메뉴 건너뛰기




Volumn 186, Issue , 2008, Pages 461-482

Pharmacological interference with protein-protein interactions mediated by coiled-coil motifs

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; GCN4 PROTEIN, S CEREVISIAE; LEUCINE ZIPPER PROTEIN; PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSCRIPTION FACTOR;

EID: 49049088412     PISSN: 01712004     EISSN: 18650325     Source Type: Book Series    
DOI: 10.1007/978-3-540-72843-6_19     Document Type: Article
Times cited : (43)

References (86)
  • 1
    • 0026845838 scopus 로고
    • Structure of the leucine zipper
    • Alber T (1992) Structure of the leucine zipper. Curr Opin Genet Dev 2:205-210
    • (1992) Curr Opin Genet Dev , vol.2 , pp. 205-210
    • Alber, T.1
  • 2
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker KA, Dutch RE, Lamb RA, Jardetzky TS (1999) Structural basis for paramyxovirus-mediated membrane fusion. Mol Cell 3:309-319
    • (1999) Mol Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 3
    • 0029127250 scopus 로고
    • SNAREs and the specificity of transport vesicle targeting
    • Bennett MK (1995) SNAREs and the specificity of transport vesicle targeting. Curr Opin Cell Biol 7:581-586
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 581-586
    • Bennett, M.K.1
  • 4
    • 0028783997 scopus 로고
    • Functional impact of syntaxin on gating of N-type and Q-type calcium channels
    • Bezprozvanny I, Scheller RH, Tsien RW (1995) Functional impact of syntaxin on gating of N-type and Q-type calcium channels. Nature 378:623-626
    • (1995) Nature , vol.378 , pp. 623-626
    • Bezprozvanny, I.1    Scheller, R.H.2    Tsien, R.W.3
  • 5
    • 0028105601 scopus 로고
    • The 2.9 Å crystal structure of T thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)
    • Biou V, Yaremchuk A, Tukalo M, Cusack S (1994) The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser). Science 263:1404-1410
    • (1994) Science , vol.263 , pp. 1404-1410
    • Biou, V.1    Yaremchuk, A.2    Tukalo, M.3    Cusack, S.4
  • 6
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC (1994) Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 7
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr CM, Kim PS (1993) A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 8
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS (1997) Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 9
    • 0029558245 scopus 로고
    • A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced confirmation
    • Chen J, Wharton SA, Weissenhorn W, Calder LJ, Hughson FM, Skehel JJ, Wiley DC (1995) A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced confirmation. Proc Natl Acad Sci USA 92:12205-12209
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12205-12209
    • Chen, J.1    Wharton, S.A.2    Weissenhorn, W.3    Calder, L.J.4    Hughson, F.M.5    Skehel, J.J.6    Wiley, D.C.7
  • 10
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC (1998) Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95:409-417
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5    Wiley, D.C.6
  • 11
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik LV, Kozlov MM (2005) Membrane hemifusion: crossing a chasm in two leaps. Cell 123:375-382
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 13
    • 0037459109 scopus 로고    scopus 로고
    • Centromeres and kinetochores: From epigenetics to mitotic checkpoint signaling
    • Cleveland DW, Mao Y, Sullivan KF (2003) Centromeres and kinetochores: from epigenetics to mitotic checkpoint signaling. Cell 112:407-421
    • (2003) Cell , vol.112 , pp. 407-421
    • Cleveland, D.W.1    Mao, Y.2    Sullivan, K.F.3
  • 14
    • 0037133153 scopus 로고    scopus 로고
    • Targeting protein inactivation through an oligomerization chain reaction
    • Contegno F, Cioce M, Pelicci PG, Minucci S (2002) Targeting protein inactivation through an oligomerization chain reaction. Proc Natl Acad Sci USA 99:1865-1869
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1865-1869
    • Contegno, F.1    Cioce, M.2    Pelicci, P.G.3    Minucci, S.4
  • 15
    • 0025130161 scopus 로고
    • Structural features in the heptad substructure and longer range repeats of two-stranded ?-fibrous proteins
    • Conway JF, Parry DA (1990) Structural features in the heptad substructure and longer range repeats of two-stranded ?-fibrous proteins. Int J Biol Macromol 12:328-334
    • (1990) Int J Biol Macromol , vol.12 , pp. 328-334
    • Conway, J.F.1    Parry, D.A.2
  • 16
    • 0026028894 scopus 로고
    • Three-stranded ?-fibrous proteins: The heptad repeat and its implications for structure
    • Conway JF, Parry DA (1991) Three-stranded ?-fibrous proteins: the heptad repeat and its implications for structure. Int J Biol Macromol 13:14-16
    • (1991) Int J Biol Macromol , vol.13 , pp. 14-16
    • Conway, J.F.1    Parry, D.A.2
  • 17
    • 0001105482 scopus 로고
    • Is ?-keratin a coiled coil?
    • Crick FHC (1952) Is ?-keratin a coiled coil? Nature 170:882-883
    • (1952) Nature , vol.170 , pp. 882-883
    • Crick, F.H.C.1
  • 18
    • 0000920828 scopus 로고
    • The packing of ?-helices: Simple coiled coils
    • Crick FH (1953) The packing of ?-helices: simple coiled coils. Acta Crystallogr 6:689-698
    • (1953) Acta Crystallogr , vol.6 , pp. 689-698
    • Crick, F.H.1
  • 19
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å
    • Cusack S, Berthet-Colominas C, Hartlein M, Nassar N, Leberman R (1990) A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. Nature 347:249-255
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Hartlein, M.3    Nassar, N.4    Leberman, R.5
  • 21
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted γhelices: Crystal structure of the protein-DNA complex
    • Ellenberger TE, Brandl CJ, Struhl K, Harrison, SC (1992) The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted γhelices: crystal structure of the protein-DNA complex. Cell 71:1223-1237
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandl, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 23
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q-and R-SNAREs
    • Fasshauer D, Sutton RB, Brünger AT, Jahn R (1998) Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q-and R-SNAREs. Proc Natl Acad Sci USA 95:15781-15786
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brünger, A.T.3    Jahn, R.4
  • 24
    • 0043162027 scopus 로고    scopus 로고
    • Long coiled-coil proteins and membrane traffic
    • Gillingham AK, Munro S (2003) Long coiled-coil proteins and membrane traffic. Biochim Biophys Acta 1641:71-85
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 71-85
    • Gillingham, A.K.1    Munro, S.2
  • 25
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • Glover JN, Harrison SC (1995) Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature 373:257-261
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.1    Harrison, S.C.2
  • 26
    • 0037615120 scopus 로고    scopus 로고
    • Advancing role of radiolabeled antibodies in the therapy of cancer
    • Goldenberg DM (2003) Advancing role of radiolabeled antibodies in the therapy of cancer. Cancer Immunol Immunother 52:281-296
    • (2003) Cancer Immunol Immunother , vol.52 , pp. 281-296
    • Goldenberg, D.M.1
  • 27
    • 16944366990 scopus 로고    scopus 로고
    • Buried polar residues and structural specificity in the GCN4 leucine zipper
    • Gonzalez L, Jr, Woolfson, DN, Alber T (1996) Buried polar residues and structural specificity in the GCN4 leucine zipper. Nat Struct Biol 3:1011-1018
    • (1996) Nat Struct Biol , vol.3 , pp. 1011-1018
    • Gonzalez, L.1    Woolfson, J.2    Alber, T.D.N.3
  • 28
    • 0034787123 scopus 로고    scopus 로고
    • Advances in pretargeting biotechnology
    • Goodwin DA, Meares CF (2001) Advances in pretargeting biotechnology. Biotechnol Adv 19:435-450
    • (2001) Biotechnol Adv , vol.19 , pp. 435-450
    • Goodwin, D.A.1    Meares, C.F.2
  • 29
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release-four years of SNARE complexes
    • Hanson PI, Heuser JE, Jahn R (1997) Neurotransmitter release-four years of SNARE complexes. Curr Opin Neurobiol 7:310-315
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 310-315
    • Hanson, P.I.1    Heuser, J.E.2    Jahn, R.3
  • 30
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury PB, Zhang T, Kim PS, Alber T (1993) A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262:1401-1407
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 31
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury PB, Kim PS, Alber T (1994) Crystal structure of an isoleucine-zipper trimer. Nature 371:80-83
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 32
    • 0001634436 scopus 로고
    • General and pathway-specific regulatory mechanisms controlling the synthesis of amino acid biosynthetic enzymes in Saccharomyces cerevisae
    • Broach JR, Jones EW, Pringle JR (eds) Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Hinnebusch AG (1992) General and pathway-specific regulatory mechanisms controlling the synthesis of amino acid biosynthetic enzymes in Saccharomyces cerevisae. In: Broach JR, Jones EW, Pringle JR (eds) The molecular and cellular biology of the yeast Saccharomyces: gene expression. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp 319-414
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression , pp. 319-414
    • Hinnebusch, A.G.1
  • 33
    • 0036463655 scopus 로고    scopus 로고
    • Gcn4p, a master regulator of gene expression, is controlled at multiple levels by diverse signals of starvation and stress
    • Hinnebusch AG, Natarajan K (2002) Gcn4p, a master regulator of gene expression, is controlled at multiple levels by diverse signals of starvation and stress. Eukaryot Cell 1:22-32
    • (2002) Eukaryot Cell , vol.1 , pp. 22-32
    • Hinnebusch, A.G.1    Natarajan, K.2
  • 35
    • 0028076788 scopus 로고
    • Reversed-phase liquid chromatography as a useful probe of hydrophobic interactions involved in protein folding and protein stability
    • Hodges RS, Zhu BY, Zhou NE, Mant CT (1994) Reversed-phase liquid chromatography as a useful probe of hydrophobic interactions involved in protein folding and protein stability. J Chromatogr A 676: 3-15
    • (1994) J Chromatogr A , vol.676 , pp. 3-15
    • Hodges, R.S.1    Zhu, B.Y.2    Zhou, N.E.3    Mant, C.T.4
  • 36
    • 0028678794 scopus 로고
    • Transcription factors 1: BZIP proteins
    • Hurst HC (1994) Transcription factors 1: bZIP proteins. Protein Profile 1(2):123-168
    • (1994) Protein Profile , vol.1 , Issue.2 , pp. 123-168
    • Hurst, H.C.1
  • 37
    • 0029174419 scopus 로고
    • Transcription factors 1: BZIP proteins
    • Hurst HC (1995) Transcription factors 1: bZIP proteins. Protein Profile 2(2):101-168
    • (1995) Protein Profile , vol.2 , Issue.2 , pp. 101-168
    • Hurst, H.C.1
  • 38
    • 0030981954 scopus 로고    scopus 로고
    • Differences in sialic acid-galactose linkages in the chicken egg amnion and allantois influence human influenza virus receptor specificity and variant selection
    • Ito T, Suzuki Y, Takada A, Kawamoto A, Otsuki K, Masuda H, Yamada M, Suzuki T, Kida H, Kawaoka Y (1997) Differences in sialic acid-galactose linkages in the chicken egg amnion and allantois influence human influenza virus receptor specificity and variant selection. J Virol 71:3357-3362
    • (1997) J Virol , vol.71 , pp. 3357-3362
    • Ito, T.1    Suzuki, Y.2    Takada, A.3    Kawamoto, A.4    Otsuki, K.5    Masuda, H.6    Yamada, M.7    Suzuki, T.8    Kida, H.9    Kawaoka, Y.10
  • 39
    • 0028609771 scopus 로고
    • Molecular mechanisms of clostridial neurotoxins
    • Jahn R, Niemann H (1994) Molecular mechanisms of clostridial neurotoxins. Ann NY Acad Sci 733:245-255
    • (1994) Ann NY Acad Sci , vol.733 , pp. 245-255
    • Jahn, R.1    Niemann, H.2
  • 41
    • 7244253012 scopus 로고    scopus 로고
    • N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion
    • Jiang S, Lu H, Liu S, Zhao Q, He Y, Debnath AK (2004) N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion. Antimicrob Agents Chemother 48:4349-4359
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4349-4359
    • Jiang, S.1    Lu, H.2    Liu, S.3    Zhao, Q.4    He, Y.5    Debnath, A.K.6
  • 42
    • 17044413582 scopus 로고    scopus 로고
    • High-throughput screening method of inhibitors that block the interaction between two helical regions of HIV-1 gp41
    • Jin BS, Lee WK, Ahn K, Lee MK, Yu YG (2005) High-throughput screening method of inhibitors that block the interaction between two helical regions of HIV-1 gp41. Biomol Screen 10:13-19
    • (2005) Biomol Screen , vol.10 , pp. 13-19
    • Jin, B.S.1    Lee, W.K.2    Ahn, K.3    Lee, M.K.4    Yu, Y.G.5
  • 43
    • 0029563634 scopus 로고
    • Crystal structure of a bZIP/DNA complex at 2.2 Å: Determinants of DNA specific recognition
    • Keller W, König P, Richmond TJ (1995) Crystal structure of a bZIP/DNA complex at 2.2 Å: determinants of DNA specific recognition. J Mol Biol 254:657-667
    • (1995) J Mol Biol , vol.254 , pp. 657-667
    • Keller, W.1    König, P.2    Richmond, T.J.3
  • 44
    • 0036353719 scopus 로고    scopus 로고
    • A buried polar residue in the hydrophobic interface of the coiled coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding
    • Knappenberger JA, Smith JE, Thorpe SH, Zitzewitz JA, Matthews CR (2002) A buried polar residue in the hydrophobic interface of the coiled coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding. J Mol Biol 321:1-6
    • (2002) J Mol Biol , vol.321 , pp. 1-6
    • Knappenberger, J.A.1    Smith, J.E.2    Thorpe, S.H.3    Zitzewitz, J.A.4    Matthews, C.R.5
  • 45
    • 0027377202 scopus 로고
    • The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility
    • König P, Richmond TJ (1993) The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. J Mol Biol 233:139-154
    • (1993) J Mol Biol , vol.233 , pp. 139-154
    • König, P.1    Richmond, T.J.2
  • 46
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: E and g interhelical interactions
    • Krylov D, Mikhailenko I, Vinson C (1994) A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions. EMBO J 13:2849-2861
    • (1994) EMBO J , vol.13 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 47
    • 0032080907 scopus 로고    scopus 로고
    • Interaction of transmembrane helices by a knobs-into-holes packing characteristic of soluble coiled coils
    • Langosch D, Heringa J (1998) Interaction of transmembrane helices by a knobs-into-holes packing characteristic of soluble coiled coils. Proteins 31:150-159
    • (1998) Proteins , vol.31 , pp. 150-159
    • Langosch, D.1    Heringa, J.2
  • 48
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled coil stability, and specificity of dimerization
    • Lavigne P, Sonnichsen FD, Kay CM, Hodges RS, Lumb KJ, Kim PS (1996) Interhelical salt bridges, coiled coil stability, and specificity of dimerization. Science 271:1136-1138
    • (1996) Science , vol.271 , pp. 1136-1138
    • Lavigne, P.1    Sonnichsen, F.D.2    Kay, C.M.3    Hodges, R.S.4    Lumb, K.J.5    Kim, P.S.6
  • 51
    • 0034808117 scopus 로고    scopus 로고
    • Comparing function and structure between entire proteomes
    • Liu J, Rost B (2001) Comparing function and structure between entire proteomes. Protein Sci 10:1970-1979
    • (2001) Protein Sci , vol.10 , pp. 1970-1979
    • Liu, J.1    Rost, B.2
  • 52
    • 0029030233 scopus 로고
    • Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
    • Lumb KJ, Kim PS (1995) Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science 268:436-439
    • (1995) Science , vol.268 , pp. 436-439
    • Lumb, K.J.1    Kim, P.S.2
  • 54
    • 2342550183 scopus 로고    scopus 로고
    • Discontinuation of the clinical development of fusion inhibitor T1249
    • Martínez-Carbonero L (2004) Discontinuation of the clinical development of fusion inhibitor T1249. AIDS Rev 6:61
    • (2004) AIDS Rev , vol.6 , pp. 61
    • Martínez-Carbonero, L.1
  • 55
    • 0016774265 scopus 로고
    • Tropomyosin coiled coil interactions: Evidence for an unstaggered structure
    • McLachlan AD, Stewart M (1975) Tropomyosin coiled coil interactions: evidence for an unstaggered structure. J Mol Biol 98:293-304
    • (1975) J Mol Biol , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 56
    • 0037595546 scopus 로고    scopus 로고
    • Comprehensive identification of human bZIP interactions with coiled coil arrays
    • Newman JR, Keating AE (2003) Comprehensive identification of human bZIP interactions with coiled coil arrays. Science 300:2097-2101
    • (2003) Science , vol.300 , pp. 2097-2101
    • Newman, J.R.1    Keating, A.E.2
  • 57
    • 0024384644 scopus 로고
    • Preferential heterodimer formation by isolated leucine zippers from fos and jun
    • O'Shea EK, Rutkowski R, Kim PS (1989) Preferential heterodimer formation by isolated leucine zippers from fos and jun. Science 245:646-648
    • (1989) Science , vol.245 , pp. 646-648
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 58
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea EK, Klemm JD, Kim PS, Alber T (1991) X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254:539-544
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 59
    • 0026571898 scopus 로고
    • Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
    • O'Shea EK, Rutkowski R, Kim PS (1992) Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell 68:699-708
    • (1992) Cell , vol.68 , pp. 699-708
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 63
    • 0028168140 scopus 로고
    • Synthesis and properties of the peptide corresponding to the mutant form of the leucine zipper of the transcriptional activator GCN4 from yeast
    • Potekhin SA, Medvedkin VN, Kashparov IA, Venyaminov SY (1994) Synthesis and properties of the peptide corresponding to the mutant form of the leucine zipper of the transcriptional activator GCN4 from yeast. Protein Eng 7:1097-1101
    • (1994) Protein Eng , vol.7 , pp. 1097-1101
    • Potekhin, S.A.1    Medvedkin, V.N.2    Kashparov, I.A.3    Venyaminov, S.Y.4
  • 64
    • 11144340301 scopus 로고    scopus 로고
    • Class i and class II viral fusion protein structures reveal similar principles in membrane fusion
    • Schibli DJ, Weissenhorn W (2004) class I and class II viral fusion protein structures reveal similar principles in membrane fusion. Mol Membr Biol 21:361-371
    • (2004) Mol Membr Biol , vol.21 , pp. 361-371
    • Schibli, D.J.1    Weissenhorn, W.2
  • 66
    • 33646202286 scopus 로고    scopus 로고
    • The SNARE motif is essential for the formation of syntaxin clusters in the plasma membrane
    • Sieber JJ, Willig KI, Heintzmann R, Hell SW, Lang T (2006) The SNARE motif is essential for the formation of syntaxin clusters in the plasma membrane. Biophys J 90:2843-2851
    • (2006) Biophys J , vol.90 , pp. 2843-2851
    • Sieber, J.J.1    Willig, K.I.2    Heintzmann, R.3    Hell, S.W.4    Lang, T.5
  • 68
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel JJ, Wiley DJ (2000) Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69:531-569
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.J.2
  • 69
    • 0015463470 scopus 로고
    • Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure
    • Sodek J, Hodges RS, Smillie LB, Jurasek L (1972) Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. Proc Natl Acad Sci USA 69:3800-3804
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 3800-3804
    • Sodek, J.1    Hodges, R.S.2    Smillie, L.B.3    Jurasek, L.4
  • 71
    • 34948827535 scopus 로고    scopus 로고
    • Synaptotagmin activates membrane fusion through a Ca2+-dependent trans interaction with phospholipids
    • Stein A, Radhakrishnan A, Riedel D, Fasshauer D, Jahn R (2007) Synaptotagmin activates membrane fusion through a Ca2+-dependent trans interaction with phospholipids. Nat Struct Mol Biol 14:904-911
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 904-911
    • Stein, A.1    Radhakrishnan, A.2    Riedel, D.3    Fasshauer, D.4    Jahn, R.5
  • 72
    • 0027160097 scopus 로고
    • Structure, function, and dynamics of keratin intermediate filaments
    • Steinert PM (1993) Structure, function, and dynamics of keratin intermediate filaments. J Invest Dermatol 100:729-734
    • (1993) J Invest Dermatol , vol.100 , pp. 729-734
    • Steinert, P.M.1
  • 73
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton RB, Fasshauer D, Jahn R, Brünger AT (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395:347-353
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brünger, A.T.4
  • 74
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K, Liu, J, Wang J-H, Shen S, Lu M (1997) Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc Natl Acad Sci USA 94:12303-12308
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.-H.3    Shen, S.4    Lu, M.5
  • 75
    • 0024370748 scopus 로고
    • Scissors-grip model for DNA recognition by a family of leucine zipper proteins
    • Vinson CR, Sigler PB, McKnight SL (1989) Scissors-grip model for DNA recognition by a family of leucine zipper proteins. Science 246:911-916
    • (1989) Science , vol.246 , pp. 911-916
    • Vinson, C.R.1    Sigler, P.B.2    McKnight, S.L.3
  • 77
    • 17244363408 scopus 로고    scopus 로고
    • Molecular organization of the Ndc80 complex, an essential kinetochore component
    • Wei RR, Sorger PK, Harrison SC (2005) Molecular organization of the Ndc80 complex, an essential kinetochore component. Proc Natl Acad Sci USA 102:5363-5367
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5363-5367
    • Wei, R.R.1    Sorger, P.K.2    Harrison, S.C.3
  • 78
    • 33744798200 scopus 로고    scopus 로고
    • Structure of a central component of the yeast kinetochore: The Spc24p/Spc25p globular domain
    • Wei RR, Schnell JR, Larsen NA, Sorger PK, Chou JJ, Harrison SC (2006) Structure of a central component of the yeast kinetochore: the Spc24p/Spc25p globular domain. Structure 14:1003-1009
    • (2006) Structure , vol.14 , pp. 1003-1009
    • Wei, R.R.1    Schnell, J.R.2    Larsen, N.A.3    Sorger, P.K.4    Chou, J.J.5    Harrison, S.C.6
  • 79
    • 33846100785 scopus 로고    scopus 로고
    • The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment
    • Wei RR, Al-Bassam J, Harrison SC (2007) The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment. Nat Struct Mol Biol 14:54-59
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 54-59
    • Wei, R.R.1    Al-Bassam, J.2    Harrison, S.C.3
  • 80
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • Wiley DC
    • Weissenhorn W, Dessen A, Harrison SC, Skehel JJ, Wiley DC (1997) Atomic structure of the ectodomain from HIV-1 gp41. Nature 387:426-430
    • (1997) Nature , vol.387 , pp. 426-430
    • Weissenhorn, W.1    Dessen, A.2    Harrison, S.C.3    Skehel, J.J.4
  • 82
    • 0022657187 scopus 로고
    • Studies of influenza haemagglutinin-mediated membrane fusion
    • Wiley DC
    • Wharton SA, Skehel JJ, Wiley DC (1986) Studies of influenza haemagglutinin-mediated membrane fusion. Virology 149:27-35
    • (1986) Virology , vol.149 , pp. 27-35
    • Wharton, S.A.1    Skehel, J.J.2
  • 83
    • 0035931755 scopus 로고    scopus 로고
    • The Ndc80p complex from Saccharomyces cerevisiae contains conserved centromere components and has a function in chromosome segregation
    • Wigge PA, Kilmartin JV (2001) The Ndc80p complex from Saccharomyces cerevisiae contains conserved centromere components and has a function in chromosome segregation. J Cell Biol 152:349-360
    • (2001) J Cell Biol , vol.152 , pp. 349-360
    • Wigge, P.A.1    Kilmartin, J.V.2
  • 84
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild C, Oas T, McDanal CB, Bolognesi D, Matthews T (1992) A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc Natl Acad Sci USA 89:10537-10541
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.B.3    Bolognesi, D.4    Matthews, T.5
  • 85
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive ?-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild C, Shugars DC, Greenwell TK, McDanal CB, Matthews TJ (1994) Peptides corresponding to a predictive ?-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc Natl Acad Sci USA 91:9770-9774
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9770-9774
    • Wild, C.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 86
    • 0019890491 scopus 로고
    • Structure of the haemeagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson IA, Skehel JJ, Wiley DC (1981) Structure of the haemeagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289:366-373
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.