메뉴 건너뛰기




Volumn 85, Issue 5, 2003, Pages 2808-2817

Enzyme-Catalyzed Gel Proteolysis: An Anomalous Diffusion-Controlled Mechanism

Author keywords

[No Author keywords available]

Indexed keywords

GELATIN; METALLOPROTEINASE;

EID: 0242353865     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74704-3     Document Type: Article
Times cited : (23)

References (36)
  • 2
    • 0031022256 scopus 로고    scopus 로고
    • Anchorage-dependent cell cycle progression
    • Assoian, R. K. 1997. Anchorage-dependent cell cycle progression. J. Cell Biol. 136:1-4.
    • (1997) J. Cell Biol. , vol.136 , pp. 1-4
    • Assoian, R.K.1
  • 4
    • 0030271595 scopus 로고    scopus 로고
    • Focalized proteolysis: Spatial and temporal regulation of extracellular matrix degradation at the cell surface
    • Basbaum, C. B., and Z. Werb. 1996. Focalized proteolysis: spatial and temporal regulation of extracellular matrix degradation at the cell surface. Curr. Opin. Cell Biol. 8:731-738.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 731-738
    • Basbaum, C.B.1    Werb, Z.2
  • 5
    • 0032774242 scopus 로고    scopus 로고
    • Oscillatory behavior of a simple kinetic model for proteolysis during cell invasion
    • Berry, H., and V. Larreta-Garde. 1999. Oscillatory behavior of a simple kinetic model for proteolysis during cell invasion. Biophys. J. 77:655-665.
    • (1999) Biophys. J. , vol.77 , pp. 655-665
    • Berry, H.1    Larreta-Garde, V.2
  • 6
    • 0034672574 scopus 로고    scopus 로고
    • Gel-sol transition can describe the proteolysis of extracellular matrix gels
    • Berry, H., J. Pelta, D. Lairez, and V. Larreta-Garde. 2000. Gel-sol transition can describe the proteolysis of extracellular matrix gels. Biochem. Biophys. Arch. 1524:110-117.
    • (2000) Biochem. Biophys. Arch. , vol.1524 , pp. 110-117
    • Berry, H.1    Pelta, J.2    Lairez, D.3    Larreta-Garde, V.4
  • 8
    • 0344288274 scopus 로고    scopus 로고
    • Scaling properties of cracks
    • Bouchaud, E. 1997. Scaling properties of cracks. J Phys. Condens. Mat. 9:4319-4344.
    • (1997) J. Phys. Condens. Mat. , vol.9 , pp. 4319-4344
    • Bouchaud, E.1
  • 9
    • 0001134242 scopus 로고
    • Weak ergodicity breaking and aging in disordered systems
    • Bouchaud, J.-P. 1992. Weak ergodicity breaking and aging in disordered systems. J. Phys. I France. 2:1705-1713.
    • (1992) J. Phys. I France , vol.2 , pp. 1705-1713
    • Bouchaud, J.-P.1
  • 10
    • 0029030448 scopus 로고
    • Matrylisin inhibitor complexes: Commons themes among metalloproteases
    • Browner, M., W. W. Smith, and A. L. Castelhano. 1995. Matrylisin inhibitor complexes: commons themes among metalloproteases. Biochemistry. 34:6602-6610.
    • (1995) Biochemistry , vol.34 , pp. 6602-6610
    • Browner, M.1    Smith, W.W.2    Castelhano, A.L.3
  • 12
    • 0003932766 scopus 로고    scopus 로고
    • W. H. Freeman and Cie, New York
    • Creighton, T. E. 1997. Proteins. W. H. Freeman and Cie, New York.
    • (1997) Proteins
    • Creighton, T.E.1
  • 13
    • 0033592238 scopus 로고    scopus 로고
    • Mathematical modelling of extracellular matrix dynamics using discrete cells: Fiber orientation and tissue regeneration
    • Dallon, J. C., J. A. Sherratt, and P. K. Maini. 1999. Mathematical modelling of extracellular matrix dynamics using discrete cells: fiber orientation and tissue regeneration. J. Theor. Biol. 199:449-471.
    • (1999) J. Theor. Biol. , vol.199 , pp. 449-471
    • Dallon, J.C.1    Sherratt, J.A.2    Maini, P.K.3
  • 14
    • 0034123653 scopus 로고    scopus 로고
    • Interactions between tumor cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer
    • DeClerck, Y. A. 2000. Interactions between tumor cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer. Eur. J. Cancer. 36:1258-1268.
    • (2000) Eur. J. Cancer , vol.36 , pp. 1258-1268
    • DeClerck, Y.A.1
  • 17
    • 0035365438 scopus 로고    scopus 로고
    • Critical behavior of gelation probed by the dynamics of latex spheres
    • Fadda, G. C., D. Lairez, and J. Pelta. 2001. Critical behavior of gelation probed by the dynamics of latex spheres. Phys. Rev. E. 63:61405.
    • (2001) Phys. Rev. E. , vol.63 , pp. 61405
    • Fadda, G.C.1    Lairez, D.2    Pelta, J.3
  • 19
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • Furie, B., and B. C. Furie. 1988. The molecular basis of blood coagulation. Cell. 53:505-507.
    • (1988) Cell , vol.53 , pp. 505-507
    • Furie, B.1    Furie, B.C.2
  • 22
    • 0028915695 scopus 로고
    • X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors
    • Grams, F., P. Reinemer, J. C. Powers, R. Kleine, M. Pieper, H. Tschesche, R. Huber, and W. Bode. 1995. X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Eur. J. Biochem. 228:830-841.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 830-841
    • Grams, F.1    Reinemer, P.2    Powers, J.C.3    Kleine, R.4    Pieper, M.5    Tschesche, H.6    Huber, R.7    Bode, W.8
  • 25
    • 0036789423 scopus 로고    scopus 로고
    • Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy
    • Hess, S., and W. Hebb. 2002. Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy. Biophys. J. 83:2300-2317.
    • (2002) Biophys. J. , vol.83 , pp. 2300-2317
    • Hess, S.1    Hebb, W.2
  • 26
    • 0023038088 scopus 로고
    • A new way of enhancing the thermostability of proteases
    • Imanaka, T., M. Shibazaki, and M. Takagi. 1986. A new way of enhancing the thermostability of proteases. Nature. 324:695-696.
    • (1986) Nature , vol.324 , pp. 695-696
    • Imanaka, T.1    Shibazaki, M.2    Takagi, M.3
  • 27
    • 0036175642 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: The technique and its applications
    • Krichevsky, O., and G. Bonnet. 2002. Fluorescence correlation spectroscopy: the technique and its applications. Rep. Prog. Phys. 65:251-297.
    • (2002) Rep. Prog. Phys. , vol.65 , pp. 251-297
    • Krichevsky, O.1    Bonnet, G.2
  • 28
    • 0036389665 scopus 로고    scopus 로고
    • Modeling extracellular matrix degradation balance with proteinase/transglutaminase cycle
    • Larreta-Garde, V., and H. Berry. 2002. Modeling extracellular matrix degradation balance with proteinase/transglutaminase cycle. J. Theor. Biol. 251:105-124.
    • (2002) J. Theor. Biol. , vol.251 , pp. 105-124
    • Larreta-Garde, V.1    Berry, H.2
  • 29
    • 0014013148 scopus 로고
    • Observations on the specificity of thermolysin with peptides
    • Matsubara, H. 1966. Observations on the specificity of thermolysin with peptides. Biochem. Biophys. Res. Commum. 24:427-430.
    • (1966) Biochem. Biophys. Res. Commum. , vol.24 , pp. 427-430
    • Matsubara, H.1
  • 30
    • 0034176764 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Multifunctional contributors to tumor progression
    • McCawley, L. J., and L. M. Matrisian. 2000. Matrix metalloproteinases: multifunctional contributors to tumor progression. Mol. Med. Today. 6:149-156.
    • (2000) Mol. Med. Today , vol.6 , pp. 149-156
    • McCawley, L.J.1    Matrisian, L.M.2
  • 31
    • 0032820711 scopus 로고    scopus 로고
    • Proteolysis and cell migration: Creating a path?
    • Murphy, G., and J. Gavrilovic. 1999. Proteolysis and cell migration: creating a path? Curr. Opin. Cell Biol. 11:614-621.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 614-621
    • Murphy, G.1    Gavrilovic, J.2
  • 32
    • 0001516161 scopus 로고
    • Computer simulation studies of anomalous diffusion in gels: Structural and probe-size dependence
    • Netz, P. A., and T. Dorfmüller. 1995. Computer simulation studies of anomalous diffusion in gels: structural and probe-size dependence. J. Chem. Phys. 103:9074-9082.
    • (1995) J. Chem. Phys. , vol.103 , pp. 9074-9082
    • Netz, P.A.1    Dorfmüller, T.2
  • 34
    • 0032767250 scopus 로고    scopus 로고
    • Extracellular matrix concentration exerts selection pressure on invasive cells
    • Perumpanani, A. J., and H. M. Byrne. 1999. Extracellular matrix concentration exerts selection pressure on invasive cells. Eur. J. Cancer. 35:1274-1280.
    • (1999) Eur. J. Cancer , vol.35 , pp. 1274-1280
    • Perumpanani, A.J.1    Byrne, H.M.2
  • 35
    • 0000713036 scopus 로고    scopus 로고
    • Scaling properties of a percolation model with long-range correlations
    • Sahimi, M., and S. Mukhopadhyay. 1996. Scaling properties of a percolation model with long-range correlations. Phys. Rev. E. 54:3870-3880.
    • (1996) Phys. Rev. E , vol.54 , pp. 3870-3880
    • Sahimi, M.1    Mukhopadhyay, S.2
  • 36
    • 0001398890 scopus 로고
    • Long-range correlated percolation
    • Weinrib, A. 1984. Long-range correlated percolation. Phys. Rev. B. 29:387-395.
    • (1984) Phys. Rev. B , vol.29 , pp. 387-395
    • Weinrib, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.