메뉴 건너뛰기




Volumn 6, Issue 5, 2007, Pages 1899-1916

Functional anthology of intrinsic disorder. 2. cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions

Author keywords

Bioinformatics; Disorder prediction; Intrinsic disorder; Intrinsically disordered proteins; Protein function; Protein structure

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; BIOINFORMATICS; CELL COMPOSITION; MOLECULAR BIOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEOMICS;

EID: 34249282661     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr060393m     Document Type: Article
Times cited : (215)

References (255)
  • 1
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 2002, 11, 739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 2
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky, V. N. What does it mean to be natively unfolded? Eur. J. Biochem. 2002, 269, 2-12.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 7
    • 85142171743 scopus 로고    scopus 로고
    • Vucetic, S.; Obradovic, Z.; Vacic, V; Radivojac, P.; Peng, K.; Iakoucheva, L. M.; Cortese, M. S.; Lawson, J. D.; Brown, C. J.; Sikes, J. G.; Newton, C. D.; Dunker, A. K. DisProt: a database of protein disorder. Bioinformatics 2005, 21, 137-140.
    • Vucetic, S.; Obradovic, Z.; Vacic, V; Radivojac, P.; Peng, K.; Iakoucheva, L. M.; Cortese, M. S.; Lawson, J. D.; Brown, C. J.; Sikes, J. G.; Newton, C. D.; Dunker, A. K. DisProt: a database of protein disorder. Bioinformatics 2005, 21, 137-140.
  • 8
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright, P. E.; Dyson, H. J. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J. Mol. Biol. 1999, 293, 321-331.
    • (1999) J. Mol. Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 9
    • 0034669882 scopus 로고    scopus 로고
    • Uversky, V. N.; Gillespie, J. R.; Fink, A. L. Why are natively unfolded proteins unstructured under physiologic conditions? Proteins 2000, 41, 415-427.
    • Uversky, V. N.; Gillespie, J. R.; Fink, A. L. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 2000, 41, 415-427.
  • 12
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • Dunker, A. K.; Brown, C. J.; Obradovic, Z. Identification and functions of usefully disordered proteins. Adv. Protein Chem. 2002, 62, 25-49.
    • (2002) Adv. Protein Chem , vol.62 , pp. 25-49
    • Dunker, A.K.1    Brown, C.J.2    Obradovic, Z.3
  • 13
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J.; Wright, P. E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 2002, 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 14
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J.; Wright, P. E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005, 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 15
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. Intrinsically unstructured proteins. Trends Biochem. Sci. 2002, 27, 527-533.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 16
    • 24944511034 scopus 로고    scopus 로고
    • Natively disordered proteins
    • Buchner, J, Kiefhaber, T, Eds, Wiley-VCH, Verlag GmbH & Co. KGaA: Weinheim, Germany
    • Daughdrill, G. W.; Pielak, G. J.; Uversky, V. N.; Cortese, M. S.; Dunker, A. K. Natively disordered proteins. In Handbook of Protein Folding; Buchner, J., Kiefhaber, T., Eds.; Wiley-VCH, Verlag GmbH & Co. KGaA: Weinheim, Germany, 2005; pp 271-353.
    • (2005) Handbook of Protein Folding , pp. 271-353
    • Daughdrill, G.W.1    Pielak, G.J.2    Uversky, V.N.3    Cortese, M.S.4    Dunker, A.K.5
  • 17
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker, A. K.; Cortese, M. S.; Romero, P.; Iakoucheva, L. M.; Uversky, V. N. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J. 2005, 272, 5129-5148.
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 18
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky, V. N.; Oldfield, C. J.; Dunker, A. K. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 2005, 18, 343-384.
    • (2005) J. Mol. Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 19
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity-linking function and disorder
    • Dunker, A. K.; Obradovic, Z. The protein trinity-linking function and disorder. Nat. Biotechnol. 2001, 19, 805-806.
    • (2001) Nat. Biotechnol , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 20
    • 33847768609 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions
    • Xie, H.; Vucetic, S.; Iakoucheva, L. M.; Oldfield, C. J.; Dunker, A. K.; Obradovic, Z.; Uversky, V. N. Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. J. Proteome Res. 2007, 5, 1882-1898.
    • (2007) J. Proteome Res , vol.5 , pp. 1882-1898
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 24
    • 0036529479 scopus 로고    scopus 로고
    • An efficient algorithm for large-scale detection of protein families
    • Enright, A. J.; Van Dongen, S.; Ouzounis, C. A. An efficient algorithm for large-scale detection of protein families. Nucleic Acids Res. 2002, 30, 1575-1584.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1575-1584
    • Enright, A.J.1    Van Dongen, S.2    Ouzounis, C.A.3
  • 25
    • 0028197368 scopus 로고
    • HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures
    • Grosschedl, R.; Giese, K.; Pagel, J. HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet. 1994, 10, 94-100.
    • (1994) Trends Genet , vol.10 , pp. 94-100
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 26
    • 0035904395 scopus 로고    scopus 로고
    • Molecular biology of HMGA proteins: Hubs of nuclear function
    • Reeves, R. Molecular biology of HMGA proteins: hubs of nuclear function. Gene 2001, 277, 63-81.
    • (2001) Gene , vol.277 , pp. 63-81
    • Reeves, R.1
  • 27
    • 0020577114 scopus 로고
    • On the presence of two new high mobility group-like proteins in HeLa S3 cells
    • Lund, T.; Holtlund, J.; Fredriksen, M.; Laland, S. G. On the presence of two new high mobility group-like proteins in HeLa S3 cells. FEBS Lett. 1983, 152, 163-167.
    • (1983) FEBS Lett , vol.152 , pp. 163-167
    • Lund, T.1    Holtlund, J.2    Fredriksen, M.3    Laland, S.G.4
  • 28
    • 0024009983 scopus 로고
    • A conformational study of the sequence specific binding of HMG-I (Y) with the bovine interleukin-2 cDNA
    • Lehn, D. A.; Elton, T. S.; Johnson, K. R.; Reeves, R. A conformational study of the sequence specific binding of HMG-I (Y) with the bovine interleukin-2 cDNA. Biochem. Int. 1988, 16, 963-971.
    • (1988) Biochem. Int , vol.16 , pp. 963-971
    • Lehn, D.A.1    Elton, T.S.2    Johnson, K.R.3    Reeves, R.4
  • 29
    • 34249325211 scopus 로고    scopus 로고
    • Evans, J. N.; Nissen, M. S.; R. R. Assignment of the 1H NMR spectrum of a consensus DNA-binding peptide from the HMG-1 protein. Bull. Magn. Reson. 1992, 14, 171-174.
    • Evans, J. N.; Nissen, M. S.; R. R. Assignment of the 1H NMR spectrum of a consensus DNA-binding peptide from the HMG-1 protein. Bull. Magn. Reson. 1992, 14, 171-174.
  • 30
    • 0028989950 scopus 로고
    • 1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding peptide from the HMG-I protein
    • Evans, J. N.; Zajicek, J.; Nissen, M. S.; Munske, G.; Smith, V.; Reeves, R. 1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding peptide from the HMG-I protein. Int. J. Pept. Protein Res. 1995, 45, 554-560.
    • (1995) Int. J. Pept. Protein Res , vol.45 , pp. 554-560
    • Evans, J.N.1    Zajicek, J.2    Nissen, M.S.3    Munske, G.4    Smith, V.5    Reeves, R.6
  • 31
    • 0037634375 scopus 로고    scopus 로고
    • Identification of both shared and distinct proteins in the major and minor spliceosomes
    • Will, C. L.; Schneider, C.; Reed, R.; Luhrmann, R. Identification of both shared and distinct proteins in the major and minor spliceosomes. Science 1999, 284, 2003-2005.
    • (1999) Science , vol.284 , pp. 2003-2005
    • Will, C.L.1    Schneider, C.2    Reed, R.3    Luhrmann, R.4
  • 33
    • 2442690346 scopus 로고    scopus 로고
    • The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome
    • Will, C.L.; Schneider, C.; Hossbach, M.; Urlaub, H.; Rauhut, R.; Elbashir, S.; Tuschl, T.; Luhrmann, R. The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome. RNA 2004, 10, 929-941.
    • (2004) RNA , vol.10 , pp. 929-941
    • Will, C.L.1    Schneider, C.2    Hossbach, M.3    Urlaub, H.4    Rauhut, R.5    Elbashir, S.6    Tuschl, T.7    Luhrmann, R.8
  • 34
    • 0029917043 scopus 로고    scopus 로고
    • Three recognition events at the branch-site adenine
    • Query, C. C.; Strobel, S. A.; Sharp, P. A. Three recognition events at the branch-site adenine. EMBO J. 1996, 15, 1392-1402.
    • (1996) EMBO J , vol.15 , pp. 1392-1402
    • Query, C.C.1    Strobel, S.A.2    Sharp, P.A.3
  • 35
    • 33344463111 scopus 로고    scopus 로고
    • Biochemical and NMR analyses of an SF3b155-p14-U2AF-RNA interaction network involved in branch point definition during pre-mRNA splicing
    • Spadaccini, R.; Reidt, U.; Dybkov, O.; Will, C.; Frank, R.; Stier, G.; Corsini, L.; Wahl, M. C.; Luhrmann, R.; Sattler, M. Biochemical and NMR analyses of an SF3b155-p14-U2AF-RNA interaction network involved in branch point definition during pre-mRNA splicing. RNA 2006, 12, 410-425.
    • (2006) RNA , vol.12 , pp. 410-425
    • Spadaccini, R.1    Reidt, U.2    Dybkov, O.3    Will, C.4    Frank, R.5    Stier, G.6    Corsini, L.7    Wahl, M.C.8    Luhrmann, R.9    Sattler, M.10
  • 36
    • 0026716104 scopus 로고
    • SR proteins: A conserved family of pre-mRNA splicing factors
    • Zahler, A. M.; Lane, W. S.; Stolk, J. A.; Roth, M. B. SR proteins: a conserved family of pre-mRNA splicing factors. Genes Dev. 1992, 6, 837-847.
    • (1992) Genes Dev , vol.6 , pp. 837-847
    • Zahler, A.M.1    Lane, W.S.2    Stolk, J.A.3    Roth, M.B.4
  • 37
    • 0029377886 scopus 로고
    • SR proteins escort the U4/U6.U5 tri-snRNP to the spliceosome
    • Roscigno, R. F.; Garcia-Blanco, M. A. SR proteins escort the U4/U6.U5 tri-snRNP to the spliceosome. RNA 1995, 2, 692-706.
    • (1995) RNA , vol.2 , pp. 692-706
    • Roscigno, R.F.1    Garcia-Blanco, M.A.2
  • 38
    • 31544433157 scopus 로고    scopus 로고
    • Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins
    • Haynes, C.; Iakoucheva, L. M. Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins. Nucleic Acids Res. 2006, 34, 305-312.
    • (2006) Nucleic Acids Res , vol.34 , pp. 305-312
    • Haynes, C.1    Iakoucheva, L.M.2
  • 39
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee, G.; Cowan, N.; Kirschner, M. The primary structure and heterogeneity of tau protein from mouse brain. Science 1988, 239, 285-288.
    • (1988) Science , vol.239 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 40
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains
    • Himmler, A.; Drechsel, D.; Kirschner, M. W.; Martin, D. W., Jr. Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains. Mol. Cell. Biol. 1989, 9, 1381-1388.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin Jr., D.W.4
  • 41
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert, M.; Spillantini, M. G.; Jakes, R.; Rutherford, D.; Crowther, R. A. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 1989, 3, 519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 42
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • Butner, K. A.; Kirschner, M. W. Tau protein binds to microtubules through a flexible array of distributed weak sites. J. Cell Biol. 1991, 115, 717-730.
    • (1991) J. Cell Biol , vol.115 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 44
    • 0031035402 scopus 로고    scopus 로고
    • Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly
    • Goode, B. L.; Denis, P. E.; Panda, D.; Radeke, M. J.; Miller, H. P.; Wilson, L.; Feinstein, S. C. Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly. Mol. Biol. Cell 1997, 8, 353-365.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 353-365
    • Goode, B.L.1    Denis, P.E.2    Panda, D.3    Radeke, M.J.4    Miller, H.P.5    Wilson, L.6    Feinstein, S.C.7
  • 46
    • 0032211829 scopus 로고    scopus 로고
    • Mandelkow, E. M.; Mandelkow, E. Tau in Alzheimer's disease. Trends Cell Biol. 1998, 8, 425-427.
    • Mandelkow, E. M.; Mandelkow, E. Tau in Alzheimer's disease. Trends Cell Biol. 1998, 8, 425-427.
  • 47
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille, H.; Drewes, G.; Biernat, J.; Mandelkow, E. M.; Mandelkow, E. Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J. Cell Biol. 1992, 118, 573-584.
    • (1992) J. Cell Biol , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 48
    • 0028170411 scopus 로고
    • Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure
    • Schweers, O.; Schonbrunn-Hanebeck, E.; Marx, A.; Mandelkow, E. Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. J. Biol. Chem. 1994, 269, 24290-24297.
    • (1994) J. Biol. Chem , vol.269 , pp. 24290-24297
    • Schweers, O.1    Schonbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 50
    • 0030708555 scopus 로고    scopus 로고
    • Entropic exclusion by neurofilament sidearms: A mechanism for maintaining interfilament spacing
    • Brown, H. G.; Hoh, J. H. Entropic exclusion by neurofilament sidearms: a mechanism for maintaining interfilament spacing. Biochemistry 1997, 36, 15035-15040.
    • (1997) Biochemistry , vol.36 , pp. 15035-15040
    • Brown, H.G.1    Hoh, J.H.2
  • 51
    • 0023653418 scopus 로고
    • Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H
    • Geisler, N.; Vandekerckhove, J.; Weber, K. Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H. FEBS Lett. 1987, 221, 403-407.
    • (1987) FEBS Lett , vol.221 , pp. 403-407
    • Geisler, N.1    Vandekerckhove, J.2    Weber, K.3
  • 52
    • 0036468982 scopus 로고    scopus 로고
    • The oncoprotein 18/stathmin family of microtubule destabilizers
    • Cassimeris, L. The oncoprotein 18/stathmin family of microtubule destabilizers. Curr. Opin. Cell Biol. 2002, 14, 18-24.
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 18-24
    • Cassimeris, L.1
  • 55
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • Ravelli, R. B.; Gigant, B.; Curmi, P. A.; Jourdain, I.; Lachkar, S.; Sobel, A.; Knossow, M. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 2004, 428, 198-202.
    • (2004) Nature , vol.428 , pp. 198-202
    • Ravelli, R.B.1    Gigant, B.2    Curmi, P.A.3    Jourdain, I.4    Lachkar, S.5    Sobel, A.6    Knossow, M.7
  • 56
    • 33744915563 scopus 로고    scopus 로고
    • Control of intrinsically disordered stathmin by multisite phosphorylation
    • Honnappa, S.; Jahnke, W.; Seelig, J.; Steinmetz, M. O. Control of intrinsically disordered stathmin by multisite phosphorylation. J. Biol. Chem. 2006, 281, 16078-16083.
    • (2006) J. Biol. Chem , vol.281 , pp. 16078-16083
    • Honnappa, S.1    Jahnke, W.2    Seelig, J.3    Steinmetz, M.O.4
  • 57
    • 33750353597 scopus 로고    scopus 로고
    • Structural and functional dynamics of human centromeric chromatin
    • Schueler, M. G.; Sullivan, B. A. Structural and functional dynamics of human centromeric chromatin. Annu. Rev. Genomics Hum. Genet. 2006, 7, 301-313.
    • (2006) Annu. Rev. Genomics Hum. Genet , vol.7 , pp. 301-313
    • Schueler, M.G.1    Sullivan, B.A.2
  • 58
    • 0345255913 scopus 로고    scopus 로고
    • Structure, function, and regulation of budding yeast kinetochores
    • McAinsh, A. D.; Tytell, J. D.; Sorger, P. K. Structure, function, and regulation of budding yeast kinetochores. Annu. Rev. Cell Dev. Biol. 2003, 19, 519-539.
    • (2003) Annu. Rev. Cell Dev. Biol , vol.19 , pp. 519-539
    • McAinsh, A.D.1    Tytell, J.D.2    Sorger, P.K.3
  • 59
    • 33645281420 scopus 로고    scopus 로고
    • The long and the short of it: Linker histone HI is required for metaphase chromosome compaction
    • Maresca, T. J.; Heald, R. The long and the short of it: linker histone HI is required for metaphase chromosome compaction. Cell Cycle 2006, 5, 589-591.
    • (2006) Cell Cycle , vol.5 , pp. 589-591
    • Maresca, T.J.1    Heald, R.2
  • 60
    • 0035931755 scopus 로고    scopus 로고
    • The Ndc80p complex from Saccharomyces cerevisiae contains conserved centromere components and has a function in chromosome segregation
    • Wigge, P. A.; Kilmartin, J. V. The Ndc80p complex from Saccharomyces cerevisiae contains conserved centromere components and has a function in chromosome segregation. J. Cell Biol. 2001, 152, 349-360.
    • (2001) J. Cell Biol , vol.152 , pp. 349-360
    • Wigge, P.A.1    Kilmartin, J.V.2
  • 61
    • 17244363408 scopus 로고    scopus 로고
    • Molecular organization of the Ndc80 complex, an essential kinetochore component
    • Wei, R. R.; Sorger, P. K.; Harrison, S. C.Molecular organization of the Ndc80 complex, an essential kinetochore component. Proc. Natl. Acad. Sci. U.SA. 2005, 102, 5363-5367.
    • (2005) Proc. Natl. Acad. Sci. U.SA , vol.102 , pp. 5363-5367
    • Wei, R.R.1    Sorger, P.K.2    Harrison, S.C.3
  • 63
    • 0035131438 scopus 로고    scopus 로고
    • Roles of partly unfolded conformations in macromolecular self-assembly
    • Namba, K. Roles of partly unfolded conformations in macromolecular self-assembly. Genes Cells 2001, 6, 1-12.
    • (2001) Genes Cells , vol.6 , pp. 1-12
    • Namba, K.1
  • 64
    • 0024227425 scopus 로고
    • Flagellin parts acquiring a regular structure during polymerization are disposed on the molecule ends
    • Kostyukova, A. S.; Pyatibratov, M. G.; Filimonov, V. V.; Fedorov, O. V. Flagellin parts acquiring a regular structure during polymerization are disposed on the molecule ends. FEBS Lett. 1988, 241, 141-144.
    • (1988) FEBS Lett , vol.241 , pp. 141-144
    • Kostyukova, A.S.1    Pyatibratov, M.G.2    Filimonov, V.V.3    Fedorov, O.V.4
  • 65
    • 0024415907 scopus 로고
    • Terminal regions of flagellin are disordered in solution
    • Vonderviszt, F.; Kanto, S.; Aizawa, S.; Namba, K. Terminal regions of flagellin are disordered in solution. J. Mol. Biol. 1989, 209, 127-133.
    • (1989) J. Mol. Biol , vol.209 , pp. 127-133
    • Vonderviszt, F.1    Kanto, S.2    Aizawa, S.3    Namba, K.4
  • 66
    • 0030852248 scopus 로고    scopus 로고
    • Locations of terminal segments of flagellin in the filament structure and their roles in polymerization and polymorphism
    • Mimori-Kiyosue, Y.; Vonderviszt, F.; Namba, K. Locations of terminal segments of flagellin in the filament structure and their roles in polymerization and polymorphism. J. Mol. Biol. 1997, 270, 222-237.
    • (1997) J. Mol. Biol , vol.270 , pp. 222-237
    • Mimori-Kiyosue, Y.1    Vonderviszt, F.2    Namba, K.3
  • 68
    • 23844523182 scopus 로고    scopus 로고
    • The role of ARF1 and rab GTPases in polarization of the Golgi stack
    • Bannykh, S. I.; Plutner, H.; Matteson, J.; Balch, W. E. The role of ARF1 and rab GTPases in polarization of the Golgi stack. Traffic 2005, 6, 803-819.
    • (2005) Traffic , vol.6 , pp. 803-819
    • Bannykh, S.I.1    Plutner, H.2    Matteson, J.3    Balch, W.E.4
  • 69
    • 33644838123 scopus 로고    scopus 로고
    • An Arabidopsis GRIP domain protein locates to the trans-Golgi and binds the small GTPase ARL1
    • Latijnhouwers, M.; Hawes, C.; Carvalho, C.; Oparka, K.; Gillingham, A. K.; Boevink, P. An Arabidopsis GRIP domain protein locates to the trans-Golgi and binds the small GTPase ARL1. Plant J. 2005, 44, 459-470.
    • (2005) Plant J , vol.44 , pp. 459-470
    • Latijnhouwers, M.1    Hawes, C.2    Carvalho, C.3    Oparka, K.4    Gillingham, A.K.5    Boevink, P.6
  • 70
    • 0037938505 scopus 로고    scopus 로고
    • CtBP/BARS: A dual-function protein involved in transcription co-repression and Golgi membrane fission
    • Nardini, M.; Spano, S.; Cericola, C.; Pesce, A.; Massaro, A.; Millo, E.; Luini, A.; Corda, D.; Bolognesi, M. CtBP/BARS: a dual-function protein involved in transcription co-repression and Golgi membrane fission. EMBO J. 2003, 22, 3122-3130.
    • (2003) EMBO J , vol.22 , pp. 3122-3130
    • Nardini, M.1    Spano, S.2    Cericola, C.3    Pesce, A.4    Massaro, A.5    Millo, E.6    Luini, A.7    Corda, D.8    Bolognesi, M.9
  • 71
    • 0034865435 scopus 로고    scopus 로고
    • The CtBP family: Enigmatic and enzymatic transcriptional co-repressors
    • Turner, J.; Crossley, M. The CtBP family: enigmatic and enzymatic transcriptional co-repressors. BioEssays 2001, 23, 683-690.
    • (2001) BioEssays , vol.23 , pp. 683-690
    • Turner, J.1    Crossley, M.2
  • 73
    • 3042795657 scopus 로고    scopus 로고
    • Hidalgo, Carcedo, C.; Bonazzi, M.; Spano, S.; Turacchio, G.; Colanzi, A.; Luini, A.; Corda, D. Mitotic Golgi partitioning is driven by the membrane-fissioning protein CtBP3/BARS. Science 2004, 305, 93-96.
    • Hidalgo, Carcedo, C.; Bonazzi, M.; Spano, S.; Turacchio, G.; Colanzi, A.; Luini, A.; Corda, D. Mitotic Golgi partitioning is driven by the membrane-fissioning protein CtBP3/BARS. Science 2004, 305, 93-96.
  • 76
    • 33644835339 scopus 로고    scopus 로고
    • Catalano, D.; Licciulli, F.; Turi, A.; Grillo, G.; Saccone, C.; D'Elia, D. MitoRes: a resource of nuclear-encoded mitochondrial genes and their products in Metazoa. BMC Bioinf. 2006, 7, 36.
    • Catalano, D.; Licciulli, F.; Turi, A.; Grillo, G.; Saccone, C.; D'Elia, D. MitoRes: a resource of nuclear-encoded mitochondrial genes and their products in Metazoa. BMC Bioinf. 2006, 7, 36.
  • 77
    • 0345451013 scopus 로고    scopus 로고
    • Flagellar mitochondrial association of the male-specific Don Juan protein in Drosophila spermatozoa
    • Santel, A.; Blumer, N.; Kampfer, M.; Renkawitz-Pohl, R. Flagellar mitochondrial association of the male-specific Don Juan protein in Drosophila spermatozoa. J. Cell Sci. 1998, 111 ( Pt. 22), 3299-3309.
    • (1998) J. Cell Sci , vol.111 , Issue.PART. 22 , pp. 3299-3309
    • Santel, A.1    Blumer, N.2    Kampfer, M.3    Renkawitz-Pohl, R.4
  • 78
    • 0030741896 scopus 로고    scopus 로고
    • The Drosophila don juan (dj) gene encodes a novel sperm specific protein component characterized by an unusual domain of a repetitive amino acid motif
    • Santel, A.; Winhauer, T.; Blumer, N.; Renkawitz-Pohl, R. The Drosophila don juan (dj) gene encodes a novel sperm specific protein component characterized by an unusual domain of a repetitive amino acid motif. Mech. Dev. 1997, 64, 19-30.
    • (1997) Mech. Dev , vol.64 , pp. 19-30
    • Santel, A.1    Winhauer, T.2    Blumer, N.3    Renkawitz-Pohl, R.4
  • 80
    • 0025829436 scopus 로고
    • The three-dimensional structure of proteasomes from Thermoplasma acidophilum as determined by electron microscopy using random conical tilting
    • Hegerl, R.; Pfeifer, G.; Puhler, G.; Dahlmann, B.; Baumeister, W. The three-dimensional structure of proteasomes from Thermoplasma acidophilum as determined by electron microscopy using random conical tilting. FEBS Lett. 1991, 283, 117-121.
    • (1991) FEBS Lett , vol.283 , pp. 117-121
    • Hegerl, R.1    Pfeifer, G.2    Puhler, G.3    Dahlmann, B.4    Baumeister, W.5
  • 82
    • 12844281837 scopus 로고    scopus 로고
    • The proteasome
    • discussion 33
    • Dalton, W. S. The proteasome. Semin. Oncol. 2004, 31, 3-9; discussion 33.
    • (2004) Semin. Oncol , vol.31 , pp. 3-9
    • Dalton, W.S.1
  • 83
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • Prakash, S.; Tian, L.; Ratliff, K. S.; Lehotzky, R. E.; Matouschek, A. An unstructured initiation site is required for efficient proteasome-mediated degradation. Nat. Struct. Mol Biol. 2004, 11, 830-837.
    • (2004) Nat. Struct. Mol Biol , vol.11 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 84
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P.; Johnson, A. E. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol 1994, 10, 87-119.
    • (1994) Annu. Rev. Cell Biol , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 85
    • 0032728066 scopus 로고    scopus 로고
    • Posttranslational protein translocation across the membrane of the endoplasmic reticulum
    • Rapoport, T. A.; Matlack, K. E.; Plath, K.; Misselwitz, B.; Staeck, O. Posttranslational protein translocation across the membrane of the endoplasmic reticulum. Biol. Chem. 1999, 380, 1143-1150.
    • (1999) Biol. Chem , vol.380 , pp. 1143-1150
    • Rapoport, T.A.1    Matlack, K.E.2    Plath, K.3    Misselwitz, B.4    Staeck, O.5
  • 86
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T. A.; Jungnickel, B.; Kutay, U. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 1996, 65, 271-303.
    • (1996) Annu. Rev. Biochem , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 87
  • 89
    • 0037310079 scopus 로고    scopus 로고
    • S-domain assembly of the signal recognition particle
    • Sauer-Eriksson, A. E.; Hainzl, T. S-domain assembly of the signal recognition particle. Curr. Opin. Struct. Biol. 2003, 13, 64-70.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 64-70
    • Sauer-Eriksson, A.E.1    Hainzl, T.2
  • 90
    • 0036290864 scopus 로고    scopus 로고
    • Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle
    • Pakhomova, O. N.; Deep, S.; Huang, Q.; Zwieb, C.; Hinck, A. P. Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle. J. Mol. Biol. 2002, 317, 145-158.
    • (2002) J. Mol. Biol , vol.317 , pp. 145-158
    • Pakhomova, O.N.1    Deep, S.2    Huang, Q.3    Zwieb, C.4    Hinck, A.P.5
  • 91
    • 0035852345 scopus 로고    scopus 로고
    • Function of a chloroplast SRP in thylakoid protein export
    • Eichacker, L. A.; Henry, R. Function of a chloroplast SRP in thylakoid protein export. Biochim. Biophys. Acta 2001, 1541, 120-134.
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 120-134
    • Eichacker, L.A.1    Henry, R.2
  • 92
    • 0035816712 scopus 로고    scopus 로고
    • Functional analysis of the protein-interacting domains of chloroplast SRP43
    • Jonas-Straube, E.; Hutin, C.; Hoffman, N. E.; Schunemann, D. Functional analysis of the protein-interacting domains of chloroplast SRP43. J. Biol. Chem. 2001, 276, 24654-24660.
    • (2001) J. Biol. Chem , vol.276 , pp. 24654-24660
    • Jonas-Straube, E.1    Hutin, C.2    Hoffman, N.E.3    Schunemann, D.4
  • 93
    • 5644297077 scopus 로고    scopus 로고
    • Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43
    • Goforth, R. L.; Peterson, E. C.; Yuan, J.; Moore, M. J.; Kight, A. D.; Lohse, M. B.; Sakon, J.; Henry, R. L. Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43. J. Biol. Chem. 2004, 279, 43077-43084.
    • (2004) J. Biol. Chem , vol.279 , pp. 43077-43084
    • Goforth, R.L.1    Peterson, E.C.2    Yuan, J.3    Moore, M.J.4    Kight, A.D.5    Lohse, M.B.6    Sakon, J.7    Henry, R.L.8
  • 95
    • 0027010551 scopus 로고
    • Functional domains of neuromodulin (GAP-43)
    • Apel, E. D.; Storm, D. R. Functional domains of neuromodulin (GAP-43). Perspect. Dev. Neurobiol 1992, 1, 3-11.
    • (1992) Perspect. Dev. Neurobiol , vol.1 , pp. 3-11
    • Apel, E.D.1    Storm, D.R.2
  • 96
    • 0030615067 scopus 로고    scopus 로고
    • Circular dichroism and 1H nuclear magnetic resonance studies on the solution and membrane structures of GAP-43 calmodulin-binding domain
    • Hayashi, N.; Matsubara, M.; Titani, K.; Taniguchi, H. Circular dichroism and 1H nuclear magnetic resonance studies on the solution and membrane structures of GAP-43 calmodulin-binding domain. J. Biol. Chem. 1997, 272, 7639-7645.
    • (1997) J. Biol. Chem , vol.272 , pp. 7639-7645
    • Hayashi, N.1    Matsubara, M.2    Titani, K.3    Taniguchi, H.4
  • 98
    • 0023049694 scopus 로고
    • Complete amino acid sequence of cyanobacterial gas-vesicle protein indicates a 70-residue molecule that corresponds in size to the crystallographic unit cell
    • Hayes, P. K.; Walsby, A. E.; Walker, J. E. Complete amino acid sequence of cyanobacterial gas-vesicle protein indicates a 70-residue molecule that corresponds in size to the crystallographic unit cell. Biochem. J. 1986, 236, 31-36.
    • (1986) Biochem. J , vol.236 , pp. 31-36
    • Hayes, P.K.1    Walsby, A.E.2    Walker, J.E.3
  • 99
    • 0026542940 scopus 로고
    • Gas vesicles are strengthened by the outer-surface protein, GvpC
    • Hayes, P. K.; Buchholz, B.; Walsby, A. E. Gas vesicles are strengthened by the outer-surface protein, GvpC.Arch. Microbiol. 1992, 157, 229-234.
    • (1992) Arch. Microbiol , vol.157 , pp. 229-234
    • Hayes, P.K.1    Buchholz, B.2    Walsby, A.E.3
  • 100
    • 0024802898 scopus 로고
    • Gas vesicle proteins
    • Walsby, A. E.; Hayes, P. K. Gas vesicle proteins. Biochem. J. 1989, 264, 313-322.
    • (1989) Biochem. J , vol.264 , pp. 313-322
    • Walsby, A.E.1    Hayes, P.K.2
  • 101
    • 0028261412 scopus 로고
    • Gas vesicles
    • Walsby, A. E. Gas vesicles. Microbiol. Rev. 1994, 58, 94-144.
    • (1994) Microbiol. Rev , vol.58 , pp. 94-144
    • Walsby, A.E.1
  • 102
    • 0346057921 scopus 로고    scopus 로고
    • Subunit structure of gas vesicles: A MALDI-TOF mass spectrometry study
    • Belenky, M.; Meyers, R.; Herzfeld, J. Subunit structure of gas vesicles: a MALDI-TOF mass spectrometry study. Biophys. J. 2004, 86, 499-505.
    • (2004) Biophys. J , vol.86 , pp. 499-505
    • Belenky, M.1    Meyers, R.2    Herzfeld, J.3
  • 103
    • 0024086944 scopus 로고
    • The protein encoded by gvpC is a minor component of gas vesicles isolated from the cyanobacteria Anabaena flos-aquae and Microcystis sp
    • Hayes, P. K.; Lazarus, C.M.; Bees, A.; Walker, J. E.; Walsby, A. E. The protein encoded by gvpC is a minor component of gas vesicles isolated from the cyanobacteria Anabaena flos-aquae and Microcystis sp. Mol. Microbiol 1988, 2, 545-552.
    • (1988) Mol. Microbiol , vol.2 , pp. 545-552
    • Hayes, P.K.1    Lazarus, C.M.2    Bees, A.3    Walker, J.E.4    Walsby, A.E.5
  • 104
    • 0037275640 scopus 로고    scopus 로고
    • Keratins: A structural scaffold with emerging functions
    • Kirfel, J.; Magin, T. M.; Reichelt, J. Keratins: a structural scaffold with emerging functions. Cell. Mol. Life Sci. 2003, 60, 56-71.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 56-71
    • Kirfel, J.1    Magin, T.M.2    Reichelt, J.3
  • 105
    • 0000013308 scopus 로고
    • The structure of hair, muscle, and related proteins
    • Pauling, L.; Corey, R. B. The structure of hair, muscle, and related proteins. Proc. Natl. Acad. Sci. USA. 1951, 37, 261-271.
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 261-271
    • Pauling, L.1    Corey, R.B.2
  • 106
    • 0032991453 scopus 로고    scopus 로고
    • Micromechanics of the equine hoof wall: Optimizing crack control and material stiffness through modulation of the properties of keratin
    • Kasapi, M. A.; Gosline, J. M. Micromechanics of the equine hoof wall: optimizing crack control and material stiffness through modulation of the properties of keratin. J. Exp. Biol. 1999, 202, 377-391.
    • (1999) J. Exp. Biol , vol.202 , pp. 377-391
    • Kasapi, M.A.1    Gosline, J.M.2
  • 107
    • 0002732819 scopus 로고
    • Compound helical configurations of polypeptide chains: Structure of proteins of the alpha-keratin type
    • Pauling, L.; Corey, R. B. Compound helical configurations of polypeptide chains: structure of proteins of the alpha-keratin type. Nature 1953, 171, 59-61.
    • (1953) Nature , vol.171 , pp. 59-61
    • Pauling, L.1    Corey, R.B.2
  • 108
    • 0036262077 scopus 로고    scopus 로고
    • Dynamic light scattering and circular dichroism studies on heat-induced gelation of hard-keratin protein aqueous solutions
    • Ikkai, F.; Naito, S. Dynamic light scattering and circular dichroism studies on heat-induced gelation of hard-keratin protein aqueous solutions. Biomacromolecules 2002, 3, 482-487.
    • (2002) Biomacromolecules , vol.3 , pp. 482-487
    • Ikkai, F.1    Naito, S.2
  • 109
    • 24944460598 scopus 로고    scopus 로고
    • Shelterin: The protein complex that shapes and safeguards human telomeres
    • de Lange, T. Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev. 2005, 19, 2100-2110.
    • (2005) Genes Dev , vol.19 , pp. 2100-2110
    • de Lange, T.1
  • 111
    • 1642473879 scopus 로고    scopus 로고
    • Structure and function of the chloroplast signal recognition particle
    • Schunemann, D. Structure and function of the chloroplast signal recognition particle. Curr. Genet. 2004, 44, 295-304.
    • (2004) Curr. Genet , vol.44 , pp. 295-304
    • Schunemann, D.1
  • 112
    • 0347379787 scopus 로고    scopus 로고
    • Role of mucins in the function of the corneal and conjunctival epithelia
    • Gipson, I. K.; Argueso, P. Role of mucins in the function of the corneal and conjunctival epithelia. Int. Rev. Cytol. 2003, 231, 1-49.
    • (2003) Int. Rev. Cytol , vol.231 , pp. 1-49
    • Gipson, I.K.1    Argueso, P.2
  • 113
    • 0021665612 scopus 로고
    • Macromolecular properties and polymeric structure of mucus glycoproteins
    • Carlstedt, I.; Sheehan, J. K. Macromolecular properties and polymeric structure of mucus glycoproteins. Ciba Found. Symp. 1984, 109, 157-172.
    • (1984) Ciba Found. Symp , vol.109 , pp. 157-172
    • Carlstedt, I.1    Sheehan, J.K.2
  • 115
    • 33750630164 scopus 로고    scopus 로고
    • Tight junctions and cell-cell interactions
    • Utech, M.; Bruwer, M.; Nusrat, A. Tight junctions and cell-cell interactions. Methods Mol. Biol. 2006, 341, 185-195.
    • (2006) Methods Mol. Biol , vol.341 , pp. 185-195
    • Utech, M.1    Bruwer, M.2    Nusrat, A.3
  • 117
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara, A.; Furuse, M.; Saitou, M.; Ando-Akatsuka, Y.; Tsukita, S. Possible involvement of phosphorylation of occludin in tight junction formation. J. Cell Biol. 1997, 137, 1393-1401.
    • (1997) J. Cell Biol , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 118
    • 16344378229 scopus 로고    scopus 로고
    • Multiple protein interactions involving proposed extracellular loop domains of the tight junction protein occludin
    • Nusrat, A.; Brown, G. T.; Tom, J.; Drake, A.; Bui, T. T.; Quan, C.; Mrsny, R. J. Multiple protein interactions involving proposed extracellular loop domains of the tight junction protein occludin. Mol. Biol. Cell 2005, 16, 1725-1734.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1725-1734
    • Nusrat, A.1    Brown, G.T.2    Tom, J.3    Drake, A.4    Bui, T.T.5    Quan, C.6    Mrsny, R.J.7
  • 119
    • 0032533711 scopus 로고    scopus 로고
    • Biochemistry of tropoelastin
    • Vrhovski, B.; Weiss, A. S. Biochemistry of tropoelastin. Eur. J. Biochem. 1998, 258, 1-18.
    • (1998) Eur. J. Biochem , vol.258 , pp. 1-18
    • Vrhovski, B.1    Weiss, A.S.2
  • 120
    • 18144374871 scopus 로고    scopus 로고
    • The hydrophobic domain 26 of human tropoelastin is unstructured in solution
    • Mackay, J. P.; Muiznieks, L. D.; Toonkool, P.; Weiss, A. S. The hydrophobic domain 26 of human tropoelastin is unstructured in solution. J. Struct. Biol. 2005, 150, 154-162.
    • (2005) J. Struct. Biol , vol.150 , pp. 154-162
    • Mackay, J.P.1    Muiznieks, L.D.2    Toonkool, P.3    Weiss, A.S.4
  • 122
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J.; Sodhi, J. S.; McGuffin, L. J.; Buxton, B. F.; Jones, D. T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol 2004, 337, 635-645.
    • (2004) J. Mol. Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 123
    • 0344721480 scopus 로고    scopus 로고
    • Consortium, M. S. Complete sequence and gene map of a human major histocompatibility complex. The MHC sequencing consortium. Nature 1999, 401, 921-923.
    • Consortium, M. S. Complete sequence and gene map of a human major histocompatibility complex. The MHC sequencing consortium. Nature 1999, 401, 921-923.
  • 124
    • 0025155682 scopus 로고
    • Cellular peptide composition governed by major histocompatibility complex class I molecules
    • Falk, K.; Rotzschke, O.; Rammensee, H. G. Cellular peptide composition governed by major histocompatibility complex class I molecules. Nature 1990, 348, 248-251.
    • (1990) Nature , vol.348 , pp. 248-251
    • Falk, K.1    Rotzschke, O.2    Rammensee, H.G.3
  • 127
  • 128
    • 0035479436 scopus 로고    scopus 로고
    • Examination of possible structural constraints of MHC-binding peptides by assessment of their native structure within their source proteins
    • Schueler-Furman, O.; Altuvia, Y.; Margalit, H. Examination of possible structural constraints of MHC-binding peptides by assessment of their native structure within their source proteins. Proteins 2001, 45, 47-54.
    • (2001) Proteins , vol.45 , pp. 47-54
    • Schueler-Furman, O.1    Altuvia, Y.2    Margalit, H.3
  • 129
    • 0024782191 scopus 로고
    • Structure and functions of the periplasmic space
    • Markiewicz, Z. Structure and functions of the periplasmic space. Acta Microbiol. Pol. 1989, 38, 199-206.
    • (1989) Acta Microbiol. Pol , vol.38 , pp. 199-206
    • Markiewicz, Z.1
  • 130
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V.; Turk, B.; Turk, D. Lysosomal cysteine proteases: facts and opportunities. EMBO J. 2001, 20, 4629-4633.
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 131
    • 0242351787 scopus 로고    scopus 로고
    • Genetic content and evolution of adenoviruses
    • Davison, A. J.; Benko, M.; Harrach, B. Genetic content and evolution of adenoviruses. J. Gen. Virol. 2003, 84, 2895-2908.
    • (2003) J. Gen. Virol , vol.84 , pp. 2895-2908
    • Davison, A.J.1    Benko, M.2    Harrach, B.3
  • 133
    • 0033661024 scopus 로고    scopus 로고
    • Type-specific epitope locations revealed by X-ray crystallographic study of adenovirus type 5 hexon
    • Rux, J. J.; Burnett, R. M. Type-specific epitope locations revealed by X-ray crystallographic study of adenovirus type 5 hexon. Mol. Ther. 2000, 1, 18-30.
    • (2000) Mol. Ther , vol.1 , pp. 18-30
    • Rux, J.J.1    Burnett, R.M.2
  • 134
    • 0028151167 scopus 로고
    • The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 A resolution
    • Athappilly, F. K.; Murali, R.; Rux, J. J.; Cai, Z.; Burnett, R. M. The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 A resolution. J. Mol. Biol. 1994, 242, 430-455.
    • (1994) J. Mol. Biol , vol.242 , pp. 430-455
    • Athappilly, F.K.1    Murali, R.2    Rux, J.J.3    Cai, Z.4    Burnett, R.M.5
  • 135
    • 0023721293 scopus 로고
    • The physiology and biochemistry of pili
    • Paranchych, W.; Frost, L. S. The physiology and biochemistry of pili. Adv. Microb. Physiol. 1988, 29, 53-114.
    • (1988) Adv. Microb. Physiol , vol.29 , pp. 53-114
    • Paranchych, W.1    Frost, L.S.2
  • 137
    • 0023183146 scopus 로고
    • Localization of the receptor-binding protein adhesin at the tip of the bacterial pilus
    • Lindberg, F.; Lund, B.; Johansson, L.; Normark, S. Localization of the receptor-binding protein adhesin at the tip of the bacterial pilus. Nature 1987, 328, 84-87.
    • (1987) Nature , vol.328 , pp. 84-87
    • Lindberg, F.1    Lund, B.2    Johansson, L.3    Normark, S.4
  • 138
    • 0033022996 scopus 로고    scopus 로고
    • Structure, assembly and regulation of expression of capsules in Escherichia coli
    • Whitfield, C.; Roberts, I. S. Structure, assembly and regulation of expression of capsules in Escherichia coli. Mol. Microbiol 1999, 31, 1307-1319.
    • (1999) Mol. Microbiol , vol.31 , pp. 1307-1319
    • Whitfield, C.1    Roberts, I.S.2
  • 139
    • 0033017192 scopus 로고    scopus 로고
    • Gene products required for surface expression of the capsular form of the group 1 K antigen in Escherichia coli (O9a:K30)
    • Drummelsmith, J.; Whitfield, C.Gene products required for surface expression of the capsular form of the group 1 K antigen in Escherichia coli (O9a:K30). Mol. Microbiol. 1999, 31, 1321-1332.
    • (1999) Mol. Microbiol , vol.31 , pp. 1321-1332
    • Drummelsmith, J.1    Whitfield, C.2
  • 140
    • 0029766843 scopus 로고    scopus 로고
    • Coating the surface: A model for expression of capsular polysialic acid in Escherichia coli K1
    • Bliss, J. M.; Silver, R. P. Coating the surface: a model for expression of capsular polysialic acid in Escherichia coli K1. Mol. Microbiol. 1996, 21, 221-231.
    • (1996) Mol. Microbiol , vol.21 , pp. 221-231
    • Bliss, J.M.1    Silver, R.P.2
  • 141
    • 0032511192 scopus 로고    scopus 로고
    • Macromolecular assembly and secretion across the bacterial cell envelope: Type II protein secretion systems
    • Russel, M. Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems. J. Mol. Biol. 1998, 279, 485-499.
    • (1998) J. Mol. Biol , vol.279 , pp. 485-499
    • Russel, M.1
  • 143
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders, R. J.; Waterham, H. R. Biochemistry of mammalian peroxisomes revisited. Annu. Rev. Biochem. 2006, 75, 295-332.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 295-332
    • Wanders, R.J.1    Waterham, H.R.2
  • 145
    • 0000691153 scopus 로고
    • A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions
    • Boyer, P. D.; Cross, R. L.; Momsen, W. A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions. Proc. Natl Acad. Sci. U.SA. 1973, 70, 2837-2839.
    • (1973) Proc. Natl Acad. Sci. U.SA , vol.70 , pp. 2837-2839
    • Boyer, P.D.1    Cross, R.L.2    Momsen, W.3
  • 146
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase-some probabilities and possibilities
    • Boyer, P. D. The binding change mechanism for ATP synthase-some probabilities and possibilities. Biochim. Biophys. Acta 1993, 1140, 215-250.
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 147
    • 0037110557 scopus 로고    scopus 로고
    • Rebuilt 3D structure of the chloroplast f1 ATPase-tentoxin complex
    • Minoletti, C.; Santolini, J.; Haraux, F.; Pothier, J.; Andre, F. Rebuilt 3D structure of the chloroplast f1 ATPase-tentoxin complex. Proteins 2002, 49, 302-320.
    • (2002) Proteins , vol.49 , pp. 302-320
    • Minoletti, C.1    Santolini, J.2    Haraux, F.3    Pothier, J.4    Andre, F.5
  • 148
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J. P.; Leslie, A. G.; Lutter, R.; Walker, J. E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 1994, 370, 621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 149
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer, J.; Epp, O.; Miki, K.; Huber, R.; Michel, H. X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 1984, 180, 385-398.
    • (1984) J. Mol. Biol , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 150
    • 20444393150 scopus 로고    scopus 로고
    • Proteins, chlorophylls and lipids: X-ray analysis of a three-way relationship
    • Fyfe, P. K.; Hughes, A. V.; Heathcote, P.; Jones, M. R. Proteins, chlorophylls and lipids: X-ray analysis of a three-way relationship. Trends Plant Sci. 2005, 10, 275-282.
    • (2005) Trends Plant Sci , vol.10 , pp. 275-282
    • Fyfe, P.K.1    Hughes, A.V.2    Heathcote, P.3    Jones, M.R.4
  • 151
    • 18844405410 scopus 로고    scopus 로고
    • Structure of cyanobacterial photo-system I
    • Grotjohann, I.; Fromme, P. Structure of cyanobacterial photo-system I. Photosynth. Res. 2005, 85, 51-72.
    • (2005) Photosynth. Res , vol.85 , pp. 51-72
    • Grotjohann, I.1    Fromme, P.2
  • 152
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan, P.; Fromme, P.; Witt, H. T.; Klukas, O.; Saenger, W.; Krauss, N. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 2001, 411, 909-917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 155
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • Burkhard, P.; Stetefeld, J.; Strelkov, S. V. Coiled coils: a highly versatile protein folding motif. Trends Cell Biol 2001, 11, 82-88.
    • (2001) Trends Cell Biol , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 156
    • 17444424974 scopus 로고    scopus 로고
    • The structure of alpha-helical coiled coils
    • Lupas, A. N.; Gruber, M. The structure of alpha-helical coiled coils. Adv. Protein Chem. 2005, 70, 37-78.
    • (2005) Adv. Protein Chem , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 157
    • 0000920828 scopus 로고
    • The packing of alpha-helices: Simple coiled-coils
    • Crick, F. H. The packing of alpha-helices: simple coiled-coils. Acta Crystallogr. 1953, 6, 689-697.
    • (1953) Acta Crystallogr , vol.6 , pp. 689-697
    • Crick, F.H.1
  • 158
    • 0344552313 scopus 로고    scopus 로고
    • Extended knobs-into-holes packing in classical and complex coiled-coil assemblies
    • Walshaw, J.; Woolfson, D. N. Extended knobs-into-holes packing in classical and complex coiled-coil assemblies. J. Struct. Biol. 2003, 144, 349-361.
    • (2003) J. Struct. Biol , vol.144 , pp. 349-361
    • Walshaw, J.1    Woolfson, D.N.2
  • 159
    • 4344685822 scopus 로고    scopus 로고
    • Scaffolds, levers, rods and springs: Diverse cellular functions of long coiled-coil proteins
    • Rose, A.; Meier, I. Scaffolds, levers, rods and springs: diverse cellular functions of long coiled-coil proteins. Cell. Mol. Life Sci. 2004, 61, 1996-2009.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 1996-2009
    • Rose, A.1    Meier, I.2
  • 161
    • 33644795360 scopus 로고    scopus 로고
    • Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin
    • Singh, A.; Hitchcock-DeGregori, S. E. Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin. Structure 2006, 14, 43-50.
    • (2006) Structure , vol.14 , pp. 43-50
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 163
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: From the cytoskeleton to the nucleus
    • Kadrmas, J. L.; Beckerle, M. C.The LIM domain: from the cytoskeleton to the nucleus. Nat. Rev. Mol. Cell Biol. 2004, 5, 920-931.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 164
    • 0035834765 scopus 로고    scopus 로고
    • Conformational heterogeneity in the C-terminal zinc fingers of human MTF-1: An NMR and zinc-binding study
    • Giedroc, D. P.; Chen, X.; Pennella, M. A.; LiWang, A. C. Conformational heterogeneity in the C-terminal zinc fingers of human MTF-1: an NMR and zinc-binding study. J. Biol. Chem. 2001, 276, 42322-42332.
    • (2001) J. Biol. Chem , vol.276 , pp. 42322-42332
    • Giedroc, D.P.1    Chen, X.2    Pennella, M.A.3    LiWang, A.C.4
  • 165
    • 0034004352 scopus 로고    scopus 로고
    • The LIM domain: Regulation by association
    • Bach, I. The LIM domain: regulation by association. Mech. Dev. 2000, 91, 5-17.
    • (2000) Mech. Dev , vol.91 , pp. 5-17
    • Bach, I.1
  • 166
    • 0042819915 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins evolve by repeat expansion
    • Tompa, P. Intrinsically unstructured proteins evolve by repeat expansion. BioEssays 2003, 25, 847-855.
    • (2003) BioEssays , vol.25 , pp. 847-855
    • Tompa, P.1
  • 167
    • 0141677840 scopus 로고    scopus 로고
    • A protein-chameleon: Conformational plasticity of alpha-synuclein, a disordered protein involved in neurode-generative disorders
    • Uversky, V. N. A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurode-generative disorders. J. Biomol Struct. Dyn. 2003, 21, 211-234.
    • (2003) J. Biomol Struct. Dyn , vol.21 , pp. 211-234
    • Uversky, V.N.1
  • 168
    • 0034308219 scopus 로고    scopus 로고
    • Chloroplast transit peptides: Structure, function and evolution
    • Bruce, B. D. Chloroplast transit peptides: structure, function and evolution. Trends Cell Biol. 2000, 10, 440-447.
    • (2000) Trends Cell Biol , vol.10 , pp. 440-447
    • Bruce, B.D.1
  • 169
    • 0032169930 scopus 로고    scopus 로고
    • The role of lipids in plastid protein transport
    • Bruce, B. D. The role of lipids in plastid protein transport. Plant Mol. Biol. 1998, 38, 223-246.
    • (1998) Plant Mol. Biol , vol.38 , pp. 223-246
    • Bruce, B.D.1
  • 170
    • 0032784582 scopus 로고    scopus 로고
    • The structural flexibility of the preferredoxin transit peptide
    • Wienk, H. L.; Czisch, M.; de Kruijff, B. The structural flexibility of the preferredoxin transit peptide. FEBS Lett. 1999, 453, 318-326.
    • (1999) FEBS Lett , vol.453 , pp. 318-326
    • Wienk, H.L.1    Czisch, M.2    de Kruijff, B.3
  • 171
    • 0033215007 scopus 로고    scopus 로고
    • A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii
    • Krimm, I.; Gans, P.; Hernandez, J. F.; Arlaud, G. J.; Lancelin, J. M. A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii. Eur. J. Biochem. 1999, 265, 171-180.
    • (1999) Eur. J. Biochem , vol.265 , pp. 171-180
    • Krimm, I.1    Gans, P.2    Hernandez, J.F.3    Arlaud, G.J.4    Lancelin, J.M.5
  • 172
    • 0026097503 scopus 로고
    • Chloroplast transit peptides. The perfect random coil?
    • von Heijne, G.; Nishikawa, K. Chloroplast transit peptides. The perfect random coil? FEBS Lett. 1991, 278, 1-3.
    • (1991) FEBS Lett , vol.278 , pp. 1-3
    • von Heijne, G.1    Nishikawa, K.2
  • 173
    • 0037459341 scopus 로고    scopus 로고
    • C.Variation on an Src-like theme
    • Harrison, S. C.Variation on an Src-like theme. Cell 2003, 112, 737-740.
    • (2003) Cell , vol.112 , pp. 737-740
    • Harrison, S.1
  • 174
    • 0037169351 scopus 로고    scopus 로고
    • Autoinhibition of c-Abl
    • Pluk, H.; Dorey, K.; Superti-Furga, G. Autoinhibition of c-Abl. Cell 2002, 108, 247-259.
    • (2002) Cell , vol.108 , pp. 247-259
    • Pluk, H.1    Dorey, K.2    Superti-Furga, G.3
  • 177
    • 20344400382 scopus 로고    scopus 로고
    • The structure of "unstructured" regions in peptides and proteins: Role of the polyproline II helix in protein folding and recognition
    • Rath, A.; Davidson, A. R.; Deber, C.M. The structure of "unstructured" regions in peptides and proteins: role of the polyproline II helix in protein folding and recognition. Biopolymers 2005, 80, 179-185.
    • (2005) Biopolymers , vol.80 , pp. 179-185
    • Rath, A.1    Davidson, A.R.2    Deber, C.M.3
  • 178
    • 0028101487 scopus 로고
    • The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase
    • Nilsson, I.; Whitley, P.; von Heijne, G. The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J. Cell Biol 1994, 126, 1127-1132.
    • (1994) J. Cell Biol , vol.126 , pp. 1127-1132
    • Nilsson, I.1    Whitley, P.2    von Heijne, G.3
  • 179
    • 33644855546 scopus 로고    scopus 로고
    • Function of positive charges following signal-anchor sequences during translocation of the N-terminal domain
    • Kida, Y.; Morimoto, F.; Mihara, K.; Sakaguchi, M. Function of positive charges following signal-anchor sequences during translocation of the N-terminal domain. J. Biol. Chem. 2006, 281, 1152-1158.
    • (2006) J. Biol. Chem , vol.281 , pp. 1152-1158
    • Kida, Y.1    Morimoto, F.2    Mihara, K.3    Sakaguchi, M.4
  • 180
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins
    • Koch, C.A.; Anderson, D.; Moran, M. F.; Ellis, C.; Pawson, T. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 1991, 252, 668-674.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 181
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • Pawson, T.; Gish, G. D.; Nash, P. SH2 domains, interaction modules and cellular wiring. Trends Cell Biol. 2001, 11, 504-511.
    • (2001) Trends Cell Biol , vol.11 , pp. 504-511
    • Pawson, T.1    Gish, G.D.2    Nash, P.3
  • 182
    • 12844283323 scopus 로고    scopus 로고
    • The SH2 domain: Versatile signaling module and pharmaceutical target
    • Machida, K.; Mayer, B. J. The SH2 domain: versatile signaling module and pharmaceutical target. Biochim. Biophys. Acta 2005, 1747, 1-25.
    • (2005) Biochim. Biophys. Acta , vol.1747 , pp. 1-25
    • Machida, K.1    Mayer, B.J.2
  • 183
    • 0027533927 scopus 로고
    • Chromosomal localization of seven PAX genes and cloning of a novel family member, PAX-9
    • Stapleton, P.; Weith, A.; Urbanek, P.; Kozmik, Z.; Busslinger, M. Chromosomal localization of seven PAX genes and cloning of a novel family member, PAX-9. Nat. Genet. 1993, 3, 292-298.
    • (1993) Nat. Genet , vol.3 , pp. 292-298
    • Stapleton, P.1    Weith, A.2    Urbanek, P.3    Kozmik, Z.4    Busslinger, M.5
  • 184
    • 0026734111 scopus 로고    scopus 로고
    • Gruss, P.; Walther, C. Pax in development. Cell 1992, 69, 719-722.
    • Gruss, P.; Walther, C. Pax in development. Cell 1992, 69, 719-722.
  • 186
    • 0028239775 scopus 로고
    • Identification of a Pax paired domain recognition sequence and evidence for DNA-dependent conformational changes
    • Epstein, J.; Cai, J.; Glaser, T.; Jepeal, L.; Maas, R. Identification of a Pax paired domain recognition sequence and evidence for DNA-dependent conformational changes. J. Biol. Chem. 1994, 269, 8355-8361.
    • (1994) J. Biol. Chem , vol.269 , pp. 8355-8361
    • Epstein, J.1    Cai, J.2    Glaser, T.3    Jepeal, L.4    Maas, R.5
  • 187
    • 0021894435 scopus 로고
    • The classical complement pathway: Activation and regulation of the first complement component
    • Cooper, N. R. The classical complement pathway: activation and regulation of the first complement component. Adv. Immunol. 1985, 37, 151-216.
    • (1985) Adv. Immunol , vol.37 , pp. 151-216
    • Cooper, N.R.1
  • 189
    • 0032477892 scopus 로고    scopus 로고
    • Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family
    • Bersch, B.; Hernandez, J. F.; Marion, D.; Arlaud, G. J. Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family. Biochemistry 1998, 37, 1204-1214.
    • (1998) Biochemistry , vol.37 , pp. 1204-1214
    • Bersch, B.1    Hernandez, J.F.2    Marion, D.3    Arlaud, G.J.4
  • 190
    • 0025939859 scopus 로고
    • Complexities of the protein kinase C pathway
    • Blumberg, P. M. Complexities of the protein kinase C pathway. Mol. Carcinog. 1991, 4, 339-344.
    • (1991) Mol. Carcinog , vol.4 , pp. 339-344
    • Blumberg, P.M.1
  • 191
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka, Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 1995, 9, 484-496.
    • (1995) FASEB J , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 192
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton, A. C. Protein kinase C: structure, function, and regulation. J. Biol. Chem. 1995, 270, 28495-28498.
    • (1995) J. Biol. Chem , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 193
    • 0021111512 scopus 로고
    • Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease
    • Kishimoto, A.; Kajikawa, N.; Shiota, M.; Nishizuka, Y. Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease. J. Biol Chem. 1983, 258, 1156-1164.
    • (1983) J. Biol Chem , vol.258 , pp. 1156-1164
    • Kishimoto, A.1    Kajikawa, N.2    Shiota, M.3    Nishizuka, Y.4
  • 194
    • 0028959121 scopus 로고
    • Identification, activity, and structural studies of peptides incorporating the phorbol esterbinding domain of protein kinase C
    • Wender, P. A.; Irie, K.; Miller, B. L. Identification, activity, and structural studies of peptides incorporating the phorbol esterbinding domain of protein kinase C.Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 239-243.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 239-243
    • Wender, P.A.1    Irie, K.2    Miller, B.L.3
  • 196
    • 0030870312 scopus 로고    scopus 로고
    • NMR studies of a viral protein that mimics the regulators of complement activation
    • Wiles, A. P.; Shaw, G.; Bright, J.; Perczel, A.; Campbell, I. D.; Barlow, P. N. NMR studies of a viral protein that mimics the regulators of complement activation. J. Mol. Biol. 1997, 272, 253-265.
    • (1997) J. Mol. Biol , vol.272 , pp. 253-265
    • Wiles, A.P.1    Shaw, G.2    Bright, J.3    Perczel, A.4    Campbell, I.D.5    Barlow, P.N.6
  • 197
    • 0035008505 scopus 로고    scopus 로고
    • Structure and flexibility of the multiple domain proteins that regulate complement activation
    • Kirkitadze, M. D.; Barlow, P. N. Structure and flexibility of the multiple domain proteins that regulate complement activation. Immunol. Rev. 2001, 180, 146-161.
    • (2001) Immunol. Rev , vol.180 , pp. 146-161
    • Kirkitadze, M.D.1    Barlow, P.N.2
  • 198
    • 33646580769 scopus 로고    scopus 로고
    • The structure of the interleukin-15 alpha receptor and its implications for ligand binding
    • Lorenzen, I.; Dingley, A. J.; Jacques, Y.; Grotzinger, J. The structure of the interleukin-15 alpha receptor and its implications for ligand binding. J. Biol. Chem. 2006, 281, 6642-6647.
    • (2006) J. Biol. Chem , vol.281 , pp. 6642-6647
    • Lorenzen, I.1    Dingley, A.J.2    Jacques, Y.3    Grotzinger, J.4
  • 199
    • 0031138034 scopus 로고    scopus 로고
    • Jeanmougin, F.; Wurtz, J. M.; Le, Douarin, B.; Chambon, P.; Losson, R. The bromodomain revisited. Trends Biochem. Sci. 1997, 22, 151-153.
    • Jeanmougin, F.; Wurtz, J. M.; Le, Douarin, B.; Chambon, P.; Losson, R. The bromodomain revisited. Trends Biochem. Sci. 1997, 22, 151-153.
  • 200
    • 0037138363 scopus 로고    scopus 로고
    • Zeng, L.; Zhou, M. M. Bromodomain: an acetyl-lysine binding domain. FEBS Lett. 2 002, 513, 124-128.
    • Zeng, L.; Zhou, M. M. Bromodomain: an acetyl-lysine binding domain. FEBS Lett. 2 002, 513, 124-128.
  • 201
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin, C.; Carlson, J. E.; Zeng, L; He, C.; Aggarwal, A. K.; Zhou, M. M. Structure and ligand of a histone acetyltransferase bromodomain. Nature 1999, 399, 491-496.
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.E.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5    Zhou, M.M.6
  • 202
    • 0021772396 scopus 로고
    • Residues Cys-1 and Cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogen
    • Trexler, M.; Patthy, L. Residues Cys-1 and Cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogen. Biochim. Biophys. Acta 1984, 787, 275-280.
    • (1984) Biochim. Biophys. Acta , vol.787 , pp. 275-280
    • Trexler, M.1    Patthy, L.2
  • 204
    • 0036132540 scopus 로고    scopus 로고
    • Structure and function of pore-forming beta-barrels from bacteria
    • Delcour, A. H. Structure and function of pore-forming beta-barrels from bacteria. J. Mol. Microbiol. Biotechnol. 2002, 4, 1-10.
    • (2002) J. Mol. Microbiol. Biotechnol , vol.4 , pp. 1-10
    • Delcour, A.H.1
  • 205
    • 1242276733 scopus 로고    scopus 로고
    • IMGT standardized criteria for statistical analysis of immunoglobulin V-REGION amino acid properties
    • Pommie, C.; Levadoux, S.; Sabatier, R.; Lefranc, G.; Lefranc, M. P. IMGT standardized criteria for statistical analysis of immunoglobulin V-REGION amino acid properties. J. Mol. Recognit. 2004, 17, 17-32.
    • (2004) J. Mol. Recognit , vol.17 , pp. 17-32
    • Pommie, C.1    Levadoux, S.2    Sabatier, R.3    Lefranc, G.4    Lefranc, M.P.5
  • 207
    • 0037025325 scopus 로고    scopus 로고
    • Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate
    • Li, H.; Ryan, T. J.; Chave, K. J.; Van Roey, P. Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate. J. Biol. Chem. 2002, 277, 24522-24529.
    • (2002) J. Biol. Chem , vol.277 , pp. 24522-24529
    • Li, H.1    Ryan, T.J.2    Chave, K.J.3    Van Roey, P.4
  • 208
    • 0036069067 scopus 로고    scopus 로고
    • Structure of CcmG/DsbE at 1.14 A resolution: High-fidelity reducing activity in an indiscriminately oxidizing environment
    • Edeling, M. A.; Guddat, L. W.; Fabianek, R. A.; Thony-Meyer, L.; Martin, J. L. Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment. Structure 2002, 10, 973-979.
    • (2002) Structure , vol.10 , pp. 973-979
    • Edeling, M.A.1    Guddat, L.W.2    Fabianek, R.A.3    Thony-Meyer, L.4    Martin, J.L.5
  • 209
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution
    • Katti, S. K.; LeMaster, D. M.; Eklund, H. Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution. J. Mol. Biol 1990, 212, 167-184.
    • (1990) J. Mol. Biol , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 210
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin, J. L.; Bardwell, J. C.; Kuriyan, J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 1993, 365, 464-468.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2    Kuriyan, J.3
  • 211
  • 212
    • 0035979799 scopus 로고    scopus 로고
    • Structure of the soluble domain of a membrane-anchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties
    • Capitani, G.; Rossmann, R.; Sargent, D. F.; Grutter, M. G.; Richmond, T. J.; Hennecke, H. Structure of the soluble domain of a membrane-anchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties. J. Mol. Biol. 2001, 311, 1037-1048.
    • (2001) J. Mol. Biol , vol.311 , pp. 1037-1048
    • Capitani, G.1    Rossmann, R.2    Sargent, D.F.3    Grutter, M.G.4    Richmond, T.J.5    Hennecke, H.6
  • 213
    • 23044489264 scopus 로고    scopus 로고
    • C.TonB-dependent outer membrane transport: Going for Baroque?
    • Wiener, M. C.TonB-dependent outer membrane transport: going for Baroque? Curr. Opin. Struct. Biol. 2005, 15, 394-400.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 394-400
    • Wiener, M.1
  • 214
    • 0027403024 scopus 로고    scopus 로고
    • Xue, F.; Cooley, L. kelch encodes a component of intercellular bridges in Drosophila egg chambers. Cell 1993, 72, 681-693.
    • Xue, F.; Cooley, L. kelch encodes a component of intercellular bridges in Drosophila egg chambers. Cell 1993, 72, 681-693.
  • 215
    • 0028231273 scopus 로고
    • Drosophila kelch motif is derived from a common enzyme fold
    • Bork, P.; Doolittle, R. F. Drosophila kelch motif is derived from a common enzyme fold. J. Mol. Biol. 1994, 236, 1277-1282.
    • (1994) J. Mol. Biol , vol.236 , pp. 1277-1282
    • Bork, P.1    Doolittle, R.F.2
  • 216
    • 0033961690 scopus 로고    scopus 로고
    • The kelch repeat superfamily of proteins: Propellers of cell function
    • Adams, J.; Kelso, R.; Cooley, L. The kelch repeat superfamily of proteins: propellers of cell function. Trends Cell Biol. 2000, 10, 17-24.
    • (2000) Trends Cell Biol , vol.10 , pp. 17-24
    • Adams, J.1    Kelso, R.2    Cooley, L.3
  • 217
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi, L. K.; Cammett, T. J.; Desrosiers, D. C.; Peng, Z. Y. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci. 2004, 13, 1435-1448.
    • (2004) Protein Sci , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1    Cammett, T.J.2    Desrosiers, D.C.3    Peng, Z.Y.4
  • 218
    • 27744463780 scopus 로고    scopus 로고
    • CBS domains: Structure, function, and pathology in human proteins
    • Ignoul, S.; Eggermont, J. CBS domains: structure, function, and pathology in human proteins. Am. J. Physiol: Cell Physiol. 2005, 289, C1369-1378.
    • (2005) Am. J. Physiol: Cell Physiol , vol.289
    • Ignoul, S.1    Eggermont, J.2
  • 220
    • 5144227841 scopus 로고    scopus 로고
    • Retroelements and the human genome: New perspectives on an old relation
    • Bannert, N.; Kurth, R. Retroelements and the human genome: new perspectives on an old relation. Proc. Natl. Acad. Sci. USA. 2004, 101 Suppl 2, 14572-14579.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.SUPPL. 2 , pp. 14572-14579
    • Bannert, N.1    Kurth, R.2
  • 221
    • 0036798062 scopus 로고    scopus 로고
    • Retroelement distributions in the human genome: Variations associated with age and proximity to genes
    • Medstrand, P.; van de Lagemaat, L. N.; Mager, D. L. Retroelement distributions in the human genome: variations associated with age and proximity to genes. Genome Res. 2002, 12, 1483-1495.
    • (2002) Genome Res , vol.12 , pp. 1483-1495
    • Medstrand, P.1    van de Lagemaat, L.N.2    Mager, D.L.3
  • 222
    • 33847783298 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. III. Ligands, postranslational modifications and diseases associated with long disordered regions
    • Xie, H.; Vucetic, S.; Iakoucheva, L. M.; Oldfield, C.J.; Dunker, A. K.; Obradovic, Z.; Uversky, V. N. Functional anthology of intrinsic disorder. III. Ligands, postranslational modifications and diseases associated with long disordered regions. J. Proteome Res. 2007, 5, 1917-1932.
    • (2007) J. Proteome Res , vol.5 , pp. 1917-1932
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 223
    • 0036389814 scopus 로고    scopus 로고
    • Structure of domain III of the blood-stage malaria vaccine candidate, Plasmodium falciparum apical membrane antigen 1 (AMA1)
    • Nair, M.; Hinds, M. G.; Coley, A. M.; Hodder, A. N.; Foley, M.; Anders, R. F.; Norton, R. S. Structure of domain III of the blood-stage malaria vaccine candidate, Plasmodium falciparum apical membrane antigen 1 (AMA1). J. Mol. Biol. 2002, 322, 741-753.
    • (2002) J. Mol. Biol , vol.322 , pp. 741-753
    • Nair, M.1    Hinds, M.G.2    Coley, A.M.3    Hodder, A.N.4    Foley, M.5    Anders, R.F.6    Norton, R.S.7
  • 224
    • 0028283971 scopus 로고
    • A cytosolic herpes simplex virus protein inhibits antigen presentation to CD8+ T lymphocytes
    • York, I. A.; Roop, C.; Andrews, D. W.; Riddell, S. R.; Graham, F. L.; Johnson, D. C.A cytosolic herpes simplex virus protein inhibits antigen presentation to CD8+ T lymphocytes. Cell 1994, 77, 525-535.
    • (1994) Cell , vol.77 , pp. 525-535
    • York, I.A.1    Roop, C.2    Andrews, D.W.3    Riddell, S.R.4    Graham, F.L.5    Johnson, D.C.6
  • 225
    • 0030994014 scopus 로고    scopus 로고
    • Structure of the viral TAP-inhibitor ICP47 induced by membrane association
    • Beinert, D.; Neumann, L.; Uebel, S.; Tampe, R. Structure of the viral TAP-inhibitor ICP47 induced by membrane association. Biochemistry 1997, 36, 4694-4700.
    • (1997) Biochemistry , vol.36 , pp. 4694-4700
    • Beinert, D.1    Neumann, L.2    Uebel, S.3    Tampe, R.4
  • 226
    • 2542507920 scopus 로고    scopus 로고
    • Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy
    • Pfander, R.; Neumann, L.; Zweckstetter, M.; Seger, C.; Holak, T. A.; Tampe, R. Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. Biochemistry 1999, 38, 13692-13698.
    • (1999) Biochemistry , vol.38 , pp. 13692-13698
    • Pfander, R.1    Neumann, L.2    Zweckstetter, M.3    Seger, C.4    Holak, T.A.5    Tampe, R.6
  • 228
    • 0023956999 scopus 로고
    • Immunoelectron microscopic localization of circumsporozoite antigen in the differentiating exoerythrocytic trophozoite of Plasmodium berghei
    • Hamilton, A. J.; Suhrbier, A.; Nicholas, J.; Sinden, R. E. Immunoelectron microscopic localization of circumsporozoite antigen in the differentiating exoerythrocytic trophozoite of Plasmodium berghei. Cell Biol. Int. Rep. 1988, 12, 123-129.
    • (1988) Cell Biol. Int. Rep , vol.12 , pp. 123-129
    • Hamilton, A.J.1    Suhrbier, A.2    Nicholas, J.3    Sinden, R.E.4
  • 231
    • 5044222204 scopus 로고    scopus 로고
    • How did alternative splicing evolve?
    • Ast, G. How did alternative splicing evolve? Nat. Rev. Genet. 2004, 5, 773-782.
    • (2004) Nat. Rev. Genet , vol.5 , pp. 773-782
    • Ast, G.1
  • 233
    • 0028911597 scopus 로고    scopus 로고
    • Housman, D. Human DNA polymorphism. N. Engl. J. Med. 1995, 332, 318-320.
    • Housman, D. Human DNA polymorphism. N. Engl. J. Med. 1995, 332, 318-320.
  • 234
    • 0028303072 scopus 로고    scopus 로고
    • Weisgraber, K. H. Apolipoprotein E: structure-function relationships. Adv. Protein Chem. 1994, 45, 249-302.
    • Weisgraber, K. H. Apolipoprotein E: structure-function relationships. Adv. Protein Chem. 1994, 45, 249-302.
  • 235
    • 0037026730 scopus 로고    scopus 로고
    • Comparison of the stabilities and unfolding pathways of human apolipoprotein E isoforms by differential scanning calorimetry and circular dichroism
    • Acharya, P.; Segall, M. L.; Zaiou, M.; Morrow, J.; Weisgraber, K. H.; Phillips, M. C.; Lund-Katz, S.; Snow, J. Comparison of the stabilities and unfolding pathways of human apolipoprotein E isoforms by differential scanning calorimetry and circular dichroism. Biochim. Biophys. Acta 2002, 2584, 9-19.
    • (2002) Biochim. Biophys. Acta , vol.2584 , pp. 9-19
    • Acharya, P.1    Segall, M.L.2    Zaiou, M.3    Morrow, J.4    Weisgraber, K.H.5    Phillips, M.C.6    Lund-Katz, S.7    Snow, J.8
  • 236
    • 31944434700 scopus 로고    scopus 로고
    • Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality
    • Ikura, M.; Ames, J. B. Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: two ways to promote multifunctionality. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 1159-1164.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 1159-1164
    • Ikura, M.1    Ames, J.B.2
  • 239
    • 0032454584 scopus 로고    scopus 로고
    • Classification and evolution of EF-hand proteins
    • Kawasaki, H.; Nakayama, S.; Kretsinger, R. H. Classification and evolution of EF-hand proteins. BioMetals 1998, 11, 277-295.
    • (1998) BioMetals , vol.11 , pp. 277-295
    • Kawasaki, H.1    Nakayama, S.2    Kretsinger, R.H.3
  • 240
    • 33645292569 scopus 로고    scopus 로고
    • Calmodulin signaling: Analysis and prediction of a disorder-dependent molecular recognition
    • Radivojac, P.; Vucetic, S.; O'Connor, T. R.; Uversky, V. N.; Obradovic, Z.; Dunker, A. K. Calmodulin signaling: analysis and prediction of a disorder-dependent molecular recognition. Proteins 2006, 63, 398-410.
    • (2006) Proteins , vol.63 , pp. 398-410
    • Radivojac, P.1    Vucetic, S.2    O'Connor, T.R.3    Uversky, V.N.4    Obradovic, Z.5    Dunker, A.K.6
  • 241
    • 0037393557 scopus 로고    scopus 로고
    • Chromosomal translocation products engender new intracellular therapeutic technologies
    • Rabbitts, T. H.; Stocks, M. R. Chromosomal translocation products engender new intracellular therapeutic technologies. Nat. Med. 2003, 9, 383-386.
    • (2003) Nat. Med , vol.9 , pp. 383-386
    • Rabbitts, T.H.1    Stocks, M.R.2
  • 244
    • 6344280796 scopus 로고    scopus 로고
    • Recombinant EWS-FLI1 oncoprotein activates transcription
    • Uren, A.; Tcherkasskaya, 0.; Toretsky, J. A. Recombinant EWS-FLI1 oncoprotein activates transcription. Biochemistry 2004, 43, 13579-13589.
    • (2004) Biochemistry , vol.43 , pp. 13579-13589
    • Uren, A.1    Tcherkasskaya 02    Toretsky, J.A.3
  • 245
    • 0347418199 scopus 로고    scopus 로고
    • Alanine tracts: The expanding story of human illness and trinucleotide repeats
    • Brown, L. Y.; Brown, S. A. Alanine tracts: the expanding story of human illness and trinucleotide repeats. Trends Genet. 2004, 20, 51-58.
    • (2004) Trends Genet , vol.20 , pp. 51-58
    • Brown, L.Y.1    Brown, S.A.2
  • 246
    • 19444364594 scopus 로고    scopus 로고
    • The other trinucleotide repeat: Polyalanine expansion disorders
    • Albrecht, A.; Mundlos, S. The other trinucleotide repeat: polyalanine expansion disorders. Curr. Opin. Genet. Dev. 2005, 15, 285-293.
    • (2005) Curr. Opin. Genet. Dev , vol.15 , pp. 285-293
    • Albrecht, A.1    Mundlos, S.2
  • 247
    • 0034640011 scopus 로고    scopus 로고
    • Fourteen and counting: Unraveling trinucleotide repeat diseases
    • Cummings, C. J.; Zoghbi, H. Y. Fourteen and counting: unraveling trinucleotide repeat diseases. Hum. Mol. Genet. 2000, 9, 909-916.
    • (2000) Hum. Mol. Genet , vol.9 , pp. 909-916
    • Cummings, C.J.1    Zoghbi, H.Y.2
  • 248
    • 0038521282 scopus 로고    scopus 로고
    • Polyglutamines placed into context
    • La Spada, A. R.; Taylor, J. P. Polyglutamines placed into context. Neuron 2003, 38, 681-684.
    • (2003) Neuron , vol.38 , pp. 681-684
    • La Spada, A.R.1    Taylor, J.P.2
  • 249
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz, M. F. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 1999, 24, 58-63.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 250
    • 15244348259 scopus 로고    scopus 로고
    • SMARCA2 and THAP11: Potential candidates for polyglutamine disorders as evidenced from polymorphism and protein-folding simulation studies
    • Pandey, N.; Mittal, U.; Srivastava, A. K.; Mukerji, M. SMARCA2 and THAP11: potential candidates for polyglutamine disorders as evidenced from polymorphism and protein-folding simulation studies. J. Hum. Genet. 2004, 49, 596-602.
    • (2004) J. Hum. Genet , vol.49 , pp. 596-602
    • Pandey, N.1    Mittal, U.2    Srivastava, A.K.3    Mukerji, M.4
  • 251
    • 0037375786 scopus 로고    scopus 로고
    • Local protein unfolding and pathogenesis of polyglutamine-expansion diseases
    • Chen, Y. W. Local protein unfolding and pathogenesis of polyglutamine-expansion diseases. Proteins 2003, 51, 68-73.
    • (2003) Proteins , vol.51 , pp. 68-73
    • Chen, Y.W.1
  • 252
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • Chen, S.; Berthelier, V.; Hamilton, J. B.; O'Nuallain, B.; Wetzel, R. Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry 2002, 41, 7391-7399.
    • (2002) Biochemistry , vol.41 , pp. 7391-7399
    • Chen, S.1    Berthelier, V.2    Hamilton, J.B.3    O'Nuallain, B.4    Wetzel, R.5
  • 253
    • 33645281939 scopus 로고    scopus 로고
    • Characterizing the conformational ensemble of monomelic polyglutamine
    • Wang, X.; Vltalis, A.; Wyczalkowski, M. A.; Pappu, R. V. Characterizing the conformational ensemble of monomelic polyglutamine. Proteins 2006, 63, 297-311.
    • (2006) Proteins , vol.63 , pp. 297-311
    • Wang, X.1    Vltalis, A.2    Wyczalkowski, M.A.3    Pappu, R.V.4
  • 254
    • 0037181179 scopus 로고    scopus 로고
    • Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins
    • Masino, L.; Kelly, G.; Leonard, K.; Trottier, Y.; Pastore, A. Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins. FEBS Lett. 2002, 513, 267-272.
    • (2002) FEBS Lett , vol.513 , pp. 267-272
    • Masino, L.1    Kelly, G.2    Leonard, K.3    Trottier, Y.4    Pastore, A.5
  • 255
    • 33646798450 scopus 로고    scopus 로고
    • p53/p63/p73 isoforms: An orchestra of isoforms to harmonise cell differentiation and response to stress
    • Murray-Zmijewski, F.; Lane, D. P.; Bourdon, J. C. p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell differentiation and response to stress. Cell Death Differ. 2006, 13, 962-972.
    • (2006) Cell Death Differ , vol.13 , pp. 962-972
    • Murray-Zmijewski, F.1    Lane, D.P.2    Bourdon, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.