메뉴 건너뛰기




Volumn 27, Issue 5, 1998, Pages 521-531

A mathematical approach to cytoskeletal assembly

Author keywords

Actin bundles and networks; Actin filaments; Cytoskeleton; Filament length distribution; Mathematical modelling

Indexed keywords

ACTIN FILAMENT; ARTICLE; BIOPHYSICS; CYTOSKELETON; MATHEMATICAL ANALYSIS; MATHEMATICAL MODEL; PHYSICAL CHEMISTRY; POLYMERIZATION; PROTEIN POLYMERIZATION; THERMODYNAMICS;

EID: 0031715906     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050162     Document Type: Article
Times cited : (16)

References (50)
  • 1
    • 0344049229 scopus 로고    scopus 로고
    • A mathematical model for ligand/receptor/G-protein dynamics and actin polymerization in human neutrophils
    • in press
    • Adams JA, Omann GM, Linderman J (1997) A mathematical model for ligand/receptor/G-protein dynamics and actin polymerization in human neutrophils. J Theor Biol (in press)
    • (1997) J Theor Biol
    • Adams, J.A.1    Omann, G.M.2    Linderman, J.3
  • 3
    • 0020825184 scopus 로고
    • Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament
    • Bonder EM, Fishind DJ, Mooseker MS (1983) Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell 34:491-501
    • (1983) Cell , vol.34 , pp. 491-501
    • Bonder, E.M.1    Fishind, D.J.2    Mooseker, M.S.3
  • 4
  • 5
    • 0026673419 scopus 로고
    • Quantitation of liquid-crystalline ordering in F-actin solutions
    • Coppin CM, Leavis P (1992) Quantitation of liquid-crystalline ordering in F-actin solutions. Biophys J 63:794-807
    • (1992) Biophys J , vol.63 , pp. 794-807
    • Coppin, C.M.1    Leavis, P.2
  • 6
    • 0028067048 scopus 로고
    • Nucleation of actin polymerization by gelsolin
    • Ditsch A, Wegner A (1994) Nucleation of actin polymerization by gelsolin. Eur J Biochem 224:223-227
    • (1994) Eur J Biochem , vol.224 , pp. 223-227
    • Ditsch, A.1    Wegner, A.2
  • 7
    • 0028902614 scopus 로고
    • Two low-affinity Ca++ binding sites of gelsolin that regulate association with actin filaments
    • Ditsch A, Wegner A (1995) Two low-affinity Ca++ binding sites of gelsolin that regulate association with actin filaments. Eur J Biochem 229:512-516
    • (1995) Eur J Biochem , vol.229 , pp. 512-516
    • Ditsch, A.1    Wegner, A.2
  • 9
    • 0032077675 scopus 로고    scopus 로고
    • Models for the length distribution of actin filaments: I: Simple polymerization and fragmentation acting alone
    • Edelstein-Keshet L, Ermentrout GB (1998) Models for the length distribution of actin filaments: I: Simple polymerization and fragmentation acting alone. Bull Math Biol 60:449-475
    • (1998) Bull Math Biol , vol.60 , pp. 449-475
    • Edelstein-Keshet, L.1    Ermentrout, G.B.2
  • 10
    • 0032078453 scopus 로고    scopus 로고
    • Models for the length distribution of actin filaments: II: Polymerization and fragmentation by gelsolin actin together
    • Ermentrout GB, Edelstein-Keshet L (1998) Models for the length distribution of actin filaments: II: Polymerization and fragmentation by gelsolin actin together. Bull Math Biol 60:477-503
    • (1998) Bull Math Biol , vol.60 , pp. 477-503
    • Ermentrout, G.B.1    Edelstein-Keshet, L.2
  • 11
    • 0026778554 scopus 로고
    • Effects of the neuronal phosphoprotein synaptin I on actin polymerization: II analytic interpretation of kinetic curves
    • Fesce R, Benfenati F, Greengard P, Valtorta F (1992) Effects of the neuronal phosphoprotein synaptin I on actin polymerization: II analytic interpretation of kinetic curves. J Biol Chem 267: 11289-11299
    • (1992) J Biol Chem , vol.267 , pp. 11289-11299
    • Fesce, R.1    Benfenati, F.2    Greengard, P.3    Valtorta, F.4
  • 13
    • 0039552510 scopus 로고
    • 2+ - Induced process at pH 8 and 20°C
    • 2+ - induced process at pH 8 and 20°C. Proc Natl Acad Sci USA 80:6513-6517
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 6513-6517
    • Frieden, C.1
  • 14
    • 0027490576 scopus 로고
    • Formation of liquid crystals from actin filaments
    • Furukawa R, Kundra R, Fechheimer M (1993) Formation of liquid crystals from actin filaments. Biochemistry 32:12346-12352
    • (1993) Biochemistry , vol.32 , pp. 12346-12352
    • Furukawa, R.1    Kundra, R.2    Fechheimer, M.3
  • 15
    • 0344211073 scopus 로고    scopus 로고
    • Integro-differential model for orientational distribution of F-actin in cells
    • submitted
    • Geigant E, Ladizhansky K, Mogilner A (1997) Integro-differential model for orientational distribution of F-actin in cells (submitted to SIAM J Appl Math)
    • (1997) SIAM J Appl Math
    • Geigant, E.1    Ladizhansky, K.2    Mogilner, A.3
  • 17
    • 0028849485 scopus 로고
    • Sequences of actin implicated in the polymerization process: A simplified mathematical approach to probe the role of these segments
    • Houmeida A, Bennes R, Benyamin Y, Roustan C (1995) Sequences of actin implicated in the polymerization process: a simplified mathematical approach to probe the role of these segments. Biophys Chem 56:201-214
    • (1995) Biophys Chem , vol.56 , pp. 201-214
    • Houmeida, A.1    Bennes, R.2    Benyamin, Y.3    Roustan, C.4
  • 19
    • 0022969835 scopus 로고
    • Structure and mobility of actin filaments as measured by quasielectric light scattering, viscometry and electron microscopy
    • Janmey PA, Peetermans J, Zaner KS, Stossel TP, Tanaka T (1986) Structure and mobility of actin filaments as measured by quasielectric light scattering, viscometry and electron microscopy. J Biol Chem 261:8357-8362
    • (1986) J Biol Chem , vol.261 , pp. 8357-8362
    • Janmey, P.A.1    Peetermans, J.2    Zaner, K.S.3    Stossel, T.P.4    Tanaka, T.5
  • 20
    • 0030025568 scopus 로고    scopus 로고
    • F-actin a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions
    • Käs J, Strey H, Tang TX, Finger D, Ezzell R, Sackmann E, Janmey PA (1996) F-actin a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions. Biophys J 70:609-625
    • (1996) Biophys J , vol.70 , pp. 609-625
    • Käs, J.1    Strey, H.2    Tang, T.X.3    Finger, D.4    Ezzell, R.5    Sackmann, E.6    Janmey, P.A.7
  • 21
    • 0014755321 scopus 로고
    • Electron microscopic particle length of F-actin polymerized in vitro
    • Kawamura M, Maruyama K (1970) Electron microscopic particle length of F-actin polymerized in vitro. J Biochem 67:437-457
    • (1970) J Biochem , vol.67 , pp. 437-457
    • Kawamura, M.1    Maruyama, K.2
  • 22
    • 0023637721 scopus 로고
    • Actin polymerization and ATP hydrolysis
    • Korn ED, Carlier M, Pantaloni D (1987) Actin polymerization and ATP hydrolysis. Science 238:638-644
    • (1987) Science , vol.238 , pp. 638-644
    • Korn, E.D.1    Carlier, M.2    Pantaloni, D.3
  • 24
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger DA, Horowitz AF (1996) Cell migration: a physically integrated molecular process, Cell 84:359-369
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horowitz, A.F.2
  • 25
    • 0027216184 scopus 로고
    • Cellular automation model of the actin cytoskeleton
    • Lumsden CJ, Dufort PA (1993) Cellular automation model of the actin cytoskeleton. Cell Motil Cytoskel 25:87-104
    • (1993) Cell Motil Cytoskel , vol.25 , pp. 87-104
    • Lumsden, C.J.1    Dufort, P.A.2
  • 26
    • 0028981496 scopus 로고
    • Actin-based movement of listeria monocytogenes: Actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface
    • Marchand J, Moreau P, Paoletti A, Cossart P, Carlier M, Pantaloni D (1995) Actin-based movement of listeria monocytogenes: actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface. J Cell Biol 130: 331-343
    • (1995) J Cell Biol , vol.130 , pp. 331-343
    • Marchand, J.1    Moreau, P.2    Paoletti, A.3    Cossart, P.4    Carlier, M.5    Pantaloni, D.6
  • 27
    • 0025339009 scopus 로고
    • Bundling of actin filaments by α-actinin depends on its molecular length
    • Meyer RK, Aebi U (1990) Bundling of actin filaments by α-actinin depends on its molecular length, J Cell Biol 110:2013-2024
    • (1990) J Cell Biol , vol.110 , pp. 2013-2024
    • Meyer, R.K.1    Aebi, U.2
  • 28
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison TJ, Cramer L (1996) Actin-based cell motility and cell locomotion. Cell 84:371-379
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.2
  • 29
    • 0001262652 scopus 로고
    • Selecting a common direction. I. how orientational order can arise from simple contact responses between interacting cells
    • Mogilner A, Edelstein-Keshet L (1995) Selecting a common direction. I. how orientational order can arise from simple contact responses between interacting cells. J Math Biol 33:619-660
    • (1995) J Math Biol , vol.33 , pp. 619-660
    • Mogilner, A.1    Edelstein-Keshet, L.2
  • 30
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • Mogilner A, Oster G (1996) Cell motility driven by actin polymerization. Biophys J 71:3030-3045
    • (1996) Biophys J , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 31
    • 0023850743 scopus 로고
    • On the elasticity of the cytoskeletal networks
    • Nossal R (1988) On the elasticity of the cytoskeletal networks. Biophys J 53:349-359
    • (1988) Biophys J , vol.53 , pp. 349-359
    • Nossal, R.1
  • 32
    • 33947613349 scopus 로고
    • A theory of linear and helical aggregations of macromolecules
    • Oosawa F, Kasai M (1962) A theory of linear and helical aggregations of macromolecules. J Mol Biol 4:10-21
    • (1962) J Mol Biol , vol.4 , pp. 10-21
    • Oosawa, F.1    Kasai, M.2
  • 33
    • 0010498030 scopus 로고
    • University of California Berkeley, Lecture Notes
    • Oster GF (1994) Biophysics of cell motility. University of California Berkeley, Lecture Notes
    • (1994) Biophysics of Cell Motility
    • Oster, G.F.1
  • 35
    • 0026955828 scopus 로고
    • Qualsielectric light scattering study of thermal excitations of F-actin solutions and of growth kinetics of actin filaments
    • Piekenbrock T, Sackmann E (1992) Qualsielectric light scattering study of thermal excitations of F-actin solutions and of growth kinetics of actin filaments. Biopolymers 32:1471-1489
    • (1992) Biopolymers , vol.32 , pp. 1471-1489
    • Piekenbrock, T.1    Sackmann, E.2
  • 36
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard TD (1986) Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J Cell Biol 103:2747-2754
    • (1986) J Cell Biol , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 37
    • 0026343674 scopus 로고
    • Rate constants and equilibrium constants for binding of actin to the 1:1 gelsolin-actin complex
    • Schoepper B, Wegner A (1991) Rate constants and equilibrium constants for binding of actin to the 1:1 gelsolin-actin complex. Eur J Biochem 202:1127-1131
    • (1991) Eur J Biochem , vol.202 , pp. 1127-1131
    • Schoepper, B.1    Wegner, A.2
  • 38
    • 0026751205 scopus 로고
    • Gelsolin binds to polymeric actin at a low rate
    • Schoepper B, Wegner A (1992) Gelsolin binds to polymeric actin at a low rate. J Biol Chem 267:13924-13927
    • (1992) J Biol Chem , vol.267 , pp. 13924-13927
    • Schoepper, B.1    Wegner, A.2
  • 40
    • 0023053136 scopus 로고
    • Rate of treadmilling of actin filaments in vitro
    • Selve N, Wegner A (1986) Rate of treadmilling of actin filaments in vitro. J Mol Biol 187:627-631
    • (1986) J Mol Biol , vol.187 , pp. 627-631
    • Selve, N.1    Wegner, A.2
  • 42
    • 0026011498 scopus 로고
    • Formation of liquid crystalline phase of actin filament solutions and its dependence on filament length as studied by optical birefringence
    • Suzuki A, Maeda T, Ito T (1991) Formation of liquid crystalline phase of actin filament solutions and its dependence on filament length as studied by optical birefringence. Biophys J 59:25-30
    • (1991) Biophys J , vol.59 , pp. 25-30
    • Suzuki, A.1    Maeda, T.2    Ito, T.3
  • 43
    • 0030012323 scopus 로고    scopus 로고
    • The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation
    • Tang JX, Janmey PA (1996) The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation. J Biol Chem 271:8556-8563
    • (1996) J Biol Chem , vol.271 , pp. 8556-8563
    • Tang, J.X.1    Janmey, P.A.2
  • 44
    • 0000247799 scopus 로고    scopus 로고
    • Temperature-induced solgel transition and microgel formation in α-actinin cross-linked actin networks: A rheological study
    • Tempel M, Isenberg G, Sackmann E (1996) Temperature-induced solgel transition and microgel formation in α-actinin cross-linked actin networks: a rheological study. Phys Rev E 54: 1802-1810
    • (1996) Phys Rev E , vol.54 , pp. 1802-1810
    • Tempel, M.1    Isenberg, G.2    Sackmann, E.3
  • 45
    • 0028065195 scopus 로고
    • Actin filament dynamics in cell motility
    • Estes JE, Higgings PJ (eds) Plenum Press, New York
    • Theriot JA (1994) Actin filament dynamics in cell motility. In: Estes JE, Higgings PJ (eds) Actin: biophysics, biochemistry, and cell biology. Plenum Press, New York, pp 133-145
    • (1994) Actin: Biophysics, Biochemistry, and Cell Biology , pp. 133-145
    • Theriot, J.A.1
  • 46
    • 0021099326 scopus 로고
    • The kinetics of actin nucleation and polymerization
    • Tobacman LS, Korn ED (1983) The kinetics of actin nucleation and polymerization. J Biol Chem 258:3206-3214
    • (1983) J Biol Chem , vol.258 , pp. 3206-3214
    • Tobacman, L.S.1    Korn, E.D.2
  • 47
    • 0027162413 scopus 로고
    • Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels
    • Wachsstock DH, Schwarz WH, Pollard TD (1993) Affinity of α-actinin for actin determines the structure and mechanical properties of actin filament gels. Biophys J 65:205-214
    • (1993) Biophys J , vol.65 , pp. 205-214
    • Wachsstock, D.H.1    Schwarz, W.H.2    Pollard, T.D.3
  • 48
    • 0028265522 scopus 로고
    • Cross-linker dynamics determine the mechanical properties of actin gels
    • Wachsstock DH, Schwarz WH, Pollard TD (1994) Cross-linker dynamics determine the mechanical properties of actin gels. Biophys J 66:801-809
    • (1994) Biophys J , vol.66 , pp. 801-809
    • Wachsstock, D.H.1    Schwarz, W.H.2    Pollard, T.D.3
  • 49
    • 0028934511 scopus 로고
    • Physics of actin networks. I. rheology of semi-dilute F-Actin
    • Zaner KS (1995) Physics of actin networks. I. rheology of semi-dilute F-Actin. Biophys 168:1019-1026
    • (1995) Biophys , vol.168 , pp. 1019-1026
    • Zaner, K.S.1
  • 50
    • 0027293382 scopus 로고
    • Recent quantitative studies of actin filament turnover during cell locomotion
    • Zigmond SH (1993) Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motil Cytoskel 25: 309-316
    • (1993) Cell Motil Cytoskel , vol.25 , pp. 309-316
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.