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Volumn 268, Issue 3, 2002, Pages 239-251

How did cells get their size?

Author keywords

Curvature; Evolution; Mechanosensitive; Membrane; Prebiotic; Pump; Shape; Surface area; Tension; Volume

Indexed keywords

ALIPHATIC HYDROCARBON; AMINO ACID; AMPHOPHILE; GENE PRODUCT; LIPOSOME;

EID: 0036828867     PISSN: 0003276X     EISSN: None     Source Type: Journal    
DOI: 10.1002/ar.10158     Document Type: Article
Times cited : (32)

References (118)
  • 1
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett MJ, Schlunegger MP, Eisenberg D. 1995. 3D domain swapping: A mechanism for oligomer assembly. Protein Sci 4:2455-2468.
    • (1995) Protein Sci , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 2
    • 0034757216 scopus 로고    scopus 로고
    • Kinetics of membrane adhesion mediated by ligand-receptor interaction studied with a biomimetic system
    • Boulbitch A, Guttenberg Z, Sackmann E. 2001. Kinetics of membrane adhesion mediated by ligand-receptor interaction studied with a biomimetic system. Biophys J 81:2743-2751.
    • (2001) Biophys J , vol.81 , pp. 2743-2751
    • Boulbitch, A.1    Guttenberg, Z.2    Sackmann, E.3
  • 3
    • 0031771711 scopus 로고    scopus 로고
    • Gigantism in a bacterium, Epulopiscium fishelsoni, correlates with complex patterns in arrangement, quantity, and segregation of DNA
    • Bresler V, Montgomery WL, Fishelson L, Pollak PE. 1998. Gigantism in a bacterium, Epulopiscium fishelsoni, correlates with complex patterns in arrangement, quantity, and segregation of DNA. J Bacteriol 180:5601-5611.
    • (1998) J Bacteriol , vol.180 , pp. 5601-5611
    • Bresler, V.1    Montgomery, W.L.2    Fishelson, L.3    Pollak, P.E.4
  • 4
    • 0034529090 scopus 로고    scopus 로고
    • Macromolecular crowding as a cell volume sensor
    • Burg MB. 2000. Macromolecular crowding as a cell volume sensor. Cell Physiol Biochem 10:251-256.
    • (2000) Cell Physiol Biochem , vol.10 , pp. 251-256
    • Burg, M.B.1
  • 5
    • 0034633997 scopus 로고    scopus 로고
    • Dynamin is membrane-active: Lipid insertion is induced by phosphoinositides and phosphatidic acid
    • Burger KN, Demel RA, Schmid SL, de Kruijff B. 2000. Dynamin is membrane-active: Lipid insertion is induced by phosphoinositides and phosphatidic acid. Biochemistry 39:12485-12493.
    • (2000) Biochemistry , vol.39 , pp. 12485-12493
    • Burger, K.N.1    Demel, R.A.2    Schmid, S.L.3    De Kruijff, B.4
  • 6
    • 0034793735 scopus 로고    scopus 로고
    • The structure of an engineered domain-swapped ribonuclease dimer and its implications for the evolution of proteins toward oligomerization
    • Canals A, Pous J, Guasch A, Benito A, Ribo M, Vilanova M, Coll M. 2001. The structure of an engineered domain-swapped ribonuclease dimer and its implications for the evolution of proteins toward oligomerization. Structure 9:967-976.
    • (2001) Structure , vol.9 , pp. 967-976
    • Canals, A.1    Pous, J.2    Guasch, A.3    Benito, A.4    Ribo, M.5    Vilanova, M.6    Coll, M.7
  • 7
    • 0033370004 scopus 로고    scopus 로고
    • The skeletal function of nongenic nuclear DNA: New evidence from ancient cell chimaeras
    • Cavalier-Smith T, Beaton MJ. 1999. The skeletal function of nongenic nuclear DNA: New evidence from ancient cell chimaeras. Genetica 106:3-13.
    • (1999) Genetica , vol.106 , pp. 3-13
    • Cavalier-Smith, T.1    Beaton, M.J.2
  • 8
    • 0028287304 scopus 로고
    • Permeation of membranes by the neutral form of amino acids and peptides: Relevance to the origin of peptide translocation
    • Chakrabarti AC, Deamer DW. 1994. Permeation of membranes by the neutral form of amino acids and peptides: Relevance to the origin of peptide translocation. J Mol Evol 39:1-5.
    • (1994) J Mol Evol , vol.39 , pp. 1-5
    • Chakrabarti, A.C.1    Deamer, D.W.2
  • 9
    • 0029781698 scopus 로고    scopus 로고
    • Formation of ordered domains in membrane-bound DNA
    • Dan N. 1996. Formation of ordered domains in membrane-bound DNA. Biophys J 71:1267-1272.
    • (1996) Biophys J , vol.71 , pp. 1267-1272
    • Dan, N.1
  • 10
    • 0030874402 scopus 로고    scopus 로고
    • Proof for a nonproteinaceous calcium-selective channel in Escherichia coli by total synthesis from (R)-3-hydroxybutanoic acid and inorganic polyphosphate
    • Das S, Lengweiler UD, Seebach D, Reusch RN.1997. Proof for a nonproteinaceous calcium-selective channel in Escherichia coli by total synthesis from (R)-3-hydroxybutanoic acid and inorganic polyphosphate. Proc Natl Acad Sci USA 94:9075-9079.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9075-9079
    • Das, S.1    Lengweiler, U.D.2    Seebach, D.3    Reusch, R.N.4
  • 11
    • 0027106778 scopus 로고
    • Polycyclic aromatic hydrocarbons: Primitive pigment systems in the prebiotic environment
    • Deamer DW. 1992. Polycyclic aromatic hydrocarbons: Primitive pigment systems in the prebiotic environment. Adv Space Res 12:183-189.
    • (1992) Adv Space Res , vol.12 , pp. 183-189
    • Deamer, D.W.1
  • 12
    • 0030741176 scopus 로고    scopus 로고
    • The first living systems: A bioenergetic perspective
    • Deamer DW. 1997. The first living systems: A bioenergetic perspective. Microbiol Mol Biol Rev 61:239-261.
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 239-261
    • Deamer, D.W.1
  • 13
    • 0342758500 scopus 로고    scopus 로고
    • Stability analysis of micropipette aspiration of neutrophils
    • Derganc J, Bozic B, Svetina S, Zeks B. 2000. Stability analysis of micropipette aspiration of neutrophils. Biophys J 79:153-162.
    • (2000) Biophys J , vol.79 , pp. 153-162
    • Derganc, J.1    Bozic, B.2    Svetina, S.3    Zeks, B.4
  • 14
    • 0030886104 scopus 로고    scopus 로고
    • Isotopic evidence for extraterrestrial non-racemic amino acids in the Murchison meteorite
    • Engel MH, Macko SA. 1997. Isotopic evidence for extraterrestrial non-racemic amino acids in the Murchison meteorite. Nature 389:265-268.
    • (1997) Nature , vol.389 , pp. 265-268
    • Engel, M.H.1    Macko, S.A.2
  • 15
    • 0035066482 scopus 로고    scopus 로고
    • Dipole potentials indicate restructuring of the membrane interface induced by gadolinium and beryllium ions
    • Ermakov YA, Averbakh AZ, Yusipovich AI, Sukharev S. 2001. Dipole potentials indicate restructuring of the membrane interface induced by gadolinium and beryllium ions. Biophys J 80:1851-1862.
    • (2001) Biophys J , vol.80 , pp. 1851-1862
    • Ermakov, Y.A.1    Averbakh, A.Z.2    Yusipovich, A.I.3    Sukharev, S.4
  • 16
    • 0026651919 scopus 로고
    • Shape changes of giant liposomes induced by an asymmetric transmembrane distribution of phospholipids
    • Farge E, Devaux PF. 1992. Shape changes of giant liposomes induced by an asymmetric transmembrane distribution of phospholipids. Biophys J 61:347-357.
    • (1992) Biophys J , vol.61 , pp. 347-357
    • Farge, E.1    Devaux, P.F.2
  • 17
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • Farsad K, Ringstad N, Takei K, Floyd SR, Rose K, De Camilli P. 2001. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J Cell Biol 155:193-200.
    • (2001) J Cell Biol , vol.155 , pp. 193-200
    • Farsad, K.1    Ringstad, N.2    Takei, K.3    Floyd, S.R.4    Rose, K.5    De Camilli, P.6
  • 18
    • 0031904167 scopus 로고    scopus 로고
    • Peptide ion channels: Design and creation of function
    • Futaki S. 1998. Peptide ion channels: Design and creation of function. Biopolymers 47:75-81.
    • (1998) Biopolymers , vol.47 , pp. 75-81
    • Futaki, S.1
  • 20
    • 0035090476 scopus 로고    scopus 로고
    • Coincidence, coevolution, or causation? DNA content, cell size, and the C-value enigma
    • Gregory TR. 2001. Coincidence, coevolution, or causation? DNA content, cell size, and the C-value enigma. Biol Rev Camb Philos Soc 76:65-101.
    • (2001) Biol Rev Camb Philos Soc , vol.76 , pp. 65-101
    • Gregory, T.R.1
  • 21
    • 0027375921 scopus 로고
    • Design of a functional calcium channel protein: Inferences about an ion channel-forming motif derived from the primary structure of voltage-gated calcium channels
    • Grove A, Tomich JM, Iwamoto T, Montal M. 1993. Design of a functional calcium channel protein: Inferences about an ion channel-forming motif derived from the primary structure of voltage-gated calcium channels. Protein Sci 2:1918-1930.
    • (1993) Protein Sci , vol.2 , pp. 1918-1930
    • Grove, A.1    Tomich, J.M.2    Iwamoto, T.3    Montal, M.4
  • 22
    • 0034995804 scopus 로고    scopus 로고
    • Stretch-activation and stretch-inactivation of Shaker-IR, a voltage-gated K+ channel
    • Gu CX, Juranka PF, Morris CE. 2001. Stretch-activation and stretch-inactivation of Shaker-IR, a voltage-gated K+ channel. Biophys J 80:2678-2693.
    • (2001) Biophys J , vol.80 , pp. 2678-2693
    • Gu, C.X.1    Juranka, P.F.2    Morris, C.E.3
  • 23
    • 0018119270 scopus 로고
    • Liposomes from ionic, single-chain amphiphiles
    • Hargreaves WR, Deamer DW. 1978. Liposomes from ionic, single-chain amphiphiles. Biochemistry 17:3759-3768.
    • (1978) Biochemistry , vol.17 , pp. 3759-3768
    • Hargreaves, W.R.1    Deamer, D.W.2
  • 24
    • 0034332317 scopus 로고    scopus 로고
    • Molecular melodies in high and low C
    • Hartl DL. 2000. Molecular melodies in high and low C. Nat Rev Genet 1:145-149.
    • (2000) Nat Rev Genet , vol.1 , pp. 145-149
    • Hartl, D.L.1
  • 25
    • 0030048284 scopus 로고    scopus 로고
    • The role of cellular hydration in the regulation of cell function
    • Haussinger D. 1996. The role of cellular hydration in the regulation of cell function. Biochem J 313:697-710.
    • (1996) Biochem J , vol.313 , pp. 697-710
    • Haussinger, D.1
  • 26
    • 0033770910 scopus 로고    scopus 로고
    • Opposing views on tensegrity as a structural framework for understanding cell mechanics
    • Heidemann SR, Lamoureaux P, Buxbaum RE. 2000. Opposing views on tensegrity as a structural framework for understanding cell mechanics. Appl Physiol 89:1670-1678.
    • (2000) Appl Physiol , vol.89 , pp. 1670-1678
    • Heidemann, S.R.1    Lamoureaux, P.2    Buxbaum, R.E.3
  • 27
    • 2542527682 scopus 로고    scopus 로고
    • Collective membrane motions of high and low amplitude, studied by dynamic light scattering and micro-interferometry
    • Hirn R, Bayerl TM, Radler JO, Sackmann E. 1998. Collective membrane motions of high and low amplitude, studied by dynamic light scattering and micro-interferometry. Faraday Discuss 111:17-30.
    • (1998) Faraday Discuss , vol.111 , pp. 17-30
    • Hirn, R.1    Bayerl, T.M.2    Radler, J.O.3    Sackmann, E.4
  • 28
    • 0021755796 scopus 로고
    • Transformation pathways of liposomes
    • Hotani H. 1984. Transformation pathways of liposomes. J Mol Biol 178:113-120.
    • (1984) J Mol Biol , vol.178 , pp. 113-120
    • Hotani, H.1
  • 30
    • 0032618124 scopus 로고    scopus 로고
    • Peptide-lipid interactions and mechanisms of antimicrobial peptides
    • Huang HW. 1999. Peptide-lipid interactions and mechanisms of antimicrobial peptides. Novartis Found Symp 225:188-200.
    • (1999) Novartis Found Symp , vol.225 , pp. 188-200
    • Huang, H.W.1
  • 31
    • 0034539308 scopus 로고    scopus 로고
    • The origin of cellular life
    • Ingber DE. 2000. The origin of cellular life. Bioessays 22:1160-1170.
    • (2000) Bioessays , vol.22 , pp. 1160-1170
    • Ingber, D.E.1
  • 32
    • 0028124584 scopus 로고
    • Design and synthesis of amphipathic 3(10)-helical peptides and their interactions with phospholipid bilayers and ion channel formation
    • Iwata T, Lee S, Oishi O, Aoyagi H, Ohno M, Anzai K, Kirino Y, Sugihara G. 1994. Design and synthesis of amphipathic 3(10)-helical peptides and their interactions with phospholipid bilayers and ion channel formation. J Biol Chem 269:4928-4933.
    • (1994) J Biol Chem , vol.269 , pp. 4928-4933
    • Iwata, T.1    Lee, S.2    Oishi, O.3    Aoyagi, H.4    Ohno, M.5    Anzai, K.6    Kirino, Y.7    Sugihara, G.8
  • 33
    • 0035811487 scopus 로고    scopus 로고
    • Morphological and ecological complexity in early eukaryotic ecosystems
    • Javaux EJ, Knoll AH, Walter MR. 2001. Morphological and ecological complexity in early eukaryotic ecosystems. Nature 412:66-69.
    • (2001) Nature , vol.412 , pp. 66-69
    • Javaux, E.J.1    Knoll, A.H.2    Walter, M.R.3
  • 34
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones LJ, Carballido-Lopez R, Errington J. 2001. Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis. Cell 104:913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 36
    • 0032545175 scopus 로고    scopus 로고
    • Morphological transformation of liposomes caused by assembly of encapsulated tubulin and determination of shape by microtubule-associated proteins (MAPs)
    • Kaneko T, Itoh TJ, Hotani H. 1998. Morphological transformation of liposomes caused by assembly of encapsulated tubulin and determination of shape by microtubule-associated proteins (MAPs). J Mol Biol 284:1671-1681.
    • (1998) J Mol Biol , vol.284 , pp. 1671-1681
    • Kaneko, T.1    Itoh, T.J.2    Hotani, H.3
  • 37
    • 0034744192 scopus 로고    scopus 로고
    • Mechanosensitive Ca(2+) release from intracellular stores in Nitella flexilis
    • Kikuyama M, Tazawa M. 2001. Mechanosensitive Ca(2+) release from intracellular stores in Nitella flexilis. Plant Cell Physiol 42:358-365.
    • (2001) Plant Cell Physiol , vol.42 , pp. 358-365
    • Kikuyama, M.1    Tazawa, M.2
  • 38
    • 0031754539 scopus 로고    scopus 로고
    • Curvature-mediated interactions between membrane proteins
    • Kim KS, Neu J, Oster G. 1998. Curvature-mediated interactions between membrane proteins. Biophys J 75:2274-2291.
    • (1998) Biophys J , vol.75 , pp. 2274-2291
    • Kim, K.S.1    Neu, J.2    Oster, G.3
  • 40
    • 0034065138 scopus 로고    scopus 로고
    • Partners in protection: Interdependence of cytoskeleton and plasma membrane in adaptations to applied forces
    • Ko KS, McCulloch CA. 2000. Partners in protection: Interdependence of cytoskeleton and plasma membrane in adaptations to applied forces. J Membr Biol 174:85-95.
    • (2000) J Membr Biol , vol.174 , pp. 85-95
    • Ko, K.S.1    McCulloch, C.A.2
  • 41
    • 0035102588 scopus 로고    scopus 로고
    • Fission of biological membranes: Interplay between dynamin and lipids
    • Kozlov MM. 2001. Fission of biological membranes: Interplay between dynamin and lipids. Traffic 2:51-65
    • (2001) Traffic , vol.2 , pp. 51-65
    • Kozlov, M.M.1
  • 42
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear JD, Wasserman ZR, DeGrado WF. 1988. Synthetic amphiphilic peptide models for protein ion channels. Science 240:1177-11781.
    • (1988) Science , vol.240 , pp. 1177-11781
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 43
    • 0035193296 scopus 로고    scopus 로고
    • Deformation-enhanced fluctuations in the red cell skeleton with theoretical relations to elasticity, connectivity, and spectrin unfolding
    • Lee JC, Discher DE. 2001. Deformation-enhanced fluctuations in the red cell skeleton with theoretical relations to elasticity, connectivity, and spectrin unfolding. Biophys J 81:3178-3192.
    • (2001) Biophys J , vol.81 , pp. 3178-3192
    • Lee, J.C.1    Discher, D.E.2
  • 44
    • 0028296746 scopus 로고
    • Two mode ion channels induced by interaction of acidic amphipathic alpha-helical peptides with lipid bilayers
    • Lee S, Tanaka T, Anzai K, Kirino Y, Aoyagi H, Sugihara G. 1994. Two mode ion channels induced by interaction of acidic amphipathic alpha-helical peptides with lipid bilayers. Biochim Biophys Acta 1191:181-189.
    • (1994) Biochim Biophys Acta , vol.1191 , pp. 181-189
    • Lee, S.1    Tanaka, T.2    Anzai, K.3    Kirino, Y.4    Aoyagi, H.5    Sugihara, G.6
  • 45
    • 0023051515 scopus 로고
    • Elasticity of synthetic phospholipid vesicles and submitochondrial particles during osmotic swelling
    • Li W, Aurora TS, Haines TH, Cummins HZ. 1986. Elasticity of synthetic phospholipid vesicles and submitochondrial particles during osmotic swelling. Biochemistry 25:8220-8229.
    • (1986) Biochemistry , vol.25 , pp. 8220-8229
    • Li, W.1    Aurora, T.S.2    Haines, T.H.3    Cummins, H.Z.4
  • 46
    • 0025968124 scopus 로고
    • The conformation of membranes
    • Lipowsky R. 1991. The conformation of membranes. Nature 349:475-481.
    • (1991) Nature , vol.349 , pp. 475-481
    • Lipowsky, R.1
  • 47
    • 0029152051 scopus 로고
    • The morphology of lipid membranes
    • Lipowsky R. 1995. The morphology of lipid membranes. Curr Opin Struct Biol 5:531-540.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 531-540
    • Lipowsky, R.1
  • 48
    • 37649032089 scopus 로고    scopus 로고
    • Random walks of cytoskeletal motors in open and closed compartments
    • Lipowsky R, Klumpp S, Nieuwenhuizen TM. 2001. Random walks of cytoskeletal motors in open and closed compartments. Phys Rev Lett 87:108101.
    • (2001) Phys Rev Lett , vol.87 , pp. 108101
    • Lipowsky, R.1    Klumpp, S.2    Nieuwenhuizen, T.M.3
  • 49
    • 0021771665 scopus 로고
    • Influence of vesicle size and oxidase content on respiratory control in reconstituted cytochrome oxidase vesicles
    • Madden TD, Hope MJ, Cullis PR. 1984. Influence of vesicle size and oxidase content on respiratory control in reconstituted cytochrome oxidase vesicles. Biochemistry 23:1413-1418.
    • (1984) Biochemistry , vol.23 , pp. 1413-1418
    • Madden, T.D.1    Hope, M.J.2    Cullis, P.R.3
  • 50
    • 0029870676 scopus 로고    scopus 로고
    • Peptide models for membrane channels
    • Marsh D. 1996. Peptide models for membrane channels. Biochem J 315:345-361.
    • (1996) Biochem J , vol.315 , pp. 345-361
    • Marsh, D.1
  • 51
    • 0035851915 scopus 로고    scopus 로고
    • Intraflagellar transport balances continuous turnover of outer doublet microtubules: Implications for flagellar length control
    • Marshall WF, Rosenbaum JL. 2001. Intraflagellar transport balances continuous turnover of outer doublet microtubules: Implications for flagellar length control. J Cell Biol 155:405-414.
    • (2001) J Cell Biol , vol.155 , pp. 405-414
    • Marshall, W.F.1    Rosenbaum, J.L.2
  • 52
    • 0035085703 scopus 로고    scopus 로고
    • Mechanosensitive channels in prokaryotes
    • Martinac B. 2001. Mechanosensitive channels in prokaryotes. Cell Physiol Biochem 11:61-76.
    • (2001) Cell Physiol Biochem , vol.11 , pp. 61-76
    • Martinac, B.1
  • 53
    • 0027264486 scopus 로고
    • Rate-limiting step in electron transport. Osmotically sensitive diffusion of quinones through voids in the bilayer
    • Mathai JC, Sauna ZE, John O, Sitaramam V. 1993. Rate-limiting step in electron transport. Osmotically sensitive diffusion of quinones through voids in the bilayer. J Biol Chem 268:15442-15454.
    • (1993) J Biol Chem , vol.268 , pp. 15442-15454
    • Mathai, J.C.1    Sauna, Z.E.2    John, O.3    Sitaramam, V.4
  • 56
    • 0026482154 scopus 로고
    • Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles
    • Miyata H, Hotani H. 1992. Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles. Proc Natl Acad Sci USA 89:11547-11551.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11547-11551
    • Miyata, H.1    Hotani, H.2
  • 58
    • 0035107292 scopus 로고    scopus 로고
    • Nutrient uptake by protocells: A liposome model system
    • Monnard PA, Deamer DW. 2001. Nutrient uptake by protocells: A liposome model system. Orig Life Evol Biosph 31:147-155.
    • (2001) Orig Life Evol Biosph , vol.31 , pp. 147-155
    • Monnard, P.A.1    Deamer, D.W.2
  • 59
    • 0025007175 scopus 로고
    • Synporins - Synthetic proteins that emulate the pore structure of biological ionic channels
    • Montal M, Montal MS, Tomich JM. 1990. Synporins - Synthetic proteins that emulate the pore structure of biological ionic channels. Proc Natl Acad Sci USA 87:6929-6933.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6929-6933
    • Montal, M.1    Montal, M.S.2    Tomich, J.M.3
  • 60
    • 0034307612 scopus 로고    scopus 로고
    • Potentiation of a voltage-gated proton current in acidosis-induced swelling of rat microglia
    • Morihata H, Nakamura F, Tsutada T, Kuno M. 2000. Potentiation of a voltage-gated proton current in acidosis-induced swelling of rat microglia. J Neurosci 20:7220-7227.
    • (2000) J Neurosci , vol.20 , pp. 7220-7227
    • Morihata, H.1    Nakamura, F.2    Tsutada, T.3    Kuno, M.4
  • 62
    • 0035232894 scopus 로고    scopus 로고
    • Mechanoprotection of the plasma membrane in neurons and other non-erythroid cells by the spectrin-based membrane skeleton
    • Morris CE. 2001. Mechanoprotection of the plasma membrane in neurons and other non-erythroid cells by the spectrin-based membrane skeleton. Cell Mol Biol Lett 6:703-720.
    • (2001) Cell Mol Biol Lett , vol.6 , pp. 703-720
    • Morris, C.E.1
  • 63
    • 0035863013 scopus 로고    scopus 로고
    • Cell surface area regulation and membrane tension
    • Morris CE, Homann U. 2001. Cell surface area regulation and membrane tension. J Membr Biol 179:79-102.
    • (2001) J Membr Biol , vol.179 , pp. 79-102
    • Morris, C.E.1    Homann, U.2
  • 64
    • 0027511501 scopus 로고
    • Osmotic properties of large unilamellar vesicles prepared by extrusion
    • Mui BL, Cullis PR, Evans EA, Madden TD. 1993. Osmotic properties of large unilamellar vesicles prepared by extrusion. Biophys J 64:443-453.
    • (1993) Biophys J , vol.64 , pp. 443-453
    • Mui, B.L.1    Cullis, P.R.2    Evans, E.A.3    Madden, T.D.4
  • 65
    • 0032763121 scopus 로고    scopus 로고
    • Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: Theory and experiment
    • Murray D, Arbuzova A, Hangyas-Mihalyne G, Gambhir A, Ben-Tal N, Honig B, McLaughlin S. 1999. Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: Theory and experiment. Biophys J 77:3176-3188.
    • (1999) Biophys J , vol.77 , pp. 3176-3188
    • Murray, D.1    Arbuzova, A.2    Hangyas-Mihalyne, G.3    Gambhir, A.4    Ben-Tal, N.5    Honig, B.6    McLaughlin, S.7
  • 66
    • 0034635960 scopus 로고    scopus 로고
    • Peptide nucleic acids rather than RNA may have been the first genetic molecule
    • Nelson KE, Levy M, Miller SL. 2000. Peptide nucleic acids rather than RNA may have been the first genetic molecule. Proc Natl Acad Sci USA 97:3868-3871.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3868-3871
    • Nelson, K.E.1    Levy, M.2    Miller, S.L.3
  • 67
    • 0033737385 scopus 로고    scopus 로고
    • Inclusion-induced bilayer deformations: Effects of monolayer equilibrium curvature
    • Nielsen C, Andersen OS. 2000. Inclusion-induced bilayer deformations: Effects of monolayer equilibrium curvature. Biophys J 79:2583-2604.
    • (2000) Biophys J , vol.79 , pp. 2583-2604
    • Nielsen, C.1    Andersen, O.S.2
  • 68
  • 70
    • 0029115961 scopus 로고
    • Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A
    • Oblatt-Montal M, Yamazaki M, Nelson R, Montal M. 1995. Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A. Protein Sci 4:1490-1497.
    • (1995) Protein Sci , vol.4 , pp. 1490-1497
    • Oblatt-Montal, M.1    Yamazaki, M.2    Nelson, R.3    Montal, M.4
  • 72
    • 0024121468 scopus 로고
    • Channel protein engineering: Synthetic 22-mer peptide from the primary structure of the voltage-sensitive sodium channel forms ionic channels in lipid bilayers
    • Oiki S, Danho W, Montal M. 1988. Channel protein engineering: Synthetic 22-mer peptide from the primary structure of the voltage-sensitive sodium channel forms ionic channels in lipid bilayers. Proc Natl Acad Sci USA 85:2393-2397.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2393-2397
    • Oiki, S.1    Danho, W.2    Montal, M.3
  • 73
    • 0028175523 scopus 로고
    • Alpha-helical hydrophobic polypeptides form proton-selective channels in lipid bilayers
    • Oliver AE, Deamer DW. 1994. Alpha-helical hydrophobic polypeptides form proton-selective channels in lipid bilayers. Biophys J 66:1364-1379.
    • (1994) Biophys J , vol.66 , pp. 1364-1379
    • Oliver, A.E.1    Deamer, D.W.2
  • 74
    • 0028157445 scopus 로고
    • Transduction of membrane tension by the ion channel alamethicin
    • Opsahl LR, Webb WW. 1994. Transduction of membrane tension by the ion channel alamethicin. Biophys J 66:71-74.
    • (1994) Biophys J , vol.66 , pp. 71-74
    • Opsahl, L.R.1    Webb, W.W.2
  • 75
    • 0032103374 scopus 로고    scopus 로고
    • Polymerization on the rocks: Theoretical introduction
    • Orgel LE. 1998. Polymerization on the rocks: Theoretical introduction. Orig Life Evol Biosph 28:227-234.
    • (1998) Orig Life Evol Biosph , vol.28 , pp. 227-234
    • Orgel, L.E.1
  • 78
    • 0030045955 scopus 로고    scopus 로고
    • Permeation of protons, potassium ions, and small polar molecules through phospholipid bilayers as a function of membrane thickness
    • Paula S, Volkov AG, Van Hoek AN, Haines TH, Deamer DW. 1996. Permeation of protons, potassium ions, and small polar molecules through phospholipid bilayers as a function of membrane thickness. Biophys J 70:339-348.
    • (1996) Biophys J , vol.70 , pp. 339-348
    • Paula, S.1    Volkov, A.G.2    Van Hoek, A.N.3    Haines, T.H.4    Deamer, D.W.5
  • 79
    • 0031982611 scopus 로고    scopus 로고
    • Permeation of halide anions through phospholipid bilayers occurs by the solubility-diffusion mechanism
    • Paula S, Volkov AG, Deamer DW. 1998. Permeation of halide anions through phospholipid bilayers occurs by the solubility-diffusion mechanism. Biophys J 74:319-327.
    • (1998) Biophys J , vol.74 , pp. 319-327
    • Paula, S.1    Volkov, A.G.2    Deamer, D.W.3
  • 80
    • 0034910318 scopus 로고    scopus 로고
    • Osmotically induced membrane tension modulates membrane permeabilization by class L amphipathic helical peptides: Nucleation model of defect formation
    • Polozov IV, Anantharamaiah GM, Segrest JP, Epand RM, 2001. Osmotically induced membrane tension modulates membrane permeabilization by class L amphipathic helical peptides: Nucleation model of defect formation. Biophys J 81:949-959.
    • (2001) Biophys J , vol.81 , pp. 949-959
    • Polozov, I.V.1    Anantharamaiah, G.M.2    Segrest, J.P.3    Epand, R.M.4
  • 81
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • Rawicz W, Olbrich KC, McIntosh T, Needham D, Evans E. 2000. Effect of chain length and unsaturation on elasticity of lipid bilayers. Biophys J 79:328-339.
    • (2000) Biophys J , vol.79 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 82
    • 0027255102 scopus 로고
    • Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. II. Transmembrane segment M2 of the brain glycine receptor is a plausible candidate for the pore-lining structure
    • Reddy GL, Iwamoto T, Tomich JM, Montal M. 1993. Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. II. Transmembrane segment M2 of the brain glycine receptor is a plausible candidate for the pore-lining structure. J Biol Chem 268:14608-14615.
    • (1993) J Biol Chem , vol.268 , pp. 14608-14615
    • Reddy, G.L.1    Iwamoto, T.2    Tomich, J.M.3    Montal, M.4
  • 83
    • 0034712651 scopus 로고    scopus 로고
    • Cooperative thermal denaturation of proteins designed by binary patterning of polar and nonpolar amino acids
    • Roy S, Hecht MH. 2000. Cooperative thermal denaturation of proteins designed by binary patterning of polar and nonpolar amino acids. Biochemistry 39:4603-4607.
    • (2000) Biochemistry , vol.39 , pp. 4603-4607
    • Roy, S.1    Hecht, M.H.2
  • 84
    • 0031627135 scopus 로고    scopus 로고
    • Mechanosensitive ion channels in nonspecialized cells
    • Sachs F, Morris CE. 1998. Mechanosensitive ion channels in nonspecialized cells. Rev Physiol Biochem Pharmacol. 132:1-77.
    • (1998) Rev Physiol Biochem Pharmacol , vol.132 , pp. 1-77
    • Sachs, F.1    Morris, C.E.2
  • 85
    • 0028275812 scopus 로고
    • The seventh Datta lecture. Membrane bending energy concept of vesicle- and cell-shapes and shape-transitions
    • Sackmann E. 1994. The seventh Datta lecture. Membrane bending energy concept of vesicle- and cell-shapes and shape-transitions. FEBS Lett 346:3-16.
    • (1994) FEBS Lett , vol.346 , pp. 3-16
    • Sackmann, E.1
  • 87
    • 0032601433 scopus 로고    scopus 로고
    • The mechanism of channel formation by alamethicin as viewed by molecular dynamics simulations
    • Sansom MS, Tieleman DP, Berendsen HJ. 1999. The mechanism of channel formation by alamethicin as viewed by molecular dynamics simulations. Novartis Found Symp 225:128-141.
    • (1999) Novartis Found Symp , vol.225 , pp. 128-141
    • Sansom, M.S.1    Tieleman, D.P.2    Berendsen, H.J.3
  • 88
    • 0035964940 scopus 로고    scopus 로고
    • The polymerization mechanism of the bacterial cell division protein FtsZ
    • Scheffers D, Driessen AJ. 2001. The polymerization mechanism of the bacterial cell division protein FtsZ. FEBS Lett 506:6-10.
    • (2001) FEBS Lett , vol.506 , pp. 6-10
    • Scheffers, D.1    Driessen, A.J.2
  • 89
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger MP, Bennett MJ, Eisenberg D. 1997. Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly. Adv Protein Chem 50:61-122.
    • (1997) Adv Protein Chem , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 91
    • 0000678654 scopus 로고    scopus 로고
    • S-layer-supported lipid membranes
    • Schuster B, Sleytr UB. 2000, S-layer-supported lipid membranes. J Biotechnol 74:233-254.
    • (2000) J Biotechnol , vol.74 , pp. 233-254
    • Schuster, B.1    Sleytr, U.B.2
  • 92
    • 0029990689 scopus 로고    scopus 로고
    • Alpha-branched 1,2-diacyl phosphatidylcholines as effectors of activity of cytochrome P450SCC (CYP11A1). Modeling the structure of the fatty acyl chain region of cardiolipin
    • Schwarz D, Kisselev P, Wessel R, Jueptner O, Schmid RD. 1996. Alpha-branched 1,2-diacyl phosphatidylcholines as effectors of activity of cytochrome P450SCC (CYP11A1). Modeling the structure of the fatty acyl chain region of cardiolipin. J Biol Chem 271:12840-12846.
    • (1996) J Biol Chem , vol.271 , pp. 12840-12846
    • Schwarz, D.1    Kisselev, P.2    Wessel, R.3    Jueptner, O.4    Schmid, R.D.5
  • 94
    • 0033571410 scopus 로고    scopus 로고
    • Division versus fusion: Dnm1p and Fzolp antagonistically regulate mitochondrial shape
    • Sesaki H, Jensen RE. 1999. Division versus fusion: Dnm1p and Fzolp antagonistically regulate mitochondrial shape. J Cell Biol 147:699-706.
    • (1999) J Cell Biol , vol.147 , pp. 699-706
    • Sesaki, H.1    Jensen, R.E.2
  • 95
    • 0035344650 scopus 로고    scopus 로고
    • Cell control by membrane-cytoskeleton adhesion
    • Sheetz MP. 2001. Cell control by membrane-cytoskeleton adhesion. Nat Rev Mol Cell Biol 2:392-396.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 392-396
    • Sheetz, M.P.1
  • 96
    • 0028340319 scopus 로고
    • Ion channel activity of a synthetic peptide with a primary structure corresponding to the presumed pore-forming region of the voltage dependent potassium channel
    • Shinozaki K, Anzai K, Kirino Y, Lee S, Aoyagi H. 1994. Ion channel activity of a synthetic peptide with a primary structure corresponding to the presumed pore-forming region of the voltage dependent potassium channel. Biochem Biophys Res Commun 198:445-450.
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 445-450
    • Shinozaki, K.1    Anzai, K.2    Kirino, Y.3    Lee, S.4    Aoyagi, H.5
  • 97
    • 0031928760 scopus 로고    scopus 로고
    • Regulation of exocytotic fusion by cell inflation
    • Solsona C, Innocenti B, Fernandez JM. 1998. Regulation of exocytotic fusion by cell inflation. Biophys J 74:1061-1073.
    • (1998) Biophys J , vol.74 , pp. 1061-1073
    • Solsona, C.1    Innocenti, B.2    Fernandez, J.M.3
  • 99
    • 0028929765 scopus 로고
    • Organ and cell allometry in Hawaiian Drosophila: How to make a big fly
    • Stevenson RD, Hill MF, Bryant PJ. 1995. Organ and cell allometry in Hawaiian Drosophila: How to make a big fly. Proc R Soc Lond B Biol Sci 259:105-110.
    • (1995) Proc R Soc Lond B Biol Sci , vol.259 , pp. 105-110
    • Stevenson, R.D.1    Hill, M.F.2    Bryant, P.J.3
  • 100
  • 101
    • 0028037553 scopus 로고
    • The reconstituted mitochondrial adenine nucleotide translocator: Effects of lipid polymorphism
    • Streicher-Scott J, Lapidus R, Sokolove PM. 1994, The reconstituted mitochondrial adenine nucleotide translocator: Effects of lipid polymorphism. Arch Biochem Biophys 315:548-554.
    • (1994) Arch Biochem Biophys , vol.315 , pp. 548-554
    • Streicher-Scott, J.1    Lapidus, R.2    Sokolove, P.M.3
  • 102
    • 0034910316 scopus 로고    scopus 로고
    • Structural models of the MscL gating mechanism
    • Sukharev S, Durell SR, Guy HR. 2001. Structural models of the MscL gating mechanism. Biophys J 81:917-936.
    • (2001) Biophys J , vol.81 , pp. 917-936
    • Sukharev, S.1    Durell, S.R.2    Guy, H.R.3
  • 104
    • 0034792022 scopus 로고    scopus 로고
    • Membrane active compounds that affect the shape of cells and cellular organelles
    • Svetina S, Zeks B. 2001. Membrane active compounds that affect the shape of cells and cellular organelles. Cell Mol Biol Lett 6:305-311.
    • (2001) Cell Mol Biol Lett , vol.6 , pp. 305-311
    • Svetina, S.1    Zeks, B.2
  • 106
    • 0036112238 scopus 로고    scopus 로고
    • Membrane stretch accelerates activation and slow inactivation in Shaker channels with S3-S4 linker deletions
    • Tabarean IV, Morris CE. 2002. Membrane stretch accelerates activation and slow inactivation in Shaker channels with S3-S4 linker deletions. Biophys J 82:2982-2994.
    • (2002) Biophys J , vol.82 , pp. 2982-2994
    • Tabarean, I.V.1    Morris, C.E.2
  • 107
    • 0035086899 scopus 로고    scopus 로고
    • Cellular membranes that undergo cyclic changes in tension: Direct measurement of force generation by an in vitro contractile vacuole of Paramecium multimicronucleaturn
    • Tani T, Allen RD, Naitoh Y. 2001. Cellular membranes that undergo cyclic changes in tension: Direct measurement of force generation by an in vitro contractile vacuole of Paramecium multimicronucleaturn. J Cell Sci 114:785-795.
    • (2001) J Cell Sci , vol.114 , pp. 785-795
    • Tani, T.1    Allen, R.D.2    Naitoh, Y.3
  • 108
    • 0007526635 scopus 로고
    • Voltage-gated channels formed in lipid bilayers by a positively charged segment of the Na-channel polypeptide
    • Tosteson MT, Auld DS, Tosteson DC. 1989. Voltage-gated channels formed in lipid bilayers by a positively charged segment of the Na-channel polypeptide. Proc Natl Acad Sci USA 86:707-710.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 707-710
    • Tosteson, M.T.1    Auld, D.S.2    Tosteson, D.C.3
  • 109
    • 0028977087 scopus 로고
    • Experimental tests of the roles of adaptation, chance, and history in evolution
    • Travisano M, Mongold JA, Bennett AF, Lenski RE. 1995. Experimental tests of the roles of adaptation, chance, and history in evolution. Science 267:87-90.
    • (1995) Science , vol.267 , pp. 87-90
    • Travisano, M.1    Mongold, J.A.2    Bennett, A.F.3    Lenski, R.E.4
  • 112
    • 0033060992 scopus 로고    scopus 로고
    • Activation of mechanosensitive currents in traumatized membrane
    • Wan X, Juranka P, Morris CE. 1999. Activation of mechanosensitive currents in traumatized membrane. Am J Physiol 276:C318-C327.
    • (1999) Am J Physiol , vol.276
    • Wan, X.1    Juranka, P.2    Morris, C.E.3
  • 113
    • 0028816201 scopus 로고
    • Membrane lipid composition and cell size of Acholeplasma laidlawii strain A are strongly influenced by lipid acyl chain length
    • Wieslander A, Nordstrom S, Dahlqvist A, Rilfors L, Lindblom G. 1995. Membrane lipid composition and cell size of Acholeplasma laidlawii strain A are strongly influenced by lipid acyl chain length. Eur J Biochem 227:734-744.
    • (1995) Eur J Biochem , vol.227 , pp. 734-744
    • Wieslander, A.1    Nordstrom, S.2    Dahlqvist, A.3    Rilfors, L.4    Lindblom, G.5
  • 114
    • 0034674445 scopus 로고    scopus 로고
    • Hierarchical self-assembly of F-actin and cationic lipid complexes: Stacked three-layer tubule networks
    • Wong GC, Tang JX, Lin A, Li Y, Janmey PA, Safinya CR. 2000. Hierarchical self-assembly of F-actin and cationic lipid complexes: Stacked three-layer tubule networks. Science 288:2035-2039.
    • (2000) Science , vol.288 , pp. 2035-2039
    • Wong, G.C.1    Tang, J.X.2    Lin, A.3    Li, Y.4    Janmey, P.A.5    Safinya, C.R.6
  • 115
    • 0034680846 scopus 로고    scopus 로고
    • Strain hardening of actin filament networks. Regulation by the dynamic cross-linking protein alpha-actinin
    • Xu J, Tseng Y, Wirtz D. 2000. Strain hardening of actin filament networks. Regulation by the dynamic cross-linking protein alpha-actinin. J Biol Chem 275:35886-35892.
    • (2000) J Biol Chem , vol.275 , pp. 35886-35892
    • Xu, J.1    Tseng, Y.2    Wirtz, D.3
  • 116
    • 0035134035 scopus 로고    scopus 로고
    • Interaction of pleurocidin and its analogs with phospholipid membrane and their antibacterial activity
    • Yoshida K, Mukai Y, Niidome T, Takashi C, Tokunaga Y, Hatakeyama T, Aoyagi H. 2001. Interaction of pleurocidin and its analogs with phospholipid membrane and their antibacterial activity. J Pept Res 57:119-126.
    • (2001) J Pept Res , vol.57 , pp. 119-126
    • Yoshida, K.1    Mukai, Y.2    Niidome, T.3    Takashi, C.4    Tokunaga, Y.5    Hatakeyama, T.6    Aoyagi, H.7
  • 117
    • 0021305372 scopus 로고
    • On the abiotic formation of amino acids. I. HCN as a precursor of amino acids detected in extracts of lunar samples. II. Formation of HCN and amino acids from simulated mixtures of gases released from lunar samples
    • Yuasa S, Flory D, Basile B, Oro J. 1984. On the abiotic formation of amino acids. I. HCN as a precursor of amino acids detected in extracts of lunar samples. II. Formation of HCN and amino acids from simulated mixtures of gases released from lunar samples. J Mol Evol 20:52-58.
    • (1984) J Mol Evol , vol.20 , pp. 52-58
    • Yuasa, S.1    Flory, D.2    Basile, B.3    Oro, J.4


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