메뉴 건너뛰기




Volumn 6, Issue 6, 2011, Pages

The cytosolic domain of Fis1 binds and reversibly clusters lipid vesicles

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; PHOSPHOLIPID; PROTEIN FIS 1; UNCLASSIFIED DRUG; MEMBRANE LIPID; MITOCHONDRIAL PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 79959585289     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0021384     Document Type: Article
Times cited : (15)

References (78)
  • 1
    • 0345600249 scopus 로고    scopus 로고
    • The division of endosymbiotic organelles
    • Osteryoung KW, Nunnari J, (2003) The division of endosymbiotic organelles. Science 302: 1698-1704.
    • (2003) Science , vol.302 , pp. 1698-1704
    • Osteryoung, K.W.1    Nunnari, J.2
  • 2
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-Mediated Mitochondrial Fission is a Multi-Step Process Requiring the Novel Integral Membrane Component Fis1p
    • Mozdy AD, McCaffery JM, Shaw JM, (2000) Dnm1p GTPase-Mediated Mitochondrial Fission is a Multi-Step Process Requiring the Novel Integral Membrane Component Fis1p. J Cell Biol 151: 367-380.
    • (2000) J Cell Biol , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 3
    • 0034676101 scopus 로고    scopus 로고
    • Mdv1p is a WD Repeat Protein that Interacts with the Dynamin-Related GTPase, Dnm1p, to Trigger Mitochondrial Division
    • Tieu Q, Nunnari J, (2000) Mdv1p is a WD Repeat Protein that Interacts with the Dynamin-Related GTPase, Dnm1p, to Trigger Mitochondrial Division. J Cell Biol 151: 353-366.
    • (2000) J Cell Biol , vol.151 , pp. 353-366
    • Tieu, Q.1    Nunnari, J.2
  • 4
    • 0035149539 scopus 로고    scopus 로고
    • Division of Mitochondria Requires a Novel DMN1-Interacting Protein, Net2p
    • Cerveny KL, McCaffery JM, Jensen RE, (2001) Division of Mitochondria Requires a Novel DMN1-Interacting Protein, Net2p. Mol Biol Cell 12: 309-321.
    • (2001) Mol Biol Cell , vol.12 , pp. 309-321
    • Cerveny, K.L.1    McCaffery, J.M.2    Jensen, R.E.3
  • 5
    • 0034676062 scopus 로고    scopus 로고
    • Gag3p, an outer membrane protein required for fission of mitochondrial tubules
    • Fekkes P, Shepard KA, Yaffe MP, (2000) Gag3p, an outer membrane protein required for fission of mitochondrial tubules. J Cell Biol 151: 333-340.
    • (2000) J Cell Biol , vol.151 , pp. 333-340
    • Fekkes, P.1    Shepard, K.A.2    Yaffe, M.P.3
  • 6
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Yoon Y, Krueger EW, Oswald BJ, McNiven MA, (2003) The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol Cell Biol 23: 5409-5420.
    • (2003) Mol Cell Biol , vol.23 , pp. 5409-5420
    • Yoon, Y.1    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 7
    • 0032547797 scopus 로고    scopus 로고
    • The Dynamin-Related GTPase, Dnm1p, Controls Mitochondrial Morphology in Yeast
    • Otsuga D, Keegan BR, Brisch E, Thatcher JW, Hermann GJ, et al. (1998) The Dynamin-Related GTPase, Dnm1p, Controls Mitochondrial Morphology in Yeast. J Cell Biol 143: 333-349.
    • (1998) J Cell Biol , vol.143 , pp. 333-349
    • Otsuga, D.1    Keegan, B.R.2    Brisch, E.3    Thatcher, J.W.4    Hermann, G.J.5
  • 9
    • 46249130452 scopus 로고    scopus 로고
    • Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p
    • Motley A, Ward GP, Hettema E, (2008) Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. J Cell Sci 121: 1633-1640.
    • (2008) J Cell Sci , vol.121 , pp. 1633-1640
    • Motley, A.1    Ward, G.P.2    Hettema, E.3
  • 10
    • 68949217889 scopus 로고    scopus 로고
    • Mechanistic analysis of a Dynamin Effector
    • Lackner LL, Horner JS, Nunnari J, (2009) Mechanistic analysis of a Dynamin Effector. Science 325: 874-877.
    • (2009) Science , vol.325 , pp. 874-877
    • Lackner, L.L.1    Horner, J.S.2    Nunnari, J.3
  • 11
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: Dynamic Organelles in Disease, Aging, and Development
    • Chan DC, (2006) Mitochondria: Dynamic Organelles in Disease, Aging, and Development. Cell 125: 1241-1252.
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 13
    • 33750300252 scopus 로고    scopus 로고
    • Mechanisms of disease: mitochondria as new therapeutic targets in diabetic neuropathy
    • Leinninger GM, Edwards JL, Lipshaw MJ, Feldman EL, (2006) Mechanisms of disease: mitochondria as new therapeutic targets in diabetic neuropathy. Nat Clin Pract Neurol 2: 620-628.
    • (2006) Nat Clin Pract Neurol , vol.2 , pp. 620-628
    • Leinninger, G.M.1    Edwards, J.L.2    Lipshaw, M.J.3    Feldman, E.L.4
  • 15
    • 1842479419 scopus 로고    scopus 로고
    • Levels of Human Fis1 at the Mitochondrial Outer Membrane Regulate Mitochondrial Morphology
    • Stojanovski D, Koutsopoulos OS, Okamoto K, Ryan MT, (2004) Levels of Human Fis1 at the Mitochondrial Outer Membrane Regulate Mitochondrial Morphology. J Cell Sci 117: 1201-1210.
    • (2004) J Cell Sci , vol.117 , pp. 1201-1210
    • Stojanovski, D.1    Koutsopoulos, O.S.2    Okamoto, K.3    Ryan, M.T.4
  • 16
    • 0242579164 scopus 로고    scopus 로고
    • The Solution Structure of Human Mitochondria Fission Protein Fis1 Reveals a Novel TPR-Like Helix Bundle
    • Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N, (2003) The Solution Structure of Human Mitochondria Fission Protein Fis1 Reveals a Novel TPR-Like Helix Bundle. J Mol Biol 334: 445-458.
    • (2003) J Mol Biol , vol.334 , pp. 445-458
    • Suzuki, M.1    Jeong, S.Y.2    Karbowski, M.3    Youle, R.J.4    Tjandra, N.5
  • 17
    • 22944440071 scopus 로고    scopus 로고
    • The WD40 Protein Caf4p is a Component of the Mitochondrial Fission Machinery and Recruits Dnm1p to Mitochondria
    • Griffin EE, Graumann J, Chan DC, (2005) The WD40 Protein Caf4p is a Component of the Mitochondrial Fission Machinery and Recruits Dnm1p to Mitochondria. J Cell Biol 170: 237-248.
    • (2005) J Cell Biol , vol.170 , pp. 237-248
    • Griffin, E.E.1    Graumann, J.2    Chan, D.C.3
  • 18
    • 33748291455 scopus 로고    scopus 로고
    • Fis1p and Caf4p, but Not Mdv1p, Determine the Polar Localization of Dnm1p Clusters on the Mitochondrial Surface
    • Schauss AC, Bewersdorf J, Jakobs S, (2006) Fis1p and Caf4p, but Not Mdv1p, Determine the Polar Localization of Dnm1p Clusters on the Mitochondrial Surface. J Cell Sci 119: 3098-3106.
    • (2006) J Cell Sci , vol.119 , pp. 3098-3106
    • Schauss, A.C.1    Bewersdorf, J.2    Jakobs, S.3
  • 19
    • 27544450920 scopus 로고    scopus 로고
    • The Role of Fis1p-Mdv1p Interactions in Mitochondrial Fission Complex Assembly
    • Karren MA, Coonrod EM, Anderson TK, Shaw JM, (2005) The Role of Fis1p-Mdv1p Interactions in Mitochondrial Fission Complex Assembly. J Cell Biol 171: 291-301.
    • (2005) J Cell Biol , vol.171 , pp. 291-301
    • Karren, M.A.1    Coonrod, E.M.2    Anderson, T.K.3    Shaw, J.M.4
  • 20
    • 20444414879 scopus 로고    scopus 로고
    • Novel Structure of the N Terminus in Yeast Fis1 Correlates with a Specialized Function in Mitochondrial Fission
    • Suzuki M, Neutzner A, Tjandra N, Youle RJ, (2005) Novel Structure of the N Terminus in Yeast Fis1 Correlates with a Specialized Function in Mitochondrial Fission. J Biol Chem 280: 21444-21452.
    • (2005) J Biol Chem , vol.280 , pp. 21444-21452
    • Suzuki, M.1    Neutzner, A.2    Tjandra, N.3    Youle, R.J.4
  • 21
    • 36749075083 scopus 로고    scopus 로고
    • Structural Basis for Recruitment of Mitochondrial Fission Complexes by Fis1
    • Zhang Y, Chan DC, (2007) Structural Basis for Recruitment of Mitochondrial Fission Complexes by Fis1. Proc Natl Acad Sci U S A 104: 18526-18530.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 18526-18530
    • Zhang, Y.1    Chan, D.C.2
  • 23
    • 33745221197 scopus 로고    scopus 로고
    • Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1
    • Bhar D, Karren MA, Babst M, Shaw JM, (2006) Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1. J Biol Chem 281: 17312-17320.
    • (2006) J Biol Chem , vol.281 , pp. 17312-17320
    • Bhar, D.1    Karren, M.A.2    Babst, M.3    Shaw, J.M.4
  • 24
    • 49749135155 scopus 로고    scopus 로고
    • Peroxisome fission in Hansenula polymorpha requires Mdv1 and Fis1, two proteins also involved in mitochondrial fission
    • Nagotu S, Krikken AM, Otzen M, Kiel JA, Veenhuis M, et al. (2008) Peroxisome fission in Hansenula polymorpha requires Mdv1 and Fis1, two proteins also involved in mitochondrial fission. Traffic 9: 1471-1484.
    • (2008) Traffic , vol.9 , pp. 1471-1484
    • Nagotu, S.1    Krikken, A.M.2    Otzen, M.3    Kiel, J.A.4    Veenhuis, M.5
  • 25
    • 36348930592 scopus 로고    scopus 로고
    • Direct Binding of the Dynamin-Like GTPase, Dnm1, to Mitochondrial Dynamics Protein Fis1 is Negatively Regulated by the Fis1 N-Terminal Arm
    • Wells RC, Picton LK, Williams SC, Tan FJ, Hill RB, (2007) Direct Binding of the Dynamin-Like GTPase, Dnm1, to Mitochondrial Dynamics Protein Fis1 is Negatively Regulated by the Fis1 N-Terminal Arm. J Biol Chem 282: 33769-33775.
    • (2007) J Biol Chem , vol.282 , pp. 33769-33775
    • Wells, R.C.1    Picton, L.K.2    Williams, S.C.3    Tan, F.J.4    Hill, R.B.5
  • 26
    • 8644284924 scopus 로고    scopus 로고
    • Mitochondrial Fission Proteins Regulate Programmed Cell Death in Yeast
    • Fannjiang Y, Cheng WC, Lee SJ, Qi B, Pevsner J, et al. (2004) Mitochondrial Fission Proteins Regulate Programmed Cell Death in Yeast. Genes Dev 18: 2785-2797.
    • (2004) Genes Dev , vol.18 , pp. 2785-2797
    • Fannjiang, Y.1    Cheng, W.C.2    Lee, S.J.3    Qi, B.4    Pevsner, J.5
  • 27
    • 70349501375 scopus 로고    scopus 로고
    • Linking new paradigms in protein chemistry to reversible membrane-protein interactions
    • Halskau O, Muga A, Martinez A, (2009) Linking new paradigms in protein chemistry to reversible membrane-protein interactions. Curr Protein Pept Sci 10: 339-359.
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 339-359
    • Halskau, O.1    Muga, A.2    Martinez, A.3
  • 28
    • 33748462297 scopus 로고    scopus 로고
    • Membrane binding domains
    • Hurley JH, (2006) Membrane binding domains. Biochim Biophys Acta 1761: 805-811.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 805-811
    • Hurley, J.H.1
  • 29
    • 0032872786 scopus 로고    scopus 로고
    • Amphitropic proteins: regulation by reversible membrane interactions (review)
    • Johnson JE, Cornell RB, (1999) Amphitropic proteins: regulation by reversible membrane interactions (review). Mol Membr Biol 16: 217-235.
    • (1999) Mol Membr Biol , vol.16 , pp. 217-235
    • Johnson, J.E.1    Cornell, R.B.2
  • 30
    • 0034947026 scopus 로고    scopus 로고
    • Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
    • Cheever ML, Sato TK, de Beer T, Kutateladze TG, Emr SD, et al. (2001) Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes. Nat Cell Biol 3: 613-618.
    • (2001) Nat Cell Biol , vol.3 , pp. 613-618
    • Cheever, M.L.1    Sato, T.K.2    de Beer, T.3    Kutateladze, T.G.4    Emr, S.D.5
  • 31
    • 33846000631 scopus 로고    scopus 로고
    • Molecular mechanism of membrane docking by the Vam7p PX domain
    • Lee SA, Kovacs J, Stahelin RV, Cheever ML, Overduin M, et al. (2006) Molecular mechanism of membrane docking by the Vam7p PX domain. J Biol Chem 281: 37091-37101.
    • (2006) J Biol Chem , vol.281 , pp. 37091-37101
    • Lee, S.A.1    Kovacs, J.2    Stahelin, R.V.3    Cheever, M.L.4    Overduin, M.5
  • 32
    • 0029825831 scopus 로고    scopus 로고
    • Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin
    • Schiavo G, Gu QM, Prestwich GD, Sollner TH, Rothman JE, (1996) Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin. Proc Natl Acad Sci U S A 93: 13327-13332.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13327-13332
    • Schiavo, G.1    Gu, Q.M.2    Prestwich, G.D.3    Sollner, T.H.4    Rothman, J.E.5
  • 33
    • 0037452791 scopus 로고    scopus 로고
    • Visualization of synaptotagmin I oligomers assembled onto lipid monolayers
    • Wu Y, He Y, Bai J, Ji SR, Tucker WC, et al. (2003) Visualization of synaptotagmin I oligomers assembled onto lipid monolayers. Proc Natl Acad Sci U S A 100: 2082-2087.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2082-2087
    • Wu, Y.1    He, Y.2    Bai, J.3    Ji, S.R.4    Tucker, W.C.5
  • 34
    • 0037150098 scopus 로고    scopus 로고
    • Membrane orientation and position of the C2 domain from cPLA2 by site-directed spin labeling
    • Frazier AA, Wisner MA, Malmberg NJ, Victor KG, Fanucci GE, et al. (2002) Membrane orientation and position of the C2 domain from cPLA2 by site-directed spin labeling. Biochemistry 41: 6282-6292.
    • (2002) Biochemistry , vol.41 , pp. 6282-6292
    • Frazier, A.A.1    Wisner, M.A.2    Malmberg, N.J.3    Victor, K.G.4    Fanucci, G.E.5
  • 35
    • 33644804207 scopus 로고    scopus 로고
    • Close membrane-membrane proximity induced by Ca(2+)-dependent multivalent binding of synaptotagmin-1 to phospholipids
    • Arac D, Chen X, Khant HA, Ubach J, Ludtke SJ, et al. (2006) Close membrane-membrane proximity induced by Ca(2+)-dependent multivalent binding of synaptotagmin-1 to phospholipids. Nat Struct Mol Biol 13: 209-217.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 209-217
    • Arac, D.1    Chen, X.2    Khant, H.A.3    Ubach, J.4    Ludtke, S.J.5
  • 36
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana T, Mackey MR, Perkins G, Ellisman MH, Latterich M, et al. (2002) Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111: 331-342.
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Perkins, G.3    Ellisman, M.H.4    Latterich, M.5
  • 37
    • 33947145756 scopus 로고    scopus 로고
    • Cell-free analysis of tail-anchor protein targeting to membranes
    • Henderson MP, Billen LP, Kim PK, Andrews DW, (2007) Cell-free analysis of tail-anchor protein targeting to membranes. Methods 41: 427-438.
    • (2007) Methods , vol.41 , pp. 427-438
    • Henderson, M.P.1    Billen, L.P.2    Kim, P.K.3    Andrews, D.W.4
  • 38
    • 33744799480 scopus 로고    scopus 로고
    • Evidence that membrane insertion of the cytosolic domain of Bcl-xL is governed by an electrostatic mechanism
    • Thuduppathy GR, Craig JW, Kholodenko V, Schon A, Hill RB, (2006) Evidence that membrane insertion of the cytosolic domain of Bcl-xL is governed by an electrostatic mechanism. J Mol Biol 359: 1045-1058.
    • (2006) J Mol Biol , vol.359 , pp. 1045-1058
    • Thuduppathy, G.R.1    Craig, J.W.2    Kholodenko, V.3    Schon, A.4    Hill, R.B.5
  • 39
    • 0032540234 scopus 로고    scopus 로고
    • Folding of beta-sheet membrane proteins: a hydrophobic hexapeptide model
    • Wimley WC, Hristova K, Ladokhin AS, Silvestro L, Axelsen PH, et al. (1998) Folding of beta-sheet membrane proteins: a hydrophobic hexapeptide model. J Mol Biol 277: 1091-1110.
    • (1998) J Mol Biol , vol.277 , pp. 1091-1110
    • Wimley, W.C.1    Hristova, K.2    Ladokhin, A.S.3    Silvestro, L.4    Axelsen, P.H.5
  • 40
    • 3042665732 scopus 로고    scopus 로고
    • Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis
    • Candiano G, Bruschi M, Musante L, Santucci L, Ghiggeri GM, et al. (2004) Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis. Electrophoresis 25: 1327-1333.
    • (2004) Electrophoresis , vol.25 , pp. 1327-1333
    • Candiano, G.1    Bruschi, M.2    Musante, L.3    Santucci, L.4    Ghiggeri, G.M.5
  • 41
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water
    • Luo P, Baldwin RL, (1997) Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 36: 8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 42
    • 0025073251 scopus 로고
    • Ionization of phospholipids and phospholipid-supported interfacial lateral diffusion of protons in membrane model systems
    • Tocanne JF, Teissie J, (1990) Ionization of phospholipids and phospholipid-supported interfacial lateral diffusion of protons in membrane model systems. Biochim Biophys Acta 1031: 111-142.
    • (1990) Biochim Biophys Acta , vol.1031 , pp. 111-142
    • Tocanne, J.F.1    Teissie, J.2
  • 44
    • 67650468643 scopus 로고    scopus 로고
    • Evidence for conformational heterogeneity of fission protein Fis1 from Saccharomyces cerevisiae
    • Picton LK, Casares S, Monahan AC, Majumdar A, Hill RB, (2009) Evidence for conformational heterogeneity of fission protein Fis1 from Saccharomyces cerevisiae. Biochemistry 48: 6598-6609.
    • (2009) Biochemistry , vol.48 , pp. 6598-6609
    • Picton, L.K.1    Casares, S.2    Monahan, A.C.3    Majumdar, A.4    Hill, R.B.5
  • 46
    • 0022788097 scopus 로고
    • Protein fluorescence quenching by small molecules: protein penetration versus solvent exposure
    • Calhoun DB, Vanderkooi JM, Holtom GR, Englander SW, (1986) Protein fluorescence quenching by small molecules: protein penetration versus solvent exposure. Proteins 1: 109-115.
    • (1986) Proteins , vol.1 , pp. 109-115
    • Calhoun, D.B.1    Vanderkooi, J.M.2    Holtom, G.R.3    Englander, S.W.4
  • 47
    • 0027328666 scopus 로고
    • Acrylamide quenching of the intrinsic fluorescence of tryptophan residues genetically engineered into the soluble colicin E1 channel peptide. Structural characterization of the insertion-competent state
    • Merrill AR, Palmer LR, Szabo AG, (1993) Acrylamide quenching of the intrinsic fluorescence of tryptophan residues genetically engineered into the soluble colicin E1 channel peptide. Structural characterization of the insertion-competent state. Biochemistry 32: 6974-6981.
    • (1993) Biochemistry , vol.32 , pp. 6974-6981
    • Merrill, A.R.1    Palmer, L.R.2    Szabo, A.G.3
  • 48
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw JE, (2000) Dynamin and its role in membrane fission. Annu Rev Cell Dev Biol 16: 483-519.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 51
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: disparate players and common principles
    • Martens S, McMahon HT, (2008) Mechanisms of membrane fusion: disparate players and common principles. Nat Rev Mol Cell Biol 9: 543-556.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 53
    • 0027233827 scopus 로고
    • The role of protein charge in protein-lipid interactions. pH-dependent changes of the electrophoretic mobility of liposomes through adsorption of water-soluble, globular proteins
    • Bergers JJ, Vingerhoeds MH, van Bloois L, Herron JN, Janssen LH, et al. (1993) The role of protein charge in protein-lipid interactions. pH-dependent changes of the electrophoretic mobility of liposomes through adsorption of water-soluble, globular proteins. Biochemistry 32: 4641-4649.
    • (1993) Biochemistry , vol.32 , pp. 4641-4649
    • Bergers, J.J.1    Vingerhoeds, M.H.2    van Bloois, L.3    Herron, J.N.4    Janssen, L.H.5
  • 54
    • 0024741788 scopus 로고
    • Penetration and fusion of phospholipid vesicles by lysozyme
    • Kim J, Kim H, (1989) Penetration and fusion of phospholipid vesicles by lysozyme. Arch Biochem Biophys 274: 100-108.
    • (1989) Arch Biochem Biophys , vol.274 , pp. 100-108
    • Kim, J.1    Kim, H.2
  • 55
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • Li H, Robertson AD, Jensen JH, (2005) Very fast empirical prediction and rationalization of protein pKa values. Proteins 61: 704-721.
    • (2005) Proteins , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 56
    • 33845273500 scopus 로고    scopus 로고
    • The N-terminal domain of Bcl-xL reversibly binds membranes in a pH-dependent manner
    • Thuduppathy GR, Terrones O, Craig JW, Basanez G, Hill RB, (2006) The N-terminal domain of Bcl-xL reversibly binds membranes in a pH-dependent manner. Biochemistry 45: 14533-14542.
    • (2006) Biochemistry , vol.45 , pp. 14533-14542
    • Thuduppathy, G.R.1    Terrones, O.2    Craig, J.W.3    Basanez, G.4    Hill, R.B.5
  • 57
    • 78650787051 scopus 로고    scopus 로고
    • The C. elegans B-cell lymphoma 2 (Bcl-2) homolog cell death abnormal 9 (CED-9) associates with and remodels lipid membranes
    • Tan FJ, Zuckerman JE, Wells RC, Hill RB, (2011) The C. elegans B-cell lymphoma 2 (Bcl-2) homolog cell death abnormal 9 (CED-9) associates with and remodels lipid membranes. Protein Sci 20: 62-74.
    • (2011) Protein Sci , vol.20 , pp. 62-74
    • Tan, F.J.1    Zuckerman, J.E.2    Wells, R.C.3    Hill, R.B.4
  • 58
    • 0003064682 scopus 로고
    • Reduction of dimensionality in biological diffusion processes
    • In: Rich A, Davidson N, editors, New York, W. H. Freeman & Co
    • Adam G, Delbruck M, (1968) Reduction of dimensionality in biological diffusion processes. In: Rich A, Davidson N, editors. Structural Chemistry and Molecular Biology New York W. H. Freeman & Co.
    • (1968) Structural Chemistry and Molecular Biology
    • Adam, G.1    Delbruck, M.2
  • 59
    • 75649088507 scopus 로고    scopus 로고
    • Properties of hydrated excess protons near phospholipid bilayers
    • Yamashita T, Voth GA, (2010) Properties of hydrated excess protons near phospholipid bilayers. J Phys Chem B 114: 592-603.
    • (2010) J Phys Chem B , vol.114 , pp. 592-603
    • Yamashita, T.1    Voth, G.A.2
  • 60
    • 33845936297 scopus 로고    scopus 로고
    • Localized proton microcircuits at the biological membrane-water interface
    • Branden M, Sanden T, Brzezinski P, Widengren J, (2006) Localized proton microcircuits at the biological membrane-water interface. Proc Natl Acad Sci U S A 103: 19766-19770.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19766-19770
    • Branden, M.1    Sanden, T.2    Brzezinski, P.3    Widengren, J.4
  • 61
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology
    • Murray D, Ben-Tal N, Honig B, McLaughlin S, (1997) Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure 5: 985-989.
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 62
    • 0029757155 scopus 로고    scopus 로고
    • Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results
    • Ben-Tal N, Honig B, Peitzsch RM, Denisov G, McLaughlin S, (1996) Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results. Biophys J 71: 561-575.
    • (1996) Biophys J , vol.71 , pp. 561-575
    • Ben-Tal, N.1    Honig, B.2    Peitzsch, R.M.3    Denisov, G.4    McLaughlin, S.5
  • 63
    • 0017812618 scopus 로고
    • Electrostatic interactions at charged lipid membranes. Measurement of surface pH with fluorescent lipoid pH indicators
    • Vaz WL, Nisksch A, Jahnig F, (1978) Electrostatic interactions at charged lipid membranes. Measurement of surface pH with fluorescent lipoid pH indicators. Eur J Biochem 83: 299-305.
    • (1978) Eur J Biochem , vol.83 , pp. 299-305
    • Vaz, W.L.1    Nisksch, A.2    Jahnig, F.3
  • 64
    • 20544468415 scopus 로고    scopus 로고
    • Analysis of functional domains of rat mitochondrial Fis1, the mitochondrial fission-stimulating protein
    • Jofuku A, Ishihara N, Mihara K, (2005) Analysis of functional domains of rat mitochondrial Fis1, the mitochondrial fission-stimulating protein. Biochem Biophys Res Commun 333: 650-659.
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 650-659
    • Jofuku, A.1    Ishihara, N.2    Mihara, K.3
  • 65
    • 84954358239 scopus 로고    scopus 로고
    • The mitochondrial outer membrane protein hFis1 regulates mitochondrial morphology and fission through self-interaction
    • Serasinghe MN, Yoon Y, (2008) The mitochondrial outer membrane protein hFis1 regulates mitochondrial morphology and fission through self-interaction. Exp Cell Res 314: 3494-3507.
    • (2008) Exp Cell Res , vol.314 , pp. 3494-3507
    • Serasinghe, M.N.1    Yoon, Y.2
  • 66
    • 0347417007 scopus 로고    scopus 로고
    • Cytosolic Domain of the Human Mitochondrial Fission Protein Fis1 Adopts a TPR Fold
    • Dohm JA, Lee SJ, Hardwick JM, Hill RB, Gittis AG, (2004) Cytosolic Domain of the Human Mitochondrial Fission Protein Fis1 Adopts a TPR Fold. Proteins 54: 153-156.
    • (2004) Proteins , vol.54 , pp. 153-156
    • Dohm, J.A.1    Lee, S.J.2    Hardwick, J.M.3    Hill, R.B.4    Gittis, A.G.5
  • 67
    • 1542465184 scopus 로고    scopus 로고
    • Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis
    • Yethon JA, Epand RF, Leber B, Epand RM, Andrews DW, (2003) Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis. J Biol Chem 278: 48935-48941.
    • (2003) J Biol Chem , vol.278 , pp. 48935-48941
    • Yethon, J.A.1    Epand, R.F.2    Leber, B.3    Epand, R.M.4    Andrews, D.W.5
  • 68
    • 0025886751 scopus 로고
    • Regulation of CTP:phosphocholine cytidylyltransferase by lipids. 1. Negative surface charge dependence for activation
    • Cornell RB, (1991) Regulation of CTP:phosphocholine cytidylyltransferase by lipids. 1. Negative surface charge dependence for activation. Biochemistry 30: 5873-5880.
    • (1991) Biochemistry , vol.30 , pp. 5873-5880
    • Cornell, R.B.1
  • 69
    • 0029857123 scopus 로고    scopus 로고
    • Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer
    • Stachowiak O, Dolder M, Wallimann T, (1996) Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer. Biochemistry 35: 15522-15528.
    • (1996) Biochemistry , vol.35 , pp. 15522-15528
    • Stachowiak, O.1    Dolder, M.2    Wallimann, T.3
  • 70
    • 70350359860 scopus 로고    scopus 로고
    • Biogenesis of tail-anchored proteins: the beginning for the end?
    • Rabu C, Schmid V, Schwappach B, High S, (2009) Biogenesis of tail-anchored proteins: the beginning for the end? J Cell Sci 122: 3605-3612.
    • (2009) J Cell Sci , vol.122 , pp. 3605-3612
    • Rabu, C.1    Schmid, V.2    Schwappach, B.3    High, S.4
  • 71
    • 34547937485 scopus 로고    scopus 로고
    • How tails guide tail-anchored proteins to their destinations
    • Borgese N, Brambillasca S, Colombo S, (2007) How tails guide tail-anchored proteins to their destinations. Curr Opin Cell Biol 19: 368-375.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 368-375
    • Borgese, N.1    Brambillasca, S.2    Colombo, S.3
  • 72
    • 0027401769 scopus 로고
    • A class of membrane proteins with a C-terminal anchor
    • Kutay U, Hartmann E, Rapoport TA, (1993) A class of membrane proteins with a C-terminal anchor. Trends Cell Biol 3: 72-75.
    • (1993) Trends Cell Biol , vol.3 , pp. 72-75
    • Kutay, U.1    Hartmann, E.2    Rapoport, T.A.3
  • 73
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu YT, Wolter KG, Youle RJ, (1997) Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci U S A 94: 3668-3672.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 74
    • 0030780106 scopus 로고    scopus 로고
    • Movement of Bax from the cytosol to mitochondria during apoptosis
    • Wolter KG, Hsu YT, Smith CL, Nechushtan A, Xi XG, et al. (1997) Movement of Bax from the cytosol to mitochondria during apoptosis. J Cell Biol 139: 1281-1292.
    • (1997) J Cell Biol , vol.139 , pp. 1281-1292
    • Wolter, K.G.1    Hsu, Y.T.2    Smith, C.L.3    Nechushtan, A.4    Xi, X.G.5
  • 75
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S, Narita M, Tsujimoto Y, (1999) Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399: 483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 76
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson B, Montessuit S, Lauper S, Eskes R, Martinou JC, (2000) Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem J 345 Pt 2: 271-278.
    • (2000) Biochem J , vol.345 Pt 2 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 77
    • 1842332735 scopus 로고    scopus 로고
    • Bcl-x(L) forms an ion channel in synthetic lipid membranes
    • Minn AJ, Velez P, Schendel SL, Liang H, Muchmore SW, et al. (1997) Bcl-x(L) forms an ion channel in synthetic lipid membranes. Nature 385: 353-357.
    • (1997) Nature , vol.385 , pp. 353-357
    • Minn, A.J.1    Velez, P.2    Schendel, S.L.3    Liang, H.4    Muchmore, S.W.5
  • 78
    • 0035903220 scopus 로고    scopus 로고
    • Pro-apoptotic cleavage products of Bcl-xL form cytochrome c-conducting pores in pure lipid membranes
    • Basanez G, Zhang J, Chau BN, Maksaev GI, Frolov VA, et al. (2001) Pro-apoptotic cleavage products of Bcl-xL form cytochrome c-conducting pores in pure lipid membranes. J Biol Chem 276: 31083-31091.
    • (2001) J Biol Chem , vol.276 , pp. 31083-31091
    • Basanez, G.1    Zhang, J.2    Chau, B.N.3    Maksaev, G.I.4    Frolov, V.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.