메뉴 건너뛰기




Volumn 418, Issue 2, 2012, Pages 217-221

Structures of the lamin A/C R335W and E347K mutants: Implications for dilated cardiolaminopathies

Author keywords

Coiled coil; Crystal structure; Dilated cardiomyopathy; Laminopathy; Nuclear lamins

Indexed keywords

LAMIN A; LAMIN C; MUTANT PROTEIN; NUCLEAR FACTOR;

EID: 84856657199     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.12.136     Document Type: Article
Times cited : (18)

References (43)
  • 1
    • 30344443662 scopus 로고    scopus 로고
    • Dysfunction of lamin A triggers a DNA damage response and cellular senescence
    • Lees-Miller S.P. Dysfunction of lamin A triggers a DNA damage response and cellular senescence. DNA Repair (Amst) 2006, 5:286-289.
    • (2006) DNA Repair (Amst) , vol.5 , pp. 286-289
    • Lees-Miller, S.P.1
  • 2
    • 0036347096 scopus 로고    scopus 로고
    • Life at the edge: the nuclear envelope and human disease
    • Burke B., Stewart C.L. Life at the edge: the nuclear envelope and human disease. Nat. Rev. Mol. Cell Biol. 2002, 3:575-585.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 575-585
    • Burke, B.1    Stewart, C.L.2
  • 4
    • 25144515509 scopus 로고    scopus 로고
    • Nuclear envelope, nuclear lamina, and inherited disease
    • Worman H.J., Courvalin J.C. Nuclear envelope, nuclear lamina, and inherited disease. Int. Rev. Cytol. 2005, 246:231-279.
    • (2005) Int. Rev. Cytol. , vol.246 , pp. 231-279
    • Worman, H.J.1    Courvalin, J.C.2
  • 6
    • 34247485356 scopus 로고    scopus 로고
    • A-type lamin networks in light of laminopathic diseases
    • Vlcek S., Foisner R. A-type lamin networks in light of laminopathic diseases. Biochim. Biophys. Acta 2007, 1773:661-674.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 661-674
    • Vlcek, S.1    Foisner, R.2
  • 7
    • 0036843975 scopus 로고    scopus 로고
    • Lamins: building blocks or regulators of gene expression?
    • Hutchison C.J. Lamins: building blocks or regulators of gene expression?. Nat. Rev. Mol. Cell Biol. 2002, 3:848-858.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 848-858
    • Hutchison, C.J.1
  • 8
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: integrating isolated clues
    • Zastrow M.S., Vlcek S., Wilson K.L. Proteins that bind A-type lamins: integrating isolated clues. J. Cell Sci. 2004, 117:979-987.
    • (2004) J. Cell Sci. , vol.117 , pp. 979-987
    • Zastrow, M.S.1    Vlcek, S.2    Wilson, K.L.3
  • 9
    • 7944219648 scopus 로고    scopus 로고
    • A-type lamins: guardians of the soma?
    • Hutchison C.J., Worman H.J. A-type lamins: guardians of the soma?. Nat. Cell Biol. 2004, 6:1062-1067.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1062-1067
    • Hutchison, C.J.1    Worman, H.J.2
  • 10
    • 0035169030 scopus 로고    scopus 로고
    • The A-type lamins: nuclear structural proteins as a focus for muscular dystrophy and cardiovascular diseases
    • Mounkes L.C., Burke B., Stewart C.L. The A-type lamins: nuclear structural proteins as a focus for muscular dystrophy and cardiovascular diseases. Trends Cardiovasc. Med. 2001, 11:280-285.
    • (2001) Trends Cardiovasc. Med. , vol.11 , pp. 280-285
    • Mounkes, L.C.1    Burke, B.2    Stewart, C.L.3
  • 11
    • 5144220584 scopus 로고    scopus 로고
    • Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins
    • Strelkov S.V., Schumacher J., Burkhard P., Aebi U., Herrmann H. Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins. J. Mol. Biol. 2004, 343:1067-1080.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1067-1080
    • Strelkov, S.V.1    Schumacher, J.2    Burkhard, P.3    Aebi, U.4    Herrmann, H.5
  • 12
    • 0027257461 scopus 로고
    • Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C
    • Lin F., Worman H.J. Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C. J. Biol. Chem. 1993, 268:16321-16326.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16321-16326
    • Lin, F.1    Worman, H.J.2
  • 13
    • 0023032014 scopus 로고
    • CDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins
    • Fisher D.Z., Chaudhary N., Blobel G. CDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Natl. Acad. Sci. USA 1986, 83:6450-6454.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 15
    • 0037335755 scopus 로고    scopus 로고
    • Molecular architecture of intermediate filaments
    • Strelkov S.V., Herrmann H., Aebi U. Molecular architecture of intermediate filaments. Bioessays 2003, 25:243-251.
    • (2003) Bioessays , vol.25 , pp. 243-251
    • Strelkov, S.V.1    Herrmann, H.2    Aebi, U.3
  • 19
  • 24
    • 32544437002 scopus 로고    scopus 로고
    • A homozygous mutation in the lamin A/C gene associated with a novel syndrome of arthropathy, tendinous calcinosis, and progeroid features
    • Van Esch H., Agarwal A.K., Debeer P., Fryns J.P., Garg A. A homozygous mutation in the lamin A/C gene associated with a novel syndrome of arthropathy, tendinous calcinosis, and progeroid features. J. Clin. Endocrinol. Metab. 2006, 91:517-521.
    • (2006) J. Clin. Endocrinol. Metab. , vol.91 , pp. 517-521
    • Van Esch, H.1    Agarwal, A.K.2    Debeer, P.3    Fryns, J.P.4    Garg, A.5
  • 27
    • 0028773466 scopus 로고
    • Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assemblies
    • Ferre-D'Amare A.R., Burley S.K. Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assemblies. Structure 1994, 2:357-359.
    • (1994) Structure , vol.2 , pp. 357-359
    • Ferre-D'Amare, A.R.1    Burley, S.K.2
  • 28
    • 0027109294 scopus 로고
    • Light scattering of proteins as a criterion for crystallization
    • Zulauf A., D'Arcy M. Light scattering of proteins as a criterion for crystallization. J. Crystal Growth 1992, 122:5.
    • (1992) J. Crystal Growth , vol.122 , pp. 5
    • Zulauf, A.1    D'Arcy, M.2
  • 29
    • 0000614826 scopus 로고    scopus 로고
    • An algorithm for automatic indexing of oscillation images using Fourier analysis
    • Steller I., Bolotovsky R., Rossmann M.G. An algorithm for automatic indexing of oscillation images using Fourier analysis. J. Appl. Crystallogr. 1997, 30:5.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 5
    • Steller, I.1    Bolotovsky, R.2    Rossmann, M.G.3
  • 30
    • 0028103275 scopus 로고
    • n. Collaborative Computational Project, The CCP4 suite: programs for protein crystallography, Acta Crystallogr.
    • n. Collaborative Computational Project, The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763.
    • (1994) D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 31
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30:4.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 4
    • Vagin, A.1    Teplyakov, A.2
  • 32
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D. Biol. Crystallogr. 2001, 57:122-133.
    • (2001) Acta Crystallogr. D. Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 38
    • 0022272929 scopus 로고
    • Intermediate filaments: structural conservation and divergence
    • Weber K., Geisler N. Intermediate filaments: structural conservation and divergence. Ann. NY Acad. Sci. 1985, 455:126-143.
    • (1985) Ann. NY Acad. Sci. , vol.455 , pp. 126-143
    • Weber, K.1    Geisler, N.2
  • 39
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly
    • Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R., Aebi U., Burkhard P. Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 2002, 21:1255-1266.
    • (2002) EMBO J. , vol.21 , pp. 1255-1266
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Wedig, T.4    Zimbelmann, R.5    Aebi, U.6    Burkhard, P.7
  • 41
    • 34249668426 scopus 로고    scopus 로고
    • Proteins that associate with lamins: many faces, many functions
    • Schirmer E.C., Foisner R. Proteins that associate with lamins: many faces, many functions. Exp. Cell Res. 2007, 313:2167-2179.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2167-2179
    • Schirmer, E.C.1    Foisner, R.2
  • 42
    • 77956083200 scopus 로고    scopus 로고
    • Lamin-binding Proteins, Cold Spring Harb Perspect, a000554.
    • K.L. Wilson, R. Foisner, Lamin-binding Proteins, Cold Spring Harb Perspect, Biol. 2 (2010) a000554.
    • Biol. , vol.2 , pp. 2010
    • Wilson, K.L.1    Foisner, R.2
  • 43
    • 33847412787 scopus 로고    scopus 로고
    • Nucleoplasmic lamins and their interaction partners, LAP2alpha, Rb, and BAF, in transcriptional regulation
    • Dorner D., Gotzmann J., Foisner R. Nucleoplasmic lamins and their interaction partners, LAP2alpha, Rb, and BAF, in transcriptional regulation. FEBS J. 2007, 274:1362-1373.
    • (2007) FEBS J. , vol.274 , pp. 1362-1373
    • Dorner, D.1    Gotzmann, J.2    Foisner, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.