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Volumn 180, Issue 1, 2012, Pages 117-124

The role of disulfide bond formation in the structural transition observed in the intermediate filaments of developing hair

Author keywords

Disulfide bonds; Hair; Hair development; Structural transition; Keratin

Indexed keywords

CYSTEINE; KERATIN;

EID: 84867000000     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.05.020     Document Type: Article
Times cited : (30)

References (27)
  • 1
    • 0020332661 scopus 로고
    • A quantitative histochemical study of sulphydryl and disulphide content during normal epidermal keratinization
    • Broekaert D., Cooreman K., Coucke P., Nsabumukunzi S., et al. A quantitative histochemical study of sulphydryl and disulphide content during normal epidermal keratinization. Histochem. J. 1982, 14:573-584.
    • (1982) Histochem. J. , vol.14 , pp. 573-584
    • Broekaert, D.1    Cooreman, K.2    Coucke, P.3    Nsabumukunzi, S.4
  • 3
    • 0022459043 scopus 로고
    • The primary structure of component 8c-1, a subunit protein of intermediate filaments in wool keratin - relationship with proteins from other intermediate filaments
    • Dowling L.M., Crewther W.G., Inglis A.S. The primary structure of component 8c-1, a subunit protein of intermediate filaments in wool keratin - relationship with proteins from other intermediate filaments. Biochem. J. 1986, 236:695-703.
    • (1986) Biochem. J. , vol.236 , pp. 695-703
    • Dowling, L.M.1    Crewther, W.G.2    Inglis, A.S.3
  • 5
    • 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., 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. 2005, 151:171-181.
    • (2005) J. Struct. Biol. , vol.151 , pp. 171-181
    • Fraser, R.D.B.1    Parry, D.A.D.2
  • 6
    • 33747807939 scopus 로고    scopus 로고
    • The three-dimensional structure of trichocyte (hard α-) keratin intermediate filaments: the nature of the repeating unit
    • Fraser R.D.B., Parry D.A.D. The three-dimensional structure of trichocyte (hard α-) keratin intermediate filaments: the nature of the repeating unit. J. Struct. Biol. 2006, 155:375-378.
    • (2006) J. Struct. Biol. , vol.155 , pp. 375-378
    • Fraser, R.D.B.1    Parry, D.A.D.2
  • 7
    • 34249934063 scopus 로고    scopus 로고
    • Structural changes in the trichocyte intermediate filaments accompanying the transition from the reduced to the oxidized form
    • Fraser R.D.B., Parry D.A.D. Structural changes in the trichocyte intermediate filaments accompanying the transition from the reduced to the oxidized form. J. Struct. Biol. 2007, 159:36-45.
    • (2007) J. Struct. Biol. , vol.159 , pp. 36-45
    • Fraser, R.D.B.1    Parry, D.A.D.2
  • 8
    • 0344519678 scopus 로고    scopus 로고
    • Structural changes in trichocyte keratin intermediate filaments during keratinization
    • Fraser R.D.B., Steinert P.M., Parry D.A.D. Structural changes in trichocyte keratin intermediate filaments during keratinization. J. Struct. Biol. 2003, 142:266-271.
    • (2003) J. Struct. Biol. , vol.142 , pp. 266-271
    • Fraser, R.D.B.1    Steinert, P.M.2    Parry, D.A.D.3
  • 9
    • 0000700060 scopus 로고
    • The coiled-coil model of α-keratin structure
    • Fraser R.D.B., MacRae T.P., Miller A. The coiled-coil model of α-keratin structure. J. Mol. Biol. 1964, 10:147-156.
    • (1964) J. Mol. Biol. , vol.10 , pp. 147-156
    • Fraser, R.D.B.1    MacRae, T.P.2    Miller, A.3
  • 11
    • 0034685607 scopus 로고    scopus 로고
    • The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly
    • Herrmann H., Strelkov S.V., Feja B., Rogers K.R., Brettel M., et al. The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly. J. Mol. Biol. 2000, 298:817-832.
    • (2000) J. Mol. Biol. , vol.298 , pp. 817-832
    • Herrmann, H.1    Strelkov, S.V.2    Feja, B.3    Rogers, K.R.4    Brettel, M.5
  • 13
    • 67349199644 scopus 로고    scopus 로고
    • Vimentin coil 1A - a molecular switch involved in the initiation of filament elongation
    • Meier M., Padilla G.P., Herrmann H., Wedig T., Hergt M., et al. Vimentin coil 1A - a molecular switch involved in the initiation of filament elongation. J. Mol. Biol. 2009, 390:245-261.
    • (2009) J. Mol. Biol. , vol.390 , pp. 245-261
    • Meier, M.1    Padilla, G.P.2    Herrmann, H.3    Wedig, T.4    Hergt, M.5
  • 15
    • 0029902659 scopus 로고    scopus 로고
    • Hard α-keratin intermediate filaments: an alternative interpretation of the low-angle equatorial X-ray diffraction pattern, and the axial disposition of putative disulphide bonds in the intra- and inter-protofilamentous networks
    • Parry D.A.D. Hard α-keratin intermediate filaments: an alternative interpretation of the low-angle equatorial X-ray diffraction pattern, and the axial disposition of putative disulphide bonds in the intra- and inter-protofilamentous networks. Int. J. Biol. Macromol. 1996, 19:207-211.
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 207-211
    • Parry, D.A.D.1
  • 16
    • 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. 2006, 155:370-374.
    • (2006) J. Struct. Biol. , vol.155 , pp. 370-374
    • Parry, D.A.D.1
  • 17
    • 18744388274 scopus 로고    scopus 로고
    • Sequence comparisons of intermediate filaments 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., Parry D.A.D. Sequence comparisons of intermediate filaments chains: evidence of a unique functional/structural role for the coiled-coil segment 1A and linker L1. J. Struct. Biol. 2002, 137:128-145.
    • (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
  • 18
    • 0024709335 scopus 로고
    • The amino acid sequence of component 7c, a type II intermediate-filament protein from wool
    • Sparrow L.G., Robinson C.P., McMahon D.T.W., Rubira M.R. The amino acid sequence of component 7c, a type II intermediate-filament protein from wool. Biochem. J. 1989, 261:1015-1022.
    • (1989) Biochem. J. , vol.261 , pp. 1015-1022
    • Sparrow, L.G.1    Robinson, C.P.2    McMahon, D.T.W.3    Rubira, M.R.4
  • 19
    • 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., 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. 1993, 268:2878-2887.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2878-2887
    • Steinert, P.M.1    Parry, D.A.D.2
  • 20
    • 0020540886 scopus 로고
    • Complete amino acid sequence of a mouse epidermal subunit and implications for the structure of intermediate filaments
    • Steinert P.M., Rice R.H., Roop D.R., Trus B.L., Steven A.C. Complete amino acid sequence of a mouse epidermal subunit and implications for the structure of intermediate filaments. Nature 1983, 302:794-800.
    • (1983) Nature , vol.302 , pp. 794-800
    • Steinert, P.M.1    Rice, R.H.2    Roop, D.R.3    Trus, B.L.4    Steven, A.C.5
  • 21
    • 0022262043 scopus 로고
    • Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits
    • Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C., Roop D.R. Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits. J. Biol. Chem. 1985, 260:7142-7149.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7142-7149
    • Steinert, P.M.1    Parry, D.A.D.2    Idler, W.W.3    Johnson, L.D.4    Steven, A.C.5    Roop, D.R.6
  • 22
    • 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., Parry D.A.D. Keratin intermediate filament structure: crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly. J. Mol. Biol. 1993, 230:436-452.
    • (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
  • 23
    • 0035793704 scopus 로고    scopus 로고
    • Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments
    • Strelkov S.V., Herrmann H., Geisler N., Lustig A., Ivaninskii S., et al. Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. J. Mol. Biol. 2001, 306:773-781.
    • (2001) J. Mol. Biol. , vol.306 , pp. 773-781
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Lustig, A.4    Ivaninskii, S.5
  • 24
    • 84856826693 scopus 로고    scopus 로고
    • Unique amino acid signatures that are evolutionarily conserved distinguish simple-type, epidermal and hair keratins
    • Strnad P., Usachov V., Debes C., Gräter F., Parry D.A.D., et al. Unique amino acid signatures that are evolutionarily conserved distinguish simple-type, epidermal and hair keratins. J. Cell Sci. 2011, 124:4221-4232.
    • (2011) J. Cell Sci. , vol.124 , pp. 4221-4232
    • Strnad, P.1    Usachov, V.2    Debes, C.3    Gräter, F.4    Parry, D.A.D.5
  • 25
    • 16244406657 scopus 로고
    • NIST Technical Note 1297 Guidelines for Evaluating and Expressing the Uncertainty of NIST Measurement Results, Physics Laboratory, National Institute of Standards and Technology.
    • Taylor, B.N., Kyatt, E.K., 1994. NIST Technical Note 1297 Guidelines for Evaluating and Expressing the Uncertainty of NIST Measurement Results, Physics Laboratory, National Institute of Standards and Technology.
    • (1994)
    • Taylor, B.N.1    Kyatt, E.K.2
  • 26
    • 79959500955 scopus 로고    scopus 로고
    • Annotation of sheep keratin intermediate filament genes and their patterns of expression
    • Yu Z., Wildermouth J.E., Wallace O.A.M., Gordon S.W., Maqbool N.J., et al. Annotation of sheep keratin intermediate filament genes and their patterns of expression. Exp. Dermatol. 2011, 20:582-588.
    • (2011) Exp. Dermatol. , vol.20 , pp. 582-588
    • Yu, Z.1    Wildermouth, J.E.2    Wallace, O.A.M.3    Gordon, S.W.4    Maqbool, N.J.5
  • 27
    • 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., et al. In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulfide bonding. J. Cell Biol. 2000, 151:1459-1468.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.