메뉴 건너뛰기




Volumn 27, Issue , 2011, Pages 79-105

Dynamin: Functional design of a membrane fission catalyst

Author keywords

Clathrin mediated endocytosis; Curvature generation; GTPase; Hemifission; Membrane curvature

Indexed keywords

CLATHRIN; DYNAMIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; NUCLEOTIDE; PLECKSTRIN;

EID: 80052248915     PISSN: 10810706     EISSN: 15308995     Source Type: Book Series    
DOI: 10.1146/annurev-cellbio-100109-104016     Document Type: Article
Times cited : (247)

References (123)
  • 1
    • 0032937051 scopus 로고    scopus 로고
    • Essential role of the dynamin pleckstrin homology domain in receptor- mediated endocytosis
    • Achiriloaie M, Barylko B, Albanesi JP. 1999. Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis. Mol. Cell Biol. 19:1410-15 (Pubitemid 29046882)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.2 , pp. 1410-1415
    • Achiriloaie, M.1    Barylko, B.2    Albanesi, J.P.3
  • 4
    • 57649215874 scopus 로고    scopus 로고
    • GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission
    • Bashkirov PV, Akimov SA, Evseev AI, Schmid SL, Zimmerberg J, Frolov VA. 2008. GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission. Cell 135:1276-86
    • (2008) Cell , vol.135 , pp. 1276-1286
    • Bashkirov, P.V.1    Akimov, S.A.2    Evseev, A.I.3    Schmid, S.L.4    Zimmerberg, J.5    Frolov, V.A.6
  • 5
    • 0242331729 scopus 로고    scopus 로고
    • Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension
    • DOI 10.1038/nature02013
    • Baumgart T, Hess ST, Webb WW. 2003. Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension. Nature 425:821-24 (Pubitemid 37351463)
    • (2003) Nature , vol.425 , Issue.6960 , pp. 821-824
    • Baumgart, T.1    Hess, S.T.2    Webb, W.W.3
  • 7
    • 29144454715 scopus 로고    scopus 로고
    • 2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • DOI 10.1083/jcb.200509095
    • Bielli A, Haney CJ, Gabreski G, Watkins SC, Bannykh SI, Aridor M. 2005. Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission. J. Cell Biol. 171:919-24 (Pubitemid 41815823)
    • (2005) Journal of Cell Biology , vol.171 , Issue.6 , pp. 919-924
    • Bielli, A.1    Haney, C.J.2    Gabreski, G.3    Watkins, S.C.4    Bannykh, S.I.5    Aridor, M.6
  • 8
    • 0034633997 scopus 로고    scopus 로고
    • Dynamin ismembrane-active: Lipid insertion is induced by phosphoinositides and phosphatidic acid
    • Burger KN, Demel RA, Schmid SL, de Kruijff B. 2000. Dynamin ismembrane-active: lipid insertion is induced by phosphoinositides and phosphatidic acid. Biochemistry 39:12485-93
    • (2000) Biochemistry , vol.39 , pp. 12485-12493
    • Burger, K.N.1    Demel, R.A.2    Schmid, S.L.3    De Kruijff, B.4
  • 9
    • 77951930470 scopus 로고    scopus 로고
    • Modeling membrane shaping by proteins: Focus on EHD2 and N-BAR domains
    • Campelo F, Fabrikant G, McMahon HT, Kozlov MM. 2010. Modeling membrane shaping by proteins: focus on EHD2 and N-BAR domains. FEBS Lett. 584:1830-39
    • (2010) FEBS Lett , vol.584 , pp. 1830-1839
    • Campelo, F.1    Fabrikant, G.2    McMahon, H.T.3    Kozlov, M.M.4
  • 10
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism ofmembrane curvature generation by proteins
    • Campelo F, McMahon HT, KozlovMM. 2008. The hydrophobic insertion mechanism ofmembrane curvature generation by proteins. Biophys. J. 95:2325-39
    • (2008) Biophys. J. , vol.95 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 11
    • 77950445786 scopus 로고    scopus 로고
    • Curvature sensing by the epsin N-terminal homology domain measured on cylindrical lipid membrane tethers
    • Capraro BR, Yoon Y, Cho W, Baumgart T. 2010. Curvature sensing by the epsin N-terminal homology domain measured on cylindrical lipid membrane tethers. J. Am. Chem. Soc. 132:1200-1
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1200-1
    • Capraro, B.R.1    Yoon, Y.2    Cho, W.3    Baumgart, T.4
  • 12
    • 0030783520 scopus 로고    scopus 로고
    • Dynamin assembles into spirals under physiological salt conditions upon the addition of GDP and γ-phosphate analogues
    • DOI 10.1074/jbc.272.44.28030
    • Carr JF, Hinshaw JE. 1997. Dynamin assembles into spirals under physiological salt conditions upon the addition of GDP and γ-phosphate analogues. J. Biol. Chem. 272:28030-35 (Pubitemid 27473610)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.44 , pp. 28030-28035
    • Carr, J.F.1    Hinshaw, J.E.2
  • 14
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F. 2010. G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature 465:435-40
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 17
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • DOI 10.1146/annurev.biochem.72.121801.161504
    • Chernomordik LV, Kozlov MM. 2003. Protein-lipid interplay in fusion and fission of biological membranes. Annu. Rev. Biochem. 72:175-207 (Pubitemid 36930445)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 20
    • 0029144334 scopus 로고
    • Bending membranes to the task: Structural intermediates in bilayer fusion
    • Chernomordik LV, Zimmerberg J. 1995. Bending membranes to the task: structural intermediates in bilayer fusion. Curr. Opin. Struct. Biol. 5:541-47
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 541-547
    • Chernomordik, L.V.1    Zimmerberg, J.2
  • 22
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • DOI 10.1083/jcb.127.4.915
    • DamkeH, Baba T, Warnock DE, Schmid SL. 1994. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell Biol. 127:915-34 (Pubitemid 24355982)
    • (1994) Journal of Cell Biology , vol.127 , Issue.4 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 23
    • 0035162334 scopus 로고    scopus 로고
    • Dynamin GTpase domain mutants block endocytic vesicle formation at morphologically distinct stages
    • DamkeH, Binns DD, Ueda H, Schmid SL, Baba T. 2001. DynaminGTPase domain mutants block endocytic vesicle formation at morphologically distinct stages. Mol. Biol. Cell 12:2578-89 (Pubitemid 33051926)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.9 , pp. 2578-2589
    • Damke, H.1    Binns, D.D.2    Ueda, H.3    Schmid, S.L.4    Baba, T.5
  • 24
    • 0035424750 scopus 로고    scopus 로고
    • Dynamin family of mechanoenzymes
    • DOI 10.1016/S0955-0674(00)00236-2
    • Danino D, Hinshaw JE. 2001. Dynamin family of mechanoenzymes. Curr. Opin. Cell Biol. 13:454-60 (Pubitemid 32709769)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.4 , pp. 454-460
    • Danino, D.1    Hinshaw, J.E.2
  • 25
    • 4344586301 scopus 로고    scopus 로고
    • Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin
    • DOI 10.1016/j.jsb.2004.04.005, PII S1047847704000991
    • Danino D, Moon KH, Hinshaw JE. 2004. Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin. J. Struct. Biol. 147:259-67 (Pubitemid 39140733)
    • (2004) Journal of Structural Biology , vol.147 , Issue.3 , pp. 259-267
    • Danino, D.1    Moon, K.-H.2    Hinshaw, J.E.3
  • 27
    • 4444224966 scopus 로고    scopus 로고
    • Endocytosis by random initiation and stabilization of clathrin-coated pits
    • DOI 10.1016/j.cell.2004.08.017, PII S0092867404007901
    • Ehrlich M, Boll W, Van Oijen A, Hariharan R, Chandran K, et al. 2004. Endocytosis by random initiation and stabilization of clathrin-coated pits. Cell 118:591-605 (Pubitemid 39179712)
    • (2004) Cell , vol.118 , Issue.5 , pp. 591-605
    • Ehrlich, M.1    Boll, W.2    Van Oijen, A.3    Hariharan, R.4    Chandran, K.5    Nibert, M.L.6    Kirchhausen, T.7
  • 30
    • 0027945789 scopus 로고
    • Crystal structure at 2 2 A resolution of the pleckstrin homology domain from human dynamin
    • Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. 1994. Crystal structure at 2. 2. A resolution of the pleckstrin homology domain from human dynamin. Cell 79:199-209
    • (1994) Cell , vol.79 , pp. 199-209
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 31
    • 0000219094 scopus 로고
    • Scaling analysis of narrow necks in curvature models of fluid lipid-bilayer vesicles
    • Fourcade B, Miao L, Rao M, Wortis M, Zia RK. 1994. Scaling analysis of narrow necks in curvature models of fluid lipid-bilayer vesicles. Phys. Rev. E 49:5276-86
    • (1994) Phys. Rev. e , vol.49 , pp. 5276-5286
    • Fourcade, B.1    Miao, L.2    Rao, M.3    Wortis, M.4    Zia, R.K.5
  • 32
    • 77951898669 scopus 로고    scopus 로고
    • Cooperative elastic stresses, the hydrophobic effect, and lipid tilt in membrane remodeling
    • Frolov VA, Zimmerberg J. 2010. Cooperative elastic stresses, the hydrophobic effect, and lipid tilt in membrane remodeling. FEBS Lett. 584:1824-29
    • (2010) FEBS Lett. , vol.584 , pp. 1824-1829
    • Frolov, V.A.1    Zimmerberg, J.2
  • 33
    • 77953028450 scopus 로고    scopus 로고
    • Structural basis of oligomerization in the stalk region of dynamin-like MxA
    • Gao S, von derMalsburg A, Paeschke S, Behlke J, Haller O, et al. 2010. Structural basis of oligomerization in the stalk region of dynamin-like MxA. Nature 465:502-6
    • (2010) Nature , vol.465 , pp. 502-506
    • Gao, S.1    Von Der Malsburg, A.2    Paeschke, S.3    Behlke, J.4    Haller, O.5
  • 34
    • 67649360250 scopus 로고    scopus 로고
    • The fusion of membranes and vesicles: Pathway and energy barriers from dissipative particle dynamics
    • Grafmuller A, Shillcock J, Lipowsky R. 2009. The fusion of membranes and vesicles: pathway and energy barriers from dissipative particle dynamics. Biophys. J. 96:2658-75
    • (2009) Biophys. J. , vol.96 , pp. 2658-2675
    • Grafmuller, A.1    Shillcock, J.2    Lipowsky, R.3
  • 35
    • 0015934086 scopus 로고
    • Temperature-sensitive mutations in Drosophila melanogaster XIV. A selectionof immobile adults
    • Grigliatti TA, Hall I, Rosenbluth R, Suzuki DT. 1973. Temperature-sensitive mutations in Drosophila melanogaster. XIV. A selectionof immobile adults. Mol. Gen. Genet. 120:107-14
    • (1973) Mol. Gen. Genet. , vol.120 , pp. 107-114
    • Grigliatti, T.A.1    Hall, I.2    Rosenbluth, R.3    Suzuki, D.T.4
  • 37
    • 0028898261 scopus 로고
    • Dynamin self assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw JE, Schmid SL. 1995. Dynamin self assembles into rings suggesting a mechanism for coated vesicle budding. Nature 374:190-92
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 38
    • 0034087155 scopus 로고    scopus 로고
    • Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes
    • Holopainen JM, Angelova MI, Kinnunen PK. 2000. Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes. Biophys. J. 78:830-38 (Pubitemid 30211840)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 830-838
    • Holopainen, J.M.1    Angelova, M.I.2    Kinnunen, P.K.J.3
  • 39
    • 56349103980 scopus 로고    scopus 로고
    • The molecular mechanism of mitochondrial fusion
    • Hoppins S, Nunnari J. 2009. The molecular mechanism of mitochondrial fusion. Biochim. Biophys. Acta 1793:20-26
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 20-26
    • Hoppins, S.1    Nunnari, J.2
  • 40
    • 76049120802 scopus 로고    scopus 로고
    • Measurement of the membrane curvature preference of phospholipids reveals only weak coupling between lipid shape and leaflet curvature
    • Kamal MM, Mills D, Grzybek M, Howard J. 2009. Measurement of the membrane curvature preference of phospholipids reveals only weak coupling between lipid shape and leaflet curvature. Proc. Natl. Acad. Sci. USA 106:22245-50
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 22245-22250
    • Kamal, M.M.1    Mills, D.2    Grzybek, M.3    Howard, J.4
  • 41
    • 77956876861 scopus 로고    scopus 로고
    • Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients
    • Kenniston JA, Lemmon MA. 2010. Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients. EMBO J. 29:3054-67
    • (2010) EMBO J. , vol.29 , pp. 3054-3067
    • Kenniston, J.A.1    Lemmon, M.A.2
  • 43
    • 0024368508 scopus 로고
    • Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval
    • Koenig JH, Ikeda K. 1989. Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval. J. Neurosci. 9:3844-60 (Pubitemid 20004879)
    • (1989) Journal of Neuroscience , vol.9 , Issue.11 , pp. 3844-3860
    • Koenig, J.H.1    Ikeda, K.2
  • 44
    • 0037974484 scopus 로고    scopus 로고
    • Membrane fission: Model for intermediate structures
    • Kozlovsky Y, Kozlov MM. 2003. Membrane fission: model for intermediate structures. Biophys. J. 85:85-96 (Pubitemid 36753619)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 85-96
    • Kozlovsky, Y.1    Kozlov, M.M.2
  • 45
    • 4143105618 scopus 로고    scopus 로고
    • Orientation and interaction of oblique cylindrical inclusions embedded in a lipid monolayer: A theoretical model for viral fusion peptides
    • DOI 10.1529/biophysj.104.041467
    • Kozlovsky Y, Zimmerberg J, Kozlov MM. 2004. Orientation and interaction of oblique cylindrical inclusions embedded in a lipid monolayer: a theoretical model for viral fusion peptides. Biophys. J. 87:999-1012 (Pubitemid 39095080)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 999-1012
    • Kozlovsky, Y.1    Zimmerberg, J.2    Kozlov, M.M.3
  • 46
    • 0032410805 scopus 로고    scopus 로고
    • The case for a common ancestor: Kinesin and myosin motor proteins and G proteins
    • DOI 10.1023/A:1005489907021
    • Kull FJ, Vale RD, Fletterick RJ. 1998. The case for a common ancestor: kinesin and myosin motor proteins and G proteins. J. Muscle Res. Cell Motil. 19:877-86 (Pubitemid 29054483)
    • (1998) Journal of Muscle Research and Cell Motility , vol.19 , Issue.8 , pp. 877-886
    • Kull, F.J.1    Vale, R.D.2    Fletterick, R.J.3
  • 47
    • 20644454019 scopus 로고    scopus 로고
    • Line tension and interaction energies of membrane rafts calculated from lipid splay and tilt
    • DOI 10.1529/biophysj.104.048223
    • Kuzmin PI, Akimov SA, Chizmadzhev YA, Zimmerberg J, Cohen FS. 2005. Line tension and interaction energies of membrane rafts calculated from lipid splay and tilt. Biophys. J. 88:1120-33 (Pubitemid 40975943)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1120-1133
    • Kuzmin, P.I.1    Akimov, S.A.2    Chizmadzhev, Y.A.3    Zimmerberg, J.4    Cohen, F.S.5
  • 48
    • 0033545702 scopus 로고    scopus 로고
    • Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain
    • DOI 10.1016/S0960-9822(99)80115-8
    • Lee A, Frank DW, Marks MS, Lemmon MA. 1999. Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain. Curr. Biol. 9:261-64 (Pubitemid 29139309)
    • (1999) Current Biology , vol.9 , Issue.5 , pp. 261-264
    • Anthony, L.1    Frank, D.W.2    Marks, M.S.3    Lemmon, M.A.4
  • 49
    • 41449085212 scopus 로고    scopus 로고
    • Calculation of free energy barriers to the fusion of small vesicles
    • Lee JY, Schick M. 2008. Calculation of free energy barriers to the fusion of small vesicles. Biophys. J. 94:1699-706
    • (2008) Biophys. J. , vol.94 , pp. 1699-706
    • Lee, J.Y.1    Schick, M.2
  • 50
    • 0001276053 scopus 로고
    • Curvature instability in membranes
    • Leibler S. 1986. Curvature instability in membranes. J. Phys. (Fr. ) 47:507-16
    • (1986) J. Phys. (Fr. ) , vol.47 , pp. 507-516
    • Leibler, S.1
  • 51
    • 48349115359 scopus 로고    scopus 로고
    • Mechanochemical action of the dynamin protein
    • Lenz M, Prost J, Joanny JF. 2008. Mechanochemical action of the dynamin protein. Phys. Rev. E 78:011911.
    • (2008) Phys. Rev. e , vol.78 , pp. 011911
    • Lenz, M.1    Prost, J.2    Joanny, J.F.3
  • 52
    • 0001335174 scopus 로고
    • Budding of membranes induced by intramembrane domains
    • Lipowsky R. 1992. Budding of membranes induced by intramembrane domains. J. Phys. II (Fr. ) 2:1825-40
    • (1992) J. Phys. II (Fr. ) , vol.2 , pp. 1825-1840
    • Lipowsky, R.1
  • 57
    • 72249102216 scopus 로고    scopus 로고
    • Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving
    • Low HH, Sachse C, Amos LA, Lowe J. 2009. Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving. Cell 139:1342-52
    • (2009) Cell , vol.139 , pp. 1342-1352
    • Low, H.H.1    Sachse, C.2    Amos, L.A.3    Lowe, J.4
  • 58
    • 30544441347 scopus 로고    scopus 로고
    • Calcium increases endocytotic vesicle size and accelerates membrane fission in insulin-secreting INS-1 cells
    • DOI 10.1242/jcs.02685
    • MacDonald PE, Eliasson L, Rorsman P. 2005. Calcium increases endocytotic vesicle size and accelerates membrane fission in insulin-secreting INS-1 cells. J. Cell Sci. 118:5911-20 (Pubitemid 43079281)
    • (2005) Journal of Cell Science , vol.118 , Issue.24 , pp. 5911-5920
    • MacDonald, P.E.1    Eliasson, L.2    Rorsman, P.3
  • 60
    • 78349295615 scopus 로고    scopus 로고
    • Dynamics and regulation of endocytotic fission pores: Role of calcium and dynamin
    • Maria Cabeza JM, Acosta J, Aĺes E. 2010. Dynamics and regulation of endocytotic fission pores: role of calcium and dynamin. Traffic 11:1579-90
    • (2010) Traffic , vol.11 , pp. 1579-1590
    • Maria Cabeza, J.M.1    Acosta, J.2    Aĺes, E.3
  • 61
    • 0035826257 scopus 로고    scopus 로고
    • GTPase activity of dynamin and resulting conformation change are essential for endocytosis
    • DOI 10.1038/35065645
    • Marks B, Stowell MH B, Vallis Y, Mills IG, Gibson A, et al. 2001. GTPase activity of dynamin and resulting conformation change are essential for endocytosis. Nature 410:231-35 (Pubitemid 32216598)
    • (2001) Nature , vol.410 , Issue.6825 , pp. 231-235
    • Marks, B.1    Stowell, M.H.B.2    Vallis, Y.3    Mills, I.G.4    Gibson, A.5    Hopkins, C.R.6    McMahon, H.T.7
  • 62
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • DOI 10.1126/science.1142614
    • Martens S, Kozlov MM, McMahon HT. 2007. How synaptotagmin promotes membrane fusion. Science 316:1205-8 (Pubitemid 46877485)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 63
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • DOI 10.1038/nrm2417, PII NRM2417
    • Martens S, McMahon HT. 2008. Mechanisms of membrane fusion: disparate players and common principles. Nat. Rev. Mol. Cell Biol. 9:543-56 (Pubitemid 351881838)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.7 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 64
    • 0032215324 scopus 로고    scopus 로고
    • Coat assembly directs v-SNARE concentration into synthetic COPII vesicles
    • Matsuoka K, Morimitsu Y, Uchida K, Schekman R. 1998. Coat assembly directs v-SNARE concentration into synthetic COPII vesicles. Mol. Cell 2:703-8 (Pubitemid 128379095)
    • (1998) Molecular Cell , vol.2 , Issue.5 , pp. 703-708
    • Matsuoka, K.1    Morimitsu, Y.2    Uchida, K.3    Schekman, R.4
  • 66
    • 77649139375 scopus 로고    scopus 로고
    • Membrane curvature in synaptic vesicle fusion and beyond
    • McMahon HT, Kozlov MM, Martens S. 2010. Membrane curvature in synaptic vesicle fusion and beyond. Cell 140:601-5
    • (2010) Cell , vol.140 , pp. 601-605
    • McMahon, H.T.1    Kozlov, M.M.2    Martens, S.3
  • 67
    • 0034161330 scopus 로고    scopus 로고
    • The dynamin family of mechanoenzymes: Pinching in new places
    • DOI 10.1016/S0968-0004(99)01538-8, PII S0968000499015388
    • McNiven MA, Cao H, Pitts KR, Yoon Y. 2000. The dynamin family of mechanoenzymes: pinching in new places. Trends Biochem. Sci. 25:115-20 (Pubitemid 30122422)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.3 , pp. 115-120
    • McNiven, M.A.1    Cao, H.2    Pitts, K.R.3    Yoon, Y.4
  • 68
    • 35148862219 scopus 로고    scopus 로고
    • A corkscrew model for dynamin constriction
    • DOI 10.1016/j.str.2007.08.012, PII S0969212607003280
    • Mears JA, Ray P, Hinshaw JE. 2007. A corkscrew model for dynamin constriction. Structure 15:1190-202 (Pubitemid 47539167)
    • (2007) Structure , vol.15 , Issue.10 , pp. 1190-1202
    • Mears, J.A.1    Ray, P.2    Hinshaw, J.E.3
  • 69
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • DOI 10.1038/ncb837
    • Merrifield CJ, Feldman ME, Wan L, Almers W. 2002. Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat. Cell Biol. 4:691-98 (Pubitemid 34993705)
    • (2002) Nature Cell Biology , vol.4 , Issue.9 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 70
    • 19344375254 scopus 로고    scopus 로고
    • Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells
    • DOI 10.1016/j.cell.2005.03.015, PII S0092867405002874
    • Merrifield CJ, Perrais D, Zenisek D. 2005. Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells. Cell 121:593-606 (Pubitemid 40720012)
    • (2005) Cell , vol.121 , Issue.4 , pp. 593-606
    • Merrifield, C.J.1    Perrais, D.2    Zenisek, D.3
  • 72
    • 77956067803 scopus 로고    scopus 로고
    • Splaying of aliphatic tails plays a central role in barrier crossing during liposome fusion
    • Mirjanian D, Dickey AN, Hoh JH, Woolf TB, Stevens MJ. 2010. Splaying of aliphatic tails plays a central role in barrier crossing during liposome fusion. J. Phys. Chem. B 114:11061-68
    • (2010) J. Phys. Chem. B , vol.114 , pp. 11061-11068
    • Mirjanian, D.1    Dickey, A.N.2    Hoh, J.H.3    Woolf, T.B.4    Stevens, M.J.5
  • 73
    • 0030809132 scopus 로고    scopus 로고
    • Domain structure and intramolecular regulation of dynamin GTPase
    • Muhlberg AB, Warnock DE, Schmid SL. 1997. Domain structure and intramolecular regulation of dynamin GTPase. EMBO J. 16:6676-83 (Pubitemid 27503480)
    • (1997) EMBO Journal , vol.16 , Issue.22 , pp. 6676-6683
    • Muhlberg, A.B.1    Warnock, D.E.2    Schmid, S.L.3
  • 74
    • 17644424000 scopus 로고    scopus 로고
    • An internal GAP domain negatively regulates presynaptic dynamin in vivo: A two-step model for dynamin function
    • DOI 10.1083/jcb.200502042
    • Narayanan R, Leonard M, Song BD, Schmid SL, Ramaswami M. 2005. An internal GAP domain negatively regulates presynaptic dynamin in vivo: a two-step model of dynamin function. J. Cell Biol. 169:117-26 (Pubitemid 40562919)
    • (2005) Journal of Cell Biology , vol.169 , Issue.1 , pp. 117-126
    • Narayanan, R.1    Leonard, M.2    Byeong, D.S.3    Schmid, S.L.4    Ramaswami, M.5
  • 75
    • 0035503309 scopus 로고    scopus 로고
    • Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms
    • DOI 10.1093/emboj/20.21.5813
    • Niemann HH, Knetsch ML, Scherer A, Manstein DJ, Kull FJ. 2001. Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms. EMBO J. 20:5813-21 (Pubitemid 33049257)
    • (2001) EMBO Journal , vol.20 , Issue.21 , pp. 5813-5821
    • Niemann, H.H.1    Knetsch, M.L.W.2    Scherer, A.3    Manstein, D.J.4    Kull, F.J.5
  • 76
    • 0030967213 scopus 로고    scopus 로고
    • Role of the basic, proline-rich region of dynamin in Src homology 3 domain binding and endocytosis
    • DOI 10.1074/jbc.272.17.11629
    • Okamoto PM, Herskovits JS, Vallee RB. 1997. Role of the basic, proline-rich region of dynamin in Src homology 3 domain binding and endocytosis. J. Biol. Chem. 272:11629-35 (Pubitemid 27184176)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.17 , pp. 11629-11635
    • Okamoto, P.M.1    Herskovits, J.S.2    Vallee, R.B.3
  • 77
    • 57649238675 scopus 로고    scopus 로고
    • Real-time visualization of dynamin-catalyzed membrane fission and vesicle release
    • Pucadyil TJ, Schmid SL. 2008. Real-time visualization of dynamin-catalyzed membrane fission and vesicle release. Cell 135:1263-75
    • (2008) Cell , vol.135 , pp. 1263-1275
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 78
    • 69949183624 scopus 로고    scopus 로고
    • Conserved functions ofmembrane activeGTPases in coated vesicle formation
    • Pucadyil TJ, Schmid SL. 2009. Conserved functions ofmembrane activeGTPases in coated vesicle formation. Science 325:1217-20
    • (2009) Science , vol.325 , pp. 1217-1220
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 79
    • 77955152146 scopus 로고    scopus 로고
    • Supported bilayers with excess membrane reservoir: A template for reconstituting membrane budding and fission
    • Pucadyil TJ, Schmid SL. 2010. Supported bilayers with excess membrane reservoir: a template for reconstituting membrane budding and fission. Biophys. J. 99:517-25
    • (2010) Biophys. J. , vol.99 , pp. 517-525
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 81
    • 73949099250 scopus 로고    scopus 로고
    • Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission
    • Ramachandran R, Pucadyil TJ, Liu YW, Acharya S, Leonard M, et al. 2009. Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission. Mol. Biol. Cell 20:4630-39
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4630-4639
    • Ramachandran, R.1    Pucadyil, T.J.2    Liu, Y.W.3    Acharya, S.4    Leonard, M.5
  • 82
    • 38049052532 scopus 로고    scopus 로고
    • Real-time detection reveals that effectors couple dynamin's GTPdependent conformational changes to the membrane
    • Ramachandran R, Schmid SL. 2008. Real-time detection reveals that effectors couple dynamin's GTPdependent conformational changes to the membrane. EMBO J. 27:27-37
    • (2008) EMBO J. , vol.27 , pp. 27-37
    • Ramachandran, R.1    Schmid, S.L.2
  • 83
    • 33846513580 scopus 로고    scopus 로고
    • The dynamin middle domain is critical for tetramerization and higher-order self-assembly
    • DOI 10.1038/sj.emboj.7601491, PII 7601491
    • Ramachandran R, Surka M, Chappie JS, Fowler DM, Foss TR, et al. 2007. The dynamin middle domain is critical for tetramerization and higher-order self-assembly. EMBO J. 26:559-66 (Pubitemid 46160955)
    • (2007) EMBO Journal , vol.26 , Issue.2 , pp. 559-566
    • Ramachandran, R.1    Surka, M.2    Chappie, J.S.3    Fowler, D.M.4    Foss, T.R.5    Song, B.D.6    Schmid, S.L.7
  • 84
    • 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. 79:328-39 (Pubitemid 30436749)
    • (2000) Biophysical Journal , vol.79 , Issue.1 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 87
    • 18444366155 scopus 로고    scopus 로고
    • Role of curvature and phase transition in lipid sorting and fission of membrane tubules
    • DOI 10.1038/sj.emboj.7600631
    • Roux A, Cuvelier D, Nassoy P, Prost J, Bassereau P, Goud B. 2005. Role of curvature and phase transition in lipid sorting and fission of membrane tubules. EMBO J. 24:1537-45 (Pubitemid 40646444)
    • (2005) EMBO Journal , vol.24 , Issue.8 , pp. 1537-1545
    • Roux, A.1    Cuvelier, D.2    Nassoy, P.3    Prost, J.4    Bassereau, P.5    Goud, B.6
  • 89
    • 33745026786 scopus 로고    scopus 로고
    • GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
    • DOI 10.1038/nature04718, PII NATURE04718
    • Roux A, Uyhazi K, Frost A, De Camilli P. 2006. GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 441:528-31 (Pubitemid 44050156)
    • (2006) Nature , vol.441 , Issue.7092 , pp. 528-531
    • Roux, A.1    Uyhazi, K.2    Frost, A.3    De Camilli, P.4
  • 90
    • 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
  • 91
    • 0029182477 scopus 로고
    • Budding, fission and domain formation in mixed lipid vesicles induced by lateral phase separation and macromolecular condensation
    • Sackmann E, Feder T. 1995. Budding, fission and domain formation in mixed lipid vesicles induced by lateral phase separation and macromolecular condensation. Mol. Membr. Biol. 12:21-28
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 21-28
    • Sackmann, E.1    Feder, T.2
  • 92
    • 0034605101 scopus 로고    scopus 로고
    • Dynamin:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis
    • Sever S, Damke H, Schmid SL. 2000. Dynamin:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis. J. Cell Biol. 150:1137-48
    • (2000) J. Cell Biol. , vol.150 , pp. 1137-1148
    • Sever, S.1    Damke, H.2    Schmid, S.L.3
  • 93
    • 0033535593 scopus 로고    scopus 로고
    • Impairment of dynamin'sGAPdomain stimulates receptor-mediated endocytosis
    • Sever S, Muhlberg AB, Schmid SL. 1999. Impairment of dynamin'sGAPdomain stimulates receptor-mediated endocytosis. Nature 398:481-86
    • (1999) Nature , vol.398 , pp. 481-486
    • Sever, S.1    Muhlberg, A.B.2    Schmid, S.L.3
  • 97
    • 0024342278 scopus 로고
    • Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules
    • DOI 10.1016/0092-8674(89)90027-5
    • Shpetner HS, Vallee RB. 1989. Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules. Cell 59:421-32 (Pubitemid 19284457)
    • (1989) Cell , vol.59 , Issue.3 , pp. 421-432
    • Shpetner, H.S.1    Vallee, R.B.2
  • 98
    • 77952395696 scopus 로고    scopus 로고
    • Solvent-exposed tails as prestalk transition states for membrane fusion at low hydration
    • Smirnova YG, Marrink SJ, Lipowsky R, Knecht V. 2010. Solvent-exposed tails as prestalk transition states for membrane fusion at low hydration. J. Am. Chem. Soc. 132:6710-18
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6710-6718
    • Smirnova, Y.G.1    Marrink, S.J.2    Lipowsky, R.3    Knecht, V.4
  • 99
    • 27744593778 scopus 로고    scopus 로고
    • Conformational changes in dynamin on GTP binding and oligomerization reported by intrinsic and extrinsic fluorescence
    • DOI 10.1042/BJ20050707
    • Solomaha E, Palfrey HC. 2005. Conformational changes in dynamin on GTP binding and oligomerization reported by intrinsic and extrinsic fluorescence. Biochem. J. 391:601-11 (Pubitemid 41634786)
    • (2005) Biochemical Journal , vol.391 , Issue.3 , pp. 601-611
    • Solomaha, E.1    Palfrey, H.C.2
  • 100
    • 4644314874 scopus 로고    scopus 로고
    • Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis
    • DOI 10.1074/jbc.M407007200
    • Song BD, Leonard M, Schmid SL. 2004b. Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis. J. Biol. Chem. 279:40431-36 (Pubitemid 39287632)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 40431-40436
    • Song, B.D.1    Leonard, M.2    Schmid, S.L.3
  • 101
    • 0037452537 scopus 로고    scopus 로고
    • A molecular motor or a regulator? Dynamin's in a class of its own
    • DOI 10.1021/bi027062h
    • Song BD, Schmid SL. 2003. A molecular motor or a regulator? Dynamin's in a class of its own. Biochemistry 42:1369-76 (Pubitemid 36205942)
    • (2003) Biochemistry , vol.42 , Issue.6 , pp. 1369-1376
    • Song, B.D.1    Schmid, S.L.2
  • 102
    • 2342473321 scopus 로고    scopus 로고
    • An Assembly-incompetent Mutant Establishes a Requirement for Dynamin Self-assembly in Clathrin-mediated Endocytosis in Vivo
    • DOI 10.1091/mbc.E04-01-0015
    • Song BD, Yarar D, Schmid SL. 2004a. An assembly-incompetent mutant establishes a requirement for dynamin in self-assembly in clathrin-mediated endocytosis in vivo. Mol. Biol. Cell 15:2243-52 (Pubitemid 38580642)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.5 , pp. 2243-2252
    • Song, B.D.1    Yarar, D.2    Schmid, S.L.3
  • 104
    • 33749154469 scopus 로고    scopus 로고
    • Domain requirements for an endocytosis-independent, isoform-specific function of dynamin-2
    • DOI 10.1016/j.yexcr.2006.07.018, PII S0014482706003053
    • Soulet F, Schmid SL, Damke H. 2006. Domain requirements for an endocytosis-independent, isoform-specific function of dynamin-2. Exp. Cell Res. 312:3539-45 (Pubitemid 44470774)
    • (2006) Experimental Cell Research , vol.312 , Issue.18 , pp. 3539-3545
    • Soulet, F.1    Schmid, S.L.2    Damke, H.3
  • 105
    • 0032476574 scopus 로고    scopus 로고
    • Reconstitution of retrograde transport from the Golgi to the ER in vitro
    • DOI 10.1083/jcb.143.3.589
    • Spang A, Schekman R. 1998. Reconstitution of retrograde transport from the Golgi to the ER in vitro. J. Cell Biol. 143:589-99 (Pubitemid 28512556)
    • (1998) Journal of Cell Biology , vol.143 , Issue.3 , pp. 589-599
    • Spang, A.1    Schekman, R.2
  • 106
    • 0035344213 scopus 로고    scopus 로고
    • The myosin swinging cross-bridge model
    • DOI 10.1038/35073086
    • Spudich JA. 2001. The myosin swinging cross-bridge model. Nat. Rev. Mol. Cell Biol. 2:387-92 (Pubitemid 33674051)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.5 , pp. 387-392
    • Spudich, J.A.1
  • 107
    • 1442299369 scopus 로고    scopus 로고
    • 2 promotes raft budding and fission from giant liposomes
    • DOI 10.1016/j.chemphyslip.2003.11.005, PII S0009308403001932
    • Staneva G, Angelova MI, Koumanov K. 2004. Phospholipase A2 promotes raft budding and fission from giant liposomes. Chem. Phys. Lipids 129:53-62 (Pubitemid 38293249)
    • (2004) Chemistry and Physics of Lipids , vol.129 , Issue.1 , pp. 53-62
    • Staneva, G.1    Angelova, M.I.2    Koumanov, K.3
  • 108
    • 11044225076 scopus 로고    scopus 로고
    • Insights into the molecular mechanism of membrane fusion from simulation: Evidence for the association of splayed tails
    • Stevens MJ, Hoh JH, Woolf TB. 2003. Insights into the molecular mechanism of membrane fusion from simulation: evidence for the association of splayed tails. Phys. Rev. Lett. 91:188102.
    • (2003) Phys. Rev. Lett. , vol.91 , pp. 188102
    • Stevens, M.J.1    Hoh, J.H.2    Woolf, T.B.3
  • 109
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring
    • Stowell MH B, Marks B, Wigge P, McMahon HT. 1999. Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring. Nat. Cell Biol. 1:27-32
    • (1999) Nat. Cell Biol. , vol.1 , pp. 27-32
    • Mhb, S.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 110
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with SNARE and SMproteins
    • Sudhof TC, Rothman JE. 2009. Membrane fusion: grappling with SNARE and SMproteins. Science 323:474-77
    • (2009) Science , vol.323 , pp. 474-477
    • Sudhof, T.C.1    Rothman, J.E.2
  • 111
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • DOI 10.1016/S0092-8674(00)81207-6
    • Sweitzer S, Hinshaw J. 1998. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell 93:1021-29 (Pubitemid 28280795)
    • (1998) Cell , vol.93 , Issue.6 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 112
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTPγS in nerve terminals
    • TakeiK, McPherson PS, Schmid SL, De Camilli P. 1995. Tubular membrane invaginations coated by dynamin rings are induced by GTPγS in nerve terminals. Nature 374:186-90
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 113
    • 0041428123 scopus 로고    scopus 로고
    • Membrane fusion: A structural perspective on the interplay of lipids and proteins
    • DOI 10.1016/S0959-440X(03)00107-6
    • Tamm LK, Crane J, Kiessling V. 2003. Membrane fusion: a structural perspective on the interplay of lipids and proteins. Curr. Opin. Struct. Biol. 13:453-66 (Pubitemid 37011450)
    • (2003) Current Opinion in Structural Biology , vol.13 , Issue.4 , pp. 453-466
    • Tamm, L.K.1    Crane, J.2    Kiessling, V.3
  • 114
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale RD, Milligan RA. 2000. The way things move: looking under the hood of molecular motor proteins. Science 288:88-95
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 115
    • 0033545698 scopus 로고    scopus 로고
    • Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis
    • DOI 10.1016/S0960-9822(99)80114-6
    • Vallis Y, Wigge P, Marks B, Evans PR, McMahon HT. 1999. Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis. Curr. Biol. 9:257-60 (Pubitemid 29139308)
    • (1999) Current Biology , vol.9 , Issue.5 , pp. 257-260
    • Valus, Y.1    Wigge, P.2    Marks, B.3    Evans, P.R.4    McMahon, H.T.5
  • 116
    • 77954906120 scopus 로고    scopus 로고
    • Dynamin 2 mutants linked to centronuclear myopathies form abnormally stable polymers
    • Wang L, Barylko B, Byers C, Ross JA, Jameson DM, Albanesi JP. 2010. Dynamin 2 mutants linked to centronuclear myopathies form abnormally stable polymers. J. Biol. Chem. 285:22753-57
    • (2010) J. Biol. Chem. , vol.285 , pp. 22753-22757
    • Wang, L.1    Barylko, B.2    Byers, C.3    Ross, J.A.4    Jameson, D.M.5    Albanesi, J.P.6
  • 117
    • 0026492542 scopus 로고
    • Membrane fusion
    • White JM. 1992. Membrane fusion. Science 258:917-24
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 118
    • 77957020175 scopus 로고    scopus 로고
    • Membrane fusion: Five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles
    • WicknerW. 2010. Membrane fusion: five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles. Annu. Rev. Cell Dev. Biol. 26:115-36
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 115-136
    • Wickner, W.1
  • 119
    • 0037501391 scopus 로고    scopus 로고
    • Budding and fission dynamics of two-component vesicles
    • Yamamoto S, Hyodo S. 2003. Budding and fission dynamics of two-component vesicles. J. Chem. Phys. 118:7937-43
    • (2003) J. Chem. Phys. , vol.118 , pp. 7937-7943
    • Yamamoto, S.1    Hyodo, S.2
  • 121
    • 18844409111 scopus 로고    scopus 로고
    • Perturbation of a lipid membrane by amphipathic peptides and its role in pore formation
    • DOI 10.1007/s00249-004-0445-9
    • Zemel A, Ben-Shaul A, May S. 2005. Perturbation of a lipid membrane by amphipathic peptides and its role in pore formation. Eur. Biophys. J. 34:230-42 (Pubitemid 40684805)
    • (2005) European Biophysics Journal , vol.34 , Issue.3 , pp. 230-242
    • Zemel, A.1    Ben-Shaul, A.2    May, S.3
  • 122
    • 0034784987 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of dynamin in the constricted state
    • DOI 10.1038/ncb1001-922
    • Zhang P, Hinshaw JE. 2001. Three-dimensional reconstruction of dynamin in the constricted state. Nat. Cell Biol. 3:922-26 (Pubitemid 32952258)
    • (2001) Nature Cell Biology , vol.3 , Issue.10 , pp. 922-926
    • Zhang, P.1    Hinshaw, J.E.2
  • 123
    • 0029978885 scopus 로고    scopus 로고
    • Identification of the binding site for acidic phospholipids on the PH domain of dynamin: Implications for stimulation of GTPase activity
    • DOI 10.1006/jmbi.1996.0002
    • Zheng J, Cahill SM, Lemmon MA, Fushman D, Schlessinger J, Cowburn D. 1996. Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity. J. Mol. Biol. 255:14-21 (Pubitemid 26104180)
    • (1996) Journal of Molecular Biology , vol.255 , Issue.1 , pp. 14-21
    • Zheng, J.1    Cahill, S.M.2    Lemmon, M.A.3    Fushman, D.4    Schlessinger, J.5    Cowburn, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.