메뉴 건너뛰기




Volumn 158, Issue 3, 2007, Pages 344-357

Sequence analyses of Type I and Type II chains in human hair and epithelial keratin intermediate filaments: Promiscuous obligate heterodimers, Type II template for molecule formation and a rationale for heterodimer formation

Author keywords

Cytokeratins; Hair; Heterodimers; Trichocyte keratins

Indexed keywords

HETERODIMER; KERATIN;

EID: 34248523318     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.12.002     Document Type: Article
Times cited : (12)

References (52)
  • 1
    • 0027236794 scopus 로고
    • Structural basis of amino acid α-helix propensity
    • Blaber M., Zhang X.J., and Matthews B.W. Structural basis of amino acid α-helix propensity. Science 260 (1993) 1637-1640
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.J.2    Matthews, B.W.3
  • 2
    • 0028222235 scopus 로고
    • Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
    • Chakrabarrty A., Kortemme T., and Baldwin R.L. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci. 3 (1994) 843-852
    • (1994) Protein Sci. , vol.3 , pp. 843-852
    • Chakrabarrty, A.1    Kortemme, T.2    Baldwin, R.L.3
  • 3
    • 0023279460 scopus 로고
    • Amino acid sequence and structural repeats in schistosome paramyosin match those of myosin
    • Cohen C., Lanar D.E., and Parry D.A.D. Amino acid sequence and structural repeats in schistosome paramyosin match those of myosin. Biosci. Rep. 7 (1987) 11-16
    • (1987) Biosci. Rep. , vol.7 , pp. 11-16
    • Cohen, C.1    Lanar, D.E.2    Parry, D.A.D.3
  • 4
    • 33749357063 scopus 로고
    • Intermediate filament structure: Analysis of sequence homologies
    • Conway J.F., and Parry D.A.D. Intermediate filament structure: Analysis of sequence homologies. Int. J. Biol. Macromol. 10 (1988) 106-112
    • (1988) Int. J. Biol. Macromol. , vol.10 , pp. 106-112
    • Conway, J.F.1    Parry, D.A.D.2
  • 5
    • 0025341392 scopus 로고
    • Elucidating the early stages of keratin filament assembly
    • Coulombe P.A., and Fuchs E. Elucidating the early stages of keratin filament assembly. J. Cell Biol. 11 (1990) 153-169
    • (1990) J. Cell Biol. , vol.11 , pp. 153-169
    • Coulombe, P.A.1    Fuchs, E.2
  • 7
    • 0037403823 scopus 로고    scopus 로고
    • Macrofibril assembly in trichocyte (hard α-) keratins
    • Fraser R.D.B., and Parry D.A.D. Macrofibril assembly in trichocyte (hard α-) keratins. J. Struct. Biol. 142 (2003) 319-325
    • (2003) J. Struct. Biol. , vol.142 , pp. 319-325
    • Fraser, R.D.B.1    Parry, D.A.D.2
  • 8
    • 23044453627 scopus 로고    scopus 로고
    • The three-dimensional structure of trichocyte (hard α-) keratin intermediate filaments: features of the molecular packing deduced from the sites of induced crosslinks
    • Fraser R.D.B., and Parry D.A.D. The three-dimensional structure of trichocyte (hard α-) keratin intermediate filaments: features of the molecular packing deduced from the sites of induced crosslinks. J. Struct. Biol. 151 (2005) 171-181
    • (2005) J. Struct. Biol. , vol.151 , pp. 171-181
    • Fraser, R.D.B.1    Parry, D.A.D.2
  • 9
    • 0020171992 scopus 로고
    • Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments
    • Geisler N., Kaufmann E., and Weber K. Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments. Cell 30 (1982) 277-286
    • (1982) Cell , vol.30 , pp. 277-286
    • Geisler, N.1    Kaufmann, E.2    Weber, K.3
  • 10
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P.B., Zhang T., Kim P.S., and Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262 (1993) 1401-1407
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 11
    • 0028290358 scopus 로고
    • Function of type I and type II keratin head domains: Their role in dimer, tetramer and filament formation
    • Hatzfeld M., and Burba M. Function of type I and type II keratin head domains: Their role in dimer, tetramer and filament formation. J. Cell Sci. 107 (1994) 1959-1972
    • (1994) J. Cell Sci. , vol.107 , pp. 1959-1972
    • Hatzfeld, M.1    Burba, M.2
  • 12
    • 0025239701 scopus 로고
    • The coiled-coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratin: use of site-specific mutagenesis and recombinant protein expression
    • Hatzfeld M., and Weber K. The coiled-coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratin: use of site-specific mutagenesis and recombinant protein expression. J. Cell Biol. 110 (1990) 1199-1210
    • (1990) J. Cell Biol. , vol.110 , pp. 1199-1210
    • Hatzfeld, M.1    Weber, K.2
  • 13
    • 0025801822 scopus 로고
    • Interactions of intermediate filament proteins from wool
    • Herrling J., and Sparrow L.G. Interactions of intermediate filament proteins from wool. Int. J. Biol. Macromol. 13 (1991) 115-119
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 115-119
    • Herrling, J.1    Sparrow, L.G.2
  • 14
    • 0032247869 scopus 로고    scopus 로고
    • Structure, assembly and dynamics of intermediate filaments
    • Herrmann H., and Harris J.R. (Eds), Plenum Press, New York
    • Herrmann H., and Aebi U. Structure, assembly and dynamics of intermediate filaments. In: Herrmann H., and Harris J.R. (Eds). Subcellular Biochemistry: Intermediate Filaments vol. 31 (1998), Plenum Press, New York 319-362
    • (1998) Subcellular Biochemistry: Intermediate Filaments , vol.31 , pp. 319-362
    • Herrmann, H.1    Aebi, U.2
  • 15
    • 0037282536 scopus 로고    scopus 로고
    • Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation
    • Herrmann H., Hesse M., Reichenzeller M., Aebi U., and Magin T.M. Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation. Int. Rev. Cytol. 223 (2003) 83-175
    • (2003) Int. Rev. Cytol. , vol.223 , pp. 83-175
    • Herrmann, H.1    Hesse, M.2    Reichenzeller, M.3    Aebi, U.4    Magin, T.M.5
  • 16
    • 0021918946 scopus 로고
    • Prediction of chain flexibility in proteins
    • Karplus P.A., and Schulz G.E. Prediction of chain flexibility in proteins. Naturwissenschaften 72 (1985) 212-213
    • (1985) Naturwissenschaften , vol.72 , pp. 212-213
    • Karplus, P.A.1    Schulz, G.E.2
  • 17
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of α-helices: Local motifs, long-range electrostatics, ionic strength dependence and predictions of NMR parameters
    • Lacroix E., Viguera A.R., and Serrano L. Elucidating the folding problem of α-helices: Local motifs, long-range electrostatics, ionic strength dependence and predictions of NMR parameters. J. Mol. Biol. 284 (1998) 173-191
    • (1998) J. Mol. Biol. , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 18
    • 16844383908 scopus 로고    scopus 로고
    • The keratins of the human hair follicle
    • Langbein L., and Schweizer J. The keratins of the human hair follicle. Int. Rev. Cytol. 243 (2006) 1-78
    • (2006) Int. Rev. Cytol. , vol.243 , pp. 1-78
    • Langbein, L.1    Schweizer, J.2
  • 19
    • 23844528832 scopus 로고    scopus 로고
    • Type II keratins precede type I keratins during early embryonic development
    • Lu H., Hesse M., Peters B., and Magin T. Type II keratins precede type I keratins during early embryonic development. Eur. J. Cell Biol. 84 (2005) 709-718
    • (2005) Eur. J. Cell Biol. , vol.84 , pp. 709-718
    • Lu, H.1    Hesse, M.2    Peters, B.3    Magin, T.4
  • 20
    • 33746196660 scopus 로고    scopus 로고
    • Keratin 5 knockout mice reveal plasticity of keratin expression in the corneal epithelium
    • Lu H., Zimek A., Chen J., Hesse M., Büssow H., Weber K., and Magin T. Keratin 5 knockout mice reveal plasticity of keratin expression in the corneal epithelium. Eur. J. Cell Biol. 85 (2006) 803-811
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 803-811
    • Lu, H.1    Zimek, A.2    Chen, J.3    Hesse, M.4    Büssow, H.5    Weber, K.6    Magin, T.7
  • 21
    • 2642684550 scopus 로고    scopus 로고
    • Lessons from keratin 18 knockout mice: formation of novel filaments, secondary loss of keratin 7 and accumulation of liver-specific keratin 8-positive aggregates
    • Magin T.M., Schröder R., Leitgeb S., Wanniger F., Zatloukal K., Grund C., and Melton D.W. Lessons from keratin 18 knockout mice: formation of novel filaments, secondary loss of keratin 7 and accumulation of liver-specific keratin 8-positive aggregates. J. Cell Biol. 140 (1998) 1441-1451
    • (1998) J. Cell Biol. , vol.140 , pp. 1441-1451
    • Magin, T.M.1    Schröder, R.2    Leitgeb, S.3    Wanniger, F.4    Zatloukal, K.5    Grund, C.6    Melton, D.W.7
  • 22
    • 0018077908 scopus 로고
    • Hydrophobic character of amino acid residues in globular proteins
    • Manavalan P., and Ponnuswamy P.K. Hydrophobic character of amino acid residues in globular proteins. Nature 275 (1978) 673-674
    • (1978) Nature , vol.275 , pp. 673-674
    • Manavalan, P.1    Ponnuswamy, P.K.2
  • 23
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: evidence for an unstaggered structure
    • McLachlan A.D., and Stewart M. Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98 (1975) 293-304
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 24
    • 0017136639 scopus 로고
    • The 14-fold periodicity in α-tropomyosin and the interaction with actin
    • McLachlan A.D., and Stewart M. The 14-fold periodicity in α-tropomyosin and the interaction with actin. J. Mol. Biol. 103 (1976) 271-298
    • (1976) J. Mol. Biol. , vol.103 , pp. 271-298
    • McLachlan, A.D.1    Stewart, M.2
  • 25
    • 0020484490 scopus 로고
    • Periodic charge distribution in the intermediate filament proteins desmin and vimentin
    • McLachlan A.D., and Stewart M. Periodic charge distribution in the intermediate filament proteins desmin and vimentin. J. Mol. Biol. 162 (1982) 693-698
    • (1982) J. Mol. Biol. , vol.162 , pp. 693-698
    • McLachlan, A.D.1    Stewart, M.2
  • 27
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximations within the AGADIR model of α-helix formation
    • Munoz V., and Serrano L. Development of the multiple sequence approximations within the AGADIR model of α-helix formation. Biopolymers 41 (1997) 495-509
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 29
    • 0035255017 scopus 로고    scopus 로고
    • Quantitative comparison of the ability of hydropathy scales to recognize surface β-strands in proteins
    • Palliser C.C., and Parry D.A.D. Quantitative comparison of the ability of hydropathy scales to recognize surface β-strands in proteins. Proteins: Struct. Funct. Genet. 42 (2001) 243-255
    • (2001) Proteins: Struct. Funct. Genet. , vol.42 , pp. 243-255
    • Palliser, C.C.1    Parry, D.A.D.2
  • 30
    • 0019873745 scopus 로고
    • Structure of rabbit skeletal myosin: analysis of the amino acid sequence of two fragments from the rod region
    • Parry D.A.D. Structure of rabbit skeletal myosin: analysis of the amino acid sequence of two fragments from the rod region. J. Mol. Biol. 153 (1981) 459-464
    • (1981) J. Mol. Biol. , vol.153 , pp. 459-464
    • Parry, D.A.D.1
  • 31
    • 17444414616 scopus 로고    scopus 로고
    • Microdissection of the sequence and structure of intermediate filament chains
    • Parry D.A.D. Microdissection of the sequence and structure of intermediate filament chains. Adv. Prot. Chem. 70 (2005) 113-142
    • (2005) Adv. Prot. Chem. , vol.70 , pp. 113-142
    • Parry, D.A.D.1
  • 32
    • 33747768593 scopus 로고    scopus 로고
    • Hendecad repeat in segment 2A and linker L2 of intermediate filament chains implies the possibility of a right-handed coiled coil structure
    • Parry D.A.D. Hendecad repeat in segment 2A and linker L2 of intermediate filament chains implies the possibility of a right-handed coiled coil structure. J. Struct. Biol. 155 (2006) 370-374
    • (2006) J. Struct. Biol. , vol.155 , pp. 370-374
    • Parry, D.A.D.1
  • 33
    • 0001292056 scopus 로고
    • Intermediate filament structure: 1. Analysis of IF protein sequence data
    • Parry D.A.D., and Fraser R.D.B. Intermediate filament structure: 1. Analysis of IF protein sequence data. Int. J. Biol. Macromol. 7 (1985) 203-213
    • (1985) Int. J. Biol. Macromol. , vol.7 , pp. 203-213
    • Parry, D.A.D.1    Fraser, R.D.B.2
  • 34
    • 0031657562 scopus 로고    scopus 로고
    • Hard α-keratin intermediate filament chains: substructure of the N- and C-terminal domains and the predicted structure and function of the C-terminal domains of type I and type II chains
    • Parry D.A.D., and North A.C.T. Hard α-keratin intermediate filament chains: substructure of the N- and C-terminal domains and the predicted structure and function of the C-terminal domains of type I and type II chains. J. Struct. Biol. 122 (1998) 67-75
    • (1998) J. Struct. Biol. , vol.122 , pp. 67-75
    • Parry, D.A.D.1    North, A.C.T.2
  • 36
    • 0033498452 scopus 로고    scopus 로고
    • Intermediate filaments: molecular architecture, assembly, dynamics and polymorphism
    • Parry D.A.D., and Steinert P.M. Intermediate filaments: molecular architecture, assembly, dynamics and polymorphism. Q. Rev. Biophys. 32 (1999) 99-187
    • (1999) Q. Rev. Biophys. , vol.32 , pp. 99-187
    • Parry, D.A.D.1    Steinert, P.M.2
  • 37
    • 0017379297 scopus 로고
    • Structure of α-keratin: structural implication of the amino acid sequences of the type I and type II chain segments
    • Parry D.A.D., Crewther W.G., Fraser R.D.B., and MacRae T.P. Structure of α-keratin: structural implication of the amino acid sequences of the type I and type II chain segments. J. Mol. Biol. 113 (1977) 449-454
    • (1977) J. Mol. Biol. , vol.113 , pp. 449-454
    • Parry, D.A.D.1    Crewther, W.G.2    Fraser, R.D.B.3    MacRae, T.P.4
  • 38
    • 0022434065 scopus 로고
    • The coiled-coil molecules of intermediate filaments consist of two parallel chains in exact axial register
    • Parry D.A.D., Steven A.C., and Steinert P.M. The coiled-coil molecules of intermediate filaments consist of two parallel chains in exact axial register. Biochem. Biophys. Res. Commun. 127 (1985) 1012-1018
    • (1985) Biochem. Biophys. Res. Commun. , vol.127 , pp. 1012-1018
    • Parry, D.A.D.1    Steven, A.C.2    Steinert, P.M.3
  • 39
    • 0035914358 scopus 로고    scopus 로고
    • Subfilamentous protofibril structures in fibrous proteins: cross-linking evidence for protofibrils in intermediate filaments
    • Parry D.A.D., Marekov L.N., and Steinert P.M. Subfilamentous protofibril structures in fibrous proteins: cross-linking evidence for protofibrils in intermediate filaments. J. Biol. Chem. 276 (2001) 39253-39258
    • (2001) J. Biol. Chem. , vol.276 , pp. 39253-39258
    • Parry, D.A.D.1    Marekov, L.N.2    Steinert, P.M.3
  • 40
    • 18744373599 scopus 로고    scopus 로고
    • A role for the 1A and L1 rod domain segments in head domain organization and function of intermediate filaments: structural analysis of trichocyte keratin
    • Parry D.A.D., Marekov L.N., Steinert P.M., and Smith T.A. A role for the 1A and L1 rod domain segments in head domain organization and function of intermediate filaments: structural analysis of trichocyte keratin. J. Struct. Biol. 137 (2002) 97-108
    • (2002) J. Struct. Biol. , vol.137 , pp. 97-108
    • Parry, D.A.D.1    Marekov, L.N.2    Steinert, P.M.3    Smith, T.A.4
  • 41
    • 0035158066 scopus 로고    scopus 로고
    • Complete cytolysis and neonatal lethality in keratin 5 knockout mice reveal its fundamental role in skin integrity and in epidermolysis bullosa simplex
    • Peters B., Kirfel J., Büssow H., Vidal M., and Magin T.M. Complete cytolysis and neonatal lethality in keratin 5 knockout mice reveal its fundamental role in skin integrity and in epidermolysis bullosa simplex. Mol. Biol. Cell. 12 (2001) 1775-1789
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 1775-1789
    • Peters, B.1    Kirfel, J.2    Büssow, H.3    Vidal, M.4    Magin, T.M.5
  • 42
    • 20544464087 scopus 로고    scopus 로고
    • Human KAP genes, only the half of it? Extensive size polymorphism in the hair-keratin-associated protein genes
    • Rogers M.A., and Schweizer J. Human KAP genes, only the half of it? Extensive size polymorphism in the hair-keratin-associated protein genes. J. Invest. Dermatol. 124 (2005) 7-9
    • (2005) J. Invest. Dermatol. , vol.124 , pp. 7-9
    • Rogers, M.A.1    Schweizer, J.2
  • 43
    • 18744388274 scopus 로고    scopus 로고
    • Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for the coiled-coil segment 1A and linker L1
    • Smith T.A., Strelkov S.V., Burkhard P., Aebi U., and Parry D.A.D. Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for the coiled-coil segment 1A and linker L1. J. Struct. Biol. 137 (2002) 128-145
    • (2002) J. Struct. Biol. , vol.137 , pp. 128-145
    • Smith, T.A.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4    Parry, D.A.D.5
  • 44
    • 0025284699 scopus 로고
    • The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type II heterodimer
    • Steinert P.M. The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type II heterodimer. J. Biol. Chem. 265 (1990) 8766-8774
    • (1990) J. Biol. Chem. , vol.265 , pp. 8766-8774
    • Steinert, P.M.1
  • 45
    • 0027476386 scopus 로고
    • The conserved H1 domain of the type II keratin 1 chain plays an essential role in the alignment of nearest-neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two- to four-molecule level of structure
    • Steinert P.M., and Parry D.A.D. The conserved H1 domain of the type II keratin 1 chain plays an essential role in the alignment of nearest-neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two- to four-molecule level of structure. J. Biol. Chem. 268 (1993) 2878-2887
    • (1993) J. Biol. Chem. , vol.268 , pp. 2878-2887
    • Steinert, P.M.1    Parry, D.A.D.2
  • 46
    • 0027160195 scopus 로고
    • Keratin intermediate filament structure: crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly
    • Steinert P.M., Marekov L.N., Fraser R.D.B., and Parry D.A.D. Keratin intermediate filament structure: crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly. J. Mol. Biol. 230 (1993) 436-452
    • (1993) J. Mol. Biol. , vol.230 , pp. 436-452
    • Steinert, P.M.1    Marekov, L.N.2    Fraser, R.D.B.3    Parry, D.A.D.4
  • 47
    • 0027501845 scopus 로고
    • Conservation of the structure of keratin intermediate filaments: molecular mechanism by which different keratin molecules integrate into pre-existing keratin intermediate filaments during differentiation
    • Steinert P.M., Marekov L.N., and Parry D.A.D. Conservation of the structure of keratin intermediate filaments: molecular mechanism by which different keratin molecules integrate into pre-existing keratin intermediate filaments during differentiation. Biochemistry 32 (1993) 10046-10056
    • (1993) Biochemistry , vol.32 , pp. 10046-10056
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.D.3
  • 48
    • 0027435278 scopus 로고
    • Diversity of intermediate filament structure: evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments
    • Steinert P.M., Marekov L.N., and Parry D.A.D. Diversity of intermediate filament structure: evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments. J. Biol. Chem. 268 (1993) 24916-24925
    • (1993) J. Biol. Chem. , vol.268 , pp. 24916-24925
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.D.3
  • 49
    • 0033555523 scopus 로고    scopus 로고
    • Molecular parameters of type IV α-internexin and type IV-type III α-internexin-vimentin copolymer intermediate filaments
    • Steinert P.M., Marekov L.N., and Parry D.A.D. Molecular parameters of type IV α-internexin and type IV-type III α-internexin-vimentin copolymer intermediate filaments. J. Biol. Chem. 274 (1999) 1657-1666
    • (1999) J. Biol. Chem. , vol.274 , pp. 1657-1666
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.D.3
  • 51
    • 0034739847 scopus 로고    scopus 로고
    • In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulfide bonding
    • Wang H., Parry D.A.D., Jones L.N., Idler W.W., Marekov L.N., and Steinert P.M. In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulfide bonding. J. Cell Biol. 151 (2000) 1459-1468
    • (2000) J. Cell Biol. , vol.151 , pp. 1459-1468
    • Wang, H.1    Parry, D.A.D.2    Jones, L.N.3    Idler, W.W.4    Marekov, L.N.5    Steinert, P.M.6
  • 52
    • 18744398716 scopus 로고    scopus 로고
    • Cryo-electron microscopy of trichocyte (hard α-keratin) intermediate filaments reveals a low-density core
    • Watts N.R., Jones L.N., Cheng N., Wall J.S., Parry D.A.D., and Steven A.C. Cryo-electron microscopy of trichocyte (hard α-keratin) intermediate filaments reveals a low-density core. J. Struct. Biol. 137 (2002) 109-118
    • (2002) J. Struct. Biol. , vol.137 , pp. 109-118
    • Watts, N.R.1    Jones, L.N.2    Cheng, N.3    Wall, J.S.4    Parry, D.A.D.5    Steven, A.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.