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Volumn 155, Issue 2, 2006, Pages 375-378

The three-dimensional structure of trichocyte (hard α-) keratin intermediate filaments: The nature of the repeating unit

Author keywords

[No Author keywords available]

Indexed keywords

KERATIN;

EID: 33747807939     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2005.12.014     Document Type: Article
Times cited : (11)

References (13)
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    • Intermediate filament structure
    • Fraser R.D.B., and MacRae T.P. Intermediate filament structure. Biosci. Rep. 5 (1985) 573-579
    • (1985) Biosci. Rep. , vol.5 , pp. 573-579
    • Fraser, R.D.B.1    MacRae, T.P.2
  • 3
    • 0023929503 scopus 로고
    • Surface lattice structure in α-keratin filaments
    • Fraser R.D.B., and MacRae T.P. Surface lattice structure in α-keratin filaments. Int. J. Biol. Macromol. 10 (1988) 175-184
    • (1988) Int. J. Biol. Macromol. , vol.10 , pp. 175-184
    • Fraser, R.D.B.1    MacRae, T.P.2
  • 4
    • 0344519678 scopus 로고    scopus 로고
    • Structural changes in trichocyte keratin intermediate filaments during keratinization
    • Fraser R.D.B., Steinert P.M., and Parry D.A.D. Structural changes in trichocyte keratin intermediate filaments during keratinization. J. Struct. Biol. 142 (2003) 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
  • 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., 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
  • 6
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann H., and Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 73 (2004) 749-789
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 8
    • 0029902659 scopus 로고    scopus 로고
    • Hard α-keratin intermediate filaments: an alternative interpretation of the low-angle X-ray pattern, and the axial disposition of 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 X-ray pattern, and the axial disposition of disulphide bonds in the intra- and inter-protofilamentous networks. Int. J. Biol. Macromol. 19 (1996) 45-50
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 45-50
    • Parry, D.A.D.1
  • 9
    • 0035914358 scopus 로고    scopus 로고
    • Subfilamentous protofibril structures in fibrous proteins
    • Parry D.A.D., Marekov L.N., and Steinert P.M. Subfilamentous protofibril structures in fibrous proteins. 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
  • 10
    • 0025933468 scopus 로고
    • Analysis of the mechanism of assembly of mouse keratin 1/keratin 10 intermediate filaments in vitro suggests that intermediate filaments are built from multiple oligomeric units rather than a unique tetrameric building block
    • Steinert P.M. Analysis of the mechanism of assembly of mouse keratin 1/keratin 10 intermediate filaments in vitro suggests that intermediate filaments are built from multiple oligomeric units rather than a unique tetrameric building block. J. Struct. Biol. 107 (1991) 175-188
    • (1991) J. Struct. Biol. , vol.107 , pp. 175-188
    • Steinert, P.M.1
  • 11
    • 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
  • 12
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    • 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.