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Volumn 4, Issue NOVEMBER2015, 2015, Pages

Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain

Author keywords

[No Author keywords available]

Indexed keywords

1,2 NAPHTHOQUINONE; 1,4 NAPHTHOQUINONE; 6 CARBOXYFLUORESCEIN; AMYLOID; APOMORPHINE; BASIC BLUE 12; DIETHYLSTILBESTROL; DIMENHYDRINATE; DOPAMINE; DOXYCYCLINE; EOSIN; EPIGALLOCATECHIN GALLATE; IMMUNOGLOBULIN LAMBDA CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; JUGLONE; METHOXY 2 NAPHTHYL PROPIONIC ACID; METHYLENE BLUE; PHENOLSULFONPHTHALEIN; PHENYLALANINE; PROTEIN INHIBITOR; QUINONE DERIVATIVE; RECOMBINANT PROTEIN; RHODAMINE 6G; SALAZOSULFAPYRIDINE; SULINDAC; TAMOXIFEN; TETRACYCLINE; THIOFLAVINE; TRYPTOPHAN; UNCLASSIFIED DRUG; UNINDEXED DRUG; LIGAND;

EID: 84957927035     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.10935     Document Type: Article
Times cited : (52)

References (55)
  • 2
  • 3
    • 0033855656 scopus 로고    scopus 로고
    • Review: Immunoglobulin light chain amyloidosis-the archetype of structural and pathogenic variability
    • Bellotti V, Mangione P, Merlini G. 2000. Review: immunoglobulin light chain amyloidosis-the archetype of structural and pathogenic variability. Journal of Structural Biology 130:280-289. doi: 10.1006/jsbi.2000.4248.
    • (2000) Journal of Structural Biology , vol.130 , pp. 280-289
    • Bellotti, V.1    Mangione, P.2    Merlini, G.3
  • 4
    • 33747078041 scopus 로고
    • Monomer-Dimer Forms of Bence Jones Proteins
    • Bernier GM, Putnam FW. 1963. Monomer-Dimer Forms of Bence Jones Proteins. Nature 200:223-225. doi: 10.1038/200223b0.
    • (1963) Nature , vol.200 , pp. 223-225
    • Bernier, G.M.1    Putnam, F.W.2
  • 5
    • 65449142488 scopus 로고    scopus 로고
    • AL-base: A visual platform analysis tool for the study of amyloidogenic immunoglobulin light chain sequences
    • Bodi K, Prokaeva T, Spencer B, Eberhard M, Connors LH, Seldin DC. 2009. AL-base: a visual platform analysis tool for the study of amyloidogenic immunoglobulin light chain sequences. Amyloid 16:1-8. doi: 10.1080/ 13506120802676781.
    • (2009) Amyloid , vol.16 , pp. 1-8
    • Bodi, K.1    Prokaeva, T.2    Spencer, B.3    Eberhard, M.4    Connors, L.H.5    Seldin, D.C.6
  • 6
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork P, Holm L, Sander C. 1994. The immunoglobulin fold. structural classification, sequence patterns and common core. Journal of Molecular Biology 242:309-320. doi: 10.1006/jmbi.1994.1582.
    • (1994) Journal of Molecular Biology , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 9
    • 0022456447 scopus 로고
    • Aberrant immunoglobulin synthesis in light chain amyloidosis. Free light chain and light chain fragment production by human bone marrow cells in short-term tissue culture
    • Buxbaum J. 1986. Aberrant immunoglobulin synthesis in light chain amyloidosis. free light chain and light chain fragment production by human bone marrow cells in short-term tissue culture. Journal of Clinical Investigation 78:798-806. doi: 10.1172/JCI112643.
    • (1986) Journal of Clinical Investigation , vol.78 , pp. 798-806
    • Buxbaum, J.1
  • 10
    • 0026585875 scopus 로고
    • Mechanisms of disease: Monoclonal immunoglobulin deposition. Amyloidosis, light chain deposition disease, and light and heavy chain deposition disease
    • Buxbaum J. 1992. Mechanisms of disease: monoclonal immunoglobulin deposition. amyloidosis, light chain deposition disease, and light and heavy chain deposition disease. Hematology/oncology Clinics of North America 6:323-346.
    • (1992) Hematology/Oncology Clinics of North America , vol.6 , pp. 323-346
    • Buxbaum, J.1
  • 12
    • 0017697661 scopus 로고
    • Crystal and molecular structure of the dimer of variable domains of the bence-jones protein ROY
    • Colman PM, Schramm HJ, Guss JM. 1977. Crystal and molecular structure of the dimer of variable domains of the bence-jones protein ROY. Journal of Molecular Biology 116:73-79. doi: 10.1016/0022-2836(77)90119-X.
    • (1977) Journal of Molecular Biology , vol.116 , pp. 73-79
    • Colman, P.M.1    Schramm, H.J.2    Guss, J.M.3
  • 14
    • 84875308108 scopus 로고    scopus 로고
    • The PyMol Molecular Graphics System
    • DeLano W, Schrödinger, Llc. The PyMol Molecular Graphics System. Version 1.7.4. 2002.
    • (2002) Version , vol.1 , Issue.7 , pp. 4
    • Delano, W.1    Schrödinger, L.2
  • 17
    • 0021258474 scopus 로고
    • A search for site-filling ligands in the mcg bence-jones dimer: Crystal binding studies of fluorescent compounds
    • Edmundson AB, Ely KR, Herron JN. 1984. A search for site-filling ligands in the mcg bence-jones dimer: crystal binding studies of fluorescent compounds. Molecular Immunology 21:561-576.
    • (1984) Molecular Immunology , vol.21 , pp. 561-576
    • Edmundson, A.B.1    Ely, K.R.2    Herron, J.N.3
  • 19
    • 0024791087 scopus 로고
    • Three-dimensional structure of a light chain dimer crystallized in water
    • Ely KR, Herron JN, Harker M, Edmundson AB. 1989. Three-dimensional structure of a light chain dimer crystallized in water. Journal of Molecular Biology 210:601-615. doi: 10.1016/0022-2836(89)90135-6.
    • (1989) Journal of Molecular Biology , vol.210 , pp. 601-615
    • Ely, K.R.1    Herron, J.N.2    Harker, M.3    Edmundson, A.B.4
  • 21
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink AL. 1998. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Folding & Design 3:R9-R23. doi: 10.1016/S1359-0278(98)00002-9.
    • (1998) Folding & Design , vol.3
    • Fink, A.L.1
  • 25
    • 0015150725 scopus 로고
    • Creation of "amyloid" fibrils from bence jones proteins in vitro
    • Glenner GG, Ein D, Eanes ED, Bladen HA, Terry W, Page DL. 1971. Creation of "amyloid" fibrils from bence jones proteins in vitro. Science 174:712-714. doi: 10.1126/science.174.4010.712.
    • (1971) Science , vol.174 , pp. 712-714
    • Glenner, G.G.1    Ein, D.2    Eanes, E.D.3    Bladen, H.A.4    Terry, W.5    Page, D.L.6
  • 26
    • 0015622846 scopus 로고
    • Immunoglobulin and amyloid fibril proteins
    • Glenner GG. 1973. Immunoglobulin and amyloid fibril proteins. British Journal of Haematology 24:533-537. doi: 10.1111/j.1365-2141.1973.tb01679.x.
    • (1973) British Journal of Haematology , vol.24 , pp. 533-537
    • Glenner, G.G.1
  • 30
    • 0035957228 scopus 로고    scopus 로고
    • Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
    • Khurana R, Gillespie JR, Talapatra A, Minert LJ, Ionescu-Zanetti C, Millett I, Fink AL. 2001. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40: 3525-3535. doi: 10.1021/bi001782b.
    • (2001) Biochemistry , vol.40 , pp. 3525-3535
    • Khurana, R.1    Gillespie, J.R.2    Talapatra, A.3    Minert, L.J.4    Ionescu-Zanetti, C.5    Millett, I.6    Fink, A.L.7
  • 31
    • 0016690743 scopus 로고
    • A type kappa bence jones protein containing a cysteinyl residue in the variable region
    • Kishida F, Azuma T, Hamaguchi K. 1975. A type kappa bence jones protein containing a cysteinyl residue in the variable region. Journal of Biochemistry 77:481-491.
    • (1975) Journal of Biochemistry , vol.77 , pp. 481-491
    • Kishida, F.1    Azuma, T.2    Hamaguchi, K.3
  • 32
    • 0034796505 scopus 로고    scopus 로고
    • Amyloidosis: A convoluted story
    • Kyle RA. 2001. Amyloidosis: a convoluted story. British Journal of Haematology 114:529-538.
    • (2001) British Journal of Haematology , vol.114 , pp. 529-538
    • Kyle, R.A.1
  • 33
    • 84969422592 scopus 로고    scopus 로고
    • Amyloidosis: A brief history
    • Kyle RA. 2011. Amyloidosis: a brief history. Amyloid 18 Suppl 1:6-7. doi: 10.3109/13506129.2011.574354001.
    • (2011) Amyloid 18 Suppl , vol.1 , pp. 6-7
    • Kyle, R.A.1
  • 38
    • 0024442433 scopus 로고
    • Evolution of variable and constant domains and joining segments of rearranging immunoglobulins
    • Marchalonis JJ, Schluter SF. 1989. Evolution of variable and constant domains and joining segments of rearranging immunoglobulins. Faseb Journal 3:2469-2479.
    • (1989) Faseb Journal , vol.3 , pp. 2469-2479
    • Marchalonis, J.J.1    Schluter, S.F.2
  • 42
    • 0032552958 scopus 로고    scopus 로고
    • Fragments of the constant region of immunoglobulin light chains are constituents of Al-amyloid proteins
    • Olsen KE, Sletten K, Westermark P. 1998. Fragments of the constant region of immunoglobulin light chains are constituents of Al-amyloid proteins. Biochemical and Biophysical Research Communications 251:642-647. doi: 10.1006/bbrc.1998.9508.
    • (1998) Biochemical and Biophysical Research Communications , vol.251 , pp. 642-647
    • Olsen, K.E.1    Sletten, K.2    Westermark, P.3
  • 44
    • 33947409120 scopus 로고    scopus 로고
    • Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation
    • Qin Z, Hu D, Zhu M, Fink AL. 2007. Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation. Biochemistry 46:3521-3531. doi: 10.1021/bi061716v.
    • (2007) Biochemistry , vol.46 , pp. 3521-3531
    • Qin, Z.1    Hu, D.2    Zhu, M.3    Fink, A.L.4
  • 45
    • 0018627375 scopus 로고
    • Sequences at the somatic recombination sites of immunoglobulin light-chain genes
    • Sakano H, Hüppi K, Heinrich G, Tonegawa S. 1979. Sequences at the somatic recombination sites of immunoglobulin light-chain genes. Nature 280:288-294. doi: 10.1038/280288a0.
    • (1979) Nature , vol.280 , pp. 288-294
    • Sakano, H.1    Hüppi, K.2    Heinrich, G.3    Tonegawa, S.4
  • 46
    • 84969001783 scopus 로고
    • The attractions of proteins for small molecules and ions
    • Scatchard G. 1949. The attractions of proteins for small molecules and ions. Annals of the New York Academy of Sciences 51:660-672. doi: 10.1111/j.1749-6632.1949.tb27297.x.
    • (1949) Annals of the New York Academy of Sciences , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 47
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe JD, Cohen AS. 2000. Review: history of the amyloid fibril. Journal of Structural Biology 130:88-98. doi: 10.1006/jsbi.2000.4221.
    • (2000) Journal of Structural Biology , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 48
    • 84908547666 scopus 로고    scopus 로고
    • Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis
    • Sipe JD, Benson MD, Buxbaum JN, Ikeda S, Merlini G, Saraiva MJ, Westermark P. 2014. Nomenclature 2014: amyloid fibril proteins and clinical classification of the amyloidosis. Amyloid 21:221-224. doi: 10.3109/13506129.2014.964858.
    • (2014) Amyloid , vol.21 , pp. 221-224
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.4    Merlini, G.5    Saraiva, M.J.6    Westermark, P.7
  • 49
    • 0029111662 scopus 로고
    • Structural and functional properties of human lambda-light-chain variable-region subgroups
    • Solomon A, Weiss DT. 1995. Structural and functional properties of human lambda-light-chain variable-region subgroups. Clinical and Diagnostic Laboratory Immunology 2:387-394.
    • (1995) Clinical and Diagnostic Laboratory Immunology , vol.2 , pp. 387-394
    • Solomon, A.1    Weiss, D.T.2
  • 50
    • 77049272061 scopus 로고
    • Comparison of the binding properties of bovine plasma albumin and polyvinylpyrrolidone
    • Spitzer R, McDonald H. 1956. Comparison of the binding properties of bovine plasma albumin and polyvinylpyrrolidone. Clinica Chimica Acta 1:545-556. doi: 10.1016/0009-8981(56)90042-0.
    • (1956) Clinica Chimica Acta , vol.1 , pp. 545-556
    • Spitzer, R.1    McDonald, H.2
  • 51
    • 0037994312 scopus 로고    scopus 로고
    • Comparison of the three-dimensional structures of a human bence-jones dimer crystallized on earth and aboard US space shuttle mission STS-95
    • Terzyan SS, Bourne CR, Ramsland PA, Bourne PC, Edmundson AB. 2003. Comparison of the three-dimensional structures of a human bence-jones dimer crystallized on earth and aboard US space shuttle mission STS-95. Journal of Molecular Recognition 16:83-90. doi: 10.1002/jmr.610.
    • (2003) Journal of Molecular Recognition , vol.16 , pp. 83-90
    • Terzyan, S.S.1    Bourne, C.R.2    Ramsland, P.A.3    Bourne, P.C.4    Edmundson, A.B.5
  • 52
    • 73949091104 scopus 로고    scopus 로고
    • Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens
    • Vrana JA, Gamez JD, Madden BJ, Theis JD, Bergen HR, Dogan A. 2009. Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens. Blood 114: 4957-4959. doi: 10.1182/blood-2009-07-230722.
    • (2009) Blood , vol.114 , pp. 4957-4959
    • Vrana, J.A.1    Gamez, J.D.2    Madden, B.J.3    Theis, J.D.4    Bergen, H.R.5    Dogan, A.6
  • 53
    • 0032830122 scopus 로고    scopus 로고
    • In vitro immunoglobulin light chain fibrillogenesis
    • Wall J, Murphy CL, Solomon A. 1999. In vitro immunoglobulin light chain fibrillogenesis. Methods in Enzymology 309:204-217. doi: 10.1016/S0076-6879(99)09016-3.
    • (1999) Methods in Enzymology , vol.309 , pp. 204-217
    • Wall, J.1    Murphy, C.L.2    Solomon, A.3
  • 54
    • 55749099657 scopus 로고    scopus 로고
    • Validation of a rapid equilibrium dialysis approach for the measurement of plasma protein binding
    • Waters NJ, Jones R, Williams G, Sohal B. 2008. Validation of a rapid equilibrium dialysis approach for the measurement of plasma protein binding. Journal of Pharmaceutical Sciences 97:4586-4595. doi: 10.1002/jps.21317.
    • (2008) Journal of Pharmaceutical Sciences , vol.97 , pp. 4586-4595
    • Waters, N.J.1    Jones, R.2    Williams, G.3    Sohal, B.4
  • 55
    • 0028298127 scopus 로고
    • Mutations and off-pathway aggregation of proteins
    • Wetzel R. 1994. Mutations and off-pathway aggregation of proteins. Trends in Biotechnology 12:193-198. doi: 10.1016/0167-7799(94)90082-5.
    • (1994) Trends in Biotechnology , vol.12 , pp. 193-198
    • Wetzel, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.