001
    • Bernengo, J.C.1
  • 37
    • 0030784351 scopus 로고    scopus 로고
    • Translational and rotational dynamics of collagen in dilute solution
    • Claire K., and Pecora R. Translational and rotational dynamics of collagen in dilute solution. Journal of Physical Chemistry B 101 (1997) 746
    • (1997) Journal of Physical Chemistry B , vol.101 , pp. 746
    • Claire, K.1    Pecora, R.2
  • 38
    • 0023425104 scopus 로고
    • Dynamic light-scattering study of semiflexible polymers: collagen
    • Kubota K., Tominaga Y., and Fujime S. Dynamic light-scattering study of semiflexible polymers: collagen. Biopolymers 26 (1987) 1717
    • (1987) Biopolymers , vol.26 , pp. 1717
    • Kubota, K.1    Tominaga, Y.2    Fujime, S.3
  • 39
    • 84985665853 scopus 로고
    • Thermal conformation transformations of tropocollagen. II. Viscometric and light-scattering studies
    • Privalov P.L., Serdyuk I.N., and Tiktopulo E.I. Thermal conformation transformations of tropocollagen. II. Viscometric and light-scattering studies. Biopolymers 10 (1971) 1777
    • (1971) Biopolymers , vol.10 , pp. 1777
    • Privalov, P.L.1    Serdyuk, I.N.2    Tiktopulo, E.I.3
  • 41
    • 0015535046 scopus 로고
    • Flexibility of tropocollagen from sedimentation and viscosity
    • Utiyama H., et al. Flexibility of tropocollagen from sedimentation and viscosity. Biopolymers 12 (1973) 53
    • (1973) Biopolymers , vol.12 , pp. 53
    • Utiyama, H.1
  • 42
    • 0021854363 scopus 로고
    • Effect of pH on collagen flexibility determined from dilute solution viscoelastic measurements
    • Amis E.J., et al. Effect of pH on collagen flexibility determined from dilute solution viscoelastic measurements. International Journal of Biological Macromolecules 7 (1985) 130
    • (1985) International Journal of Biological Macromolecules , vol.7 , pp. 130
    • Amis, E.J.1
  • 43
    • 0036064087 scopus 로고    scopus 로고
    • Direct quantification of the flexibility of type I collagen monomer
    • Sun Y.-L., et al. Direct quantification of the flexibility of type I collagen monomer. Biochemical and Biophysical Research Communications 295 (2002) 382
    • (2002) Biochemical and Biophysical Research Communications , vol.295 , pp. 382
    • Sun, Y.-L.1
  • 44
    • 0003005891 scopus 로고
    • Fundamentals of interstitial collagen self-assembly
    • Yurchenko P.D., Birk David E., and Mecham R.P. (Eds), Academic Press, San Diego, CA
    • Veis A., and George A. Fundamentals of interstitial collagen self-assembly. In: Yurchenko P.D., Birk David E., and Mecham R.P. (Eds). Extracellular Matrix Assembly and Structure (1994), Academic Press, San Diego, CA 13
    • (1994) Extracellular Matrix Assembly and Structure , pp. 13
    • Veis, A.1    George, A.2
  • 45
    • 0345082759 scopus 로고
    • Collagen aggregation phenomena
    • Cassel J.M. Collagen aggregation phenomena. Biopolymers 4 (1966) 989
    • (1966) Biopolymers , vol.4 , pp. 989
    • Cassel, J.M.1
  • 46
    • 0020616598 scopus 로고
    • Description of collagen fibril formation by a theory of polymer crystallization
    • Wallace D.G., and Thompson A. Description of collagen fibril formation by a theory of polymer crystallization. Biopolymers 22 (1983) 1793
    • (1983) Biopolymers , vol.22 , pp. 1793
    • Wallace, D.G.1    Thompson, A.2
  • 47
    • 0029992496 scopus 로고    scopus 로고
    • Collagen fibril formation
    • Kadler K.E., et al. Collagen fibril formation. The Biochemical Journal 316 (1996) 1
    • (1996) The Biochemical Journal , vol.316 , pp. 1
    • Kadler, K.E.1
  • 48
    • 0001472055 scopus 로고
    • Heat precipitation of collagen from neutral salt solutions: some rate-regulating factors
    • Gross J., and Kirk D. Heat precipitation of collagen from neutral salt solutions: some rate-regulating factors. Journal of Biological Chemistry 233 (1958) 355
    • (1958) Journal of Biological Chemistry , vol.233 , pp. 355
    • Gross, J.1    Kirk, D.2
  • 49
    • 0023748662 scopus 로고
    • Assembly of type I collagen fibrils de novo. Between 37 and 41 °C the process is limited by micro-unfolding of monomers
    • Kadler K.E., Hojima Y., and Prockop D.J. Assembly of type I collagen fibrils de novo. Between 37 and 41 °C the process is limited by micro-unfolding of monomers. Journal of Biological Chemistry 263 (1988) 10517
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 10517
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 50
    • 0019992204 scopus 로고
    • Structure and assembly of the native collagen fibril
    • Piez K.A. Structure and assembly of the native collagen fibril. Connective Tissue Research 10 (1982) 25
    • (1982) Connective Tissue Research , vol.10 , pp. 25
    • Piez, K.A.1
  • 51
    • 0345514243 scopus 로고
    • The heterogeneity of collagen solutions and its effect on fibril formation
    • Wood G.C. The heterogeneity of collagen solutions and its effect on fibril formation. The Biochemical Journal 84 (1962) 429
    • (1962) The Biochemical Journal , vol.84 , pp. 429
    • Wood, G.C.1
  • 52
    • 0001358433 scopus 로고
    • The formation of fibrils from collagen solutions. 1. The effect of experimental conditions: kinetic and electron-microscope studies
    • Wood G.C., and Keech M.K. The formation of fibrils from collagen solutions. 1. The effect of experimental conditions: kinetic and electron-microscope studies. The Biochemical Journal 75 (1960) 588
    • (1960) The Biochemical Journal , vol.75 , pp. 588
    • Wood, G.C.1    Keech, M.K.2
  • 53
    • 0021942111 scopus 로고
    • Collagen fibrillogenesis in vitro: a characterization of fibril quality as a function of assembly conditions
    • McPherson J.M., et al. Collagen fibrillogenesis in vitro: a characterization of fibril quality as a function of assembly conditions. Collagen and Related Research 5 (1985) 119
    • (1985) Collagen and Related Research , vol.5 , pp. 119
    • McPherson, J.M.1
  • 54
    • 0018079235 scopus 로고
    • Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results
    • Williams B.R., et al. Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results. Journal of Biological Chemistry 253 (1978) 6578
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 6578
    • Williams, B.R.1
  • 55
    • 0020794735 scopus 로고
    • Aggregation of a type I collagen precursor containing N-terminal propeptides
    • Miyahara M., et al. Aggregation of a type I collagen precursor containing N-terminal propeptides. Collagen and Related Research 3 (1983) 279
    • (1983) Collagen and Related Research , vol.3 , pp. 279
    • Miyahara, M.1
  • 56
    • 0021133408 scopus 로고
    • Formation of collagen fibrils by enzymic cleavage of precursors of type I collagen in vitro
    • Miyahara M., et al. Formation of collagen fibrils by enzymic cleavage of precursors of type I collagen in vitro. Journal of Biological Chemistry 259 (1984) 9891
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 9891
    • Miyahara, M.1
  • 57
    • 0023862569 scopus 로고
    • Hydrodynamic theory for the hindered transport of flexible macromolecules in porous membranes
    • Davidson M.G., and Deen W.M. Hydrodynamic theory for the hindered transport of flexible macromolecules in porous membranes. Journal of Membrane Science 35 (1988) 167
    • (1988) Journal of Membrane Science , vol.35 , pp. 167
    • Davidson, M.G.1    Deen, W.M.2
  • 58
    • 0023422845 scopus 로고
    • Hindered transport of large molecules in liquid-filled pores
    • Deen W.M. Hindered transport of large molecules in liquid-filled pores. AIChE Journal 33 (1987) 1409
    • (1987) AIChE Journal , vol.33 , pp. 1409
    • Deen, W.M.1
  • 59
    • 0001653395 scopus 로고
    • Thermodynamic analysis of the permeability of biological membranes to nonelectrolytes
    • Kedem O., and Katchalsky A. Thermodynamic analysis of the permeability of biological membranes to nonelectrolytes. Biochimica et Biophysica Acta 27 (1958) 229
    • (1958) Biochimica et Biophysica Acta , vol.27 , pp. 229
    • Kedem, O.1    Katchalsky, A.2
  • 61
    • 46349093154 scopus 로고
    • Solutions of flexible polymers. Neutron experiments and interpretation
    • Daoud M., et al. Solutions of flexible polymers. Neutron experiments and interpretation. Annales de Physique (Paris, France) 1 (1976) 127
    • (1976) Annales de Physique (Paris, France) , vol.1 , pp. 127
    • Daoud, M.1
  • 62
    • 0002920676 scopus 로고
    • Statistics of macromolecular solutions trapped in small pores
    • Daoud M., and De Gennes P.G. Statistics of macromolecular solutions trapped in small pores. Journal de Physique (Paris) 38 (1977) 85
    • (1977) Journal de Physique (Paris) , vol.38 , pp. 85
    • Daoud, M.1    De Gennes, P.G.2
  • 63
    • 0001704167 scopus 로고
    • Flows of flexible polymer solutions in pores
    • Daoudi S., and Brochard F. Flows of flexible polymer solutions in pores. Macromolecules 11 (1978) 751
    • (1978) Macromolecules , vol.11 , pp. 751
    • Daoudi, S.1    Brochard, F.2
  • 64
    • 26244435935 scopus 로고    scopus 로고
    • Simulations of sieving characteristics of macromolecules in porous membranes at high concentrations
    • Cifra P., and Bleha T. Simulations of sieving characteristics of macromolecules in porous membranes at high concentrations. Journal of Membrane Science 265 (2005) 51
    • (2005) Journal of Membrane Science , vol.265 , pp. 51
    • Cifra, P.1    Bleha, T.2
  • 66
    • 0000003163 scopus 로고
    • Diffusion of large flexible polymer chains through model porous membranes
    • Guillot G., Leger L., and Rondelez F. Diffusion of large flexible polymer chains through model porous membranes. Macromolecules 18 (1985) 2531
    • (1985) Macromolecules , vol.18 , pp. 2531
    • Guillot, G.1    Leger, L.2    Rondelez, F.3
  • 68
    • 0009133023 scopus 로고
    • Simultaneous static and dynamic light scattering
    • Bantle S., Schmidt M., and Burchard W. Simultaneous static and dynamic light scattering. Macromolecules 15 (1982) 1604
    • (1982) Macromolecules , vol.15 , pp. 1604
    • Bantle, S.1    Schmidt, M.2    Burchard, W.3
  • 69
    • 0000233598 scopus 로고
    • Static and dynamic solution properties of pullulan in a dilute solution
    • Kato T., Katsuki T., and Takahashi A. Static and dynamic solution properties of pullulan in a dilute solution. Macromolecules 17 (1984) 1726
    • (1984) Macromolecules , vol.17 , pp. 1726
    • Kato, T.1    Katsuki, T.2    Takahashi, A.3
  • 70
    • 0027623763 scopus 로고
    • Laser light-scattering characterization of the molecular weight distribution of dextran
    • Wu C. Laser light-scattering characterization of the molecular weight distribution of dextran. Macromolecules 26 (1993) 3821
    • (1993) Macromolecules , vol.26 , pp. 3821
    • Wu, C.1
  • 72
    • 0018997676 scopus 로고
    • Polymer chain dimensions and the dependence of viscoelastic properties on concentration, molecular weight, and solvent power
    • Graessley W.W. Polymer chain dimensions and the dependence of viscoelastic properties on concentration, molecular weight, and solvent power. Polymer 21 (1980) 258
    • (1980) Polymer , vol.21 , pp. 258
    • Graessley, W.W.1
  • 73
    • 84985551906 scopus 로고
    • Statistical evaluation of sieve constants in ultrafiltration
    • Ferry J.D. Statistical evaluation of sieve constants in ultrafiltration. Journal of General Physiology 20 (1936) 95
    • (1936) Journal of General Physiology , vol.20 , pp. 95
    • Ferry, J.D.1
  • 74
    • 0000560829 scopus 로고
    • Filtration, diffusion, and molecular sieving through porous cellulose membranes
    • Renkin E.M. Filtration, diffusion, and molecular sieving through porous cellulose membranes. Journal of General Physiology 38 (1954) 225
    • (1954) Journal of General Physiology , vol.38 , pp. 225
    • Renkin, E.M.1
  • 75
    • 84957794434 scopus 로고
    • Filtration, diffusion, and molecular sieving through peripheral capillary membranes. The pore theory of capillary permeability
    • Pappenheimer J.R., Renkin E.M., and Borrero L.M. Filtration, diffusion, and molecular sieving through peripheral capillary membranes. The pore theory of capillary permeability. American Journal of Physiology 167 (1951) 13
    • (1951) American Journal of Physiology , vol.167 , pp. 13
    • Pappenheimer, J.R.1    Renkin, E.M.2    Borrero, L.M.3
  • 76
    • 0015821449 scopus 로고
    • Measurement of the permeability of biological membranes. Application to the glomerular wall
    • Verniory A., et al. Measurement of the permeability of biological membranes. Application to the glomerular wall. Journal of General Physiology 62 (1973) 489
    • (1973) Journal of General Physiology , vol.62 , pp. 489
    • Verniory, A.1
  • 77
    • 0020764089 scopus 로고
    • Characterization of ultrafiltration membranes. Part IV. Influence of the deformation of macromolecular solutes on the transport through ultrafiltration membranes
    • Nguyen Quang T., and Neel J. Characterization of ultrafiltration membranes. Part IV. Influence of the deformation of macromolecular solutes on the transport through ultrafiltration membranes. Journal of Membrane Science 14 (1983) 111
    • (1983) Journal of Membrane Science , vol.14 , pp. 111
    • Nguyen Quang, T.1    Neel, J.2
  • 78
    • 0016023565 scopus 로고
    • Mechanism of osmotic flow in porous membranes
    • Anderson J.L., and Malone D.M. Mechanism of osmotic flow in porous membranes. Biophysical Journal 14 (1974) 957
    • (1974) Biophysical Journal , vol.14 , pp. 957
    • Anderson, J.L.1    Malone, D.M.2
  • 80
    • 2942530873 scopus 로고    scopus 로고
    • Peptide attachment to vapor deposited polymeric thin films
    • Murthy S.K., Olsen B.D., and Gleason K.K. Peptide attachment to vapor deposited polymeric thin films. Langmuir 20 (2004) 4774
    • (2004) Langmuir , vol.20 , pp. 4774
    • Murthy, S.K.1    Olsen, B.D.2    Gleason, K.K.3
  • 81
    • 0032526793 scopus 로고    scopus 로고
    • Effect of chain density on inhibition of protein adsorption by poly(ethylene glycol) based coatings
    • Malmsten M., Emoto K., and Alstine J.M.V. Effect of chain density on inhibition of protein adsorption by poly(ethylene glycol) based coatings. Journal of Colloid and Interface Science 202 (1998) 507
    • (1998) Journal of Colloid and Interface Science , vol.202 , pp. 507
    • Malmsten, M.1    Emoto, K.2    Alstine, J.M.V.3
  • 83
    • 3042591776 scopus 로고    scopus 로고
    • Rapid cryofixation/freeze fracture for the study of nanobubbles at solid-liquid interfaces
    • Switkes M., and Ruberti J.W. Rapid cryofixation/freeze fracture for the study of nanobubbles at solid-liquid interfaces. Applied Physics Letters 84 (2004) 4759
    • (2004) Applied Physics Letters , vol.84 , pp. 4759
    • Switkes, M.1    Ruberti, J.W.2
  • 84
    • 33747848433 scopus 로고    scopus 로고
    • Nanobubbles in solid-state nanopores
    • 088101/1
    • Smeets R.M.M., et al. Nanobubbles in solid-state nanopores. Physical Review Letters 97 (2006) 088101/1
    • (2006) Physical Review Letters , vol.97
    • Smeets, R.M.M.1
  • 85
    • 12044254336 scopus 로고
    • Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide)-a model system using self-assembled monolayers
    • Prime K.L., and Whitesides G.M. Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide)-a model system using self-assembled monolayers. Journal of the American Chemical Society 115 (1993) 10714
    • (1993) Journal of the American Chemical Society , vol.115 , pp. 10714
    • Prime, K.L.1    Whitesides, G.M.2
  • 89
    • 0031106803 scopus 로고    scopus 로고
    • Viscosity and elasticity during collagen assembly in vitro: relevance to matrix-driven translocation
    • Newman S., et al. Viscosity and elasticity during collagen assembly in vitro: relevance to matrix-driven translocation. Biopolymers 41 (1997) 337
    • (1997) Biopolymers , vol.41 , pp. 337
    • Newman, S.1
  • 91
    • 0141453851 scopus 로고    scopus 로고
    • Liquid crystalline assemblies of collagen in bone and in vitro systems
    • Giraud-Guille M.-M., Besseau L., and Martin R. Liquid crystalline assemblies of collagen in bone and in vitro systems. Journal of Biomechanics 36 (2003) 1571
    • (2003) Journal of Biomechanics , vol.36 , pp. 1571
    • Giraud-Guille, M.-M.1    Besseau, L.2    Martin, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.