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Volumn 125, Issue 2, 1999, Pages 422-429

Molecular structure of the amyloid-forming protein kappa I Bre

Author keywords

Amyloidosis; Bence Jones protein; Fibril model; X ray crystallography

Indexed keywords

AMYLOID PROTEIN; BENCE JONES PROTEIN; WATER;

EID: 0033032082     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022303     Document Type: Article
Times cited : (11)

References (26)
  • 2
    • 0000304402 scopus 로고
    • Eine spezifische Amyloidfärbung wit Kongorot
    • Bennhold, H. (1922) Eine spezifische Amyloidfärbung wit Kongorot. Meunch. Med. Wocheschr. 69, 1537-1538
    • (1922) Meunch. Med. Wocheschr. , vol.69 , pp. 1537-1538
    • Bennhold, H.1
  • 3
    • 0000504561 scopus 로고
    • Sur les propriétés optiques de l'amyloïde. c.r. Soc
    • Divry, P. and Florkin, M. (1927) Sur les propriétés optiques de l'amyloïde. c.r. soc. Belge biol. 97, 1808-1810
    • (1927) Belge Biol. , vol.97 , pp. 1808-1810
    • Divry, P.1    Florkin, M.2
  • 4
    • 0001611370 scopus 로고
    • Electron microscope observations on a fibrous component in amyloid of diverse origins
    • Cohen, A.S. and Calkins, E. (1959) Electron microscope observations on a fibrous component in amyloid of diverse origins. Nature 183, 1202-1203
    • (1959) Nature , vol.183 , pp. 1202-1203
    • Cohen, A.S.1    Calkins, E.2
  • 5
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes, E.D. and Glenner, G.G. (1968) X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16, 673-677
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 6
    • 0015268596 scopus 로고
    • Infra red spectroscopy of human amyloid fibrils and immuno globulin proteins
    • Termine, J.K., Eanes, E.D., Ein, D., and Glenner, G.G. (1972) Infra red spectroscopy of human amyloid fibrils and immuno globulin proteins. Biopolymers 11, 1103-1113
    • (1972) Biopolymers , vol.11 , pp. 1103-1113
    • Termine, J.K.1    Eanes, E.D.2    Ein, D.3    Glenner, G.G.4
  • 8
    • 0010551538 scopus 로고
    • Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy
    • Costa, P.P., Figueira, A.S., and Bravo, F.R. (1978) Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc. Natl. Acad. Sci. USA 75, 4499-4503
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4499-4503
    • Costa, P.P.1    Figueira, A.S.2    Bravo, F.R.3
  • 9
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
    • Blake, C.C.F., Geisow, J.J., Oatley, S.J., Rerat, B., and Rerat, C. (1978) Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J. Mol. Biol. 121, 339-356
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.F.1    Geisow, J.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 10
    • 0027476367 scopus 로고
    • The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30→Met variant to 1.7 Å resolution
    • Hamilton, J.A., Steinrauf, L.K., Braden, B.C., Liepnieks, J., Benson, M.D., Holmgren, G., Sandgren, O., and Steen, L. (1993) The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30→Met variant to 1.7 Å resolution. J. Biol. Chem. 268, 2416-2424
    • (1993) J. Biol. Chem. , vol.268 , pp. 2416-2424
    • Hamilton, J.A.1    Steinrauf, L.K.2    Braden, B.C.3    Liepnieks, J.4    Benson, M.D.5    Holmgren, G.6    Sandgren, O.7    Steen, L.8
  • 12
    • 0002369913 scopus 로고    scopus 로고
    • Structural changes in transthyretin produced by the Ile109Ser mutation which results in decreased affinity for retinol-binding protein
    • Hamilton, J.A., Steinrauf, L.K., Braden, B.C., Murrell, J.R., and Benson, M.D. (1996) Structural changes in transthyretin produced by the Ile109Ser mutation which results in decreased affinity for retinol-binding protein. Amyloid: int. J. Exp. Clin. Invest. 3, 1-12
    • (1996) Amyloid: Int. J. Exp. Clin. Invest. , vol.3 , pp. 1-12
    • Hamilton, J.A.1    Steinrauf, L.K.2    Braden, B.C.3    Murrell, J.R.4    Benson, M.D.5
  • 13
    • 0027459456 scopus 로고
    • X-ray crystal structure of the Ala-109→Thr variant of human transthyretin which produces euthyroid hyper-thyroxinemia
    • Steinrauf, L.K., Hamilton, J.A., Braden, B.C., Murrell, J.R., and Benson, M.D. (1993) X-ray crystal structure of the Ala-109→Thr variant of human transthyretin which produces euthyroid hyper-thyroxinemia. J. Biol. Chem. 268, 2425-2430
    • (1993) J. Biol. Chem. , vol.268 , pp. 2425-2430
    • Steinrauf, L.K.1    Hamilton, J.A.2    Braden, B.C.3    Murrell, J.R.4    Benson, M.D.5
  • 15
    • 0028818272 scopus 로고
    • Tertiary structure of an amyloid immunoglobulin light chain protein: A proposed model for amyloid fibril formation
    • Schormann, N., Murrell, J.R., Liepnieks, J.J., and Benson, M.D. (1995) Tertiary structure of an amyloid immunoglobulin light chain protein: A proposed model for amyloid fibril formation. Proc. Natl. Acad. Sci. USA 92, 9490-9494
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9490-9494
    • Schormann, N.1    Murrell, J.R.2    Liepnieks, J.J.3    Benson, M.D.4
  • 16
    • 0017697661 scopus 로고
    • Crystal and molecular structure of the dimer of the variable domain of the Bence-Jones protein ROY
    • Colman, P.M., Schramm, H.J., and Gurs, J.M. (1977) Crystal and molecular structure of the dimer of the variable domain of the Bence-Jones protein ROY. J. Mol. Biol. 116, 73-79
    • (1977) J. Mol. Biol. , vol.116 , pp. 73-79
    • Colman, P.M.1    Schramm, H.J.2    Gurs, J.M.3
  • 17
    • 0016236512 scopus 로고
    • Crystal and molecular structure of a dimer composed of the variable portion of the Bence-Jones protein Rei
    • Epp, O., Colman, P., Fehlhammer, H., Bode, W., Schiffer, M., Huber, R., and Palm, W. (1974) Crystal and molecular structure of a dimer composed of the variable portion of the Bence-Jones protein Rei. Eur. J. Biochem. 45, 513-524
    • (1974) Eur. J. Biochem. , vol.45 , pp. 513-524
    • Epp, O.1    Colman, P.2    Fehlhammer, H.3    Bode, W.4    Schiffer, M.5    Huber, R.6    Palm, W.7
  • 19
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, W.A. (1985) Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115, 252-270
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 20
    • 0022333120 scopus 로고
    • Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO
    • Jones, T.A. (1985) Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO. Methods Enzymol. 115, 157-171
    • (1985) Methods Enzymol , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 21
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sheldrick, G. (1997) SHELXL: High-resolution refinement. Methods Enzymol. 277, 319-343
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.1
  • 24
    • 0026597444 scopus 로고
    • Free-R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992) Free-R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 25
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structure cristallines
    • Luzzati, V. (1952) Traitement statistique des erreurs dans la determination des structure cristallines. Acta Cryst. 5, 802-810
    • (1952) Acta Cryst. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 26
    • 0028556362 scopus 로고
    • Comparison of crystal structures of two homologous proteins: Structural origin of altered domain interactions in immunoglobulin light-chain dimers
    • Huang, D.-B., Chang, C.-H., Ainsworth, C., Brunger, A.T., Eulitz, M., Solomon, A., Stevens, F.J., and Schiffer, M. (1994) Comparison of crystal structures of two homologous proteins: structural origin of altered domain interactions in immunoglobulin light-chain dimers. Biochemistry 33, 14848-14857
    • (1994) Biochemistry , vol.33 , pp. 14848-14857
    • Huang, D.-B.1    Chang, C.-H.2    Ainsworth, C.3    Brunger, A.T.4    Eulitz, M.5    Solomon, A.6    Stevens, F.J.7    Schiffer, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.